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Conserved domains on  [gi|19114010|ref|NP_593098|]
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dehydrogenase [Schizosaccharomyces pombe]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10143212)

SDR family NAD(P)-dependent oxidoreductase such as NADP-dependent L-serine/L-allothreonine dehydrogenase YdfG

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
7-256 7.05e-145

classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


:

Pssm-ID: 187604 [Multi-domain]  Cd Length: 249  Bit Score: 405.51  E-value: 7.05e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   7 KTILITGASSGIGKSTAFEIAKVAKvKLILAARRFSTVEEIAKELESKYEVSVLPLKLDVSDLKSIPGVIESLPKEFADI 86
Cdd:cd05346   1 KTVLITGASSGIGEATARRFAKAGA-KLILTGRRAERLQELADELGAKFPVKVLPLQLDVSDRESIEAALENLPEEFRDI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  87 DVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSALA 166
Cdd:cd05346  80 DILVNNAGLALGLDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYAGGNVYCATKAAVR 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010 167 QFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGDKQKADNVYKNSEPLTPEDIAEVILFALTRRENVVIADTLVFPS 246
Cdd:cd05346 160 QFSLNLRKDLIGTGIRVTNIEPGLVETEFSLVRFHGDKEKADKVYEGVEPLTPEDIAETILWVASRPAHVNINDIEIMPV 239
                       250
                ....*....|
gi 19114010 247 HQGGANHVYR 256
Cdd:cd05346 240 NQASAGHIHR 249
 
Name Accession Description Interval E-value
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
7-256 7.05e-145

classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187604 [Multi-domain]  Cd Length: 249  Bit Score: 405.51  E-value: 7.05e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   7 KTILITGASSGIGKSTAFEIAKVAKvKLILAARRFSTVEEIAKELESKYEVSVLPLKLDVSDLKSIPGVIESLPKEFADI 86
Cdd:cd05346   1 KTVLITGASSGIGEATARRFAKAGA-KLILTGRRAERLQELADELGAKFPVKVLPLQLDVSDRESIEAALENLPEEFRDI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  87 DVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSALA 166
Cdd:cd05346  80 DILVNNAGLALGLDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYAGGNVYCATKAAVR 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010 167 QFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGDKQKADNVYKNSEPLTPEDIAEVILFALTRRENVVIADTLVFPS 246
Cdd:cd05346 160 QFSLNLRKDLIGTGIRVTNIEPGLVETEFSLVRFHGDKEKADKVYEGVEPLTPEDIAETILWVASRPAHVNINDIEIMPV 239
                       250
                ....*....|
gi 19114010 247 HQGGANHVYR 256
Cdd:cd05346 240 NQASAGHIHR 249
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
1-245 2.54e-81

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 443365 [Multi-domain]  Cd Length: 240  Bit Score: 243.94  E-value: 2.54e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   1 MSRlDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELEskyeVSVLPLKLDVSDLKSIPGVIESLP 80
Cdd:COG4221   1 MSD-KGKVALITGASSGIGAATARALAA-AGARVVLAARRAERLEALAAELG----GRALAVPLDVTDEAAVEAAVAAAV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  81 KEFADIDVLINNAGLALGTDkVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCS 160
Cdd:COG4221  75 AEFGRLDVLVNNAGVALLGP-LEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010 161 TKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGDKQKADNVYKNSEPLTPEDIAEVILFALTRRENVVIAD 240
Cdd:COG4221 154 TKAAVRGLSESLRAELRPTGIRVTVIEPGAVDTEFLDSVFDGDAEAAAAVYEGLEPLTPEDVAEAVLFALTQPAHVNVNE 233

                ....*
gi 19114010 241 TLVFP 245
Cdd:COG4221 234 LVLRP 238
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
9-256 3.20e-64

bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase YdfG;


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 200.75  E-value: 3.20e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    9 ILITGASSGIGKSTAFE-IAKVAKVklILAARRFSTVEEIAKELESkyevSVLPLKLDVSDLKSIPGVIESLPKEFADID 87
Cdd:PRK10538   3 VLVTGATAGFGECITRRfIQQGHKV--IATGRRQERLQELKDELGD----NLYIAQLDVRNRAAIEEMLASLPAEWRNID 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   88 VLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSALAQ 167
Cdd:PRK10538  77 VLVNNAGLALGLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFVRQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  168 FTSALRKETIDTRIRIMEVDPGLVE-TEFSVVRFHGDKQKADNVYKNSEPLTPEDIAEVILFALTRRENVVIADTLVFPS 246
Cdd:PRK10538 157 FSLNLRTDLHGTAVRVTDIEPGLVGgTEFSNVRFKGDDGKAEKTYQNTVALTPEDVSEAVWWVATLPAHVNINTLEMMPV 236
                        250
                 ....*....|.
gi 19114010  247 HQGGAN-HVYR 256
Cdd:PRK10538 237 TQSFAGlNVHR 247
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
7-194 2.26e-50

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 163.55  E-value: 2.26e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010     7 KTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLPKEFADI 86
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAK-EGAKVVLVDRSEEKLEAVAKELGAL-GGKALFIQGDVTDRAQVKALVEQAVERLGRL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    87 DVLINNAGLALGTDkVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSALA 166
Cdd:pfam00106  79 DILVNNAGITGLGP-FSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVI 157
                         170       180
                  ....*....|....*....|....*...
gi 19114010   167 QFTSALRKETIDTRIRIMEVDPGLVETE 194
Cdd:pfam00106 158 GFTRSLALELAPHGIRVNAVAPGGVDTD 185
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
10-197 2.98e-12

sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain dehydrogenase/reductase family. The enzyme catalyzes the last step in the biosynthesis of tetrahydrobiopterin. A similar enzyme in Bacillus cereus was isolated for its ability to convert benzil to (S)-benzoin, a property sepiapterin reductase also shares. Cutoff scores for this model are set such that benzil reductase scores between trusted and noise cutoffs.


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 64.55  E-value: 2.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    10 LITGASSGIGKSTAFEIAKVAKVK---LILAARRFSTVEEIAKELESkyEVSVLPLKLDVSDLKSIPGVIESL------- 79
Cdd:TIGR01500   4 LVTGASRGFGRTIAQELAKCLKSPgsvLVLSARNDEALRQLKAEIGA--ERSGLRVVRVSLDLGAEAGLEQLLkalrelp 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    80 -PKEFADIdVLINNAGlALGTDKVIDLNIDDAVTM---ITTNVLGMMAMTRAVLPIFYSKNKGD--ILNVGSIAGRESYV 153
Cdd:TIGR01500  82 rPKGLQRL-LLINNAG-TLGDVSKGFVDLSDSTQVqnyWALNLTSMLCLTSSVLKAFKDSPGLNrtVVNISSLCAIQPFK 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 19114010   154 GGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSV 197
Cdd:TIGR01500 160 GWALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDMQQ 203
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
7-94 1.51e-04

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 41.31  E-value: 1.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010      7 KTILITGASSGIGKSTAFEIAKVAKVKLILAARR---FSTVEEIAKELESkYEVSVLPLKLDVSDLKSIPGVIESLPKEF 83
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGARRLVLLSRSgpdAPGAAALLAELEA-AGARVTVVACDVADRDALAAVLAAIPAVE 79
                           90
                   ....*....|.
gi 19114010     84 ADIDVLINNAG 94
Cdd:smart00822  80 GPLTGVIHAAG 90
 
Name Accession Description Interval E-value
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
7-256 7.05e-145

classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187604 [Multi-domain]  Cd Length: 249  Bit Score: 405.51  E-value: 7.05e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   7 KTILITGASSGIGKSTAFEIAKVAKvKLILAARRFSTVEEIAKELESKYEVSVLPLKLDVSDLKSIPGVIESLPKEFADI 86
Cdd:cd05346   1 KTVLITGASSGIGEATARRFAKAGA-KLILTGRRAERLQELADELGAKFPVKVLPLQLDVSDRESIEAALENLPEEFRDI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  87 DVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSALA 166
Cdd:cd05346  80 DILVNNAGLALGLDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYAGGNVYCATKAAVR 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010 167 QFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGDKQKADNVYKNSEPLTPEDIAEVILFALTRRENVVIADTLVFPS 246
Cdd:cd05346 160 QFSLNLRKDLIGTGIRVTNIEPGLVETEFSLVRFHGDKEKADKVYEGVEPLTPEDIAETILWVASRPAHVNINDIEIMPV 239
                       250
                ....*....|
gi 19114010 247 HQGGANHVYR 256
Cdd:cd05346 240 NQASAGHIHR 249
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
1-245 2.54e-81

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 443365 [Multi-domain]  Cd Length: 240  Bit Score: 243.94  E-value: 2.54e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   1 MSRlDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELEskyeVSVLPLKLDVSDLKSIPGVIESLP 80
Cdd:COG4221   1 MSD-KGKVALITGASSGIGAATARALAA-AGARVVLAARRAERLEALAAELG----GRALAVPLDVTDEAAVEAAVAAAV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  81 KEFADIDVLINNAGLALGTDkVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCS 160
Cdd:COG4221  75 AEFGRLDVLVNNAGVALLGP-LEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010 161 TKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGDKQKADNVYKNSEPLTPEDIAEVILFALTRRENVVIAD 240
Cdd:COG4221 154 TKAAVRGLSESLRAELRPTGIRVTVIEPGAVDTEFLDSVFDGDAEAAAAVYEGLEPLTPEDVAEAVLFALTQPAHVNVNE 233

                ....*
gi 19114010 241 TLVFP 245
Cdd:COG4221 234 LVLRP 238
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
9-256 3.20e-64

bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase YdfG;


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 200.75  E-value: 3.20e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    9 ILITGASSGIGKSTAFE-IAKVAKVklILAARRFSTVEEIAKELESkyevSVLPLKLDVSDLKSIPGVIESLPKEFADID 87
Cdd:PRK10538   3 VLVTGATAGFGECITRRfIQQGHKV--IATGRRQERLQELKDELGD----NLYIAQLDVRNRAAIEEMLASLPAEWRNID 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   88 VLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSALAQ 167
Cdd:PRK10538  77 VLVNNAGLALGLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFVRQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  168 FTSALRKETIDTRIRIMEVDPGLVE-TEFSVVRFHGDKQKADNVYKNSEPLTPEDIAEVILFALTRRENVVIADTLVFPS 246
Cdd:PRK10538 157 FSLNLRTDLHGTAVRVTDIEPGLVGgTEFSNVRFKGDDGKAEKTYQNTVALTPEDVSEAVWWVATLPAHVNINTLEMMPV 236
                        250
                 ....*....|.
gi 19114010  247 HQGGAN-HVYR 256
Cdd:PRK10538 237 TQSFAGlNVHR 247
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-237 4.31e-63

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 198.17  E-value: 4.31e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   1 MSrLDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLP 80
Cdd:COG0300   1 MS-LTGKTVLITGASSGIGRALARALAA-RGARVVLVARDAERLEALAAELRAA-GARVEVVALDVTDPDAVAALAEAVL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  81 KEFADIDVLINNAGLALGTDkVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCS 160
Cdd:COG0300  78 ARFGPIDVLVNNAGVGGGGP-FEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAA 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19114010 161 TKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSvvrfhgdkqKADNVYKNSEPLTPEDIAEVILFALTRRENVV 237
Cdd:COG0300 157 SKAALEGFSESLRAELAPTGVRVTAVCPGPVDTPFT---------ARAGAPAGRPLLSPEEVARAILRALERGRAEV 224
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
4-248 9.93e-54

clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent reduction of clavulanate-9-aldehyde to clavulanic acid, a beta-lactamase inhibitor. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187639 [Multi-domain]  Cd Length: 243  Bit Score: 173.88  E-value: 9.93e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   4 LDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLPKEF 83
Cdd:cd08934   1 LQGKVALVTGASSGIGEATARALAA-EGAAVAIAARRVDRLEALADELEAE-GGKALVLELDVTDEQQVDAAVERTVEAL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  84 ADIDVLINNAGLALgTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKS 163
Cdd:cd08934  79 GRLDILVNNAGIML-LGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVYNATKF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010 164 ALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGD-KQKADNVYKNSEPLTPEDIAEVILFALTRRENVVIADTL 242
Cdd:cd08934 158 GVNAFSEGLRQEVTERGVRVVVIEPGTVDTELRDHITHTItKEAYEERISTIRKLQAEDIAAAVRYAVTAPHHVTVNEIL 237

                ....*.
gi 19114010 243 VFPSHQ 248
Cdd:cd08934 238 IRPTDQ 243
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
9-233 6.79e-53

classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212491 [Multi-domain]  Cd Length: 234  Bit Score: 171.31  E-value: 6.79e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   9 ILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELEskYEVSVLPLKLDVSDLKSIPGVIESLPKEFADIDV 88
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAR-EGAKVVLADRNEEALAELAAIEA--LGGNAVAVQADVSDEEDVEALVEEALEEFGRLDI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  89 LINNAGLALGTDkVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSALAQF 168
Cdd:cd05233  78 LVNNAGIARPGP-LEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGL 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19114010 169 TSALRKETIDTRIRIMEVDPGLVETEF-SVVRFHGDKQKADNVYKNSEPLTPEDIAEVILFALTRR 233
Cdd:cd05233 157 TRSLALELAPYGIRVNAVAPGLVDTPMlAKLGPEEAEKELAAAIPLGRLGTPEEVAEAVVFLASDE 222
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
1-231 6.53e-51

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 166.88  E-value: 6.53e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   1 MSRLDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLP 80
Cdd:COG1028   1 MTRLKGKVALVTGGSSGIGRAIARALAA-EGARVVITDRDAEALEAAAAELRAA-GGRALAVAADVTDEAAVEALVAAAV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  81 KEFADIDVLINNAGLAlGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCS 160
Cdd:COG1028  79 AAFGRLDILVNNAGIT-PPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAA 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19114010 161 TKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGDKQKADnvYKNSEPL----TPEDIAEVILFALT 231
Cdd:COG1028 158 SKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVREA--LAARIPLgrlgTPEEVAAAVLFLAS 230
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
7-231 1.35e-50

17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187632 [Multi-domain]  Cd Length: 248  Bit Score: 165.87  E-value: 1.35e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   7 KTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESkyevSVLPLKLDVSDLKSIPGVIESLPKEFADI 86
Cdd:cd05374   1 KVVLITGCSSGIGLALALALAA-QGYRVIATARNPDKLESLGELLND----NLEVLELDVTDEESIKAAVKEVIERFGRI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  87 DVLINNAGLAL-GTdkVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSAL 165
Cdd:cd05374  76 DVLVNNAGYGLfGP--LEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAAL 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010 166 AQFTSALRKETIDTRIRIMEVDPGLVETEFS---------VVRF----HGDKQKADNVYKN-SEPLTPEDIAEVILFALT 231
Cdd:cd05374 154 EALSESLRLELAPFGIKVTIIEPGPVRTGFAdnaagsaleDPEIspyaPERKEIKENAAGVgSNPGDPEKVADVIVKALT 233
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
7-194 2.26e-50

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 163.55  E-value: 2.26e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010     7 KTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLPKEFADI 86
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAK-EGAKVVLVDRSEEKLEAVAKELGAL-GGKALFIQGDVTDRAQVKALVEQAVERLGRL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    87 DVLINNAGLALGTDkVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSALA 166
Cdd:pfam00106  79 DILVNNAGITGLGP-FSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVI 157
                         170       180
                  ....*....|....*....|....*...
gi 19114010   167 QFTSALRKETIDTRIRIMEVDPGLVETE 194
Cdd:pfam00106 158 GFTRSLALELAPHGIRVNAVAPGGVDTD 185
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
4-238 6.30e-50

11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human 11beta_HSD1 catalyzes the NADP(H)-dependent interconversion of cortisone and cortisol. This subgroup also includes human dehydrogenase/reductase SDR family member 7C (DHRS7C) and DHRS7B. These proteins have the GxxxGxG nucleotide binding motif and S-Y-K catalytic triad characteristic of the SDRs, but have an atypical C-terminal domain that contributes to homodimerization contacts. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187593 [Multi-domain]  Cd Length: 257  Bit Score: 164.30  E-value: 6.30e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   4 LDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKYEVSVLPLKLDVSDLKSIPGVIESLPKEF 83
Cdd:cd05332   1 LQGKVVIITGASSGIGEELAYHLAR-LGARLVLSARREERLEEVKSECLELGAPSPHVVPLDMSDLEDAEQVVEEALKLF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  84 ADIDVLINNAGLALGTdKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKS 163
Cdd:cd05332  80 GGLDILINNAGISMRS-LFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAASKH 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19114010 164 ALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGD-KQKADNVYKNSEPLTPEDIAEVILFALTRRENVVI 238
Cdd:cd05332 159 ALQGFFDSLRAELSEPNISVTVVCPGLIDTNIAMNALSGDgSMSAKMDDTTANGMSPEECALEILKAIALRKREVF 234
PRK07454 PRK07454
SDR family oxidoreductase;
1-251 1.99e-44

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 149.72  E-value: 1.99e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLP 80
Cdd:PRK07454   1 MSLNSMPRALITGASSGIGKATALAFAK-AGWDLALVARSQDALEALAAELRST-GVKAAAYSIDLSNPEAIAPGIAELL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   81 KEFADIDVLINNAGLALgTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCS 160
Cdd:PRK07454  79 EQFGCPDVLINNAGMAY-TGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAARNAFPQWGAYCV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  161 TKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFsvvrFHGDKQKADnvYKNSEPLTPEDIAEVILFALTRRENVVIAD 240
Cdd:PRK07454 158 SKAALAAFTKCLAEEERSHGIRVCTITLGAVNTPL----WDTETVQAD--FDRSAMLSPEQVAQTILHLAQLPPSAVIED 231
                        250
                 ....*....|.
gi 19114010  241 TLVFPShqGGA 251
Cdd:PRK07454 232 LTLMPS--AGA 240
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
1-246 2.22e-44

human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These proteins are members of the SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187601 [Multi-domain]  Cd Length: 250  Bit Score: 149.97  E-value: 2.22e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   1 MSRLDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKYEVSVLPLKLDVSDLKSIPGVIESLP 80
Cdd:cd05343   1 MERWRGRVALVTGASVGIGAAVARALVQ-HGMKVVGCARRVDKIEALAAECQSAGYPTLFPYQCDLSNEEQILSMFSAIR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  81 KEFADIDVLINNAGLALgTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKN--KGDILNVGSIAGRESYVGG--S 156
Cdd:cd05343  80 TQHQGVDVCINNAGLAR-PEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNvdDGHIININSMSGHRVPPVSvfH 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010 157 VYCSTKSALAQFTSALRKE--TIDTRIRIMEVDPGLVETEFSVVRFHGDKQKADNVYKNSEPLTPEDIAEVILFALTRRE 234
Cdd:cd05343 159 FYAATKHAVTALTEGLRQElrEAKTHIRATSISPGLVETEFAFKLHDNDPEKAAATYESIPCLKPEDVANAVLYVLSTPP 238
                       250
                ....*....|..
gi 19114010 235 NVVIADTLVFPS 246
Cdd:cd05343 239 HVQIHDILLRPT 250
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-244 4.73e-44

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 148.68  E-value: 4.73e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFEIAKVAkVKLILAARRFSTVEEIAKELEsKYEVSVLPLKLDVSDLKSIPGVIESLP 80
Cdd:PRK07666   2 AQSLQGKNALITGAGRGIGRAVAIALAKEG-VNVGLLARTEENLKAVAEEVE-AYGVKVVIATADVSDYEEVTAAIEQLK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   81 KEFADIDVLINNAGLAlGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCS 160
Cdd:PRK07666  80 NELGSIDILINNAGIS-KFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKGAAVTSAYSA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  161 TKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVvrfhgdkqkaDNVYKNSEP---LTPEDIAEVILFALTRRENVV 237
Cdd:PRK07666 159 SKFGVLGLTESLMQEVRKHNIRVTALTPSTVATDMAV----------DLGLTDGNPdkvMQPEDLAEFIVAQLKLNKRTF 228

                 ....*..
gi 19114010  238 IADTLVF 244
Cdd:PRK07666 229 IKSAGLW 235
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
2-228 2.27e-39

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 136.83  E-value: 2.27e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    2 SRLDGKTILITGASSGIGKSTAFEIAKV-AKVklILAARRFSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLP 80
Cdd:PRK05653   1 MSLQGKTALVTGASRGIGRAIALRLAADgAKV--VIYDSNEEAAEALAAELRAA-GGEARVLVFDVSDEAAVRALIEAAV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   81 KEFADIDVLINNAGLAlGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCS 160
Cdd:PRK05653  78 EAFGALDILVNNAGIT-RDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNPGQTNYSA 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19114010  161 TKSALAQFTSALRKETIDTRIRIMEVDPGLVETEfsVVRFHGDKQKADnvYKNSEPL----TPEDIAEVILF 228
Cdd:PRK05653 157 AKAGVIGFTKALALELASRGITVNAVAPGFIDTD--MTEGLPEEVKAE--ILKEIPLgrlgQPEEVANAVAF 224
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
4-243 2.34e-39

classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187622 [Multi-domain]  Cd Length: 253  Bit Score: 137.16  E-value: 2.34e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   4 LDGKTILITGASSGIGKSTAFEIAKVAkVKLILAARRFSTVEEIAKELE--SKYEVSVLPLKLDVSDLKSIPGVIESLPK 81
Cdd:cd05364   1 LSGKVAIITGSSSGIGAGTAILFARLG-ARLALTGRDAERLEETRQSCLqaGVSEKKILLVVADLTEEEGQDRIISTTLA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  82 EFADIDVLINNAGlALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPiFYSKNKGDILNVGSIAGRESYVGGSVYCST 161
Cdd:cd05364  80 KFGRLDILVNNAG-ILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVP-HLIKTKGEIVNVSSVAGGRSFPGVLYYCIS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010 162 KSALAQFTSALRKETIDTRIRIMEVDPGLVETEfsvvrFHGDKQKADNVY-------KNSEPL----TPEDIAEVILFAL 230
Cdd:cd05364 158 KAALDQFTRCTALELAPKGVRVNSVSPGVIVTG-----FHRRMGMPEEQYikflsraKETHPLgrpgTVDEVAEAIAFLA 232
                       250
                ....*....|...
gi 19114010 231 TRRENVVIADTLV 243
Cdd:cd05364 233 SDASSFITGQLLP 245
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
6-199 2.55e-39

17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) SDRs; This subgroup includes various 17-beta-hydroxysteroid dehydrogenases and 3-ketoacyl-CoA reductase, these are members of the SDR family, and contain the canonical active site tetrad and glycine-rich NAD-binding motif of the classical SDRs. 3-ketoacyl-CoA reductase (KAR, aka 17beta-HSD type 12, encoded by HSD17B12) acts in fatty acid elongation; 17beta- hydroxysteroid dehydrogenases are isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. 17beta-estradiol dehydrogenase (aka 17beta-HSD type 1, encoded by HSD17B1) converts estrone to estradiol. Estradiol is the predominant female sex hormone. 17beta-HSD type 3 (aka testosterone 17-beta-dehydrogenase 3, encoded by HSD17B3) catalyses the reduction of androstenedione to testosterone, it also accepts estrogens as substrates. This subgroup also contains a putative steroid dehydrogenase let-767 from Caenorhabditis elegans, mutation in which results in hypersensitivity to cholesterol limitation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187614 [Multi-domain]  Cd Length: 239  Bit Score: 136.58  E-value: 2.55e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   6 GKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKYEVSVLPLKLDVSDLKSIpgvIESLPKEFA- 84
Cdd:cd05356   1 GTWAVVTGATDGIGKAYAEELAK-RGFNVILISRTQEKLDAVAKEIEEKYGVETKTIAADFSAGDDI---YERIEKELEg 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  85 -DIDVLINNAGLALG-TDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTK 162
Cdd:cd05356  77 lDIGILVNNVGISHSiPEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASK 156
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 19114010 163 SALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVR 199
Cdd:cd05356 157 AFLDFFSRALYEEYKSQGIDVQSLLPYLVATKMSKIR 193
PRK07326 PRK07326
SDR family oxidoreductase;
1-246 1.08e-38

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 134.75  E-value: 1.08e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKYEVsvLPLKLDVSDLKSIPGVIESLP 80
Cdd:PRK07326   1 MMSLKGKVALITGGSKGIGFAIAEALLA-EGYKVAITARDQKELEEAAAELNNKGNV--LGLAADVRDEADVQRAVDAIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   81 KEFADIDVLINNAGLALgTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFySKNKGDILNVGSIAGRESYVGGSVYCS 160
Cdd:PRK07326  78 AAFGGLDVLIANAGVGH-FAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPAL-KRGGGYIINISSLAGTNFFAGGAAYNA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  161 TKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSvvrfhGDKQKADNVYKnsepLTPEDIAEVILFALTRRENVVIAD 240
Cdd:PRK07326 156 SKFGLVGFSEAAMLDLRQYGIKVSTIMPGSVATHFN-----GHTPSEKDAWK----IQPEDIAQLVLDLLKMPPRTLPSK 226

                 ....*.
gi 19114010  241 TLVFPS 246
Cdd:PRK07326 227 IEVRPS 232
PRK06181 PRK06181
SDR family oxidoreductase;
6-238 1.53e-38

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 135.11  E-value: 1.53e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    6 GKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESkYEVSVLPLKLDVSDLKSIPGVIESLPKEFAD 85
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLAR-AGAQLVLAARNETRLASLAQELAD-HGGEALVVPTDVSDAEACERLIEAAVARFGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   86 IDVLINNAGLAL--GTDKVIDLNIDDAVTMIttNVLGMMAMTRAVLPiFYSKNKGDILNVGSIAGRESYVGGSVYCSTKS 163
Cdd:PRK06181  79 IDILVNNAGITMwsRFDELTDLSVFERVMRV--NYLGAVYCTHAALP-HLKASRGQIVVVSSLAGLTGVPTRSGYAASKH 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19114010  164 ALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGDKQKADN-VYKNSEPLTPEDIAEVILFALTRRENVVI 238
Cdd:PRK06181 156 ALHGFFDSLRIELADDGVAVTVVCPGFVATDIRKRALDGDGKPLGKsPMQESKIMSAEECAEAILPAIARRKRLLV 231
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
3-228 6.82e-36

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 128.04  E-value: 6.82e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    3 RLDGKTILITGASSGIGKSTAFEIAKV-AKVkLILAARRFSTVEEIAKELESkYEVSVLPLKLDVSDLKSIPGVIESLPK 81
Cdd:PRK05565   2 KLMGKVAIVTGASGGIGRAIAELLAKEgAKV-VIAYDINEEAAQELLEEIKE-EGGDAIAVKADVSSEEDVENLVEQIVE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   82 EFADIDVLINNAGLALGTDkVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCST 161
Cdd:PRK05565  80 KFGKIDILVNNAGISNFGL-VTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCEVLYSAS 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19114010  162 KSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGDKQKADNVYKNSEPLTPEDIAEVILF 228
Cdd:PRK05565 159 KGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEMWSSFSEEDKEGLAEEIPLGRLGKPEEIAKVVLF 225
PRK08264 PRK08264
SDR family oxidoreductase;
1-242 1.83e-35

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 126.54  E-value: 1.83e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFE-IAKVAKvKLILAARRFSTVEEiakeleskYEVSVLPLKLDVSDlksiPGVIESL 79
Cdd:PRK08264   1 MMDIKGKVVLVTGANRGIGRAFVEQlLARGAA-KVYAAARDPESVTD--------LGPRVVPLQLDVTD----PASVAAA 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   80 PKEFADIDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYC 159
Cdd:PRK08264  68 AEAASDVTILVNNAGIFRTGSLLLEGDEDALRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVLSVLSWVNFPNLGTYS 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  160 STKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVvrfHGDKQKADnvyknsepltPEDIAEVILFALTRRENVVIA 239
Cdd:PRK08264 148 ASKAAAWSLTQALRAELAPQGTRVLGVHPGPIDTDMAA---GLDAPKAS----------PADVARQILDALEAGDEEVLP 214

                 ...
gi 19114010  240 DTL 242
Cdd:PRK08264 215 DEM 217
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
3-196 2.39e-35

Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 126.43  E-value: 2.39e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   3 RLDGKTILITGASSGIGkstaFEIAKV---AKVKLILAARRFSTVEEIAKELESkyevsVLPLKLDVSDLKSIPGVIESL 79
Cdd:COG3967   2 KLTGNTILITGGTSGIG----LALAKRlhaRGNTVIITGRREEKLEEAAAANPG-----LHTIVLDVADPASIAALAEQV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  80 PKEFADIDVLINNAGLALGTDKVIDLN-IDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVY 158
Cdd:COG3967  73 TAEFPDLNVLINNAGIMRAEDLLDEAEdLADAEREITTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGLAFVPLAVTPTY 152
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 19114010 159 CSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFS 196
Cdd:COG3967 153 SATKAALHSYTQSLRHQLKDTSVKVIELAPPAVDTDLT 190
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
4-228 9.81e-35

3-ketoacyl-(acyl-carrier-protein) reductase; Validated


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 124.92  E-value: 9.81e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    4 LDGKTILITGASSGIGKSTAFEIAKV-AKVkLILAARRFSTVEEIAKELEsKYEVSVLPLKLDVSDLKSIPGVIESLPKE 82
Cdd:PRK05557   3 LEGKVALVTGASRGIGRAIAERLAAQgANV-VINYASSEAGAEALVAEIG-ALGGKALAVQGDVSDAESVERAVDEAKAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   83 FADIDVLINNAGLALGTDkVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTK 162
Cdd:PRK05557  81 FGGVDILVNNAGITRDNL-LMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGQANYAASK 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19114010  163 SALAQFTSALRKEtIDTR-IRIMEVDPGLVETE-FSVVRfhgDKQKADnvYKNSEPL----TPEDIAEVILF 228
Cdd:PRK05557 160 AGVIGFTKSLARE-LASRgITVNAVAPGFIETDmTDALP---EDVKEA--ILAQIPLgrlgQPEEIASAVAF 225
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
9-194 1.35e-34

classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a canonical active site tetrad and a fairly well conserved typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187608 [Multi-domain]  Cd Length: 239  Bit Score: 124.36  E-value: 1.35e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   9 ILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELES---KYEVSVLplklDVSDLKSIPGVIESLPKEFAD 85
Cdd:cd05350   1 VLITGASSGIGRALAREFAK-AGYNVALAARRTDRLDELKAELLNpnpSVEVEIL----DVTDEERNQLVIAELEAELGG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  86 IDVLINNAGLALGTdKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSAL 165
Cdd:cd05350  76 LDLVIINAGVGKGT-SLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKAAL 154
                       170       180
                ....*....|....*....|....*....
gi 19114010 166 AQFTSALRKETIDTRIRIMEVDPGLVETE 194
Cdd:cd05350 155 SSLAESLRYDVKKRGIRVTVINPGFIDTP 183
FabG-like PRK07231
SDR family oxidoreductase;
3-228 1.85e-34

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 124.17  E-value: 1.85e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    3 RLDGKTILITGASSGIGKSTAFEIAKV-AKVklILAARRFSTVEEIAKELESkyEVSVLPLKLDVSDLKSIPGVIESLPK 81
Cdd:PRK07231   2 RLEGKVAIVTGASSGIGEGIARRFAAEgARV--VVTDRNEEAAERVAAEILA--GGRAIAVAADVSDEADVEAAVAAALE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   82 EFADIDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCST 161
Cdd:PRK07231  78 RFGSVDILVNNAGTTHRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGLGWYNAS 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19114010  162 KSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGDKQKADNVYKNSEPL----TPEDIAEVILF 228
Cdd:PRK07231 158 KGAVITLTKALAAELGPDKIRVNAVAPVVVETGLLEAFMGEPTPENRAKFLATIPLgrlgTPEDIANAALF 228
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
4-194 1.97e-34

classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka Tyrosine-dependent oxidoreductases) are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187628 [Multi-domain]  Cd Length: 228  Bit Score: 123.57  E-value: 1.97e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   4 LDGKTILITGASSGIGKSTAFEIAKVAKvKLILAARRFSTVEEIAKELES-KYEVsvlplkLDVSDLKSIPGVIESLPKE 82
Cdd:cd05370   3 LTGNTVLITGGTSGIGLALARKFLEAGN-TVIITGRREERLAEAKKELPNiHTIV------LDVGDAESVEALAEALLSE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  83 FADIDVLINNAGLALGTD-KVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCST 161
Cdd:cd05370  76 YPNLDILINNAGIQRPIDlRDPASDLDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANPVYCAT 155
                       170       180       190
                ....*....|....*....|....*....|...
gi 19114010 162 KSALAQFTSALRKETIDTRIRIMEVDPGLVETE 194
Cdd:cd05370 156 KAALHSYTLALRHQLKDTGVEVVEIVPPAVDTE 188
PRK09072 PRK09072
SDR family oxidoreductase;
3-236 2.30e-34

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 124.28  E-value: 2.30e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    3 RLDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELEskYEVSVLPLKLDVSDLKSIPGVIEsLPKE 82
Cdd:PRK09072   2 DLKDKRVLLTGASGGIGQALAEALAA-AGARLLLVGRNAEKLEALAARLP--YPGRHRWVVADLTSEAGREAVLA-RARE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   83 FADIDVLINNAG---LALGTDKVidlniDDAVT-MITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVY 158
Cdd:PRK09072  78 MGGINVLINNAGvnhFALLEDQD-----PEAIErLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGSTFGSIGYPGYASY 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  159 CSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFsvvrfhgdkqkadnvykNSEPLT------------PEDIAEVI 226
Cdd:PRK09072 153 CASKFALRGFSEALRRELADTGVRVLYLAPRATRTAM-----------------NSEAVQalnralgnamddPEDVAAAV 215
                        250
                 ....*....|
gi 19114010  227 LFALTRRENV 236
Cdd:PRK09072 216 LQAIEKERAE 225
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-228 3.31e-34

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 123.44  E-value: 3.31e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFEIAKVAKVKLILAARRFSTVEEIAKELESkYEVSVLPLKLDVSDLKSIPGVIESLP 80
Cdd:PRK12825   1 MGSLMGRVALVTGAARGLGRAIALRLARAGADVVVHYRSDEEAAEELVEAVEA-LGRRAQAVQADVTDKAALEAAVAAAV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   81 KEFADIDVLINNAGLAlGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCS 160
Cdd:PRK12825  80 ERFGRIDILVNNAGIF-EDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGLPGWPGRSNYAA 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19114010  161 TKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGDKQKADNVYKNSEPLTPEDIAEVILF 228
Cdd:PRK12825 159 AKAGLVGLTKALARELAEYGITVNMVAPGDIDTDMKEATIEEAREAKDAETPLGRSGTPEDIARAVAF 226
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
6-240 2.07e-33

classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a canonical active site triad (and also an active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187612 [Multi-domain]  Cd Length: 235  Bit Score: 120.97  E-value: 2.07e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   6 GKTILITGASSGIGKSTAFEIAKVAKVKLILAARRFSTveeiAKELESKYEVSVLPLKLDVSDLKSIPGVIESLPkefaD 85
Cdd:cd05354   3 DKTVLVTGANRGIGKAFVESLLAHGAKKVYAAVRDPGS----AAHLVAKYGDKVVPLRLDVTDPESIKAAAAQAK----D 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  86 IDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSAL 165
Cdd:cd05354  75 VDVVINNAGVLKPATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKNFPAMGTYSASKSAA 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19114010 166 AQFTSALRKETIDTRIRIMEVDPGLVETEFSVvrfHGDKQKADnvyknsepltPEDIAEVILFALTRRENVVIAD 240
Cdd:cd05354 155 YSLTQGLRAELAAQGTLVLSVHPGPIDTRMAA---GAGGPKES----------PETVAEAVLKALKAGEFHVFPD 216
PRK06182 PRK06182
short chain dehydrogenase; Validated
7-195 3.38e-33

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 121.61  E-value: 3.38e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    7 KTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAkeleskyEVSVLPLKLDVSDLKSIPGVIESLPKEFADI 86
Cdd:PRK06182   4 KVALVTGASSGIGKATARRLAA-QGYTVYGAARRVDKMEDLA-------SLGVHPLSLDVTDEASIKAAVDTIIAEEGRI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   87 DVLINNAGLAL-GTdkVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSAL 165
Cdd:PRK06182  76 DVLVNNAGYGSyGA--IEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKIYTPLGAWYHATKFAL 153
                        170       180       190
                 ....*....|....*....|....*....|
gi 19114010  166 AQFTSALRKETIDTRIRIMEVDPGLVETEF 195
Cdd:PRK06182 154 EGFSDALRLEVAPFGIDVVVIEPGGIKTEW 183
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
6-242 7.92e-33

3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These proteins include members identified as KDSR, ribitol type dehydrogenase, and others. The group shows strong conservation of the active site tetrad and glycine rich NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 119.67  E-value: 7.92e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   6 GKTILITGASSGIGKSTAFEIAKVAKvKLILAARRFSTVEEIAKELESKYEVS---VLPLKLDVSDLKSIPGVIESLPKE 82
Cdd:cd08939   1 GKHVLITGGSSGIGKALAKELVKEGA-NVIIVARSESKLEEAVEEIEAEANASgqkVSYISADLSDYEEVEQAFAQAVEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  83 FADIDVLINNAGLALGTDkVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTK 162
Cdd:cd08939  80 GGPPDLVVNCAGISIPGL-FEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGIYGYSAYCPSK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010 163 SALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGDKQKADNVYKNSEPLTPEDIAEVILFALTRRENVVIADTL 242
Cdd:cd08939 159 FALRGLAESLRQELKPYNIRVSVVYPPDTDTPGFEEENKTKPEETKAIEGSSGPITPEEAARIIVKGLDRGYDDVFTDFI 238
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
9-238 1.06e-32

classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a canonical active site triad (and also active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187618 [Multi-domain]  Cd Length: 233  Bit Score: 119.41  E-value: 1.06e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   9 ILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLPKEFADIDV 88
Cdd:cd05360   3 VVITGASSGIGRATALAFAE-RGAKVVLAARSAEALHELAREVREL-GGEAIAVVADVADAAQVERAADTAVERFGRIDT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  89 LINNAGLALgTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSALAQF 168
Cdd:cd05360  81 WVNNAGVAV-FGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRSAPLQAAYSASKHAVRGF 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19114010 169 TSALRKETI-DTR-IRIMEVDPGLVETEFsvvrFHGDKQKADNVYKNSEPL-TPEDIAEVILFALTRRENVVI 238
Cdd:cd05360 160 TESLRAELAhDGApISVTLVQPTAMNTPF----FGHARSYMGKKPKPPPPIyQPERVAEAIVRAAEHPRREVK 228
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
7-230 1.58e-32

classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187634 [Multi-domain]  Cd Length: 226  Bit Score: 118.76  E-value: 1.58e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   7 KTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKyevsVLPLKLDVSDLKSIPGVIESLPKEFADI 86
Cdd:cd08929   1 KAALVTGASRGIGEATARLLHA-EGYRVGICARDEARLAAAAAQELEG----VLGLAGDVRDEADVRRAVDAMEEAFGGL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  87 DVLINNAGLALgTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSALA 166
Cdd:cd08929  76 DALVNNAGVGV-MKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGLL 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19114010 167 QFTSALRKETIDTRIRIMEVDPGLVETEFsvvrfhgdkqkADNVYKNSEPLTPEDIAEVILFAL 230
Cdd:cd08929 155 GLSEAAMLDLREANIRVVNVMPGSVDTGF-----------AGSPEGQAWKLAPEDVAQAVLFAL 207
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
8-230 5.51e-32

human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid dehydrogenases (17betaHSD) are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. 17betaHSD type XI, a classical SDR, preferentially converts 3alpha-Adiol to androsterone but not numerous other tested steroids. This subgroup of classical SDRs also includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187598 [Multi-domain]  Cd Length: 243  Bit Score: 117.73  E-value: 5.51e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   8 TILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKYeVSVLPLKLDVSDLKSIPGVIESLPKEFADID 87
Cdd:cd05339   1 IVLITGGGSGIGRLLALEFAK-RGAKVVILDINEKGAEETANNVRKAG-GKVHYYKCDVSKREEVYEAAKKIKKEVGDVT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  88 VLINNAGLALGTdKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSALAQ 167
Cdd:cd05339  79 ILINNAGVVSGK-KLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCASKAAAVG 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19114010 168 FTSALRKETI---DTRIRIMEVDPGLVETEFsvvrFHGDKQKADNVYKnsePLTPEDIAEVILFAL 230
Cdd:cd05339 158 FHESLRLELKaygKPGIKTTLVCPYFINTGM----FQGVKTPRPLLAP---ILEPEYVAEKIVRAI 216
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
7-196 5.68e-32

Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187585 [Multi-domain]  Cd Length: 225  Bit Score: 116.95  E-value: 5.68e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   7 KTILITGASSGIGKSTAFEIAKVAKVKLILAARRFSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLPKEFADI 86
Cdd:cd05324   1 KVALVTGANRGIGFEIVRQLAKSGPGTVILTARDVERGQAAVEKLRAE-GLSVRFHQLDVTDDASIEAAADFVEEKYGGL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  87 DVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGresyVGGSVYCSTKSALA 166
Cdd:cd05324  80 DILVNNAGIAFKGFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLG----SLTSAYGVSKAALN 155
                       170       180       190
                ....*....|....*....|....*....|
gi 19114010 167 QFTSALRKETIDTRIRIMEVDPGLVETEFS 196
Cdd:cd05324 156 ALTRILAKELKETGIKVNACCPGWVKTDMG 185
PRK12826 PRK12826
SDR family oxidoreductase;
1-228 1.33e-31

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 116.94  E-value: 1.33e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFEIAKV-AKVklILAARRFSTVEEIAKELESKYEvSVLPLKLDVSDLKSIPGVIESL 79
Cdd:PRK12826   1 TRDLEGRVALVTGAARGIGRAIAVRLAADgAEV--IVVDICGDDAAATAELVEAAGG-KARARQVDVRDRAALKAAVAAG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   80 PKEFADIDVLINNAGLAlGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRES-YVGGSVY 158
Cdd:PRK12826  78 VEDFGRLDILVANAGIF-PLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGPRVgYPGLAHY 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19114010  159 CSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRfhGDKQKADNVyKNSEPL----TPEDIAEVILF 228
Cdd:PRK12826 157 AASKAGLVGFTRALALELAARNITVNSVHPGGVDTPMAGNL--GDAQWAEAI-AAAIPLgrlgEPEDIAAAVLF 227
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
8-230 4.19e-31

sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, catalyzes the NADP-dependent reduction of sepiaptern to 7,8-dihydrobiopterin (BH2). In addition to SPRs, this subgroup also contains Bacillus cereus yueD, a benzil reductase, which catalyzes the stereospecific reduction of benzil to (S)-benzoin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 115.08  E-value: 4.19e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   8 TILITGASSGIGKSTAFEIAK-VAKVKLILAARRfstvEEIAKEL--ESKYEVSVLPLKLDVSDLKSIPGVIESLPKEFA 84
Cdd:cd05367   1 VIILTGASRGIGRALAEELLKrGSPSVVVLLARS----EEPLQELkeELRPGLRVTTVKADLSDAAGVEQLLEAIRKLDG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  85 DIDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIF-YSKNKGDILNVGSIAGRESYVGGSVYCSTKS 163
Cdd:cd05367  77 ERDLLINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFkKRGLKKTVVNVSSGAAVNPFKGWGLYCSSKA 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19114010 164 ALAQFTSALRKETIDTriRIMEVDPGLVETE-FSVVRFHGDKQKADN----VYKNSEPLTPEDIAEVILFAL 230
Cdd:cd05367 157 ARDMFFRVLAAEEPDV--RVLSYAPGVVDTDmQREIRETSADPETRSrfrsLKEKGELLDPEQSAEKLANLL 226
PRK06180 PRK06180
short chain dehydrogenase; Provisional
5-199 5.36e-31

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 115.78  E-value: 5.36e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    5 DGKTILITGASSGIGKSTAfEIAKVAKVKLILAARRFSTVEEIAKELESKyevsVLPLKLDVSDLKSIPGVIESLPKEFA 84
Cdd:PRK06180   3 SMKTWLITGVSSGFGRALA-QAALAAGHRVVGTVRSEAARADFEALHPDR----ALARLLDVTDFDAIDAVVADAEATFG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   85 DIDVLINNAGLalGTDKVIDLNIDDAV-TMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKS 163
Cdd:PRK06180  78 PIDVLVNNAGY--GHEGAIEESPLAEMrRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGLITMPGIGYYCGSKF 155
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 19114010  164 ALAQFTSALRKETIDTRIRIMEVDPGLVETEF---SVVR 199
Cdd:PRK06180 156 ALEGISESLAKEVAPFGIHVTAVEPGSFRTDWagrSMVR 194
PRK07825 PRK07825
short chain dehydrogenase; Provisional
2-234 2.13e-30

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 114.27  E-value: 2.13e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    2 SRLDGKTILITGASSGIGKSTAFEIAKV-AKVklILAARRFSTVEEIAKELESkyevsVLPLKLDVSDLKSIPGVIESLP 80
Cdd:PRK07825   1 DDLRGKVVAITGGARGIGLATARALAALgARV--AIGDLDEALAKETAAELGL-----VVGGPLDVTDPASFAAFLDAVE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   81 KEFADIDVLINNAGL-ALG-----TDKVIDLNIDdavtmitTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVG 154
Cdd:PRK07825  74 ADLGPIDVLVNNAGVmPVGpfldePDAVTRRILD-------VNVYGVILGSKLAAPRMVPRGRGHVVNVASLAGKIPVPG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  155 GSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGDKQKadnvyknsePLTPEDIAEVILFALTRRE 234
Cdd:PRK07825 147 MATYCASKHAVVGFTDAARLELRGTGVHVSVVLPSFVNTELIAGTGGAKGFK---------NVEPEDVAAAIVGTVAKPR 217
PRK05693 PRK05693
SDR family oxidoreductase;
7-221 7.32e-30

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 112.96  E-value: 7.32e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    7 KTILITGASSGIGKSTAFEIaKVAKVKLILAARRFSTVEEIAkeleskyEVSVLPLKLDVSDLKSIPGVIESLPKEFADI 86
Cdd:PRK05693   2 PVVLITGCSSGIGRALADAF-KAAGYEVWATARKAEDVEALA-------AAGFTAVQLDVNDGAALARLAEELEAEHGGL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   87 DVLINNAGL-ALGtdKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFySKNKGDILNVGSIAGRESYVGGSVYCSTKSAL 165
Cdd:PRK05693  74 DVLINNAGYgAMG--PLLDGGVEAMRRQFETNVFAVVGVTRALFPLL-RRSRGLVVNIGSVSGVLVTPFAGAYCASKAAV 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 19114010  166 AQFTSALRKETIDTRIRIMEVDPGLVETEFsvvrfhgdkqkADNVYKNSEPLTPED 221
Cdd:PRK05693 151 HALSDALRLELAPFGVQVMEVQPGAIASQF-----------ASNASREAEQLLAEQ 195
PRK07109 PRK07109
short chain dehydrogenase; Provisional
1-234 1.71e-29

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 113.09  E-value: 1.71e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESkYEVSVLPLKLDVSDLKSIPGVIESLP 80
Cdd:PRK07109   3 LKPIGRQVVVITGASAGVGRATARAFAR-RGAKVVLLARGEEGLEALAAEIRA-AGGEALAVVADVADAEAVQAAADRAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   81 KEFADIDVLINNAGLAL-GTdkVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYC 159
Cdd:PRK07109  81 EELGPIDTWVNNAMVTVfGP--FEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALAYRSIPLQSAYC 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  160 STKSALAQFTSALRKETID--TRIRIMEVDPGLVET-EFSVVRFHGDK--QKADNVYknseplTPEDIAEVILFALT--R 232
Cdd:PRK07109 159 AAKHAIRGFTDSLRCELLHdgSPVSVTMVQPPAVNTpQFDWARSRLPVepQPVPPIY------QPEVVADAILYAAEhpR 232

                 ..
gi 19114010  233 RE 234
Cdd:PRK07109 233 RE 234
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
6-231 1.75e-29

retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) OxidoReductase (LPOR) and related proteins, classical (c) SDRs; Classical SDR subgroup containing retinol-DHs, LPORs, and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Pchlide reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14, dehydrogenase/reductase SDR family member (DHRS)-12 , -13 and -X (a DHRS on chromosome X), and WWOX (WW domain-containing oxidoreductase), as well as a Neurospora crassa SDR encoded by the blue light inducible bli-4 gene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 111.55  E-value: 1.75e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   6 GKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKYEVS-VLPLKLDVSDLKSIPGVIESLPKEFA 84
Cdd:cd05327   1 GKVVVITGANSGIGKETARELAK-RGAHVIIACRNEEKGEEAAAEIKKETGNAkVEVIQLDLSSLASVRQFAEEFLARFP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  85 DIDVLINNAGLALGTDKvidLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIA--------------GRE 150
Cdd:cd05327  80 RLDILINNAGIMAPPRR---LTKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAhragpidfndldleNNK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010 151 SYVGGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFsVVRFHGDKQkadnVYKNSEPL---TPEDIAEVIL 227
Cdd:cd05327 157 EYSPYKAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTEL-LRRNGSFFL----LYKLLRPFlkkSPEQGAQTAL 231

                ....
gi 19114010 228 FALT 231
Cdd:cd05327 232 YAAT 235
PRK06914 PRK06914
SDR family oxidoreductase;
6-189 2.18e-29

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 111.65  E-value: 2.18e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    6 GKTILITGASSGIGKSTAFEIAKvAKVKLILAARRfstvEEIAKELESKYEVSVLP-----LKLDVSDLKSIPgVIESLP 80
Cdd:PRK06914   3 KKIAIVTGASSGFGLLTTLELAK-KGYLVIATMRN----PEKQENLLSQATQLNLQqnikvQQLDVTDQNSIH-NFQLVL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   81 KEFADIDVLINNAGLALGtDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCS 160
Cdd:PRK06914  77 KEIGRIDLLVNNAGYANG-GFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRVGFPGLSPYVS 155
                        170       180
                 ....*....|....*....|....*....
gi 19114010  161 TKSALAQFTSALRKETIDTRIRIMEVDPG 189
Cdd:PRK06914 156 SKYALEGFSESLRLELKPFGIDVALIEPG 184
PRK08263 PRK08263
short chain dehydrogenase; Provisional
6-196 4.55e-29

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 110.90  E-value: 4.55e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    6 GKTILITGASSGIGKSTAfEIAKVAKVKLILAARRFSTVeeiaKELESKYEVSVLPLKLDVSDLKSIPGVIESLPKEFAD 85
Cdd:PRK08263   3 EKVWFITGASRGFGRAWT-EAALERGDRVVATARDTATL----ADLAEKYGDRLLPLALDVTDRAAVFAAVETAVEHFGR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   86 IDVLINNAGLALgTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSAL 165
Cdd:PRK08263  78 LDIVVNNAGYGL-FGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGGISAFPMSGIYHASKWAL 156
                        170       180       190
                 ....*....|....*....|....*....|.
gi 19114010  166 AQFTSALRKETIDTRIRIMEVDPGLVETEFS 196
Cdd:PRK08263 157 EGMSEALAQEVAEFGIKVTLVEPGGYSTDWA 187
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
4-194 5.59e-29

gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent conversion of carbon source D-gluconate and 5-keto-D-gluconate. This SDR subgroup has a classical Gly-rich NAD(P)-binding motif and a conserved active site tetrad pattern. However, it has been proposed that Arg104 (Streptococcus suis Ga5DH numbering), as well as an active site Ca2+, play a critical role in catalysis. In addition to Ga5DHs this subgroup contains Erwinia chrysanthemi KduD which is involved in pectin degradation, and is a putative 2,5-diketo-3-deoxygluconate dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107,15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187605 [Multi-domain]  Cd Length: 248  Bit Score: 109.75  E-value: 5.59e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   4 LDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELEsKYEVSVLPLKLDVSDLKSIPGVIESLPKEF 83
Cdd:cd05347   3 LKGKVALVTGASRGIGFGIASGLAE-AGANIVINSRNEEKAEEAQQLIE-KEGVEATAFTCDVSDEEAIKAAVEAIEEDF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  84 ADIDVLINNAGLALgTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKS 163
Cdd:cd05347  81 GKIDILVNNAGIIR-RHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPAYAASKG 159
                       170       180       190
                ....*....|....*....|....*....|.
gi 19114010 164 ALAQFTSALRKETIDTRIRIMEVDPGLVETE 194
Cdd:cd05347 160 GVAGLTKALATEWARHGIQVNAIAPGYFATE 190
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
7-235 1.25e-28

HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC 7120 HetN, a putative oxidoreductase involved in heterocyst differentiation, and related proteins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212493 [Multi-domain]  Cd Length: 223  Bit Score: 108.22  E-value: 1.25e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   7 KTILITGASSGIGKSTAFEIAKvAKVKLILAARrfsTVEEIAKELESKYEVSVLPLklDVSDLKSIPGVIESLPKEFADI 86
Cdd:cd08932   1 KVALVTGASRGIGIEIARALAR-DGYRVSLGLR---NPEDLAALSASGGDVEAVPY--DARDPEDARALVDALRDRFGRI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  87 DVLINNAGLALGTDkVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSALA 166
Cdd:cd08932  75 DVLVHNAGIGRPTT-LREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSASKFALR 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19114010 167 QFTSALRKETIDTRIRIMEVDPGLVETefsvvrfhgDKQKADNVYKNSEPL---TPEDIAEVILFALTRREN 235
Cdd:cd08932 154 ALAHALRQEGWDHGVRVSAVCPGFVDT---------PMAQGLTLVGAFPPEemiQPKDIANLVRMVIELPEN 216
PRK06179 PRK06179
short chain dehydrogenase; Provisional
7-231 1.78e-28

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 109.22  E-value: 1.78e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    7 KTILITGASSGIGKSTAfeiakvakvkLILAA---RRFSTVEEIAKElESKYEVSVLPLklDVSDLKSIPGVIESLPKEF 83
Cdd:PRK06179   5 KVALVTGASSGIGRATA----------EKLARagyRVFGTSRNPARA-APIPGVELLEL--DVTDDASVQAAVDEVIARA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   84 ADIDVLINNAGLAL--GTDkviDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAG--RESYVGgsVYC 159
Cdd:PRK06179  72 GRIDVLVNNAGVGLagAAE---ESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVLGflPAPYMA--LYA 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  160 STKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSV--------------VRFHGDKQKADNVYKNSEpltPEDIAEV 225
Cdd:PRK06179 147 ASKHAVEGYSESLDHEVRQFGIRVSLVEPAYTKTNFDAnapepdsplaeydrERAVVSKAVAKAVKKADA---PEVVADT 223

                 ....*.
gi 19114010  226 ILFALT 231
Cdd:PRK06179 224 VVKAAL 229
PRK08251 PRK08251
SDR family oxidoreductase;
7-194 2.03e-28

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 108.48  E-value: 2.03e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    7 KTILITGASSGIGKSTAFEIAKVAKvKLILAARRFSTVEEIAKELESKY-EVSVLPLKLDVSDLKSIPGVIESLPKEFAD 85
Cdd:PRK08251   3 QKILITGASSGLGAGMAREFAAKGR-DLALCARRTDRLEELKAELLARYpGIKVAVAALDVNDHDQVFEVFAEFRDELGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   86 IDVLINNAGL----ALGTDKvIDLNIDDAvtmiTTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGG-SVYCS 160
Cdd:PRK08251  82 LDRVIVNAGIgkgaRLGTGK-FWANKATA----ETNFVAALAQCEAAMEIFREQGSGHLVLISSVSAVRGLPGVkAAYAA 156
                        170       180       190
                 ....*....|....*....|....*....|....
gi 19114010  161 TKSALAQFTSALRKETIDTRIRIMEVDPGLVETE 194
Cdd:PRK08251 157 SKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSE 190
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
7-228 2.82e-28

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187594 [Multi-domain]  Cd Length: 240  Bit Score: 107.63  E-value: 2.82e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   7 KTILITGASSGIGKSTAFEIAK-VAKVklILAARRFSTVEEIAKELEsKYEVSVLPLKLDVSDLKSIPGVIESLPKEFAD 85
Cdd:cd05333   1 KVALVTGASRGIGRAIALRLAAeGAKV--AVTDRSEEAAAETVEEIK-ALGGNAAALEADVSDREAVEALVEKVEAEFGP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  86 IDVLINNAGLAlgTDKV-IDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSA 164
Cdd:cd05333  78 VDILVNNAGIT--RDNLlMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYAASKAG 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19114010 165 LAQFTSALRKETIDTRIRIMEVDPGLVETEfsVVRFHGDKQKADnvYKNSEPL----TPEDIAEVILF 228
Cdd:cd05333 156 VIGFTKSLAKELASRGITVNAVAPGFIDTD--MTDALPEKVKEK--ILKQIPLgrlgTPEEVANAVAF 219
PRK08219 PRK08219
SDR family oxidoreductase;
7-245 5.51e-28

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 106.56  E-value: 5.51e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    7 KTILITGASSGIGKSTAFEIAKvaKVKLILAARRFSTVEEIAKELESkyevsVLPLKLDVSDLKSIPGVIESLPKefadI 86
Cdd:PRK08219   4 PTALITGASRGIGAAIARELAP--THTLLLGGRPAERLDELAAELPG-----ATPFPVDLTDPEAIAAAVEQLGR----L 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   87 DVLINNAGLA-LGTdkVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSkNKGDILNVGSIAGRESYVGGSVYCSTKSAL 165
Cdd:PRK08219  73 DVLVHNAGVAdLGP--VAESTVDEWRATLEVNVVAPAELTRLLLPALRA-AHGHVVFINSGAGLRANPGWGSYAASKFAL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  166 AQFTSALRKETiDTRIRIMEVDPGLVETEF--SVVRFHGdkqkadNVYKNSEPLTPEDIAEVILFALTRRENVVIADTLV 243
Cdd:PRK08219 150 RALADALREEE-PGNVRVTSVHPGRTDTDMqrGLVAQEG------GEYDPERYLRPETVAKAVRFAVDAPPDAHITEVVV 222

                 ..
gi 19114010  244 FP 245
Cdd:PRK08219 223 RP 224
PRK12829 PRK12829
short chain dehydrogenase; Provisional
1-228 7.52e-28

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 107.45  E-value: 7.52e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAfEIAKVAKVKLILAARRFSTVEEIAKELEskyEVSVLPLKLDVSDLKSIPGVIESLP 80
Cdd:PRK12829   6 LKPLDGLRVLVTGGASGIGRAIA-EAFAEAGARVHVCDVSEAALAATAARLP---GAKVTATVADVADPAQVERVFDTAV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   81 KEFADIDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFY-SKNKGDILNVGSIAGRESYVGGSVYC 159
Cdd:PRK12829  82 ERFGGLDVLVNNAGIAGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKaSGHGGVIIALSSVAGRLGYPGRTPYA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  160 STKSALAQFTSALRKETIDTRIRIMEVDPGLVETEfSVVRFHGDKQKADNV--------YKNSEPL----TPEDIAEVIL 227
Cdd:PRK12829 162 ASKWAVVGLVKSLAIELGPLGIRVNAILPGIVRGP-RMRRVIEARAQQLGIgldemeqeYLEKISLgrmvEPEDIAATAL 240

                 .
gi 19114010  228 F 228
Cdd:PRK12829 241 F 241
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
9-227 9.89e-28

carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl reductase of the classical SDR family. Studies in Drosophila melanogaster implicate Sniffer in the prevention of neurodegeneration due to aging and oxidative-stress. This subgroup also includes Rhodococcus sp. AD45 IsoH, which is an NAD-dependent 1-hydroxy-2-glutathionyl-2-methyl-3-butene dehydrogenase involved in isoprene metabolism, Aspergillus nidulans StcE encoded by a gene which is part of a proposed sterigmatocystin biosynthesis gene cluster, Bacillus circulans SANK 72073 BtrF encoded by a gene found in the butirosin biosynthesis gene cluster, and Aspergillus parasiticus nor-1 involved in the biosynthesis of aflatoxins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187586 [Multi-domain]  Cd Length: 233  Bit Score: 106.23  E-value: 9.89e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   9 ILITGASSGIGKSTAFEIAKVAKVKLILAARRFSTVEEIAKELESKYEVSVLplKLDVSDLksIPGVIESLPKEFAD--I 86
Cdd:cd05325   1 VLITGASRGIGLELVRQLLARGNNTVIATCRDPSAATELAALGASHSRLHIL--ELDVTDE--IAESAEAVAERLGDagL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  87 DVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILN----VGSIAGRESyvGGSV-YCST 161
Cdd:cd05325  77 DVLINNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINissrVGSIGDNTS--GGWYsYRAS 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19114010 162 KSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSvvrfhgdkqkaDNVYKNSEPLTPEDIAEVIL 227
Cdd:cd05325 155 KAALNMLTKSLAVELKRDGITVVSLHPGWVRTDMG-----------GPFAKNKGPITPEESVAGLL 209
PRK06138 PRK06138
SDR family oxidoreductase;
3-243 2.07e-27

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 106.00  E-value: 2.07e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    3 RLDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKYEVSVLPlkLDVSDLKSIPGVIESLPKE 82
Cdd:PRK06138   2 RLAGRVAIVTGAGSGIGRATAKLFAR-EGARVVVADRDAEAAERVAAAIAAGGRAFARQ--GDVGSAEAVEALVDFVAAR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   83 FADIDVLINNAGLALGTdKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTK 162
Cdd:PRK06138  79 WGRLDVLVNNAGFGCGG-TVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGRAAYVASK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  163 SALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRF--HGDKQKADNVYKNSEPL----TPEDIAEVILFALTRRENV 236
Cdd:PRK06138 158 GAIASLTRAMALDHATDGIRVNAVAPGTIDTPYFRRIFarHADPEALREALRARHPMnrfgTAEEVAQAALFLASDESSF 237

                 ....*..
gi 19114010  237 VIADTLV 243
Cdd:PRK06138 238 ATGTTLV 244
PRK12939 PRK12939
short chain dehydrogenase; Provisional
1-231 2.55e-27

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 105.44  E-value: 2.55e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFEIAKV-AKVKL--ILAARrfstVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIE 77
Cdd:PRK12939   2 ASNLAGKRALVTGAARGLGAAFAEALAEAgATVAFndGLAAE----ARELAAALEAA-GGRAHAIAADLADPASVQRFFD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   78 SLPKEFADIDVLINNAGLALGTDkVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSV 157
Cdd:PRK12939  77 AAAAALGGLDGLVNNAGITNSKS-ATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPKLGA 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19114010  158 YCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSvvrFHGDKQKADNVYKNSEPL----TPEDIAEVILFALT 231
Cdd:PRK12939 156 YVASKGAVIGMTRSLARELGGRGITVNAIAPGLTATEAT---AYVPADERHAYYLKGRALerlqVPDDVAGAVLFLLS 230
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
4-228 3.42e-27

glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR family, it catalyzes the NAD(P)-dependent oxidation of beta-D-glucose to D-glucono-delta-lactone. GlcDH has a typical NAD-binding site glycine-rich pattern as well as the canonical active site tetrad (YXXXK motif plus upstream Ser and Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187616 [Multi-domain]  Cd Length: 253  Bit Score: 105.16  E-value: 3.42e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   4 LDGKTILITGASSGIGKSTAFEIAKvAKVKLILAAR-RFSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLPKE 82
Cdd:cd05358   1 LKGKVALVTGASSGIGKAIAIRLAT-AGANVVVNYRsKEDAAEEVVEEIKAV-GGKAIAVQADVSKEEDVVALFQSAIKE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  83 FADIDVLINNAGLAlGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIF-YSKNKGDILNVGSIAGRESYVGGSVYCST 161
Cdd:cd05358  79 FGTLDILVNNAGLQ-GDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFrKSKIKGKIINMSSVHEKIPWPGHVNYAAS 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19114010 162 KSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGDKQKADNVYKnsEPL----TPEDIAEVILF 228
Cdd:cd05358 158 KGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPINAEAWDDPEQRADLLSL--IPMgrigEPEEIAAAAAW 226
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
3-228 4.97e-27

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 104.97  E-value: 4.97e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    3 RLDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLPKE 82
Cdd:PRK12429   1 MLKGKVALVTGAASGIGLEIALALAK-EGAKVVIADLNDEAAAAAAEALQKA-GGKAIGVAMDVTDEEAINAGIDYAVET 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   83 FADIDVLINNAGLALgTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTK 162
Cdd:PRK12429  79 FGGVDILVNNAGIQH-VAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVGSAGKAAYVSAK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  163 SALAQFTSALRKETIDTRIRIMEVDPGLVETEfsVVRFHGDKQKA------DNVYKN--------SEPLTPEDIAEVILF 228
Cdd:PRK12429 158 HGLIGLTKVVALEGATHGVTVNAICPGYVDTP--LVRKQIPDLAKergiseEEVLEDvllplvpqKRFTTVEEIADYALF 235
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
1-228 9.48e-27

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 104.21  E-value: 9.48e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELEsKYEVSVLPLKLDVSDLKSIPGVIESLP 80
Cdd:PRK13394   2 MSNLNGKTAVVTGAASGIGKEIALELAR-AGAAVAIADLNQDGANAVADEIN-KAGGKAIGVAMDVTNEDAVNAGIDKVA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   81 KEFADIDVLINNAGLALgTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFY-SKNKGDILNVGSIAGRESYVGGSVYC 159
Cdd:PRK13394  80 ERFGSVDILVSNAGIQI-VNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYkDDRGGVVIYMGSVHSHEASPLKSAYV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  160 STKSALAQFTSALRKETIDTRIRIMEVDPGLVET------------------EFSVVRFHGDKQkADNVYknsepLTPED 221
Cdd:PRK13394 159 TAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTplvdkqipeqakelgiseEEVVKKVMLGKT-VDGVF-----TTVED 232

                 ....*..
gi 19114010  222 IAEVILF 228
Cdd:PRK13394 233 VAQTVLF 239
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
4-228 1.28e-26

tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6,8-tetrahydroxynaphthalene reductase (4HNR) of Magnaporthe grisea and the related 1,3,8-trihydroxynaphthalene reductase (3HNR) are typical members of the SDR family containing the canonical glycine rich NAD(P)-binding site and active site tetrad, and function in fungal melanin biosynthesis. This subgroup also includes an SDR from Norway spruce that may function to protect against both biotic and abitoic stress. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187620 [Multi-domain]  Cd Length: 243  Bit Score: 103.51  E-value: 1.28e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   4 LDGKTILITGASSGIGKSTAFEIAKV-AKVKLILAARRfSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLPKE 82
Cdd:cd05362   1 LAGKVALVTGASRGIGRAIAKRLARDgASVVVNYASSK-AAAEEVVAEIEAA-GGKAIAVQADVSDPSQVARLFDAAEKA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  83 FADIDVLINNAGLALGTDkVIDLNIDDAVTMITTNVLGMMAMTRAVLPifYSKNKGDILNVGSIAGRESYVGGSVYCSTK 162
Cdd:cd05362  79 FGGVDILVNNAGVMLKKP-IAETSEEEFDRMFTVNTKGAFFVLQEAAK--RLRDGGRIINISSSLTAAYTPNYGAYAGSK 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19114010 163 SALAQFTSALRKETIDTRIRIMEVDPGLVETEFsvvrFHGDKQKAD-NVYKNSEPL----TPEDIAEVILF 228
Cdd:cd05362 156 AAVEAFTRVLAKELGGRGITVNAVAPGPVDTDM----FYAGKTEEAvEGYAKMSPLgrlgEPEDIAPVVAF 222
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
7-228 1.75e-26

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 103.31  E-value: 1.75e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    7 KTILITGASSGIGKSTAFEIakVAKVKLILAArrFSTVEEIAKELESKY---EVSVLPLKLDVSDLKSIPGVIESLPKEF 83
Cdd:PRK12824   3 KIALVTGAKRGIGSAIAREL--LNDGYRVIAT--YFSGNDCAKDWFEEYgftEDQVRLKELDVTDTEECAEALAEIEEEE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   84 ADIDVLINNAGLAlgTDKVI-DLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTK 162
Cdd:PRK12824  79 GPVDILVNNAGIT--RDSVFkRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQFGQTNYSAAK 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19114010  163 SALAQFTSALRKETIDTRIRIMEVDPGLVETEFSvvrfhgdKQKADNV---YKNSEPL----TPEDIAEVILF 228
Cdd:PRK12824 157 AGMIGFTKALASEGARYGITVNCIAPGYIATPMV-------EQMGPEVlqsIVNQIPMkrlgTPEEIAAAVAF 222
PRK06125 PRK06125
short chain dehydrogenase; Provisional
3-233 2.80e-26

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 103.20  E-value: 2.80e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    3 RLDGKTILITGASSGIGKSTAFEIAKVAkVKLILAARRFSTVEEIAKELESKYEVSVLPLKLDVSDlksiPGVIESLPKE 82
Cdd:PRK06125   4 HLAGKRVLITGASKGIGAAAAEAFAAEG-CHLHLVARDADALEALAADLRAAHGVDVAVHALDLSS----PEAREQLAAE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   83 FADIDVLINNAGLALGTDKvidlnidDAVTMIT------TNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRE---SYV 153
Cdd:PRK06125  79 AGDIDILVNNAGAIPGGGL-------DDVDDAAwragweLKVFGYIDLTRLAYPRMKARGSGVIVNVIGAAGENpdaDYI 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  154 GGSvycSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFH-------GDKQKADNVYKN---SEPLTPEDIA 223
Cdd:PRK06125 152 CGS---AGNAALMAFTRALGGKSLDDGVRVVGVNPGPVATDRMLTLLKgraraelGDESRWQELLAGlplGRPATPEEVA 228
                        250
                 ....*....|
gi 19114010  224 EVILFALTRR 233
Cdd:PRK06125 229 DLVAFLASPR 238
PRK09242 PRK09242
SDR family oxidoreductase;
1-193 2.99e-26

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 102.90  E-value: 2.99e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFEIAKVAkVKLILAARRFSTVEEIAKELESKY-EVSVLPLKLDVSDLKSIPGVIESL 79
Cdd:PRK09242   4 RWRLDGQTALITGASKGIGLAIAREFLGLG-ADVLIVARDADALAQARDELAEEFpEREVHGLAADVSDDEDRRAILDWV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   80 PKEFADIDVLINNAGLALgTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYC 159
Cdd:PRK09242  83 EDHWDGLHILVNNAGGNI-RKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSGAPYG 161
                        170       180       190
                 ....*....|....*....|....*....|....
gi 19114010  160 STKSALAQFTSALRKETIDTRIRIMEVDPGLVET 193
Cdd:PRK09242 162 MTKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRT 195
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
16-228 3.63e-26

Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) reductases.


Pssm-ID: 433310 [Multi-domain]  Cd Length: 236  Bit Score: 102.12  E-value: 3.63e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    16 SGIGKSTAFEIAKvAKVKLILA---ARRFSTVEEIAKELESKYevsvlpLKLDVSDLKSIPGVIESLPKEFADIDVLINN 92
Cdd:pfam13561   6 SGIGWAIARALAE-EGAEVVLTdlnEALAKRVEELAEELGAAV------LPCDVTDEEQVEALVAAAVEKFGRLDILVNN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    93 AGLALGTDK-VIDLNIDDAVTMITTNVLGMMAMTRAVLPIFysKNKGDILNVGSIAGRESYVGGSVYCSTKSALAQFTSA 171
Cdd:pfam13561  79 AGFAPKLKGpFLDTSREDFDRALDVNLYSLFLLAKAALPLM--KEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19114010   172 LRKETIDTRIRIMEVDPGLVETEfSVVRFHGDKQKADNVYKNSePL----TPEDIAEVILF 228
Cdd:pfam13561 157 LAVELGPRGIRVNAISPGPIKTL-AASGIPGFDELLAAAEARA-PLgrlgTPEEVANAAAF 215
PRK07102 PRK07102
SDR family oxidoreductase;
6-237 7.49e-26

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 101.54  E-value: 7.49e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    6 GKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKYEVSVLPLKLDVSDLKSIPGVIESLPkefAD 85
Cdd:PRK07102   1 MKKILIIGATSDIARACARRYAA-AGARLYLAARDVERLERLADDLRARGAVAVSTHELDILDTASHAAFLDSLP---AL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   86 IDVLINNAGLaLGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIA---GRES-YvggsVYCST 161
Cdd:PRK07102  77 PDIVLIAVGT-LGDQAACEADPALALREFRTNFEGPIALLTLLANRFEARGSGTIVGISSVAgdrGRASnY----VYGSA 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19114010  162 KSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSvvrfHGDKQKAdnvyknsePLT--PEDIAEVILFALTRRENVV 237
Cdd:PRK07102 152 KAALTAFLSGLRNRLFKSGVHVLTVKPGFVRTPMT----AGLKLPG--------PLTaqPEEVAKDIFRAIEKGKDVI 217
PRK07201 PRK07201
SDR family oxidoreductase;
3-233 9.68e-26

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 105.80  E-value: 9.68e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    3 RLDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESK-YEVSVLPlkLDVSDLKSIPGVIESLPK 81
Cdd:PRK07201 368 PLVGKVVLITGASSGIGRATAIKVAE-AGATVFLVARNGEALDELVAEIRAKgGTAHAYT--CDLTDSAAVDHTVKDILA 444
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   82 EFADIDVLINNAG------LALGTDKVIDLNiddaVTMiTTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGG 155
Cdd:PRK07201 445 EHGHVDYLVNNAGrsirrsVENSTDRFHDYE----RTM-AVNYFGAVRLILGLLPHMRERRFGHVVNVSSIGVQTNAPRF 519
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19114010  156 SVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVvrfhgdkqkADNVYKNSEPLTPEDIAEVILFALTRR 233
Cdd:PRK07201 520 SAYVASKAALDAFSDVAASETLSDGITFTTIHMPLVRTPMIA---------PTKRYNNVPTISPEEAADMVVRAIVEK 588
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
3-196 1.87e-25

mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes the conversion of fructose to mannitol, an acyclic 6-carbon sugar. MDH is a tetrameric member of the SDR family. This subgroup also includes various other tetrameric SDRs, including Pichia stipitis D-arabinitol dehydrogenase (aka polyol dehydrogenase), Candida albicans Sou1p, a sorbose reductase, and Candida parapsilosis (S)-specific carbonyl reductase (SCR, aka S-specific alcohol dehydrogenase) which catalyzes the enantioselective reduction of 2-hydroxyacetophenone into (S)-1-phenyl-1,2-ethanediol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187610 [Multi-domain]  Cd Length: 252  Bit Score: 100.48  E-value: 1.87e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   3 RLDGKTILITGASSGIGkstaFEIAKV-----AKVKLILAARrfSTVEEIAKELESKYEVSVLPLKLDVSDLKSIPGVIE 77
Cdd:cd05352   5 SLKGKVAIVTGGSRGIG----LAIARAlaeagADVAIIYNSA--PRAEEKAEELAKKYGVKTKAYKCDVSSQESVEKTFK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  78 SLPKEFADIDVLINNAGLALGTDkVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGresYVGG-- 155
Cdd:cd05352  79 QIQKDFGKIDILIANAGITVHKP-ALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSG---TIVNrp 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 19114010 156 ---SVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFS 196
Cdd:cd05352 155 qpqAAYNASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLT 198
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
3-193 2.03e-25

tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup includes TR-I and TR-II; these proteins are members of the SDR family. TRs catalyze the NADPH-dependent reductions of the 3-carbonyl group of tropinone, to a beta-hydroxyl group. TR-I and TR-II produce different stereoisomers from tropinone, TR-I produces tropine (3alpha-hydroxytropane), and TR-II, produces pseudotropine (sigma-tropine, 3beta-hydroxytropane). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187590 [Multi-domain]  Cd Length: 251  Bit Score: 100.60  E-value: 2.03e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   3 RLDGKTILITGASSGIGKSTAFEIAKVAkVKLILAARRFSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLPKE 82
Cdd:cd05329   3 NLEGKTALVTGGTKGIGYAIVEELAGLG-AEVYTCARNQKELDECLTEWREK-GFKVEGSVCDVSSRSERQELMDTVASH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  83 F-ADIDVLINNAGLALgTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCST 161
Cdd:cd05329  81 FgGKLNILVNNAGTNI-RKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGAT 159
                       170       180       190
                ....*....|....*....|....*....|..
gi 19114010 162 KSALAQFTSALRKETIDTRIRIMEVDPGLVET 193
Cdd:cd05329 160 KGALNQLTRSLACEWAKDNIRVNAVAPWVIAT 191
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
6-228 4.46e-25

meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases (BDHs) catalyze the NAD+ dependent conversion of 2,3-butanediol to acetonin; BDHs are classified into types according to their stereospecificity as to substrates and products. Included in this subgroup are Klebsiella pneumonia meso-BDH which catalyzes meso-2,3-butanediol to D(-)-acetonin, and Corynebacterium glutamicum L-BDH which catalyzes lX+)-2,3-butanediol to L(+)-acetonin. This subgroup is comprised of classical SDRs with the characteristic catalytic triad and NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187624 [Multi-domain]  Cd Length: 257  Bit Score: 99.76  E-value: 4.46e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   6 GKTILITGASSGIGKSTAFEIAK----VAKVKLILAARRFSTVEEIakeleSKYEVSVLPLKLDVSDLKSIPGVIESLPK 81
Cdd:cd05366   2 SKVAIITGAAQGIGRAIAERLAAdgfnIVLADLNLEEAAKSTIQEI-----SEAGYNAVAVGADVTDKDDVEALIDQAVE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  82 EFADIDVLINNAGLALgTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKN-KGDILNVGSIAGRESYVGGSVYCS 160
Cdd:cd05366  77 KFGSFDVMVNNAGIAP-ITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGhGGKIINASSIAGVQGFPNLGAYSA 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19114010 161 TKSALAQFTSALRKETIDTRIRIMEVDPGLVETEF------SVVRFHG-DKQKADNVYKNSEPL----TPEDIAEVILF 228
Cdd:cd05366 156 SKFAVRGLTQTAAQELAPKGITVNAYAPGIVKTEMwdyideEVGEIAGkPEGEGFAEFSSSIPLgrlsEPEDVAGLVSF 234
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
1-226 5.47e-25

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 99.87  E-value: 5.47e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFEIAKVAkVKLILAARRfSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLP 80
Cdd:PRK08226   1 MGKLTGKTALITGALQGIGEGIARVFARHG-ANLILLDIS-PEIEKLADELCGR-GHRCTAVVADVRDPASVAAAIKRAK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   81 KEFADIDVLINNAGLA-LGTdkVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGR-ESYVGGSVY 158
Cdd:PRK08226  78 EKEGRIDILVNNAGVCrLGS--FLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSVTGDmVADPGETAY 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19114010  159 CSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFsvvrfhgdkqkADNVYKNSEPLTPE----DIAEVI 226
Cdd:PRK08226 156 ALTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRTPM-----------AESIARQSNPEDPEsvltEMAKAI 216
PRK12828 PRK12828
short chain dehydrogenase; Provisional
1-231 6.30e-25

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 99.10  E-value: 6.30e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARrfstveEIAKELESKYEVSVLPLKL---DVSDLKSIPGVIE 77
Cdd:PRK12828   2 EHSLQGKVVAITGGFGGLGRATAAWLAA-RGARVALIGR------GAAPLSQTLPGVPADALRIggiDLVDPQAARRAVD 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   78 SLPKEFADIDVLINNAGlALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSV 157
Cdd:PRK12828  75 EVNRQFGRLDALVNIAG-AFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAGPGMGA 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19114010  158 YCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEfsvvRFHGDKQKADnvykNSEPLTPEDIAEVILFALT 231
Cdd:PRK12828 154 YAAAKAGVARLTEALAAELLDRGITVNAVLPSIIDTP----PNRADMPDAD----FSRWVTPEQIAAVIAFLLS 219
PRK06841 PRK06841
short chain dehydrogenase; Provisional
3-238 1.34e-24

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 98.58  E-value: 1.34e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    3 RLDGKTILITGASSGIGKSTA--FeIAKVAKVKLIlaaRRFSTVEEIAKELESKyevSVLPLKLDVSDLKSIPGVIESLP 80
Cdd:PRK06841  12 DLSGKVAVVTGGASGIGHAIAelF-AAKGARVALL---DRSEDVAEVAAQLLGG---NAKGLVCDVSDSQSVEAAVAAVI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   81 KEFADIDVLINNAGLALgTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCS 160
Cdd:PRK06841  85 SAFGRIDILVNSAGVAL-LAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVVALERHVAYCA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  161 TKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGDKQKAdnvYKNSEPL----TPEDIAEVILF------AL 230
Cdd:PRK06841 164 SKAGVVGMTKVLALEWGPYGITVNAISPTVVLTELGKKAWAGEKGER---AKKLIPAgrfaYPEEIAAAALFlasdaaAM 240

                 ....*...
gi 19114010  231 TRRENVVI 238
Cdd:PRK06841 241 ITGENLVI 248
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
4-192 1.65e-24

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 98.54  E-value: 1.65e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    4 LDGKTILITGASSGIGKSTAFEI----AKVAKVKLilaarrfstveeiaKELESKYEvSVLPLKLDVSDLKSIPGVIESL 79
Cdd:PRK06171   7 LQGKIIIVTGGSSGIGLAIVKELlangANVVNADI--------------HGGDGQHE-NYQFVPTDVSSAEEVNHTVAEI 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   80 PKEFADIDVLINNAGLAL--------GTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRES 151
Cdd:PRK06171  72 IEKFGRIDGLVNNAGINIprllvdekDPAGKYELNEAAFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGLEG 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 19114010  152 YVGGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVE 192
Cdd:PRK06171 152 SEGQSCYAATKAALNSFTRSWAKELGKHNIRVVGVAPGILE 192
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
4-228 2.30e-24

2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 97.65  E-value: 2.30e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    4 LDGKTILITGASSGIGKSTAfeiakvakvkLILAARRfSTVEEIAKELESKYEVSVLPLKLDVSDLKSIPGVIESLPKEF 83
Cdd:PRK08220   6 FSGKTVWVTGAAQGIGYAVA----------LAFVEAG-AKVIGFDQAFLTQEDYPFATFVLDVSDAAAVAQVCQRLLAET 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   84 ADIDVLINNAGLaLGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKS 163
Cdd:PRK08220  75 GPLDVLVNAAGI-LRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAAHVPRIGMAAYGASKA 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19114010  164 ALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHgDKQKADNV-------YKNSEPL----TPEDIAEVILF 228
Cdd:PRK08220 154 ALTSLAKCVGLELAPYGVRCNVVSPGSTDTDMQRTLWV-DEDGEQQViagfpeqFKLGIPLgkiaRPQEIANAVLF 228
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
2-228 4.51e-24

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 97.16  E-value: 4.51e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    2 SRLDGKTILITGASSGIGKSTAFEIAKVAKVKLILaarrFSTVEEIAKELESKyevSVLPLKLDVSDLKSIPGVIESLPK 81
Cdd:PRK06463   3 MRFKGKVALITGGTRGIGRAIAEAFLREGAKVAVL----YNSAENEAKELREK---GVFTIKCDVGNRDQVKKSKEVVEK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   82 EFADIDVLINNAGLALgTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAG-RESYVGGSVYCS 160
Cdd:PRK06463  76 EFGRVDVLVNNAGIMY-LMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGiGTAAEGTTFYAI 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19114010  161 TKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVV-RFHGDKQKADNVYKNSEPL----TPEDIAEVILF 228
Cdd:PRK06463 155 TKAGIIILTRRLAFELGKYGIRVNAVAPGWVETDMTLSgKSQEEAEKLRELFRNKTVLkttgKPEDIANIVLF 227
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
7-230 4.54e-24

human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical SDR subgroup includes human type 1 17beta-HSD, human retinol dehydrogenase 8, zebrafish photoreceptor associated retinol dehydrogenase type 2, and a chicken ovary-specific 17beta-hydroxysteroid dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 97.15  E-value: 4.54e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   7 KTILITGASSGIGKSTAFEIAKVAK--VKLILAARRFSTVEEIAKELESKYEVSVLPLKLDVSDLKSIPGVIESLPKEfa 84
Cdd:cd09806   1 TVVLITGCSSGIGLHLAVRLASDPSkrFKVYATMRDLKKKGRLWEAAGALAGGTLETLQLDVCDSKSVAAAVERVTER-- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  85 DIDVLINNAGLALgTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSA 164
Cdd:cd09806  79 HVDVLVCNAGVGL-LGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDVYCASKFA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010 165 LAQFTSALRKETIDTRIRIMEVDPGLVETEF--------SVVRFHG-DKQKAD---NVY-KNSEPL------TPEDIAEV 225
Cdd:cd09806 158 LEGLCESLAVQLLPFNVHLSLIECGPVHTAFmekvlgspEEVLDRTaDDITTFhffYQYlAHSKQVfreaaqNPEEVAEV 237

                ....*
gi 19114010 226 ILFAL 230
Cdd:cd09806 238 FLTAI 242
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
1-194 6.24e-24

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 96.63  E-value: 6.24e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTA----FEIAKVAKVKlILAARRFSTVEEIAKEleskyevsVLPLKLDVSDLKSIPGVI 76
Cdd:PRK07067   1 MMRLQGKVALLTGAASGIGEAVAerylAEGARVVIAD-IKPARARLAALEIGPA--------AIAVSLDVTRQDSIDRIV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   77 ESLPKEFADIDVLINNAGLaLGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKG-DILNVGSIAGR--ESYV 153
Cdd:PRK07067  72 AAAVERFGGIDILFNNAAL-FDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQGRGgKIINMASQAGRrgEALV 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 19114010  154 ggSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETE 194
Cdd:PRK07067 151 --SHYCATKAAVISYTQSAALALIRHGINVNAIAPGVVDTP 189
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
6-233 6.27e-24

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup resembles the SDR family, but does not have a perfect match to the NAD-binding motif or the catalytic tetrad characteristic of the SDRs. It includes the SDRs, Q9HYA2 from Pseudomonas aeruginosa PAO1 and APE0912 from Aeropyrum pernix K1. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187602 [Multi-domain]  Cd Length: 253  Bit Score: 96.57  E-value: 6.27e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   6 GKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELeSKYEVSVLPLKLDVSDLKSIPGVIESLPKEFAD 85
Cdd:cd05344   1 GKVALVTAASSGIGLAIARALAR-EGARVAICARNRENLERAASEL-RAGGAGVLAVVADLTDPEDIDRLVEKAGDAFGR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  86 IDVLINNAGLALGTDkVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSAL 165
Cdd:cd05344  79 VDILVNNAGGPPPGP-FAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEPEPNLVLSNVARAGL 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19114010 166 AQFTSALRKETIDTRIRIMEVDPGLVETE--FSVVRFHGDKQK--ADNVYKNSE---PL----TPEDIAEVILFALTRR 233
Cdd:cd05344 158 IGLVKTLSRELAPDGVTVNSVLPGYIDTErvRRLLEARAEKEGisVEEAEKEVAsqiPLgrvgKPEELAALIAFLASEK 236
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
6-228 6.46e-24

d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, catalyzes the interconversion of D-3-hydroxybutyrate and acetoacetate. It is a classical SDR, with the canonical NAD-binding motif and active site tetrad. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187644 [Multi-domain]  Cd Length: 258  Bit Score: 96.75  E-value: 6.46e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   6 GKTILITGASSGIGKSTAFEIAKvAKVKLILAArrFSTVEEIAKE---LESKYEVSVLPLKLDVSDLKSIPGVIESLPKE 82
Cdd:cd08940   2 GKVALVTGSTSGIGLGIARALAA-AGANIVLNG--FGDAAEIEAVragLAAKHGVKVLYHGADLSKPAAIEDMVAYAQRQ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  83 FADIDVLINNAGLALgTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTK 162
Cdd:cd08940  79 FGGVDILVNNAGIQH-VAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVASANKSAYVAAK 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19114010 163 SALAQFTSALRKETIDTRIRIMEVDPGLVETEF--------SVVRFHGDKQKADNVYKNSEP----LTPEDIAEVILF 228
Cdd:cd08940 158 HGVVGLTKVVALETAGTGVTCNAICPGWVLTPLvekqisalAQKNGVPQEQAARELLLEKQPskqfVTPEQLGDTAVF 235
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
5-228 1.02e-23

human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are classical SDRs, with a canonical active site tetrad and a close match to the typical Gly-rich NAD-binding motif. Human DHRS6 is a cytosolic type 2 (R)-hydroxybutyrate dehydrogenase, which catalyses the conversion of (R)-hydroxybutyrate to acetoacetate. Also included in this subgroup is Escherichia coli UcpA (upstream cys P). Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. Note: removed : needed to make this chiodl smaller when drew final trees: rmeoved text form description: Other proteins in this subgroup include Thermoplasma acidophilum aldohexose dehydrogenase, which has high dehydrogenase activity against D-mannose, Bacillus subtilis BacC involved in the biosynthesis of the dipeptide bacilysin and its antibiotic moiety anticapsin, Sphingomonas paucimobilis strain B90 LinC, involved in the degradation of hexachlorocyclohexane isomers...... P).


Pssm-ID: 187626 [Multi-domain]  Cd Length: 241  Bit Score: 95.61  E-value: 1.02e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   5 DGKTILITGASSGIGKSTAFEIAKVAkVKLILAarrfSTVEEIAKELESKYEVSVlpLKLDVSDLKSipgvIESLPKEFA 84
Cdd:cd05368   1 DGKVALITAAAQGIGRAIALAFAREG-ANVIAT----DINEEKLKELERGPGITT--RVLDVTDKEQ----VAALAKEEG 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  85 DIDVLINNAGLA-LGTdkVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGR-ESYVGGSVYCSTK 162
Cdd:cd05368  70 RIDVLFNCAGFVhHGS--ILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASSiKGVPNRFVYSTTK 147
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19114010 163 SALAQFTSALRKETIDTRIRIMEVDPGLVETEF--SVVRFHGDKQKADNVYKNSEPL----TPEDIAEVILF 228
Cdd:cd05368 148 AAVIGLTKSVAADFAQQGIRCNAICPGTVDTPSleERIQAQPDPEEALKAFAARQPLgrlaTPEEVAALAVY 219
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-230 1.22e-23

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 95.94  E-value: 1.22e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFEIAKVAKVKLILAARRFSTVEEIAKELEsKYEVSVLPLKLDVSDLKSIPGVIESLP 80
Cdd:PRK06077   1 MYSLKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKKRAEEMNETLKMVK-ENGGEGIGVLADVSTREGCETLAKATI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   81 KEFADIDVLINNAGLALGTdkvIDLNIDDAVT--MITTNVLGMMAMTRAVLPIFysKNKGDILNVGSIAGRESYVGGSVY 158
Cdd:PRK06077  80 DRYGVADILVNNAGLGLFS---PFLNVDDKLIdkHISTDFKSVIYCSQELAKEM--REGGAIVNIASVAGIRPAYGLSIY 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19114010  159 CSTKSALAQFTSALRKEtIDTRIRIMEVDPGLVETEF--SVVRFHGDKQK--ADNVYKNSEPLTPEDIAEVILFAL 230
Cdd:PRK06077 155 GAMKAAVINLTKYLALE-LAPKIRVNAIAPGFVKTKLgeSLFKVLGMSEKefAEKFTLMGKILDPEEVAEFVAAIL 229
PRK09291 PRK09291
SDR family oxidoreductase;
6-241 7.03e-23

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 93.91  E-value: 7.03e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    6 GKTILITGASSGIGKSTAFEIAKVAKvKLILAARRFSTVEEIAKELEsKYEVSVLPLKLDVSDLKSIPGVIESlpkefaD 85
Cdd:PRK09291   2 SKTILITGAGSGFGREVALRLARKGH-NVIAGVQIAPQVTALRAEAA-RRGLALRVEKLDLTDAIDRAQAAEW------D 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   86 IDVLINNAGLALGtDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSAL 165
Cdd:PRK09291  74 VDVLLNNAGIGEA-GAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLITGPFTGAYCASKHAL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  166 AQFTSALRKETIDTRIRIMEVDPGLVETEF------SVVRFHGDkqkADNVYKNSEPLTPE---DIAEVIlfalTRRENV 236
Cdd:PRK09291 153 EAIAEAMHAELKPFGIQVATVNPGPYLTGFndtmaeTPKRWYDP---ARNFTDPEDLAFPLeqfDPQEMI----DAMVEV 225

                 ....*
gi 19114010  237 VIADT 241
Cdd:PRK09291 226 IPADT 230
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
3-228 7.33e-23

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 93.86  E-value: 7.33e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    3 RLDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLPKE 82
Cdd:PRK08213   9 DLSGKTALVTGGSRGLGLQIAEALGE-AGARVVLSARKAEELEEAAAHLEAL-GIDALWIAADVADEADIERLAEETLER 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   83 FADIDVLINNAGLALGT----------DKVIDLniddavtmittNVLGMMAMTRAVLPI-FYSKNKGDILNVGSIAGres 151
Cdd:PRK08213  87 FGHVDILVNNAGATWGApaedhpveawDKVMNL-----------NVRGLFLLSQAVAKRsMIPRGYGRIINVASVAG--- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  152 yVGGS--------VYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRF--HGDKQKADNvyknsePL---- 217
Cdd:PRK08213 153 -LGGNppevmdtiAYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMTRGTLerLGEDLLAHT------PLgrlg 225
                        250
                 ....*....|.
gi 19114010  218 TPEDIAEVILF 228
Cdd:PRK08213 226 DDEDLKGAALL 236
PRK06482 PRK06482
SDR family oxidoreductase;
6-197 1.01e-22

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 94.03  E-value: 1.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    6 GKTILITGASSGIGKstafeiakvAKVKLILAA--RRFSTVEEIA--KELESKYEVSVLPLKLDVSDLKSIPGVIESLPK 81
Cdd:PRK06482   2 SKTWFITGASSGFGR---------GMTERLLARgdRVAATVRRPDalDDLKARYGDRLWVLQLDVTDSAAVRAVVDRAFA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   82 EFADIDVLINNAGLAL--GTDKVIDLNIDDavtMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYC 159
Cdd:PRK06482  73 ALGRIDVVVSNAGYGLfgAAEELSDAQIRR---QIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQIAYPGFSLYH 149
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 19114010  160 STKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSV 197
Cdd:PRK06482 150 ATKWGIEGFVEAVAQEVAPFGIEFTIVEPGPARTNFGA 187
PRK05867 PRK05867
SDR family oxidoreductase;
4-195 1.20e-22

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 93.18  E-value: 1.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    4 LDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELeSKYEVSVLPLKLDVSDLKSIPGVIESLPKEF 83
Cdd:PRK05867   7 LHGKRALITGASTGIGKRVALAYVE-AGAQVAIAARHLDALEKLADEI-GTSGGKVVPVCCDVSQHQQVTSMLDQVTAEL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   84 ADIDVLINNAGLaLGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGD-ILNVGSIAGRESYVGGSV--YCS 160
Cdd:PRK05867  85 GGIDIAVCNAGI-ITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQGQGGvIINTASMSGHIINVPQQVshYCA 163
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 19114010  161 TKSALAQFTSALRKETIDTRIRIMEVDPGLVETEF 195
Cdd:PRK05867 164 SKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTEL 198
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
6-228 1.55e-22

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 92.33  E-value: 1.55e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    6 GKTILITGASSGIGkstafeiakVAKVKLILAARrfSTVEEIAKELESKYEVSVLPLKLDVSDlksipgVIESLPKEFAD 85
Cdd:PRK06550   5 TKTVLITGAASGIG---------LAQARAFLAQG--AQVYGVDKQDKPDLSGNFHFLQLDLSD------DLEPLFDWVPS 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   86 IDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSAL 165
Cdd:PRK06550  68 VDILCNTAGILDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAGGGGAAYTASKHAL 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19114010  166 AQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFhGDKQKADNVYKNSeP----LTPEDIAEVILF 228
Cdd:PRK06550 148 AGFTKQLALDYAKDGIQVFGIAPGAVKTPMTAADF-EPGGLADWVARET-PikrwAEPEEVAELTLF 212
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
3-228 2.57e-22

classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187613 [Multi-domain]  Cd Length: 270  Bit Score: 92.74  E-value: 2.57e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   3 RLDGKTILITGASSGIGKSTAFEIAKV-AKVKLILAARRFSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLPK 81
Cdd:cd05355  23 KLKGKKALITGGDSGIGRAVAIAFAREgADVAINYLPEEEDDAEETKKLIEEE-GRKCLLIPGDLGDESFCRDLVKEVVK 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  82 EFADIDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPifYSKNKGDILNVGSIAGREsyvgGSV---- 157
Cdd:cd05355 102 EFGKLDILVNNAAYQHPQESIEDITTEQLEKTFRTNIFSMFYLTKAALP--HLKKGSSIINTTSVTAYK----GSPhlld 175
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19114010 158 YCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFsvVRFHGDKQKADNVYKNS---EPLTPEDIAEVILF 228
Cdd:cd05355 176 YAATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPL--IPSSFPEEKVSEFGSQVpmgRAGQPAEVAPAYVF 247
PRK07890 PRK07890
short chain dehydrogenase; Provisional
4-189 2.85e-22

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 92.33  E-value: 2.85e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    4 LDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLPKEF 83
Cdd:PRK07890   3 LKGKVVVVSGVGPGLGRTLAVRAAR-AGADVVLAARTAERLDEVAAEIDDL-GRRALAVPTDITDEDQCANLVALALERF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   84 ADIDVLINNAgLALGTDK-VIDLNIDDAVTMITTNVLGMMAMTRAVLPIFySKNKGDILNVGSIAGRESYVGGSVYCSTK 162
Cdd:PRK07890  81 GRVDALVNNA-FRVPSMKpLADADFAHWRAVIELNVLGTLRLTQAFTPAL-AESGGSIVMINSMVLRHSQPKYGAYKMAK 158
                        170       180
                 ....*....|....*....|....*..
gi 19114010  163 SALAQFTSALRKETIDTRIRIMEVDPG 189
Cdd:PRK07890 159 GALLAASQSLATELGPQGIRVNSVAPG 185
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
6-243 3.92e-22

classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad and domain size of the classical SDRs, but has an atypical NAD-binding motif ([ST]G[GA]XGXXG). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187635 [Multi-domain]  Cd Length: 250  Bit Score: 91.63  E-value: 3.92e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   6 GKTILITGASSGIGKSTAfEIAKVAKVKLILAARRFSTVEEIAKELESKYEVSVLPLKLDVSDLKSIPGVIESLPKEFAD 85
Cdd:cd08930   2 DKIILITGAAGLIGKAFC-KALLSAGARLILADINAPALEQLKEELTNLYKNRVIALELDITSKESIKELIESYLEKFGR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  86 IDVLINNAGLA--LGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAG-----RESYVGGS-- 156
Cdd:cd08930  81 IDILINNAYPSpkVWGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGviapdFRIYENTQmy 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010 157 ---VYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVEtefsvvrfhgDKQKADNV--YKNSEP----LTPEDIAEVIL 227
Cdd:cd08930 161 spvEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGIL----------NNQPSEFLekYTKKCPlkrmLNPEDLRGAII 230
                       250
                ....*....|....*.
gi 19114010 228 FALTRRENVVIADTLV 243
Cdd:cd08930 231 FLLSDASSYVTGQNLV 246
PRK06701 PRK06701
short chain dehydrogenase; Provisional
3-223 4.85e-22

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 92.40  E-value: 4.85e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    3 RLDGKTILITGASSGIGKSTAF----EIAKVAKVKLilaarrfsTVEEIAKELESKYE---VSVLPLKLDVSDLKSIPGV 75
Cdd:PRK06701  43 KLKGKVALITGGDSGIGRAVAVlfakEGADIAIVYL--------DEHEDANETKQRVEkegVKCLLIPGDVSDEAFCKDA 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   76 IESLPKEFADIDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPifYSKNKGDILNVGSIAGREsyvgG 155
Cdd:PRK06701 115 VEETVRELGRLDILVNNAAFQYPQQSLEDITAEQLDKTFKTNIYSYFHMTKAALP--HLKQGSAIINTGSITGYE----G 188
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19114010  156 SV----YCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGDKQK---ADNVYKnsEPLTPEDIA 223
Cdd:PRK06701 189 NEtlidYSATKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTPLIPSDFDEEKVSqfgSNTPMQ--RPGQPEELA 261
PRK06172 PRK06172
SDR family oxidoreductase;
1-228 6.92e-22

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 91.35  E-value: 6.92e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIA---KELESKyevsVLPLKLDVSDLKSIPGVIE 77
Cdd:PRK06172   2 SMTFSGKVALVTGGAAGIGRATALAFAR-EGAKVVVADRDAAGGEETValiREAGGE----ALFVACDVTRDAEVKALVE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   78 SLPKEFADIDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSV 157
Cdd:PRK06172  77 QTIAAYGRLDYAFNNAGIEIEQGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPKMSI 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19114010  158 YCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGD---KQKADNVYKNSEPLTPEDIAEVILF 228
Cdd:PRK06172 157 YAASKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDMFRRAYEADprkAEFAAAMHPVGRIGKVEEVASAVLY 230
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
7-231 7.47e-22

insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains insect type ADH, and 15-hydroxyprostaglandin dehydrogenase (15-PGDH) type I; these proteins are classical SDRs. ADH catalyzes the NAD+-dependent oxidation of alcohols to aldehydes/ketones. This subgroup is distinct from the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase/reductase family, and evolved in fruit flies to allow the digestion of fermenting fruit. 15-PGDH catalyzes the NAD-dependent interconversion of (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, and has a typical SDR glycine-rich NAD-binding motif, which is not fully present in ADH. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 90.82  E-value: 7.47e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   7 KTILITGASSGIGKSTAFEIAKVAKvKLILAARRFSTveEIAKELESKY-EVSVLPLKLDVSDLKSIPGVIESLPKEFAD 85
Cdd:cd05323   1 KVAIITGGASGIGLATAKLLLKKGA-KVAILDRNENP--GAAAELQAINpKVKATFVQCDVTSWEQLAAAFKKAIEKFGR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  86 IDVLINNAGLA--LGTDKVIDLNIDDAVTmITTNVLGMMAMTRAVLPIFYSKNKGD---ILNVGSIAGRESYVGGSVYCS 160
Cdd:cd05323  78 VDILINNAGILdeKSYLFAGKLPPPWEKT-IDVNLTGVINTTYLALHYMDKNKGGKggvIVNIGSVAGLYPAPQFPVYSA 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19114010 161 TKSALAQFTSALRKETI-DTRIRIMEVDPGLVETEFsvvrFHGDKQKADNVYKNSEPLTPEDIAEVILFALT 231
Cdd:cd05323 157 SKHGVVGFTRSLADLLEyKTGVRVNAICPGFTNTPL----LPDLVAKEAEMLPSAPTQSPEVVAKAIVYLIE 224
PRK08267 PRK08267
SDR family oxidoreductase;
7-229 9.79e-22

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 90.77  E-value: 9.79e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    7 KTILITGASSGIGKSTAfeiakvakvklilaaRRF--------------STVEEIAKELESKyevSVLPLKLDVSDLKSI 72
Cdd:PRK08267   2 KSIFITGAASGIGRATA---------------LLFaaegwrvgaydineAGLAALAAELGAG---NAWTGALDVTDRAAW 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   73 PGVIEslpkEFAD-----IDVLINNAGLALGTDkVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIA 147
Cdd:PRK08267  64 DAALA----DFAAatggrLDVLFNNAGILRGGP-FEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSSAS 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  148 GRESYVGGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETefSVVRFHGDKQKADNVYKNSEPLTPEDIAEVIL 227
Cdd:PRK08267 139 AIYGQPGLAVYSATKFAVRGLTEALDLEWRRHGIRVADVMPLFVDT--AMLDGTSNEVDAGSTKRLGVRLTPEDVAEAVW 216

                 ..
gi 19114010  228 FA 229
Cdd:PRK08267 217 AA 218
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
4-232 1.00e-21

RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is an SDR-family beta-ketoacyl reductase involved in Rhamnolipid biosynthesis. RhlG is similar to but distinct from the FabG family of beta-ketoacyl-acyl carrier protein (ACP) of type II fatty acid synthesis. RhlG and related proteins are classical SDRs, with a canonical active site tetrad and glycine-rich NAD(P)-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187646 [Multi-domain]  Cd Length: 250  Bit Score: 90.62  E-value: 1.00e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   4 LDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKYEVSVLPlkLDVSDLKSIPGVIESLPKEF 83
Cdd:cd08942   4 VAGKIVLVTGGSRGIGRMIAQGFLE-AGARVIISARKAEACADAAEELSAYGECIAIP--ADLSSEEGIEALVARVAERS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  84 ADIDVLINNAGLALGT----------DKVIDLniddavtmittNVLGMMAMTRAVLPIFYS----KNKGDILNVGSIAG- 148
Cdd:cd08942  81 DRLDVLVNNAGATWGApleafpesgwDKVMDI-----------NVKSVFFLTQALLPLLRAaataENPARVINIGSIAGi 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010 149 RESYVGGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEfsVVRFHGDKQKADNVYKNSEPL----TPEDIAE 224
Cdd:cd08942 150 VVSGLENYSYGASKAAVHQLTRKLAKELAGEHITVNAIAPGRFPSK--MTAFLLNDPAALEAEEKSIPLgrwgRPEDMAG 227

                ....*...
gi 19114010 225 VILFALTR 232
Cdd:cd08942 228 LAIMLASR 235
PRK06139 PRK06139
SDR family oxidoreductase;
1-193 1.00e-21

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 92.09  E-value: 1.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESK-YEVSVLPlkLDVSDLKSIPGVIESL 79
Cdd:PRK06139   2 MGPLHGAVVVITGASSGIGQATAEAFAR-RGARLVLAARDEEALQAVAEECRALgAEVLVVP--TDVTDADQVKALATQA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   80 PKEFADIDVLINNAGL-ALGTDKVIDLNIDDAVtmITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVY 158
Cdd:PRK06139  79 ASFGGRIDVWVNNVGVgAVGRFEETPIEAHEQV--IQTNLIGYMRDAHAALPIFKKQGHGIFINMISLGGFAAQPYAAAY 156
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 19114010  159 CSTKSALAQFTSALRKETIDTR-IRIMEVDPGLVET 193
Cdd:PRK06139 157 SASKFGLRGFSEALRGELADHPdIHVCDVYPAFMDT 192
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
4-242 1.05e-21

xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins identified as L-xylulose reductase (XR) and carbonyl reductase; they are members of the SDR family. XR, catalyzes the NADP-dependent reduction of L-xyulose and other sugars. Tetrameric mouse carbonyl reductase is involved in the metabolism of biogenic and xenobiotic carbonyl compounds. This subgroup also includes tetrameric chicken liver D-erythrulose reductase, which catalyzes the reduction of D-erythrulose to D-threitol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187609 [Multi-domain]  Cd Length: 244  Bit Score: 90.61  E-value: 1.05e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   4 LDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESkyevsVLPLKLDVSDLKSipgVIESLPKEF 83
Cdd:cd05351   5 FAGKRALVTGAGKGIGRATVKALAK-AGARVVAVSRTQADLDSLVRECPG-----IEPVCVDLSDWDA---TEEALGSVG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  84 AdIDVLINNAGLALgTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKN-KGDILNVGSIAGRESYVGGSVYCSTK 162
Cdd:cd05351  76 P-VDLLVNNAAVAI-LQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGvPGSIVNVSSQASQRALTNHTVYCSTK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010 163 SALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFhGDKQKADNVyKNSEPLTP----EDIAEVILFALTRRENVVI 238
Cdd:cd05351 154 AALDMLTKVMALELGPHKIRVNSVNPTVVMTDMGRDNW-SDPEKAKKM-LNRIPLGKfaevEDVVNAILFLLSDKSSMTT 231

                ....
gi 19114010 239 ADTL 242
Cdd:cd05351 232 GSTL 235
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
9-228 1.29e-21

2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 dihydrozybenzoate dehydrogenase shares the characteristics of the classical SDRs. This subgroup includes Escherichai coli EntA which catalyzes the NAD+-dependent oxidation of 2,3-dihydro-2,3-dihydroxybenzoate to 2,3-dihydroxybenzoate during biosynthesis of the siderophore Enterobactin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187592 [Multi-domain]  Cd Length: 244  Bit Score: 90.22  E-value: 1.29e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   9 ILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKyevsvlplKLDVSDLKSIPGVIESLPKEFADIDV 88
Cdd:cd05331   1 VIVTGAAQGIGRAVARHLLQ-AGATVIALDLPFVLLLEYGDPLRLT--------PLDVADAAAVREVCSRLLAEHGPIDA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  89 LINNAG-LALG-TDKvidLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSALA 166
Cdd:cd05331  72 LVNCAGvLRPGaTDP---LSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRISMAAYGASKAALA 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19114010 167 QFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGDKQKADNV------YKNSEPL----TPEDIAEVILF 228
Cdd:cd05331 149 SLSKCLGLELAPYGVRCNVVSPGSTDTAMQRTLWHDEDGAAQVIagvpeqFRLGIPLgkiaQPADIANAVLF 220
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
3-228 1.44e-21

3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes members identified as 3beta17beta hydroxysteroid dehydrogenase, 20beta hydroxysteroid dehydrogenase, and R-alcohol dehydrogenase. These proteins exhibit the canonical active site tetrad and glycine rich NAD(P)-binding motif of the classical SDRs. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187600 [Multi-domain]  Cd Length: 247  Bit Score: 90.13  E-value: 1.44e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   3 RLDGKTILITGASSGIGKSTAFEIAKV-AKVKL--ILAARRFSTVEEIAKEleSKYevsvlpLKLDVSDLKSIPGVIESL 79
Cdd:cd05341   2 RLKGKVAIVTGGARGLGLAHARLLVAEgAKVVLsdILDEEGQAAAAELGDA--ARF------FHLDVTDEDGWTAVVDTA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  80 PKEFADIDVLINNAGLALGTDkVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYC 159
Cdd:cd05341  74 REAFGRLDVLVNNAGILTGGT-VETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALAAYN 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19114010 160 STKSALAQFT--SALRKETIDTRIRIMEVDPGLVETefSVVRFHGDKQKADNVYKNSePL----TPEDIAEVILF 228
Cdd:cd05341 153 ASKGAVRGLTksAALECATQGYGIRVNSVHPGYIYT--PMTDELLIAQGEMGNYPNT-PMgragEPDEIAYAVVY 224
PRK07060 PRK07060
short chain dehydrogenase; Provisional
1-231 1.56e-21

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 90.16  E-value: 1.56e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKyevsvlPLKLDVSDlksiPGVIESLP 80
Cdd:PRK07060   4 AFDFSGKSVLVTGASSGIGRACAVALAQ-RGARVVAAARNAAALDRLAGETGCE------PLRLDVGD----DAAIRAAL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   81 KEFADIDVLINNAGLALGtDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNK-GDILNVGSIAGRESYVGGSVYC 159
Cdd:PRK07060  73 AAAGAFDGLVNCAGIASL-ESALDMTAEGFDRVMAVNARGAALVARHVARAMIAAGRgGSIVNVSSQAALVGLPDHLAYC 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19114010  160 STKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSvVRFHGDKQKADNVYKNSePL----TPEDIAEVILFALT 231
Cdd:PRK07060 152 ASKAALDAITRVLCVELGPHGIRVNSVNPTVTLTPMA-AEAWSDPQKSGPMLAAI-PLgrfaEVDDVAAPILFLLS 225
PRK05650 PRK05650
SDR family oxidoreductase;
9-226 1.69e-21

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 90.48  E-value: 1.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    9 ILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKEL-ESKYEVSVLPLklDVSDLKSIPGVIESLPKEFADID 87
Cdd:PRK05650   3 VMITGAASGLGRAIALRWAR-EGWRLALADVNEEGGEETLKLLrEAGGDGFYQRC--DVRDYSQLTALAQACEEKWGGID 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   88 VLINNAGLALGtDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSALAQ 167
Cdd:PRK05650  80 VIVNNAGVASG-GFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAMSSYNVAKAGVVA 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19114010  168 FTSALRKETIDTRIRIMEVDPGLVETEF-SVVRFHGDKQKAdNVYK--NSEPLTPEDIAEVI 226
Cdd:PRK05650 159 LSETLLVELADDEIGVHVVCPSFFQTNLlDSFRGPNPAMKA-QVGKllEKSPITAADIADYI 219
PRK08589 PRK08589
SDR family oxidoreductase;
1-228 1.74e-21

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 90.61  E-value: 1.74e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFEIAKVAKVklILAARRFSTVEEIAKELESKYEvSVLPLKLDVSDLKSIPGVIESLP 80
Cdd:PRK08589   1 MKRLENKVAVITGASTGIGQASAIALAQEGAY--VLAVDIAEAVSETVDKIKSNGG-KAKAYHVDISDEQQVKDFASEIK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   81 KEFADIDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYsKNKGDILNVGSIAGRESYVGGSVYCS 160
Cdd:PRK08589  78 EQFGRVDVLFNNAGVDNAAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMM-EQGGSIINTSSFSGQAADLYRSGYNA 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19114010  161 TKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFsVVRFHGDK-----QKADNVYKNSEPL----TPEDIAEVILF 228
Cdd:PRK08589 157 AKGAVINFTKSIAIEYGRDGIRANAIAPGTIETPL-VDKLTGTSedeagKTFRENQKWMTPLgrlgKPEEVAKLVVF 232
PRK06949 PRK06949
SDR family oxidoreductase;
4-194 2.69e-21

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 89.82  E-value: 2.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    4 LDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLPKEF 83
Cdd:PRK06949   7 LEGKVALVTGASSGLGARFAQVLAQ-AGAKVVLASRRVERLKELRAEIEAE-GGAAHVVSLDVTDYQSIKAAVAHAETEA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   84 ADIDVLINNAGLAlGTDKVIDLNIDDAVTMITTNVLG-----------MMAMTRAVLPifySKNKGDILNVGSIAGRESY 152
Cdd:PRK06949  85 GTIDILVNNSGVS-TTQKLVDVTPADFDFVFDTNTRGaffvaqevakrMIARAKGAGN---TKPGGRIINIASVAGLRVL 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 19114010  153 VGGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETE 194
Cdd:PRK06949 161 PQIGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTE 202
PRK06484 PRK06484
short chain dehydrogenase; Validated
6-243 3.90e-21

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 92.22  E-value: 3.90e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    6 GKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKYevsvLPLKLDVSDLKSIPGVIESLPKEFAD 85
Cdd:PRK06484   5 SRVVLVTGAAGGIGRAACQRFAR-AGDQVVVADRNVERARERADSLGPDH----HALAMDVSDEAQIREGFEQLHREFGR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   86 IDVLINNAGLALGTDK-VIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGD-ILNVGSIAGRESYVGGSVYCSTKS 163
Cdd:PRK06484  80 IDVLVNNAGVTDPTMTaTLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGHGAaIVNVASGAGLVALPKRTAYSASKA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  164 ALAQFTSALRKETIDTRIRIMEVDPGLVETEfsVVRFHGDKQKAD-NVYKNSEPL----TPEDIAEVILFALTRRENVVI 238
Cdd:PRK06484 160 AVISLTRSLACEWAAKGIRVNAVLPGYVRTQ--MVAELERAGKLDpSAVRSRIPLgrlgRPEEIAEAVFFLASDQASYIT 237

                 ....*
gi 19114010  239 ADTLV 243
Cdd:PRK06484 238 GSTLV 242
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
4-253 6.35e-21

Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER is a peroxisomal protein with a proposed role in fatty acid elongation. Fatty acid synthesis is known to occur in the both endoplasmic reticulum and mitochondria; peroxisomal TER has been proposed as an additional fatty acid elongation system, it reduces the double bond at C-2 as the last step of elongation. This system resembles the mitochondrial system in that acetyl-CoA is used as a carbon donor. TER may also function in phytol metabolism, reducting phytenoyl-CoA to phytanoyl-CoA in peroxisomes. DECR processes double bonds in fatty acids to increase their utility in fatty acid metabolism; it reduces 2,4-dienoyl-CoA to an enoyl-CoA. DECR is active in mitochondria and peroxisomes. This subgroup has the Gly-rich NAD-binding motif of the classical SDR family, but does not display strong identity to the canonical active site tetrad, and lacks the characteristic Tyr at the usual position. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187627 [Multi-domain]  Cd Length: 249  Bit Score: 88.41  E-value: 6.35e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   4 LDGKTILITGASSGIGKSTAFEIAKV-AKVklILAARRFSTVEEIAKELESKYEVSVLPLKLDVSDLKSIPGVIESLPKE 82
Cdd:cd05369   1 LKGKVAFITGGGTGIGKAIAKAFAELgASV--AIAGRKPEVLEAAAEEISSATGGRAHPIQCDVRDPEAVEAAVDETLKE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  83 FADIDVLINNAG---LAlGTDKvIDLNIDDAVtmITTNVLGMMAMTRAVLP-IFYSKNKGDILNVGSIAGRESYVGGSVY 158
Cdd:cd05369  79 FGKIDILINNAAgnfLA-PAES-LSPNGFKTV--IDIDLNGTFNTTKAVGKrLIEAKHGGSILNISATYAYTGSPFQVHS 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010 159 CSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGDKQKADNVyKNSEPL----TPEDIAEVILFALTRRE 234
Cdd:cd05369 155 AAAKAGVDALTRSLAVEWGPYGIRVNAIAPGPIPTTEGMERLAPSGKSEKKM-IERVPLgrlgTPEEIANLALFLLSDAA 233
                       250
                ....*....|....*....
gi 19114010 235 NVVIADTLVFpshQGGANH 253
Cdd:cd05369 234 SYINGTTLVV---DGGQWL 249
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
4-243 8.32e-21

classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site tetrad and glycine-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187648 [Multi-domain]  Cd Length: 246  Bit Score: 87.93  E-value: 8.32e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   4 LDGKTILITGASSGIGKSTAFEIAKVAkVKLILAARRFSTVEEIAkeleSKYEVSVLPLKLDVSDLKSIPGVIESLPKEF 83
Cdd:cd08944   1 LEGKVAIVTGAGAGIGAACAARLAREG-ARVVVADIDGGAAQAVV----AQIAGGALALRVDVTDEQQVAALFERAVEEF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  84 ADIDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKS 163
Cdd:cd08944  76 GGLDLLVNNAGAMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGDPGYGAYGASKA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010 164 ALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGDKQKADN-------VYKNSEPLTPEDIAEVILFALTRRENV 236
Cdd:cd08944 156 AIRNLTRTLAAELRHAGIRCNALAPGLIDTPLLLAKLAGFEGALGPggfhlliHQLQGRLGRPEDVAAAVVFLLSDDASF 235

                ....*..
gi 19114010 237 VIADTLV 243
Cdd:cd08944 236 ITGQVLC 242
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
6-194 1.01e-20

retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup containing retinol-DHs and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 88.29  E-value: 1.01e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   6 GKTILITGASSGIGKSTAFEIAKVAkVKLILAARRFSTVEEIAKELESKYEVS-VLPLKLDVSDLKSIPGVIESLPKEFA 84
Cdd:cd09807   1 GKTVIITGANTGIGKETARELARRG-ARVIMACRDMAKCEEAAAEIRRDTLNHeVIVRHLDLASLKSIRAFAAEFLAEED 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  85 DIDVLINNAGLALGTDKVIDlniDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIA------------GRESY 152
Cdd:cd09807  80 RLDVLINNAGVMRCPYSKTE---DGFEMQFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSSLAhkagkinfddlnSEKSY 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 19114010 153 VGGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETE 194
Cdd:cd09807 157 NTGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTE 198
PRK06947 PRK06947
SDR family oxidoreductase;
5-231 2.19e-20

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 87.17  E-value: 2.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    5 DGKTILITGASSGIGKSTAFEIAKVAKVKLILAARRFSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLPKEFA 84
Cdd:PRK06947   1 MRKVVLITGASRGIGRATAVLAAARGWSVGINYARDAAAAEETADAVRAA-GGRACVVAGDVANEADVIAMFDAVQSAFG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   85 DIDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAV---LPIFYSKNKGDILNVGSIAGR----ESYVGgsv 157
Cdd:PRK06947  80 RLDALVNNAGIVAPSMPLADMDAARLRRMFDTNVLGAYLCAREAarrLSTDRGGRGGAIVNVSSIASRlgspNEYVD--- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  158 YCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEfsvvrFHGDKQKADNVYK--NSEPL----TPEDIAEVILFALT 231
Cdd:PRK06947 157 YAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETE-----IHASGGQPGRAARlgAQTPLgragEADEVAETIVWLLS 231
PRK06128 PRK06128
SDR family oxidoreductase;
1-193 2.31e-20

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 87.99  E-value: 2.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFEIAKV-AKVKLILAARRFSTVEEIAKELESKYEVSVlPLKLDVSDLKSIPGVIESL 79
Cdd:PRK06128  50 FGRLQGRKALITGADSGIGRATAIAFAREgADIALNYLPEEEQDAAEVVQLIQAEGRKAV-ALPGDLKDEAFCRQLVERA 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   80 PKEFADIDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPifYSKNKGDILNVGSIAGRESYVGGSVYC 159
Cdd:PRK06128 129 VKELGGLDILVNIAGKQTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIP--HLPPGASIINTGSIQSYQPSPTLLDYA 206
                        170       180       190
                 ....*....|....*....|....*....|....
gi 19114010  160 STKSALAQFTSALRKETIDTRIRIMEVDPGLVET 193
Cdd:PRK06128 207 STKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWT 240
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
4-194 2.91e-20

Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter sphaeroides SDH, and other SDHs. SDH preferentially interconverts D-sorbitol (D-glucitol) and D-fructose, but also interconverts L-iditol/L-sorbose and galactitol/D-tagatose. SDH is NAD-dependent and is a dimeric member of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187621 [Multi-domain]  Cd Length: 254  Bit Score: 86.90  E-value: 2.91e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   4 LDGKTILITGASSGIGKSTA----FEIAKVAKVKLILAARRfSTVEEIakeleskyEVSVLPLKLDVSDLKSIPGVIESL 79
Cdd:cd05363   1 LDGKTALITGSARGIGRAFAqayvREGARVAIADINLEAAR-ATAAEI--------GPAACAISLDVTDQASIDRCVAAL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  80 PKEFADIDVLINNAGLaLGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKG-DILNVGSIAGRESYVGGSVY 158
Cdd:cd05363  72 VDRWGSIDILVNNAAL-FDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQGRGgKIINMASQAGRRGEALVGVY 150
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 19114010 159 CSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETE 194
Cdd:cd05363 151 CATKAAVISLTQSAGLNLIRHGINVNAIAPGVVDGE 186
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
3-243 3.45e-20

secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; Podophyllum secoisolariciresinol-DH is a homo tetrameric, classical SDR that catalyzes the NAD-dependent conversion of (-)-secoisolariciresinol to (-)-matairesinol via a (-)-lactol intermediate. (-)-Matairesinol is an intermediate to various 8'-lignans, including the cancer-preventive mammalian lignan, and those involved in vascular plant defense. This subgroup also includes rice momilactone A synthase which catalyzes the conversion of 3beta-hydroxy-9betaH-pimara-7,15-dien-19,6beta-olide into momilactone A, Arabidopsis ABA2 which during abscisic acid (ABA) biosynthesis, catalyzes the conversion of xanthoxin to abscisic aldehyde and, maize Tasselseed2 which participate in the maize sex determination pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187587 [Multi-domain]  Cd Length: 249  Bit Score: 86.36  E-value: 3.45e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   3 RLDGKTILITGASSGIGKSTAFEIAKV-AKVklILAARRFSTVEEIAKELESKyEVSVLplKLDVSDLKSIPGVIESLPK 81
Cdd:cd05326   1 RLDGKVAIITGGASGIGEATARLFAKHgARV--VIADIDDDAGQAVAAELGDP-DISFV--HCDVTVEADVRAAVDTAVA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  82 EFADIDVLINNAGLaLGT-------------DKVIDLNIDDAVtmittnvLGMMAMTRAVLPifysKNKGDILNVGSIAG 148
Cdd:cd05326  76 RFGRLDIMFNNAGV-LGApcysiletsleefERVLDVNVYGAF-------LGTKHAARVMIP----AKKGSIVSVASVAG 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010 149 RESYVGGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGDKQKADNVYKNSE-----PLTPEDIA 223
Cdd:cd05326 144 VVGGLGPHAYTASKHAVLGLTRSAATELGEHGIRVNCVSPYGVATPLLTAGFGVEDEAIEEAVRGAAnlkgtALRPEDIA 223
                       250       260
                ....*....|....*....|
gi 19114010 224 EVILFALTRRENVVIADTLV 243
Cdd:cd05326 224 AAVLYLASDDSRYVSGQNLV 243
PRK06500 PRK06500
SDR family oxidoreductase;
1-228 3.78e-20

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 86.55  E-value: 3.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFE-IAKVAKVklILAARRFSTVEEIAKELESkyevSVLPLKLDVSDLKSIPGVIESL 79
Cdd:PRK06500   1 MSRLQGKTALITGGTSGIGLETARQfLAEGARV--AITGRDPASLEAARAELGE----SALVIRADAGDVAAQKALAQAL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   80 PKEFADIDVLINNAGLAL----------GTDKVIDlniddavtmitTNVLGMMAMTRAVLPIFyskNKGD--ILNvGSIA 147
Cdd:PRK06500  75 AEAFGRLDAVFINAGVAKfapledwdeaMFDRSFN-----------TNVKGPYFLIQALLPLL---ANPAsiVLN-GSIN 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  148 GRESYVGGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETE-FSVVRFHGDKQKADNV-YKNSEPL----TPED 221
Cdd:PRK06500 140 AHIGMPNSSVYAASKAALLSLAKTLSGELLPRGIRVNAVSPGPVQTPlYGKLGLPEATLDAVAAqIQALVPLgrfgTPEE 219

                 ....*..
gi 19114010  222 IAEVILF 228
Cdd:PRK06500 220 IAKAVLY 226
PRK07063 PRK07063
SDR family oxidoreductase;
1-194 6.70e-20

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 85.87  E-value: 6.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKYE-VSVLPLKLDVSDLKSIPGVIESL 79
Cdd:PRK07063   2 MNRLAGKVALVTGAAQGIGAAIARAFAR-EGAAVALADLDAALAERAAAAIARDVAgARVLAVPADVTDAASVAAAVAAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   80 PKEFADIDVLINNAGLALGTDKvIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYC 159
Cdd:PRK07063  81 EEAFGPLDVLVNNAGINVFADP-LAMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASTHAFKIIPGCFPYP 159
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 19114010  160 STKSALAQFTSALRKETIDTRIRIMEVDPGLVETE 194
Cdd:PRK07063 160 VAKHGLLGLTRALGIEYAARNVRVNAIAPGYIETQ 194
PRK09730 PRK09730
SDR family oxidoreductase;
7-237 9.98e-20

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 85.29  E-value: 9.98e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    7 KTILITGASSGIGKSTAFEIAKVAKVKLILAARRFSTVEEIAKELESkYEVSVLPLKLDVSDLKSIPGVIESLPKEFADI 86
Cdd:PRK09730   2 AIALVTGGSRGIGRATALLLAQEGYTVAVNYQQNLHAAQEVVNLITQ-AGGKAFVLQADISDENQVVAMFTAIDQHDEPL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   87 DVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGD---ILNVGSIAGRESYVGGSV-YCSTK 162
Cdd:PRK09730  81 AALVNNAGILFTQCTVENLTAERINRVLSTNVTGYFLCCREAVKRMALKHGGSggaIVNVSSAASRLGAPGEYVdYAASK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  163 SALAQFTSALRKETIDTRIRIMEVDPGLVETEfsvvrFH---GDKQKADNVyKNSEPL----TPEDIAEVILFALTRREN 235
Cdd:PRK09730 161 GAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTE-----MHasgGEPGRVDRV-KSNIPMqrggQPEEVAQAIVWLLSDKAS 234

                 ..
gi 19114010  236 VV 237
Cdd:PRK09730 235 YV 236
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
4-250 1.04e-19

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 85.55  E-value: 1.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    4 LDGKTILITGASSGIGKSTAFEIAKvAKVKLILAAR-RFSTVEEIAKELESKYEVSVLpLKLDVSDLKSIPGVIESLPKE 82
Cdd:PRK08936   5 LEGKVVVITGGSTGLGRAMAVRFGK-EKAKVVINYRsDEEEANDVAEEIKKAGGEAIA-VKGDVTVESDVVNLIQTAVKE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   83 FADIDVLINNAGLALGTDKViDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKN-KGDILNVGSIAGRESYVGGSVYCST 161
Cdd:PRK08936  83 FGTLDVMINNAGIENAVPSH-EMSLEDWNKVINTNLTGAFLGSREAIKYFVEHDiKGNIINMSSVHEQIPWPLFVHYAAS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  162 KSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGDKQKADNVykNSEPL----TPEDIAEVILFALTRRENVV 237
Cdd:PRK08936 162 KGGVKLMTETLAMEYAPKGIRVNNIGPGAINTPINAEKFADPKQRADVE--SMIPMgyigKPEEIAAVAAWLASSEASYV 239
                        250       260
                 ....*....|....*....|
gi 19114010  238 IADTL-------VFPSHQGG 250
Cdd:PRK08936 240 TGITLfadggmtLYPSFQAG 259
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
5-242 1.54e-19

Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR with a characteristic NAD-binding pattern and active site tetrad. Aromatic polyketides include various aromatic compounds of pharmaceutical interest. Polyketide KR, part of the type II polyketide synthase (PKS) complex, is comprised of stand-alone domains that resemble the domains found in fatty acid synthase and multidomain type I PKS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187649 [Multi-domain]  Cd Length: 258  Bit Score: 84.90  E-value: 1.54e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   5 DGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKEL-ESKYEVSVLPLklDVSDLKSIPGVIESLPKEF 83
Cdd:cd08945   2 DSEVALVTGATSGIGLAIARRLGK-EGLRVFVCARGEEGLATTVKELrEAGVEADGRTC--DVRSVPEIEALVAAAVARY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  84 ADIDVLINNAGlALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPI--FYSKNKGDILNVGSIAGRESYVGGSVYCST 161
Cdd:cd08945  79 GPIDVLVNNAG-RSGGGATAELADELWLDVVETNLTGVFRVTKEVLKAggMLERGTGRIINIASTGGKQGVVHAAPYSAS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010 162 KSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSV-VRFH------GDKQKADNVYKNSEPL----TPEDIAEVILFAL 230
Cdd:cd08945 158 KHGVVGFTKALGLELARTGITVNAVCPGFVETPMAAsVREHyadiweVSTEEAFDRITARVPLgryvTPEEVAGMVAYLI 237
                       250
                ....*....|..
gi 19114010 231 TRRENVVIADTL 242
Cdd:cd08945 238 GDGAAAVTAQAL 249
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
1-194 1.67e-19

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 84.67  E-value: 1.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFEIAKVAKVKLILAARRFSTVEEIAKELESKYEvSVLPLKLDVSDLKSIPGVIESLP 80
Cdd:PRK12935   1 MVQLNGKVAIVTGGAKGIGKAITVALAQEGAKVVINYNSSKEAAENLVNELGKEGH-DVYAVQADVSKVEDANRLVEEAV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   81 KEFADIDVLINNAGLAlgTDKVID-LNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYC 159
Cdd:PRK12935  80 NHFGKVDILVNNAGIT--RDRTFKkLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFGQTNYS 157
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 19114010  160 STKSALAQFTSALRKETIDTRIRIMEVDPGLVETE 194
Cdd:PRK12935 158 AAKAGMLGFTKSLALELAKTNVTVNAICPGFIDTE 192
PRK05866 PRK05866
SDR family oxidoreductase;
3-233 3.18e-19

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 84.79  E-value: 3.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    3 RLDGKTILITGASSGIGKSTAFEIAKV-AKVklILAARRFSTVEEIAKE-LESKYEVSVLPlkLDVSDLKSIPGVIESLP 80
Cdd:PRK05866  37 DLTGKRILLTGASSGIGEAAAEQFARRgATV--VAVARREDLLDAVADRiTRAGGDAMAVP--CDLSDLDAVDALVADVE 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   81 KEFADIDVLINNAG------LALGTDKVIDLNiddaVTMiTTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIA-GRESYV 153
Cdd:PRK05866 113 KRIGGVDILINNAGrsirrpLAESLDRWHDVE----RTM-VLNYYAPLRLIRGLAPGMLERGDGHIINVATWGvLSEASP 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  154 GGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSvvrfhgdkqKADNVYKNSEPLTPEDIAEVILFALTRR 233
Cdd:PRK05866 188 LFSVYNASKAALSAVSRVIETEWGDRGVHSTTLYYPLVATPMI---------APTKAYDGLPALTADEAAEWMVTAARTR 258
PRK07774 PRK07774
SDR family oxidoreductase;
1-231 3.55e-19

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 83.64  E-value: 3.55e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLP 80
Cdd:PRK07774   1 MGRFDDKVAIVTGAAGGIGQAYAEALAR-EGASVVVADINAEGAERVAKQIVAD-GGTAIAVQVDVSDPDSAKAMADATV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   81 KEFADIDVLINNAGLALGT--DKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAgreSYVGGSVY 158
Cdd:PRK07774  79 SAFGGIDYLVNNAAIYGGMklDLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTA---AWLYSNFY 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19114010  159 CSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEfsVVRFHGDKQKADNVYKNSePL----TPEDIAEVILFALT 231
Cdd:PRK07774 156 GLAKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTE--ATRTVTPKEFVADMVKGI-PLsrmgTPEDLVGMCLFLLS 229
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
6-193 3.67e-19

17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as amyloid-peptide-binding alcohol dehydrogenase (ABAD), was previously identified as a L-3-hydroxyacyl-CoA dehydrogenase, HADH2. In fatty acid metabolism, HADH2 catalyzes the third step of beta-oxidation, the conversion of a hydroxyl to a keto group in the NAD-dependent oxidation of L-3-hydroxyacyl CoA. In addition to alcohol dehydrogenase and HADH2 activites, HSD10 has steroid dehydrogenase activity. Although the mechanism is unclear, HSD10 is implicated in the formation of amyloid beta-petide in the brain (which is linked to the development of Alzheimer's disease). Although HSD10 is normally concentrated in the mitochondria, in the presence of amyloid beta-peptide it translocates into the plasma membrane, where it's action may generate cytotoxic aldehydes and may lower estrogen levels through its use of 17-beta-estradiol as a substrate. HSD10 is a member of the SRD family, but differs from other SDRs by the presence of two insertions of unknown function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 83.88  E-value: 3.67e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   6 GKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKeLESKYEVSvlplKLDVSDLKSIPGVIESLPKEFAD 85
Cdd:cd05371   2 GLVAVVTGGASGLGLATVERLLA-QGAKVVILDLPNSPGETVAK-LGDNCRFV----PVDVTSEKDVKAALALAKAKFGR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  86 IDVLINNAGLALGTdKVIDLNIDDAVTM------ITTNVLGMMAMTRAVLPiFYSKN-------KGDILNVGSIAGRESY 152
Cdd:cd05371  76 LDIVVNCAGIAVAA-KTYNKKGQQPHSLelfqrvINVNLIGTFNVIRLAAG-AMGKNepdqggeRGVIINTASVAAFEGQ 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 19114010 153 VGGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVET 193
Cdd:cd05371 154 IGQAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDT 194
PRK05872 PRK05872
short chain dehydrogenase; Provisional
1-175 5.86e-19

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 83.87  E-value: 5.86e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFEIAkVAKVKLILAARRFSTVEEIAKELESkyEVSVLPLKLDVSDLKSIPGVIESLP 80
Cdd:PRK05872   4 MTSLAGKVVVVTGAARGIGAELARRLH-ARGAKLALVDLEEAELAALAAELGG--DDRVLTVVADVTDLAAMQAAAEEAV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   81 KEFADIDVLINNAGLALGtDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYsKNKGDILNVGSIAGRESYVGGSVYCS 160
Cdd:PRK05872  81 ERFGGIDVVVANAGIASG-GSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALI-ERRGYVLQVSSLAAFAAAPGMAAYCA 158
                        170
                 ....*....|....*
gi 19114010  161 TKSALAQFTSALRKE 175
Cdd:PRK05872 159 SKAGVEAFANALRLE 173
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
3-194 7.89e-19

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 82.86  E-value: 7.89e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    3 RLDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRfSTVEEIAKELESKYEvSVLPLKLDVSDLKSIPGVIESLPKE 82
Cdd:PRK06935  12 SLDGKVAIVTGGNTGLGQGYAVALAK-AGADIIITTHG-TNWDETRRLIEKEGR-KVTFVQVDLTKPESAEKVVKEALEE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   83 FADIDVLINNAGLaLGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAgreSYVGGSV---YC 159
Cdd:PRK06935  89 FGKIDILVNNAGT-IRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASML---SFQGGKFvpaYT 164
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 19114010  160 STKSALAQFTSALRKETIDTRIRIMEVDPGLVETE 194
Cdd:PRK06935 165 ASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKTA 199
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
2-228 7.94e-19

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) SDR; This subgroup includes the putative Brucella melitensis biovar Abortus 2308 BKR, FabG, Mesorhizobium loti MAFF303099 FabG, and other classical SDRs. BKR, a member of the SDR family, catalyzes the NADPH-dependent reduction of acyl carrier protein in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of 4 elongation steps, which are repeated to extend the fatty acid chain thru the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I Fas utilizes one or 2 multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187603 [Multi-domain]  Cd Length: 248  Bit Score: 82.82  E-value: 7.94e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   2 SRLDGKTILITGASSGIGKSTAFEIAKV-AKVklILAARRFSTVEEIAKELESkyevSVLPLKLDVSDLKSIPGVIESLP 80
Cdd:cd05345   1 MRLEGKVAIVTGAGSGFGEGIARRFAQEgARV--VIADINADGAERVAADIGE----AAIAIQADVTKRADVEAMVEAAL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  81 KEFADIDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCS 160
Cdd:cd05345  75 SKFGRLDILVNNAGITHRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGLRPRPGLTWYNA 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19114010 161 TKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFsVVRFHG-DKQKADNVYKNSEPL----TPEDIAEVILF 228
Cdd:cd05345 155 SKGWVVTATKAMAVELAPRNIRVNCLCPVAGETPL-LSMFMGeDTPENRAKFRATIPLgrlsTPDDIANAALY 226
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
7-255 8.66e-19

cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol reductases,including (6R)-2,2,6-trimethyl-1,4-cyclohexanedione (levodione) reductase of Corynebacterium aquaticum, catalyze the reversible oxidoreduction of hydroxycyclohexanone derivatives. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187591 [Multi-domain]  Cd Length: 257  Bit Score: 82.95  E-value: 8.66e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   7 KTILITGASSGIGKSTAFEIAKVAkVKLILAARRFSTVEEIAKEL-ESKYEVSVLPLKLDVSDLKSIPGVIESLPKEFAD 85
Cdd:cd05330   4 KVVLITGGGSGLGLATAVRLAKEG-AKLSLVDLNEEGLEAAKAALlEIAPDAEVLLIKADVSDEAQVEAYVDATVEQFGR 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  86 IDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSAL 165
Cdd:cd05330  83 IDGFFNNAGIEGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQSGYAAAKHGV 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010 166 AQFTSALRKETIDTRIRIMEVDPGLVET---EFSVVRFHG-DKQKADNVYKNSEPLT----PEDIAEVILFALTRRENVV 237
Cdd:cd05330 163 VGLTRNSAVEYGQYGIRINAIAPGAILTpmvEGSLKQLGPeNPEEAGEEFVSVNPMKrfgePEEVAAVVAFLLSDDAGYV 242
                       250
                ....*....|....*...
gi 19114010 238 IADTLVFpshQGGANHVY 255
Cdd:cd05330 243 NAAVVPI---DGGQSYKY 257
PRK06124 PRK06124
SDR family oxidoreductase;
4-194 8.86e-19

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 82.84  E-value: 8.86e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    4 LDGKTILITGASSGIGkstaFEIAKV---AKVKLILAARRFSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLP 80
Cdd:PRK06124   9 LAGQVALVTGSARGLG----FEIARAlagAGAHVLVNGRNAATLEAAVAALRAA-GGAAEALAFDIADEEAVAAAFARID 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   81 KEFADIDVLINNAGlALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCS 160
Cdd:PRK06124  84 AEHGRLDILVNNVG-ARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQVARAGDAVYPA 162
                        170       180       190
                 ....*....|....*....|....*....|....
gi 19114010  161 TKSALAQFTSALRKETIDTRIRIMEVDPGLVETE 194
Cdd:PRK06124 163 AKQGLTGLMRALAAEFGPHGITSNAIAPGYFATE 196
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
7-228 2.39e-18

putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) SDR; This subgroup includes Rhizobium sp. NGR234 FabG1. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187607 [Multi-domain]  Cd Length: 246  Bit Score: 81.35  E-value: 2.39e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   7 KTILITGASSGIGKSTAFEIAKVAKVKLILAARRFSTVEEIAKELESKyevsVLPLKLDVSDLKSIPGVIESLPKEFADI 86
Cdd:cd05349   1 QVVLVTGASRGLGAAIARSFAREGARVVVNYYRSTESAEAVAAEAGER----AIAIQADVRDRDQVQAMIEEAKNHFGPV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  87 DVLINNAGL-----ALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCST 161
Cdd:cd05349  77 DTIVNNALIdfpfdPDQRKTFDTIDWEDYQQQLEGAVKGALNLLQAVLPDFKERGSGRVINIGTNLFQNPVVPYHDYTTA 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19114010 162 KSALAQFTSALRKETIDTRIRIMEVDPGLVETEfsvvRFHGDKQKAD-NVYKNSEPL----TPEDIAEVILF 228
Cdd:cd05349 157 KAALLGFTRNMAKELGPYGITVNMVSGGLLKVT----DASAATPKEVfDAIAQTTPLgkvtTPQDIADAVLF 224
PRK06198 PRK06198
short chain dehydrogenase; Provisional
1-237 2.95e-18

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 81.59  E-value: 2.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFEIAKVAKVKLILAARRFSTVEEIAKELEsKYEVSVLPLKLDVSDLKSIPGVIESLP 80
Cdd:PRK06198   1 MGRLDGKVALVTGGTQGLGAAIARAFAERGAAGLVICGRNAEKGEAQAAELE-ALGAKAVFVQADLSDVEDCRRVVAAAD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   81 KEFADIDVLINNAGLalgTDK--VIDLNIDDAVTMITTNVLG-MMAMTRAVLPIFYSKNKGDILNVGSIA--GRESYVgg 155
Cdd:PRK06198  80 EAFGRLDALVNAAGL---TDRgtILDTSPELFDRHFAVNVRApFFLMQEAIKLMRRRKAEGTIVNIGSMSahGGQPFL-- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  156 SVYCSTKSALAQFTS----ALRKEtidtRIRIMEVDPGLVETEFSVV---RFHGDKQKADNVYKNSEP----LTPEDIAE 224
Cdd:PRK06198 155 AAYCASKGALATLTRnaayALLRN----RIRVNGLNIGWMATEGEDRiqrEFHGAPDDWLEKAAATQPfgrlLDPDEVAR 230
                        250
                 ....*....|...
gi 19114010  225 VILFALTRRENVV 237
Cdd:PRK06198 231 AVAFLLSDESGLM 243
PRK06484 PRK06484
short chain dehydrogenase; Validated
5-228 4.11e-18

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 83.36  E-value: 4.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    5 DGKTILITGASSGIGKSTAFEIAKVAKvKLILAARRFSTVEEIAKELESKYevsvLPLKLDVSDLKSIPGVIESLPKEFA 84
Cdd:PRK06484 268 SPRVVAITGGARGIGRAVADRFAAAGD-RLLIIDRDAEGAKKLAEALGDEH----LSVQADITDEAAVESAFAQIQARWG 342
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   85 DIDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKnkGDILNVGSIAGRESYVGGSVYCSTKSA 164
Cdd:PRK06484 343 RLDVLVNNAGIAEVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQG--GVIVNLGSIASLLALPPRNAYCASKAA 420
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19114010  165 LAQFTSALRKETIDTRIRIMEVDPGLVETEfSVVRFHGDKQKADNVYKNSEPL----TPEDIAEVILF 228
Cdd:PRK06484 421 VTMLSRSLACEWAPAGIRVNTVAPGYIETP-AVLALKASGRADFDSIRRRIPLgrlgDPEEVAEAIAF 487
PRK12827 PRK12827
short chain dehydrogenase; Provisional
1-228 4.39e-18

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 80.92  E-value: 4.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFEIAKVAKVKLIL---AARRFSTVEEIAKELESKYEvSVLPLKLDVSDLKSIPGVIE 77
Cdd:PRK12827   1 MASLDSRRVLITGGSGGLGRAIAVRLAADGADVIVLdihPMRGRAEADAVAAGIEAAGG-KALGLAFDVRDFAATRAALD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   78 SLPKEFADIDVLINNAGLAlgTDKVID-LNIDDAVTMITTNVLGMMAMTRAVL-PIFYSKNKGDILNVGSIAGRESYVGG 155
Cdd:PRK12827  80 AGVEEFGRLDILVNNAGIA--TDAAFAeLSIEEWDDVIDVNLDGFFNVTQAALpPMIRARRGGRIVNIASVAGVRGNRGQ 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19114010  156 SVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGDKqkadnvYKNSEPLT----PEDIAEVILF 228
Cdd:PRK12827 158 VNYAASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPMADNAAPTEH------LLNPVPVQrlgePDEVAALVAF 228
PRK07024 PRK07024
SDR family oxidoreductase;
9-193 5.29e-18

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 80.74  E-value: 5.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    9 ILITGASSGIGKSTAFEIAKVAKVkLILAARRFSTVEEIAKELESKYEVSVLPlkLDVSDLKSIPGVIESLPKEFADIDV 88
Cdd:PRK07024   5 VFITGASSGIGQALAREYARQGAT-LGLVARRTDALQAFAARLPKAARVSVYA--ADVRDADALAAAAADFIAAHGLPDV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   89 LINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMA--------MTRAvlpifyskNKGDILNVGSIAGRESYVGGSVYCS 160
Cdd:PRK07024  82 VIANAGISVGTLTEEREDLAVFREVMDTNYFGMVAtfqpfiapMRAA--------RRGTLVGIASVAGVRGLPGAGAYSA 153
                        170       180       190
                 ....*....|....*....|....*....|...
gi 19114010  161 TKSALAQFTSALRKETIDTRIRIMEVDPGLVET 193
Cdd:PRK07024 154 SKAAAIKYLESLRVELRPAGVRVVTIAPGYIRT 186
PRK07814 PRK07814
SDR family oxidoreductase;
3-228 5.96e-18

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 80.59  E-value: 5.96e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    3 RLDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKYEvSVLPLKLDVSDLKSIPGVIESLPKE 82
Cdd:PRK07814   7 RLDDQVAVVTGAGRGLGAAIALAFAE-AGADVLIAARTESQLDEVAEQIRAAGR-RAHVVAADLAHPEATAGLAGQAVEA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   83 FADIDVLINNAGlALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLP-IFYSKNKGDILNVGSIAGRESYVGGSVYCST 161
Cdd:PRK07814  85 FGRLDIVVNNVG-GTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPlMLEHSGGGSVINISSTMGRLAGRGFAAYGTA 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19114010  162 KSALAQFTSaLRKETIDTRIRIMEVDPGLVETEFSVVRFHGDKQKADNVYKNsePL----TPEDIAEVILF 228
Cdd:PRK07814 164 KAALAHYTR-LAALDLCPRIRVNAIAPGSILTSALEVVAANDELRAPMEKAT--PLrrlgDPEDIAAAAVY 231
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
10-243 8.83e-18

1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup contains classical SDR proteins, including members identified as 1-cyclohexenylcarbonyl coenzyme A reductase. ChcA of Streptomyces collinus is implicated in the final reduction step of shikimic acid to ansatrienin. ChcA shows sequence similarity to the SDR family of NAD-binding proteins, but it lacks the conserved Tyr of the characteristic catalytic site. This subgroup also contains the NADH-dependent enoyl-[acyl-carrier-protein(ACP)] reductase FabL from Bacillus subtilis. This enzyme participates in bacterial fatty acid synthesis, in type II fatty-acid synthases and catalyzes the last step in each elongation cycle. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187617 [Multi-domain]  Cd Length: 242  Bit Score: 79.70  E-value: 8.83e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  10 LITGASSGIGKSTAFEIA----KVAKVKLILAARRFSTVEEIAKEleskyEVSVLPLKLDVSDLKSIPGVIESLPKEFAD 85
Cdd:cd05359   2 LVTGGSRGIGKAIALRLAergaDVVINYRKSKDAAAEVAAEIEEL-----GGKAVVVRADVSQPQDVEEMFAAVKERFGR 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  86 IDVLINNAGLALGTDkVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSAL 165
Cdd:cd05359  77 LDVLVSNAAAGAFRP-LSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALPNYLAVGTAKAAL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010 166 AQFTSALRKETIDTRIRIMEVDPGLVETEfSVVRFHGDKQKADNVYKNS---EPLTPEDIAEVILFALTRRENVVIADTL 242
Cdd:cd05359 156 EALVRYLAVELGPRGIRVNAVSPGVIDTD-ALAHFPNREDLLEAAAANTpagRVGTPQDVADAVGFLCSDAARMITGQTL 234

                .
gi 19114010 243 V 243
Cdd:cd05359 235 V 235
PLN02780 PLN02780
ketoreductase/ oxidoreductase
6-199 9.07e-18

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 81.07  E-value: 9.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    6 GKTILITGASSGIGKSTAFEIAKVAkVKLILAARRFSTVEEIAKELESKY-EVSVLPLKLDVSD-----LKSIPGVIESL 79
Cdd:PLN02780  53 GSWALVTGPTDGIGKGFAFQLARKG-LNLVLVARNPDKLKDVSDSIQSKYsKTQIKTVVVDFSGdidegVKRIKETIEGL 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   80 pkefaDIDVLINNAGLALGTDKVIDlNIDDAV--TMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGR--ESYVGG 155
Cdd:PLN02780 132 -----DVGVLINNVGVSYPYARFFH-EVDEELlkNLIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAIviPSDPLY 205
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 19114010  156 SVYCSTKSALAQFTSAL----RKETIDTRIRImevdPGLVETEFSVVR 199
Cdd:PLN02780 206 AVYAATKAYIDQFSRCLyveyKKSGIDVQCQV----PLYVATKMASIR 249
PRK07775 PRK07775
SDR family oxidoreductase;
5-193 9.90e-18

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 80.18  E-value: 9.90e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    5 DGKTILITGASSGIGKSTAFEIAK----VAkvkliLAARRFSTVEEIAKELESKYEVSVlPLKLDVSDLKSIPGVIESLP 80
Cdd:PRK07775   9 DRRPALVAGASSGIGAATAIELAAagfpVA-----LGARRVEKCEELVDKIRADGGEAV-AFPLDVTDPDSVKSFVAQAE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   81 KEFADIDVLINNAG-LALGtdKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYC 159
Cdd:PRK07775  83 EALGEIEVLVSGAGdTYFG--KLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALRQRPHMGAYG 160
                        170       180       190
                 ....*....|....*....|....*....|....
gi 19114010  160 STKSALAQFTSALRKETIDTRIRIMEVDPGLVET 193
Cdd:PRK07775 161 AAKAGLEAMVTNLQMELEGTGVRASIVHPGPTLT 194
PRK12743 PRK12743
SDR family oxidoreductase;
7-228 1.24e-17

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 79.69  E-value: 1.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    7 KTILITGASSGIGKSTAFEIAKVAKVKLILAARRFSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLPKEFADI 86
Cdd:PRK12743   3 QVAIVTASDSGIGKACALLLAQQGFDIGITWHSDEEGAKETAEEVRSH-GVRAEIRQLDLSDLPEGAQALDKLIQRLGRI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   87 DVLINNAGlALGTDKVIDLNIDDAVTMITTNVLG-MMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSAL 165
Cdd:PRK12743  82 DVLVNNAG-AMTKAPFLDMDFDEWRKIFTVDVDGaFLCSQIAARHMVKQGQGGRIINITSVHEHTPLPGASAYTAAKHAL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  166 AQFTSALRKETIDTRIRIMEVDPGLVETEFSvvrfhgdKQKADNVYKNSEPLTP-------EDIAEVILF 228
Cdd:PRK12743 161 GGLTKAMALELVEHGILVNAVAPGAIATPMN-------GMDDSDVKPDSRPGIPlgrpgdtHEIASLVAW 223
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
4-194 1.40e-17

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human DHRS1 and human HSDL2 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187597 [Multi-domain]  Cd Length: 246  Bit Score: 79.36  E-value: 1.40e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   4 LDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFS------------TVEEIAKELESKyEVSVLPLKLDVSDLKS 71
Cdd:cd05338   1 LSGKVAFVTGASRGIGRAIALRLAK-AGATVVVAAKTASegdngsakslpgTIEETAEEIEAA-GGQALPIVVDVRDEDQ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  72 IPGVIESLPKEFADIDVLINNAGlALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRES 151
Cdd:cd05338  79 VRALVEATVDQFGRLDILVNNAG-AIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLSLRP 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 19114010 152 YVGGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETE 194
Cdd:cd05338 158 ARGDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPSTAIET 200
PRK12937 PRK12937
short chain dehydrogenase; Provisional
4-228 1.68e-17

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 79.02  E-value: 1.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    4 LDGKTILITGASSGIGKSTAFEIAKVAKVKLILAARRFSTVEEIAKELESKYEvSVLPLKLDVSDLKSIPGVIESLPKEF 83
Cdd:PRK12937   3 LSNKVAIVTGASRGIGAAIARRLAADGFAVAVNYAGSAAAADELVAEIEAAGG-RAIAVQADVADAAAVTRLFDAAETAF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   84 ADIDVLINNAGLaLGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPifYSKNKGDILNVGSIAGRESYVGGSVYCSTKS 163
Cdd:PRK12937  82 GRIDVLVNNAGV-MPLGTIADFDLEDFDRTIATNLRGAFVVLREAAR--HLGQGGRIINLSTSVIALPLPGYGPYAASKA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  164 ALAQFTSALRKETIDTRIRIMEVDPGLVETEfsvVRFHG-DKQKADNVYKNSePL----TPEDIAEVILF 228
Cdd:PRK12937 159 AVEGLVHVLANELRGRGITVNAVAPGPVATE---LFFNGkSAEQIDQLAGLA-PLerlgTPEEIAAAVAF 224
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
3-194 5.14e-17

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 77.96  E-value: 5.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    3 RLDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKYEVSVlPLKLDVSDLKSIPGVIESLPKE 82
Cdd:PRK06113   8 RLDGKCAIITGAGAGIGKEIAITFAT-AGASVVVSDINADAANHVVDEIQQLGGQAF-ACRCDITSEQELSALADFALSK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   83 FADIDVLINNAGLalGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTK 162
Cdd:PRK06113  86 LGKVDILVNNAGG--GGPKPFDMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYASSK 163
                        170       180       190
                 ....*....|....*....|....*....|..
gi 19114010  163 SALAQFTSALRKETIDTRIRIMEVDPGLVETE 194
Cdd:PRK06113 164 AAASHLVRNMAFDLGEKNIRVNGIAPGAILTD 195
PRK07035 PRK07035
SDR family oxidoreductase;
4-196 7.58e-17

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 77.36  E-value: 7.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    4 LDGKTILITGASSGIGKSTAFEIAKV-AKVklILAARRFSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLPKE 82
Cdd:PRK07035   6 LTGKIALVTGASRGIGEAIAKLLAQQgAHV--IVSSRKLDGCQAVADAIVAA-GGKAEALACHIGEMEQIDALFAHIRER 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   83 FADIDVLINNA------GLALGTD-----KVIDLNIDdavtmittnvlGMMAMTRAVLPIFYSKNKGDILNVGSIAGRES 151
Cdd:PRK07035  83 HGRLDILVNNAaanpyfGHILDTDlgafqKTVDVNIR-----------GYFFMSVEAGKLMKEQGGGSIVNVASVNGVSP 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 19114010  152 YVGGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFS 196
Cdd:PRK07035 152 GDFQGIYSITKAAVISMTKAFAKECAPFGIRVNALLPGLTDTKFA 196
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
3-194 8.24e-17

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 77.31  E-value: 8.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    3 RLDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLPKE 82
Cdd:PRK08217   2 DLKDKVIVITGGAQGLGRAMAEYLAQ-KGAKLALIDLNQEKLEEAVAECGAL-GTEVRGYAANVTDEEDVEATFAQIAED 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   83 FADIDVLINNAGLALgtD----KVIDLNIDDAVTM------ITTNVLGMMAMTR-AVLPIFYSKNKGDILNVGSIAgRES 151
Cdd:PRK08217  80 FGQLNGLINNAGILR--DgllvKAKDGKVTSKMSLeqfqsvIDVNLTGVFLCGReAAAKMIESGSKGVIINISSIA-RAG 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 19114010  152 YVGGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETE 194
Cdd:PRK08217 157 NMGQTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETE 199
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
7-226 8.82e-17

classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187636 [Multi-domain]  Cd Length: 227  Bit Score: 76.72  E-value: 8.82e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   7 KTILITGASSGIGKSTAFEIAKVA-KVKLIlaARRFSTVEEIAKELESKyevSVLPLKLDVSDLKSIPGVIESL-PKEFA 84
Cdd:cd08931   1 KAIFITGAASGIGRETALLFARNGwFVGLY--DIDEDGLAALAAELGAE---NVVAGALDVTDRAAWAAALADFaAATGG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  85 DIDVLINNAGLALGtDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSA 164
Cdd:cd08931  76 RLDALFNNAGVGRG-GPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAIYGQPDLAVYSATKFA 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19114010 165 LAQFTSALRKETIDTRIRIMEVDPGLVETEFsvvrFHGDKQKADNVYKNSEPLTPEDIAEVI 226
Cdd:cd08931 155 VRGLTEALDVEWARHGIRVADVWPWFVDTPI----LTKGETGAAPKKGLGRVLPVSDVAKVV 212
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
7-194 1.14e-16

human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical-SDR subgroup includes the human proteins: type 2 17beta-HSD, type 6 17beta-HSD, type 2 11beta-HSD, dehydrogenase/reductase SDR family member 9, short-chain dehydrogenase/reductase family 9C member 7, 3-hydroxybutyrate dehydrogenase type 1, and retinol dehydrogenase 5. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187665 [Multi-domain]  Cd Length: 281  Bit Score: 77.32  E-value: 1.14e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   7 KTILITGASSGIGKSTAfeiAKVAKVKLILAARRFSTVEEIAKELESKYEVSVLPLKLDVSDLKSIPGVIESLPKEFADI 86
Cdd:cd09805   1 KAVLITGCDSGFGNLLA---KKLDSLGFTVLAGCLTKNGPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  87 DV--LINNAG-LALGTDKVIdLNIDDAVTMITTNVLGMMAMTRAVLPiFYSKNKGDILNVGSIAGRESYVGGSVYCSTKS 163
Cdd:cd09805  78 GLwgLVNNAGiLGFGGDEEL-LPMDDYRKCMEVNLFGTVEVTKAFLP-LLRRAKGRVVNVSSMGGRVPFPAGGAYCASKA 155
                       170       180       190
                ....*....|....*....|....*....|.
gi 19114010 164 ALAQFTSALRKETIDTRIRIMEVDPGLVETE 194
Cdd:cd09805 156 AVEAFSDSLRRELQPWGVKVSIIEPGNFKTG 186
PRK07831 PRK07831
SDR family oxidoreductase;
4-190 1.24e-16

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 77.00  E-value: 1.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    4 LDGKTILITGAS-SGIGKSTA----FEIAKVakvkLI--LAARRFS-TVEEIAKELESKyevSVLPLKLDVSDLKSIPGV 75
Cdd:PRK07831  15 LAGKVVLVTAAAgTGIGSATArralEEGARV----VIsdIHERRLGeTADELAAELGLG---RVEAVVCDVTSEAQVDAL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   76 IESLPKEFADIDVLINNAGLAlGTDKVIDLNID--DAVTMITTNvlGMMAMTRAVLPIFYS-KNKGDILNVGSIAGRESY 152
Cdd:PRK07831  88 IDAAVERLGRLDVLVNNAGLG-GQTPVVDMTDDewSRVLDVTLT--GTFRATRAALRYMRArGHGGVIVNNASVLGWRAQ 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 19114010  153 VGGSVYCSTKSALAQFT--SALrkETIDTRIRIMEVDPGL 190
Cdd:PRK07831 165 HGQAHYAAAKAGVMALTrcSAL--EAAEYGVRINAVAPSI 202
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
4-228 1.35e-16

Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related proteins have a canonical classical SDR nucleotide-binding motif and active site tetrad. They are predicted oxoacyl-(acyl carrier protein/ACP) reductases. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 76.46  E-value: 1.35e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   4 LDGKTILITGASSGIGKSTAFEIAKVAkVKLILAARRFSTVEEIAKELESKYEVS--VLPLKLDVSDLKSIPGVIESLPK 81
Cdd:cd05340   2 LNDRIILVTGASDGIGREAALTYARYG-ATVILLGRNEEKLRQVADHINEEGGRQpqWFILDLLTCTSENCQQLAQRIAV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  82 EFADIDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCST 161
Cdd:cd05340  81 NYPRLDGVLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAVS 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010 162 KSALAQFTSALRKETIDTRIRIMEVDPGLVETefsvvrfhGDKQKAdnvYKNSEPL---TPEDIAEVILF 228
Cdd:cd05340 161 KFATEGL*QVLADEYQQRNLRVNCINPGGTRT--------AMRASA---FPTEDPQklkTPADIMPLYLW 219
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
7-157 1.36e-16

light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical SDR-like subgroup containing LPOR and related proteins. Protochlorophyllide (Pchlide) reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 77.56  E-value: 1.36e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   7 KTILITGASSGIGKSTAFEIAKVAKVKLILAARRFSTVEEIAKEL---ESKYEVsvlpLKLDVSDLKSIPGVIESLPKEF 83
Cdd:cd09810   2 GTVVITGASSGLGLAAAKALARRGEWHVVMACRDFLKAEQAAQEVgmpKDSYSV----LHCDLASLDSVRQFVDNFRRTG 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19114010  84 ADIDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGD--ILNVGSIAGRESYVGGSV 157
Cdd:cd09810  78 RPLDALVCNAAVYLPTAKEPRFTADGFELTVGVNHLGHFLLTNLLLEDLQRSENASprIVIVGSITHNPNTLAGNV 153
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
8-227 1.62e-16

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) SDR; This subgroup includes Escherichia coli CFT073 FabG. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187596 [Multi-domain]  Cd Length: 255  Bit Score: 76.73  E-value: 1.62e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   8 TILITGASSGIGKSTAFEIAKVAKVKLILAARRFSTVEEIAKELEsKYEVSVLPLKLDVSDLKSIPGVIESLPKEFADID 87
Cdd:cd05337   3 VAIVTGASRGIGRAIATELAARGFDIAINDLPDDDQATEVVAEVL-AAGRRAIYFQADIGELSDHEALLDQAWEDFGRLD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  88 VLINNAGLA-LGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVL------PIFYSKNKGDILNVGSIAGRESYVGGSVYCS 160
Cdd:cd05337  82 CLVNNAGIAvRPRGDLLDLTEDSFDRLIAINLRGPFFLTQAVArrmveqPDRFDGPHRSIIFVTSINAYLVSPNRGEYCI 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19114010 161 TKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSV-VRFHGDKQKADNVYKNSEPLTPEDIAEVIL 227
Cdd:cd05337 162 SKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTApVKEKYDELIAAGLVPIRRWGQPEDIAKAVR 229
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
7-231 1.68e-16

pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR family, catalyzes the NAD-dependent reduction of folic acid, dihydrofolate and related compounds. In Leishmania, pteridine reductase (PTR1) acts to circumvent the anti-protozoan drugs that attack dihydrofolate reductase activity. Proteins in this subgroup have an N-terminal NAD-binding motif and a YxxxK active site motif, but have an Asp instead of the usual upstream catalytic Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187615 [Multi-domain]  Cd Length: 234  Bit Score: 76.16  E-value: 1.68e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   7 KTILITGASSGIGKSTAFEIAKvAKVKLILAARRFST-VEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLPKEFAD 85
Cdd:cd05357   1 AVALVTGAAKRIGRAIAEALAA-EGYRVVVHYNRSEAeAQRLKDELNAL-RNSAVLVQADLSDFAACADLVAAAFRAFGR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  86 IDVLINNAGlALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSAL 165
Cdd:cd05357  79 CDVLVNNAS-AFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIIDAMTDRPLTGYFAYCMSKAAL 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010 166 AQFTSALRKEtIDTRIRIMEVDPGLveTEFSVvrfHGDKQKADNvYKNSEPL----TPEDIAEVILFALT 231
Cdd:cd05357 158 EGLTRSAALE-LAPNIRVNGIAPGL--ILLPE---DMDAEYREN-ALRKVPLkrrpSAEEIADAVIFLLD 220
PRK07856 PRK07856
SDR family oxidoreductase;
4-228 1.71e-16

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 76.51  E-value: 1.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    4 LDGKTILITGASSGIGK--STAFeIAKVAKVkLILAARRFSTVEEIAKELESkyevsvlplkLDVSDLKSIPGVIESLPK 81
Cdd:PRK07856   4 LTGRVVLVTGGTRGIGAgiARAF-LAAGATV-VVCGRRAPETVDGRPAEFHA----------ADVRDPDQVAALVDAIVE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   82 EFADIDVLINNAG-----LALG-----TDKVIDLniddavtmittNVLGMMAMTRAVLPIFYSKNK-GDILNVGSIAGRE 150
Cdd:PRK07856  72 RHGRLDVLVNNAGgspyaLAAEasprfHEKIVEL-----------NLLAPLLVAQAANAVMQQQPGgGSIVNIGSVSGRR 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  151 SYVGGSVYCSTKSALAQFTSALRKETIdTRIRIMEVDPGLVETEFSvVRFHGDKQKADNVYKNSePL----TPEDIAEVI 226
Cdd:PRK07856 141 PSPGTAAYGAAKAGLLNLTRSLAVEWA-PKVRVNAVVVGLVRTEQS-ELHYGDAEGIAAVAATV-PLgrlaTPADIAWAC 217

                 ..
gi 19114010  227 LF 228
Cdd:PRK07856 218 LF 219
PRK08265 PRK08265
short chain dehydrogenase; Provisional
1-231 2.21e-16

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 76.20  E-value: 2.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESkyevSVLPLKLDVSDLKSIPGVIESLP 80
Cdd:PRK08265   1 MIGLAGKVAIVTGGATLIGAAVARALVA-AGARVAIVDIDADNGAAVAASLGE----RARFIATDITDDAAIERAVATVV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   81 KEFADIDVLINNAGLALgtDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSkNKGDILNVGSIAGRESYVGGSVYCS 160
Cdd:PRK08265  76 ARFGRVDILVNLACTYL--DDGLASSRADWLAALDVNLVSAAMLAQAAHPHLAR-GGGAIVNFTSISAKFAQTGRWLYPA 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19114010  161 TKSALAQFTSALRKETIDTRIRIMEVDPGL----VETEFSvvrfHGDKQKADNVYKNSEPL----TPEDIAEVILFALT 231
Cdd:PRK08265 153 SKAAIRQLTRSMAMDLAPDGIRVNSVSPGWtwsrVMDELS----GGDRAKADRVAAPFHLLgrvgDPEEVAQVVAFLCS 227
PRK06123 PRK06123
SDR family oxidoreductase;
7-231 2.48e-16

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 75.97  E-value: 2.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    7 KTILITGASSGIGKSTAFEIAKVAKVKLILAARRFSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLPKEFADI 86
Cdd:PRK06123   3 KVMIITGASRGIGAATALLAAERGYAVCLNYLRNRDAAEAVVQAIRRQ-GGEALAVAADVADEADVLRLFEAVDRELGRL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   87 DVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTR-AV--LPIFYSKNKGDILNVGSIAGRESYVGGSV-YCSTK 162
Cdd:PRK06123  82 DALVNNAGILEAQMRLEQMDAARLTRIFATNVVGSFLCAReAVkrMSTRHGGRGGAIVNVSSMAARLGSPGEYIdYAASK 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19114010  163 SALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVrfHGDKQKADNVyKNSEPL----TPEDIAEVILFALT 231
Cdd:PRK06123 162 GAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEIHAS--GGEPGRVDRV-KAGIPMgrggTAEEVARAILWLLS 231
PRK07074 PRK07074
SDR family oxidoreductase;
7-228 3.41e-16

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 75.58  E-value: 3.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    7 KTILITGASSGIGKSTAFEIAKVAKVKLiLAARRFSTVEEIAKELEskyEVSVLPLKLDVSDLKSIPGVIESLPKEFADI 86
Cdd:PRK07074   3 RTALVTGAAGGIGQALARRFLAAGDRVL-ALDIDAAALAAFADALG---DARFVPVACDLTDAASLAAALANAAAERGPV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   87 DVLINNAGLALGTdkviDLNIDDAVTMITTNVLGMMAM---TRAVLPIFYSKNKGDILNVGSIAGRESYvGGSVYCSTKS 163
Cdd:PRK07074  79 DVLVANAGAARAA----SLHDTTPASWRADNALNLEAAylcVEAVLEGMLKRSRGAVVNIGSVNGMAAL-GHPAYSAAKA 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19114010  164 ALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRfhgdKQKADNVYKNSE---PL----TPEDIAEVILF 228
Cdd:PRK07074 154 GLIHYTKLLAVEYGRFGIRANAVAPGTVKTQAWEAR----VAANPQVFEELKkwyPLqdfaTPDDVANAVLF 221
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
4-194 4.16e-16

putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes the NAD-dependent interconversion of D-mannonate and D-fructuronate. This subgroup includes Bacillus subtitils UxuB/YjmF, a putative D-mannonate oxidoreductase; the B. subtilis UxuB gene is part of a putative ten-gene operon (the Yjm operon) involved in hexuronate catabolism. Escherichia coli UxuB does not belong to this subgroup. This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187640 [Multi-domain]  Cd Length: 271  Bit Score: 75.57  E-value: 4.16e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   4 LDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKYEvSVLPLKLDVSDLKSIPGVIESLPKEF 83
Cdd:cd08935   3 LKNKVAVITGGTGVLGGAMARALAQ-AGAKVAALGRNQEKGDKVAKEITALGG-RAIALAADVLDRASLERAREEIVAQF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  84 ADIDVLINNAG------------LALGTDK-VIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRE 150
Cdd:cd08935  81 GTVDILINGAGgnhpdattdpehYEPETEQnFFDLDEEGWEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINISSMNAFS 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 19114010 151 SYVGGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETE 194
Cdd:cd08935 161 PLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTP 204
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
6-228 4.92e-16

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 75.15  E-value: 4.92e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    6 GKTILITGASSGIGKSTAFEIAKVAkVKLILAARRFSTVEEIAKELeSKYEVSVLPLKLDVSDLKSIPGVIESLPKEFAD 85
Cdd:PRK08643   2 SKVALVTGAGQGIGFAIAKRLVEDG-FKVAIVDYNEETAQAAADKL-SKDGGKAIAVKADVSDRDQVFAAVRQVVDTFGD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   86 IDVLINNAGLALGTD-KVIDLNIDDAVTMIttNVLGMMAMTRAVLPIFYSKNK-GDILNVGSIAGRESYVGGSVYCSTKS 163
Cdd:PRK08643  80 LNVVVNNAGVAPTTPiETITEEQFDKVYNI--NVGGVIWGIQAAQEAFKKLGHgGKIINATSQAGVVGNPELAVYSSTKF 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19114010  164 ALAQFTSALRKETIDTRIRIMEVDPGLVETEfsvVRFHGDKQKADNVYKNSEPLT--------------PEDIAEVILF 228
Cdd:PRK08643 158 AVRGLTQTAARDLASEGITVNAYAPGIVKTP---MMFDIAHQVGENAGKPDEWGMeqfakditlgrlsePEDVANCVSF 233
PRK09135 PRK09135
pteridine reductase; Provisional
1-230 6.77e-16

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 74.58  E-value: 6.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKstafEIAKV---AKVKLILAARRFST-VEEIAKELESKYEVSVLPLKLDVSDLKSIPGVI 76
Cdd:PRK09135   1 MMTDSAKVALITGGARRIGA----AIARTlhaAGYRVAIHYHRSAAeADALAAELNALRPGSAAALQADLLDPDALPELV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   77 ESLPKEFADIDVLINNAGLALGTDkVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFySKNKGDILNVGSIAGRESYVGGS 156
Cdd:PRK09135  77 AACVAAFGRLDALVNNASSFYPTP-LGSITEAQWDDLFASNLKAPFFLSQAAAPQL-RKQRGAIVNITDIHAERPLKGYP 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  157 VYCSTKSALAQFTSALRKEtIDTRIRIMEVDPGlvetefsVVRFHGDKQKADNVYK----NSEPL----TPEDIAEVILF 228
Cdd:PRK09135 155 VYCAAKAALEMLTRSLALE-LAPEVRVNAVAPG-------AILWPEDGNSFDEEARqailARTPLkrigTPEDIAEAVRF 226

                 ..
gi 19114010  229 AL 230
Cdd:PRK09135 227 LL 228
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
3-243 7.28e-16

enoyl-[acyl-carrier-protein] reductase FabL;


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 74.76  E-value: 7.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    3 RLDGKTILITGASSGIGKSTAFEIAKVAKVKLILAARRFSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLPKE 82
Cdd:PRK08063   1 VFSGKVALVTGSSRGIGKAIALRLAEEGYDIAVNYARSRKAAEETAEEIEAL-GRKALAVKANVGDVEKIKEMFAQIDEE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   83 FADIDVLINNAglALGTDK-VIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNV---GSIAGRESY--VGGS 156
Cdd:PRK08063  80 FGRLDVFVNNA--ASGVLRpAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLsslGSIRYLENYttVGVS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  157 vycstKSALAQFTSALRKETIDTRIRIMEVDPGLVETEfSVVRFHGDKQKADNVYKNS---EPLTPEDIAEVILFALTRR 233
Cdd:PRK08063 158 -----KAALEALTRYLAVELAPKGIAVNAVSGGAVDTD-ALKHFPNREELLEDARAKTpagRMVEPEDVANAVLFLCSPE 231
                        250
                 ....*....|
gi 19114010  234 ENVVIADTLV 243
Cdd:PRK08063 232 ADMIRGQTII 241
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
7-227 7.41e-16

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 74.72  E-value: 7.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    7 KTILITGASSGIGKSTAFEIAKvAKVKLILAARRfsTVEEIAKELESKYEvSVLPLKLDVSDLKSIPG----VIESLPKE 82
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLE-KGTHVISISRT--ENKELTKLAEQYNS-NLTFHSLDLQDVHELETnfneILSSIQED 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   83 FADIDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKN-KGDILNVGSIAGRESYVGGSVYCST 161
Cdd:PRK06924  78 NVSSIHLINNAGMVAPIKPIEKAESEELITNVHLNLLAPMILTSTFMKHTKDWKvDKRVINISSGAAKNPYFGWSAYCSS 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19114010  162 KSALAQFTS--ALRKETIDTRIRIMEVDPGLVETEF-SVVR------FHgDKQKADNVYKNSEPLTPEDIAEVIL 227
Cdd:PRK06924 158 KAGLDMFTQtvATEQEEEEYPVKIVAFSPGVMDTNMqAQIRssskedFT-NLDRFITLKEEGKLLSPEYVAKALR 231
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
1-206 1.46e-15

3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 73.80  E-value: 1.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFEIAKVAKVkLILAARRFSTVEEIAKELESKyeVSVLPLKLdvSDLKSIPGVIESLP 80
Cdd:PRK12936   1 MFDLSGRKALVTGASGGIGEEIARLLHAQGAI-VGLHGTRVEKLEALAAELGER--VKIFPANL--SDRDEVKALGQKAE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   81 KEFADIDVLINNAGLAlgTDKV-IDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYC 159
Cdd:PRK12936  76 ADLEGVDILVNNAGIT--KDGLfVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVGVTGNPGQANYC 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 19114010  160 STKSALAQFTSALRKETIDTRIRIMEVDPGLVETefSVVRFHGDKQK 206
Cdd:PRK12936 154 ASKAGMIGFSKSLAQEIATRNVTVNCVAPGFIES--AMTGKLNDKQK 198
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
10-228 1.51e-15

7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial subgroup contains 7 alpha-HSDHs, including Escherichia coli 7 alpha-HSDH. 7 alpha-HSDH, a member of the SDR family, catalyzes the NAD+ -dependent dehydrogenation of a hydroxyl group at position 7 of the steroid skeleton of bile acids. In humans the two primary bile acids are cholic and chenodeoxycholic acids, these are formed from cholesterol in the liver. Escherichia coli 7 alpha-HSDH dehydroxylates these bile acids in the human intestine. Mammalian 7 alpha-HSDH activity has been found in livers. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187623 [Multi-domain]  Cd Length: 242  Bit Score: 73.76  E-value: 1.51e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  10 LITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKYEvSVLPLKLDVSDLKSIPGVIESLPKEFADIDVL 89
Cdd:cd05365   3 IVTGGAAGIGKAIAGTLAK-AGASVVIADLKSEGAEAVAAAIQQAGG-QAIGLECNVTSEQDLEAVVKATVSQFGGITIL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  90 INNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSALAQFT 169
Cdd:cd05365  81 VNNAGGGGPKPFDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRIAAYGSSKAAVNHMT 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19114010 170 SALRKETIDTRIRIMEVDPGLVETEF--SVVRFHGDKQK-ADNVYKNSEplTPEDIAEVILF 228
Cdd:cd05365 161 RNLAFDLGPKGIRVNAVAPGAVKTDAlaSVLTPEIERAMlKHTPLGRLG--EPEDIANAALF 220
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
7-194 1.76e-15

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 73.84  E-value: 1.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    7 KTILITGASSGIGKSTAFEIAKVAKVKLILAARRFSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLPKEFADI 86
Cdd:PRK12745   3 PVALVTGGRRGIGLGIARALAAAGFDLAINDRPDDEELAATQQELRAL-GVEVIFFPADVADLSAHEAMLDAAQAAWGRI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   87 DVLINNAGLA-LGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVL----------PIFYsknkGDILNVGSIAGRESYVGG 155
Cdd:PRK12745  82 DCLVNNAGVGvKVRGDLLDLTPESFDRVLAINLRGPFFLTQAVAkrmlaqpepeELPH----RSIVFVSSVNAIMVSPNR 157
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 19114010  156 SVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETE 194
Cdd:PRK12745 158 GEYCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTD 196
PRK09186 PRK09186
flagellin modification protein A; Provisional
4-230 1.89e-15

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 73.49  E-value: 1.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    4 LDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKYEVSVLPL-KLDVSDLKSIPGVIESLPKE 82
Cdd:PRK09186   2 LKGKTILITGAGGLIGSALVKAILE-AGGIVIAADIDKEALNELLESLGKEFKSKKLSLvELDITDQESLEEFLSKSAEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   83 FADIDVLINNA---GLALGTdKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGR-----ESYVG 154
Cdd:PRK09186  81 YGKIDGAVNCAyprNKDYGK-KFFDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGGGNLVNISSIYGVvapkfEIYEG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  155 GSV-----YCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVEtefsvvrfhgDKQKAD--NVYKNSEP----LTPEDIA 223
Cdd:PRK09186 160 TSMtspveYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPGGIL----------DNQPEAflNAYKKCCNgkgmLDPDDIC 229

                 ....*..
gi 19114010  224 EVILFAL 230
Cdd:PRK09186 230 GTLVFLL 236
PRK05855 PRK05855
SDR family oxidoreductase;
3-237 2.05e-15

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 75.40  E-value: 2.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    3 RLDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKYEVsVLPLKLDVSDLKSIPGVIESLPKE 82
Cdd:PRK05855 312 PFSGKLVVVTGAGSGIGRETALAFAR-EGAEVVASDIDEAAAERTAELIRAAGAV-AHAYRVDVSDADAMEAFAEWVRAE 389
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   83 FADIDVLINNAGLALGtDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNK-GDILNVGSIAGRESYVGGSVYCST 161
Cdd:PRK05855 390 HGVPDIVVNNAGIGMA-GGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVERGTgGHIVNVASAAAYAPSRSLPAYATS 468
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  162 KSALAQFTSALRKETIDTRIRIMEVDPGLVETEF-SVVRFHGDK--------QKADNVYKnSEPLTPEDIAEVILFALTR 232
Cdd:PRK05855 469 KAAVLMLSECLRAELAAAGIGVTAICPGFVDTNIvATTRFAGADaedearrrGRADKLYQ-RRGYGPEKVAKAIVDAVKR 547

                 ....*
gi 19114010  233 RENVV 237
Cdd:PRK05855 548 NKAVV 552
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
3-199 2.19e-15

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; DHB DH (aka 1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase) catalyzes the NAD-dependent conversion of 1,2-dihydroxycyclohexa-3,4-diene carboxylate to a catechol. This subgroup also contains Pseudomonas putida F1 CmtB, 2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase, the second enzyme in the pathway for catabolism of p-cumate catabolism. This subgroup shares the glycine-rich NAD-binding motif of the classical SDRs and shares the same catalytic triad; however, the upstream Asn implicated in cofactor binding or catalysis in other SDRs is generally substituted by a Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187642 [Multi-domain]  Cd Length: 256  Bit Score: 73.33  E-value: 2.19e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   3 RLDGKTILITGASSGIGKSTAFEIAkvAKVKLILAARRFSTVEEIAKELESKYEvSVLPLKLDVSDLKSIPGVIESLPKE 82
Cdd:cd08937   1 RFEGKVVVVTGAAQGIGRGVAERLA--GEGARVLLVDRSELVHEVLAEILAAGD-AAHVHTADLETYAGAQGVVRAAVER 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  83 FADIDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYvgGSVYCSTK 162
Cdd:cd08937  78 FGRVDVLINNVGGTIWAKPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSIATRGIY--RIPYSAAK 155
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 19114010 163 SALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVR 199
Cdd:cd08937 156 GGVNALTASLAFEHARDGIRVNAVAPGGTEAPPRKIP 192
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
3-175 2.28e-15

(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids in eukaryotes occurs by a four-reaction cycle, that may take place in mitochondria or in peroxisomes. (3R)-hydroxyacyl-CoA dehydrogenase is part of rat peroxisomal multifunctional MFE-2, it is a member of the NAD-dependent SDRs, but contains an additional small C-terminal domain that completes the active site pocket and participates in dimerization. The atypical, additional C-terminal extension allows for more extensive dimerization contact than other SDRs. MFE-2 catalyzes the second and third reactions of the peroxisomal beta oxidation cycle. Proteins in this subgroup have a typical catalytic triad, but have a His in place of the usual upstream Asn. This subgroup also contains members identified as 17-beta-hydroxysteroid dehydrogenases, including human peroxisomal 17-beta-hydroxysteroid dehydrogenase type 4 (17beta-HSD type 4, aka MFE-2, encoded by HSD17B4 gene) which is involved in fatty acid beta-oxidation and steroid metabolism. This subgroup also includes two SDR domains of the Neurospora crassa and Saccharomyces cerevisiae multifunctional beta-oxidation protein (MFP, aka Fox2). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187611 [Multi-domain]  Cd Length: 250  Bit Score: 73.13  E-value: 2.28e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   3 RLDGKTILITGASSGIGKSTAFEIAKV-AKV-------------KLILAArrFSTVEEIAKelesKYEVSVLplklDVSD 68
Cdd:cd05353   2 RFDGRVVLVTGAGGGLGRAYALAFAERgAKVvvndlggdrkgsgKSSSAA--DKVVDEIKA----AGGKAVA----NYDS 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  69 LKSIPGVIESLPKEFADIDVLINNAGLAlgTDKVIdLNIDDAV--TMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSI 146
Cdd:cd05353  72 VEDGEKIVKTAIDAFGRVDILVNNAGIL--RDRSF-AKMSEEDwdLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSA 148
                       170       180
                ....*....|....*....|....*....
gi 19114010 147 AGRESYVGGSVYCSTKSALAQFTSALRKE 175
Cdd:cd05353 149 AGLYGNFGQANYSAAKLGLLGLSNTLAIE 177
PRK12746 PRK12746
SDR family oxidoreductase;
1-228 2.80e-15

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 73.14  E-value: 2.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFEIAKVAKVKLILAARRFSTVEEIAKELESKYEVSVLpLKLDVSDLKSIPGVIESLP 80
Cdd:PRK12746   1 MKNLDGKVALVTGASRGIGRAIAMRLANDGALVAIHYGRNKQAADETIREIESNGGKAFL-IEADLNSIDGVKKLVEQLK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   81 KEF------ADIDVLINNAGlaLGTDKVIDLNIDDAV-TMITTNVLGMMAMTRAVLPIFysKNKGDILNVGSIAGRESYV 153
Cdd:PRK12746  80 NELqirvgtSEIDILVNNAG--IGTQGTIENTTEEIFdEIMAVNIKAPFFLIQQTLPLL--RAEGRVINISSAEVRLGFT 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19114010  154 GGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFhgDKQKADNVYKNSEPL----TPEDIAEVILF 228
Cdd:PRK12746 156 GSIAYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDINAKLL--DDPEIRNFATNSSVFgrigQVEDIADAVAF 232
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
4-228 3.06e-15

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 73.17  E-value: 3.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    4 LDGKTILITGASSGIGkstaFEIAKV---AKVKLILAArrfSTVEEIAKELESKYE--VSVLPLKLDVSDLKSIPGVIES 78
Cdd:PRK07097   8 LKGKIALITGASYGIG----FAIAKAyakAGATIVFND---INQELVDKGLAAYRElgIEAHGYVCDVTDEDGVQAMVSQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   79 LPKEFADIDVLINNAGLALGTdKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIA---GRESYvgg 155
Cdd:PRK07097  81 IEKEVGVIDILVNNAGIIKRI-PMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMMselGRETV--- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  156 SVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETE----FSVVRFHGDKQKADNVYKNSEP----LTPEDIAEVIL 227
Cdd:PRK07097 157 SAYAAAKGGLKMLTKNIASEYGEANIQCNGIGPGYIATPqtapLRELQADGSRHPFDQFIIAKTPaarwGDPEDLAGPAV 236

                 .
gi 19114010  228 F 228
Cdd:PRK07097 237 F 237
PRK06398 PRK06398
aldose dehydrogenase; Validated
1-233 5.92e-15

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 72.17  E-value: 5.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAfeiakvakvklilaaRRFstVEEIAK----ELESKYEVSVLPLKLDVSDLKSIPGVI 76
Cdd:PRK06398   1 DLGLKDKVAIVTGGSQGIGKAVV---------------NRL--KEEGSNvinfDIKEPSYNDVDYFKVDVSNKEQVIKGI 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   77 ESLPKEFADIDVLINNAGLALgTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGS 156
Cdd:PRK06398  64 DYVISKYGRIDILVNNAGIES-YGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRNAA 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  157 VYCSTKSALAQFTSALrkeTID--TRIRIMEVDPGLVET-------EFSVVRFHGDKQKADNVYKNSEPL----TPEDIA 223
Cdd:PRK06398 143 AYVTSKHAVLGLTRSI---AVDyaPTIRCVAVCPGSIRTpllewaaELEVGKDPEHVERKIREWGEMHPMkrvgKPEEVA 219
                        250
                 ....*....|
gi 19114010  224 EVILFALTRR 233
Cdd:PRK06398 220 YVVAFLASDL 229
PRK07832 PRK07832
SDR family oxidoreductase;
7-238 6.75e-15

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 72.38  E-value: 6.75e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    7 KTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKYEVSVLPLKLDVSDLKSIPGVIESLPKEFADI 86
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAA-QGAELFLTDRDADGLAQTVADARALGGTVPEHRALDISDYDAVAAFAADIHAAHGSM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   87 DVLINNAGLAL-GTdkVIDLNIDDAVTMITTNVLGMMAMTRA-VLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSA 164
Cdd:PRK07832  80 DVVMNIAGISAwGT--VDRLTHEQWRRMVDVNLMGPIHVIETfVPPMVAAGRGGHLVNVSSAAGLVALPWHAAYSASKFG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  165 LAQFTSALRKETIDTRIRIMEVDPGLVETEF-SVVRFHGDKQKADNVYKNSE-----PLTPEDIAEVILFALTRRENVVI 238
Cdd:PRK07832 158 LRGLSEVLRFDLARHGIGVSVVVPGAVKTPLvNTVEIAGVDREDPRVQKWVDrfrghAVTPEKAAEKILAGVEKNRYLVY 237
PRK07023 PRK07023
SDR family oxidoreductase;
10-227 8.23e-15

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 71.58  E-value: 8.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   10 LITGASSGIGKSTAFEIAkVAKVKLI---------LAARRFSTVEEIAkeleskyevsvlplkLDVSDLKSIPGVIES-L 79
Cdd:PRK07023   5 IVTGHSRGLGAALAEQLL-QPGIAVLgvarsrhpsLAAAAGERLAEVE---------------LDLSDAAAAAAWLAGdL 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   80 PKEF---ADIDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGS 156
Cdd:PRK07023  69 LAAFvdgASRVLLINNAGTVEPIGPLATLDAAAIARAVGLNVAAPLMLTAALAQAASDAAERRILHISSGAARNAYAGWS 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19114010  157 VYCSTKSALAQFTSALRKETiDTRIRIMEVDPGLVETEF-------SVVRFHGdKQKADNVYKNSEPLTPEDIAEVIL 227
Cdd:PRK07023 149 VYCATKAALDHHARAVALDA-NRALRIVSLAPGVVDTGMqatiratDEERFPM-RERFRELKASGALSTPEDAARRLI 224
PRK05993 PRK05993
SDR family oxidoreductase;
7-233 8.46e-15

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 71.98  E-value: 8.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    7 KTILITGASSGIGKSTAFEIaKVAKVKLILAARRFSTVEEIAKE-LESkyevsvlpLKLDVSDLKSIPGVIESLpKEFAD 85
Cdd:PRK05993   5 RSILITGCSSGIGAYCARAL-QSDGWRVFATCRKEEDVAALEAEgLEA--------FQLDYAEPESIAALVAQV-LELSG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   86 --IDVLINNAglALG-TDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTK 162
Cdd:PRK05993  75 grLDALFNNG--AYGqPGAVEDLPTEALRAQFEANFFGWHDLTRRVIPVMRKQGQGRIVQCSSILGLVPMKYRGAYNASK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  163 SALAQFTSALRKETIDTRIRIMEVDPGLVETEF----------------SVVR--FHGDKQKADNVYKNSE-PLTPEDIA 223
Cdd:PRK05993 153 FAIEGLSLTLRMELQGSGIHVSLIEPGPIETRFranalaafkrwidienSVHRaaYQQQMARLEGGGSKSRfKLGPEAVY 232
                        250
                 ....*....|
gi 19114010  224 EVILFALTRR 233
Cdd:PRK05993 233 AVLLHALTAP 242
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
4-243 9.00e-15

Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine peroxisomal carbonyl reductase and similar proteins. The porcine enzyme efficiently reduces retinals. This subgroup also includes human dehydrogenase/reductase (SDR family) member 4 (DHRS4), and human DHRS4L1. DHRS4 is a peroxisomal enzyme with 3beta-hydroxysteroid dehydrogenase activity; it catalyzes the reduction of 3-keto-C19/C21-steroids into 3beta-hydroxysteroids more efficiently than it does the retinal reduction. The human DHRS4 gene cluster contains DHRS4, DHRS4L2 and DHRS4L1. DHRS4L2 and DHRS4L1 are paralogs of DHRS4, DHRS4L2 being the most recent member. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187641 [Multi-domain]  Cd Length: 256  Bit Score: 71.80  E-value: 9.00e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   4 LDGKTILITGASSGIGKSTAFEIAKVAkVKLILAARRFSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLPKEF 83
Cdd:cd08936   8 LANKVALVTASTDGIGLAIARRLAQDG-AHVVVSSRKQQNVDRAVATLQGE-GLSVTGTVCHVGKAEDRERLVATAVNLH 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  84 ADIDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKS 163
Cdd:cd08936  86 GGVDILVSNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAAFHPFPGLGPYNVSKT 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010 164 ALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHgDKQKADNVYKN---SEPLTPEDIAEVILFALTRRENVVIAD 240
Cdd:cd08936 166 ALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSSALWM-DKAVEESMKETlriRRLGQPEDCAGIVSFLCSEDASYITGE 244

                ...
gi 19114010 241 TLV 243
Cdd:cd08936 245 TVV 247
PRK06523 PRK06523
short chain dehydrogenase; Provisional
3-228 1.02e-14

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 71.47  E-value: 1.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    3 RLDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARrfSTVEEIAKELESkyevsvlpLKLDVSDLKSIPGVIESLPKE 82
Cdd:PRK06523   6 ELAGKRALVTGGTKGIGAATVARLLE-AGARVVTTAR--SRPDDLPEGVEF--------VAADLTTAEGCAAVARAVLER 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   83 FADIDVLINNAG---------LALGTDKVID-LNIddavtmittNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGR--- 149
Cdd:PRK06523  75 LGGVDILVHVLGgssapaggfAALTDEEWQDeLNL---------NLLAAVRLDRALLPGMIARGSGVIIHVTSIQRRlpl 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  150 -ESYVGgsvYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVV---RFH----GDKQKADNVYKNS------- 214
Cdd:PRK06523 146 pESTTA---YAAAKAALSTYSKSLSKEVAPKGVRVNTVSPGWIETEAAVAlaeRLAeaagTDYEGAKQIIMDSlggiplg 222
                        250
                 ....*....|....
gi 19114010  215 EPLTPEDIAEVILF 228
Cdd:PRK06523 223 RPAEPEEVAELIAF 236
PLN02253 PLN02253
xanthoxin dehydrogenase
3-256 2.14e-14

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 71.01  E-value: 2.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    3 RLDGKTILITGASSGIGKSTAFEIAKVAkVKLILAARRFSTVEEIAKELESKYEVSVLplKLDVSDLKSIPGVIESLPKE 82
Cdd:PLN02253  15 RLLGKVALVTGGATGIGESIVRLFHKHG-AKVCIVDLQDDLGQNVCDSLGGEPNVCFF--HCDVTVEDDVSRAVDFTVDK 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   83 FADIDVLINNAGL--ALGTD----------KVIDLNIDDAVtmittnvLGMMAMTRAVLPifysKNKGDILNVGSIAGRE 150
Cdd:PLN02253  92 FGTLDIMVNNAGLtgPPCPDirnvelsefeKVFDVNVKGVF-------LGMKHAARIMIP----LKKGSIVSLCSVASAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  151 SYVGGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGDKQKADN-------VYKNSE----PLTP 219
Cdd:PLN02253 161 GGLGPHAYTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALALAHLPEDERTEDAlagfrafAGKNANlkgvELTV 240
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 19114010  220 EDIAEVILFALTRRENVVIADTLVFPSHQGGANHVYR 256
Cdd:PLN02253 241 DDVANAVLFLASDEARYISGLNLMIDGGFTCTNHSLR 277
PRK08628 PRK08628
SDR family oxidoreductase;
3-233 5.50e-14

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 69.60  E-value: 5.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    3 RLDGKTILITGASSGIGKSTAFEIAKVAKVKLILA--ARRFSTVEEIaKELESKYEVsvlpLKLDVSDLKSIPGVIESLP 80
Cdd:PRK08628   4 NLKDKVVIVTGGASGIGAAISLRLAEEGAIPVIFGrsAPDDEFAEEL-RALQPRAEF----VQVDLTDDAQCRDAVEQTV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   81 KEFADIDVLINNAGLalgTDKV-IDLNIDDAVTMITTNVLGMMAMTRAVLPiFYSKNKGDILNVGSIAGRESYVGGSVYC 159
Cdd:PRK08628  79 AKFGRIDGLVNNAGV---NDGVgLEAGREAFVASLERNLIHYYVMAHYCLP-HLKASRGAIVNISSKTALTGQGGTSGYA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  160 STKSALAQFTSALRKETIDTRIRIMEVDPGLVET---EFSVVRFHGDKQKADNVYKNSePL-----TPEDIAEVILFALT 231
Cdd:PRK08628 155 AAKGAQLALTREWAVALAKDGVRVNAVIPAEVMTplyENWIATFDDPEAKLAAITAKI-PLghrmtTAEEIADTAVFLLS 233

                 ..
gi 19114010  232 RR 233
Cdd:PRK08628 234 ER 235
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
8-228 8.26e-14

alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, which catalyzes the NAD-dependent oxidoreduction of hydroxysteroids, is a dimeric member of the classical SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187589 [Multi-domain]  Cd Length: 250  Bit Score: 69.06  E-value: 8.26e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   8 TILITGASSGIGKSTAfEIAKVAKVKLILAARRFSTVEEiakeleskyevsvlplklDVSDLKSIPGVIESLP-KEFADI 86
Cdd:cd05328   1 TIVITGAASGIGAATA-ELLEDAGHTVIGIDLREADVIA------------------DLSTPEGRAAAIADVLaRCSGVL 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  87 DVLINNAGLALGTdkvidlNIDDAVTMittNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAG----------RESYVGGS 156
Cdd:cd05328  62 DGLVNCAGVGGTT------VAGLVLKV---NYFGLRALMEALLPRLRKGHGPAAVVVSSIAGagwaqdklelAKALAAGT 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010 157 -----------------VYCSTKSALAQFTSALRKETIDTR-IRIMEVDPGLVET----EFSVVRFHGDKQKADnVYKNS 214
Cdd:cd05328 133 earavalaehagqpgylAYAGSKEALTVWTRRRAATWLYGAgVRVNTVAPGPVETpilqAFLQDPRGGESVDAF-VTPMG 211
                       250
                ....*....|....
gi 19114010 215 EPLTPEDIAEVILF 228
Cdd:cd05328 212 RRAEPDEIAPVIAF 225
PRK07985 PRK07985
SDR family oxidoreductase;
3-240 8.39e-14

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 69.64  E-value: 8.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    3 RLDGKTILITGASSGIGKSTAFEIAKV-AKVKLILAARRFSTVEEIAKELESKYEVSVLpLKLDVSDLKSIPGVIESLPK 81
Cdd:PRK07985  46 RLKDRKALVTGGDSGIGRAAAIAYAREgADVAISYLPVEEEDAQDVKKIIEECGRKAVL-LPGDLSDEKFARSLVHEAHK 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   82 EFADIDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFysKNKGDILNVGSIAGRESYVGGSVYCST 161
Cdd:PRK07985 125 ALGGLDIMALVAGKQVAIPDIADLTSEQFQKTFAINVFALFWLTQEAIPLL--PKGASIITTSSIQAYQPSPHLLDYAAT 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  162 KSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVrfHGDKQKADNVYKNSEPL----TPEDIAEVILFALTRRENVV 237
Cdd:PRK07985 203 KAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTALQIS--GGQTQDKIPQFGQQTPMkragQPAELAPVYVYLASQESSYV 280

                 ...
gi 19114010  238 IAD 240
Cdd:PRK07985 281 TAE 283
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
4-193 9.05e-14

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 68.95  E-value: 9.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    4 LDGKTILITGAS--SGIGKSTAFEIAK----------VAKVKLILAARRFSTVEEIAKELESkYEVSVLPLKLDVSDLKS 71
Cdd:PRK12748   3 LMKKIALVTGASrlNGIGAAVCRRLAAkgidifftywSPYDKTMPWGMHDKEPVLLKEEIES-YGVRCEHMEIDLSQPYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   72 IPGVIESLPKEFADIDVLINNAglALGTD---KVIDLNIDDAVTMIttNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAG 148
Cdd:PRK12748  82 PNRVFYAVSERLGDPSILINNA--AYSTHtrlEELTAEQLDKHYAV--NVRATMLLSSAFAKQYDGKAGGRIINLTSGQS 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 19114010  149 RESYVGGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVET 193
Cdd:PRK12748 158 LGPMPDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDT 202
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
3-251 9.32e-14

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 68.63  E-value: 9.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    3 RLDGKTILITGASSGIGKSTA-FEIAKVAKVklILAARRFSTVEEIAKELESKYEVSVLPlkLDVSDLKSIPGVIESLPK 81
Cdd:PRK05786   2 RLKGKKVAIIGVSEGLGYAVAyFALKEGAQV--CINSRNENKLKRMKKTLSKYGNIHYVV--GDVSSTESARNVIEKAAK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   82 EFADIDVLINNAG--LALGTDKVIDLNiddavTMITTNVLGMMAMTRAVLPIFysKNKGDILNVGSIAGRESYVGGSV-Y 158
Cdd:PRK05786  78 VLNAIDGLVVTVGgyVEDTVEEFSGLE-----EMLTNHIKIPLYAVNASLRFL--KEGSSIVLVSSMSGIYKASPDQLsY 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  159 CSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEF------SVVRFHGDKQKAdnvyknsepltPEDIAEVILFALTR 232
Cdd:PRK05786 151 AVAKAGLAKAVEILASELLGRGIRVNGIAPTTISGDFepernwKKLRKLGDDMAP-----------PEDFAKVIIWLLTD 219
                        250
                 ....*....|....*....
gi 19114010  233 RENVViaDTLVFPSHqGGA 251
Cdd:PRK05786 220 EADWV--DGVVIPVD-GGA 235
PRK06101 PRK06101
SDR family oxidoreductase;
8-193 1.04e-13

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 68.74  E-value: 1.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    8 TILITGASSGIGKSTAFEIAKvAKVKLILAARRfstvEEIAKELESKYEvSVLPLKLDVSDLKSIPGVIESLPkefADID 87
Cdd:PRK06101   3 AVLITGATSGIGKQLALDYAK-QGWQVIACGRN----QSVLDELHTQSA-NIFTLAFDVTDHPGTKAALSQLP---FIPE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   88 VLINNAGLAlgtdKVIDLNIDDAVTM---ITTNVLGMMAMTRAVLPIFYSKNKgdILNVGSIAGRESYVGGSVYCSTKSA 164
Cdd:PRK06101  74 LWIFNAGDC----EYMDDGKVDATLMarvFNVNVLGVANCIEGIQPHLSCGHR--VVIVGSIASELALPRAEAYGASKAA 147
                        170       180
                 ....*....|....*....|....*....
gi 19114010  165 LAQFTSALRKETIDTRIRIMEVDPGLVET 193
Cdd:PRK06101 148 VAYFARTLQLDLRPKGIEVVTVFPGFVAT 176
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
1-192 1.31e-13

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 68.43  E-value: 1.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFEIAkvAKVKLILAARRFSTVEEIAKELESKyEVSVLPLkldVSDLKSIPG---VIE 77
Cdd:PRK12823   3 NQRFAGKVVVVTGAAQGIGRGVALRAA--AEGARVVLVDRSELVHEVAAELRAA-GGEALAL---TADLETYAGaqaAMA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   78 SLPKEFADIDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGResyvggSV 157
Cdd:PRK12823  77 AAVEAFGRIDVLINNVGGTIWAKPFEEYEEEQIEAEIRRSLFPTLWCCRAVLPHMLAQGGGAIVNVSSIATR------GI 150
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 19114010  158 ----YCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVE 192
Cdd:PRK12823 151 nrvpYSAAKGGVNALTASLAFEYAEHGIRVNAVAPGGTE 189
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
11-194 1.95e-13

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 67.73  E-value: 1.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   11 ITGASSGIGKSTAfeiAKVAKVKLILAARRFSTVEEIAKELESKYEV--SVLPLKLDVSDLKSIPGVIESLPKEFADIDV 88
Cdd:PRK12938   8 VTGGMGGIGTSIC---QRLHKDGFKVVAGCGPNSPRRVKWLEDQKALgfDFIASEGNVGDWDSTKAAFDKVKAEVGEIDV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   89 LINNAGLalgTDKVI--DLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSALA 166
Cdd:PRK12938  85 LVNNAGI---TRDVVfrKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFGQTNYSTAKAGIH 161
                        170       180
                 ....*....|....*....|....*...
gi 19114010  167 QFTSALRKETIDTRIRIMEVDPGLVETE 194
Cdd:PRK12938 162 GFTMSLAQEVATKGVTVNTVSPGYIGTD 189
PRK07478 PRK07478
short chain dehydrogenase; Provisional
1-228 3.73e-13

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 67.26  E-value: 3.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLP 80
Cdd:PRK07478   1 MMRLNGKVAIITGASSGIGRAAAKLFAR-EGAKVVVGARRQAELDQLVAEIRAE-GGEAVALAGDVRDEAYAKALVALAV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   81 KEFADIDVLINNAGlALGTDK-VIDLNIDDAVTMITTNV----LGMMAMTRAVLpifysKNKGdilnvGSIAGRESYVGG 155
Cdd:PRK07478  79 ERFGGLDIAFNNAG-TLGEMGpVAEMSLEGWRETLATNLtsafLGAKHQIPAML-----ARGG-----GSLIFTSTFVGH 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  156 SV-------YCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSvvRFHGDKQKADNVYKNSEPL----TPEDIAE 224
Cdd:PRK07478 148 TAgfpgmaaYAASKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMG--RAMGDTPEALAFVAGLHALkrmaQPEEIAQ 225

                 ....
gi 19114010  225 VILF 228
Cdd:PRK07478 226 AALF 229
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
4-167 3.95e-13

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 68.72  E-value: 3.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    4 LDGKTILITGASSGIGKSTAFEIAKV-AKVklILAARRFSTVEEIAKELESKyeVSVLPLKLDVSDLKSIPGVIESLPKE 82
Cdd:PRK08324 420 LAGKVALVTGAAGGIGKATAKRLAAEgACV--VLADLDEEAAEAAAAELGGP--DRALGVACDVTDEAAVQAAFEEAALA 495
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   83 FADIDVLINNAGLAL------GTDKVIDLNIDdavtmitTNVLGMMAMTRAVLPIFYSKNKG-DILNVGSIAGRESYVGG 155
Cdd:PRK08324 496 FGGVDIVVSNAGIAIsgpieeTSDEDWRRSFD-------VNATGHFLVAREAVRIMKAQGLGgSIVFIASKNAVNPGPNF 568
                        170
                 ....*....|..
gi 19114010  156 SVYCSTKSALAQ 167
Cdd:PRK08324 569 GAYGAAKAAELH 580
PRK08278 PRK08278
SDR family oxidoreductase;
1-130 1.11e-12

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 66.08  E-value: 1.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKstafEIAKVA---KVKLILAARRFS-------TVEEIAKELESKyEVSVLPLKLDVSDLK 70
Cdd:PRK08278   1 MMSLSGKTLFITGASRGIGL----AIALRAardGANIVIAAKTAEphpklpgTIHTAAEEIEAA-GGQALPLVGDVRDED 75
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   71 SIPGVIESLPKEFADIDVLINNAGlALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLP 130
Cdd:PRK08278  76 QVAAAVAKAVERFGGIDICVNNAS-AINLTGTEDTPMKRFDLMQQINVRGTFLVSQACLP 134
PRK06196 PRK06196
oxidoreductase; Provisional
4-193 1.43e-12

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 66.24  E-value: 1.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    4 LDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELEskyEVSVLPLklDVSDLKSIPGVIESLPKEF 83
Cdd:PRK06196  24 LSGKTAIVTGGYSGLGLETTRALAQ-AGAHVIVPARRPDVAREALAGID---GVEVVML--DLADLESVRAFAERFLDSG 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   84 ADIDVLINNAG-LALGTDKVidlnIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRES----------- 151
Cdd:PRK06196  98 RRIDILINNAGvMACPETRV----GDGWEAQFATNHLGHFALVNLLWPALAAGAGARVVALSSAGHRRSpirwddphftr 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 19114010  152 -YVGGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVET 193
Cdd:PRK06196 174 gYDKWLAYGQSKTANALFAVHLDKLGKDQGVRAFSVHPGGILT 216
PLN00015 PLN00015
protochlorophyllide reductase
10-158 2.17e-12

protochlorophyllide reductase


Pssm-ID: 177654  Cd Length: 308  Bit Score: 65.50  E-value: 2.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   10 LITGASSGIGKSTAFEIAKVAKVKLILAARRFSTVEEIAKEL---ESKYEVsvlpLKLDVSDLKSIPGVIESLPKEFADI 86
Cdd:PLN00015   1 IITGASSGLGLATAKALAETGKWHVVMACRDFLKAERAAKSAgmpKDSYTV----MHLDLASLDSVRQFVDNFRRSGRPL 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19114010   87 DVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGD--ILNVGSIAGRESYVGGSVY 158
Cdd:PLN00015  77 DVLVCNAAVYLPTAKEPTFTADGFELSVGTNHLGHFLLSRLLLDDLKKSDYPSkrLIIVGSITGNTNTLAGNVP 150
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
9-241 2.50e-12

Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase (KR) domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 63.69  E-value: 2.50e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   9 ILITGASSGIGKSTAFEIAKVAKVKLILAARRfstveeiakeleskyevsvlplkldvsdlksipgvieslpkefadiDV 88
Cdd:cd02266   1 VLVTGGSGGIGGAIARWLASRGSPKVLVVSRR----------------------------------------------DV 34
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  89 LINNAGLALgTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSALAQF 168
Cdd:cd02266  35 VVHNAAILD-DGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAALDGL 113
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19114010 169 TSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGDKQKADNVYKNSEPLTPEDIAEVILFALTRRENVVIADT 241
Cdd:cd02266 114 AQQWASEGWGNGLPATAVACGTWAGSGMAKGPVAPEEILGNRRHGVRTMPPEEVARALLNALDRPKAGVCYII 186
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
4-193 2.53e-12

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 64.89  E-value: 2.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    4 LDGKTILITGASSGIGKSTAFEIAK----VAKVKLILAARRFSTVEEIAKELeskyevsvLPLKLDVSDLKSIPGVIESL 79
Cdd:PRK08993   8 LEGKVAVVTGCDTGLGQGMALGLAEagcdIVGINIVEPTETIEQVTALGRRF--------LSLTADLRKIDGIPALLERA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   80 PKEFADIDVLINNAGLALGTDkVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSK-NKGDILNVGSIAgreSYVGG--- 155
Cdd:PRK08993  80 VAEFGHIDILVNNAGLIRRED-AIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQgNGGKIINIASML---SFQGGirv 155
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 19114010  156 SVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVET 193
Cdd:PRK08993 156 PSYTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMAT 193
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
3-228 2.61e-12

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 64.73  E-value: 2.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    3 RLDGKTILITGASSGIGKStafeIAKVakvkliLAARRFSTV------EEIAKELESKYEVSVLPLKLDVSDLKSIPGVI 76
Cdd:PRK08642   2 QISEQTVLVTGGSRGLGAA----IARA------FAREGARVVvnyhqsEDAAEALADELGDRAIALQADVTDREQVQAMF 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   77 ESLPKEF-ADIDVLINNAGLALGTD-----KVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRE 150
Cdd:PRK08642  72 ATATEHFgKPITTVVNNALADFSFDgdarkKADDITWEDFQQQLEGSVKGALNTIQAALPGMREQGFGRIINIGTNLFQN 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  151 SYVGGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLV-ETEFSVVrfhgdkqKADNVY---KNSEPL----TPEDI 222
Cdd:PRK08642 152 PVVPYHDYTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLrTTDASAA-------TPDEVFdliAATTPLrkvtTPQEF 224

                 ....*.
gi 19114010  223 AEVILF 228
Cdd:PRK08642 225 ADAVLF 230
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
4-194 2.63e-12

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 64.92  E-value: 2.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    4 LDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKYEVSvLPLKLDVSDLKSIPGVIESLPKEF 83
Cdd:PRK08277   8 LKGKVAVITGGGGVLGGAMAKELAR-AGAKVAILDRNQEKAEAVVAEIKAAGGEA-LAVKADVLDKESLEQARQQILEDF 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   84 ADIDVLINNAG-------------LALGTDKVI-DLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGR 149
Cdd:PRK08277  86 GPCDILINGAGgnhpkattdnefhELIEPTKTFfDLDEEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINISSMNAF 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 19114010  150 ESYVGGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETE 194
Cdd:PRK08277 166 TPLTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTE 210
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
6-145 2.85e-12

human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like SDRs; Classical SDR-like subgroup containing human DHRS-12/FLJ13639, the 36K protein of zebrafish CNS myelin, and related proteins. DHRS-12/FLJ13639 is expressed in neurons and oligodendrocytes in the human cerebral cortex. Proteins in this subgroup share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 64.92  E-value: 2.85e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   6 GKTILITGASSGIGKSTAFEIAKVAKVkLILAARRFSTVEEIAKELESKY-EVSVLPLKLDVSDLKSIPGVIESLPKEFA 84
Cdd:cd09808   1 GRSFLITGANSGIGKAAALAIAKRGGT-VHMVCRNQTRAEEARKEIETESgNQNIFLHIVDMSDPKQVWEFVEEFKEEGK 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19114010  85 DIDVLINNAGLALGTDkviDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGS 145
Cdd:cd09808  80 KLHVLINNAGCMVNKR---ELTEDGLEKNFATNTLGTYILTTHLIPVLEKEEDPRVITVSS 137
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
10-197 2.98e-12

sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain dehydrogenase/reductase family. The enzyme catalyzes the last step in the biosynthesis of tetrahydrobiopterin. A similar enzyme in Bacillus cereus was isolated for its ability to convert benzil to (S)-benzoin, a property sepiapterin reductase also shares. Cutoff scores for this model are set such that benzil reductase scores between trusted and noise cutoffs.


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 64.55  E-value: 2.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    10 LITGASSGIGKSTAFEIAKVAKVK---LILAARRFSTVEEIAKELESkyEVSVLPLKLDVSDLKSIPGVIESL------- 79
Cdd:TIGR01500   4 LVTGASRGFGRTIAQELAKCLKSPgsvLVLSARNDEALRQLKAEIGA--ERSGLRVVRVSLDLGAEAGLEQLLkalrelp 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    80 -PKEFADIdVLINNAGlALGTDKVIDLNIDDAVTM---ITTNVLGMMAMTRAVLPIFYSKNKGD--ILNVGSIAGRESYV 153
Cdd:TIGR01500  82 rPKGLQRL-LLINNAG-TLGDVSKGFVDLSDSTQVqnyWALNLTSMLCLTSSVLKAFKDSPGLNrtVVNISSLCAIQPFK 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 19114010   154 GGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSV 197
Cdd:TIGR01500 160 GWALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDMQQ 203
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
6-228 3.50e-12

rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has bifunctional proteins with an N-terminal aldolase and a C-terminal classical SDR domain. One member is identified as a rhamnulose-1-phosphate aldolase/alcohol dehydrogenase. The SDR domain has a canonical SDR glycine-rich NAD(P) binding motif and a match to the characteristic active site triad. However, it lacks an upstream active site Asn typical of SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187647 [Multi-domain]  Cd Length: 250  Bit Score: 64.34  E-value: 3.50e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   6 GKTILITGASSGIGKSTAFEIAkvAKVKLILAARRFSTVEEIAKElESKYEVSVLPLKLDVSDLKSIPGVIESLPKEFAD 85
Cdd:cd08943   1 GKVALVTGGASGIGLAIAKRLA--AEGAAVVVADIDPEIAEKVAE-AAQGGPRALGVQCDVTSEAQVQSAFEQAVLEFGG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  86 IDVLINNAGLALgTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNK-GDILNVGSIAGRESYVGGSVYCSTKSA 164
Cdd:cd08943  78 LDIVVSNAGIAT-SSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGIgGNIVFNASKNAVAPGPNAAAYSAAKAA 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19114010 165 LAQFTSALRKETIDTRIRIMEVDP-----GLVETEFSVVRFHG-------DKQKADNVYKNSepLTPEDIAEVILF 228
Cdd:cd08943 157 EAHLARCLALEGGEDGIRVNTVNPdavfrGSKIWEGVWRAARAkayglleEEYRTRNLLKRE--VLPEDVAEAVVA 230
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
3-193 3.56e-12

retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the short-chain dehydrogenases/reductase family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187638 [Multi-domain]  Cd Length: 261  Bit Score: 64.48  E-value: 3.56e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   3 RLDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKYEVSVLPLKLDVSDLKSIPGVIESLPKE 82
Cdd:cd08933   6 RYADKVVIVTGGSRGIGRGIVRAFVE-NGAKVVFCARGEAAGQALESELNRAGPGSCKFVPCDVTKEEDIKTLISVTVER 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  83 FADIDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPiFYSKNKGDILNVGSIAGRESYVGGSVYCSTK 162
Cdd:cd08933  85 FGRIDCLVNNAGWHPPHQTTDETSAQEFRDLLNLNLISYFLASKYALP-HLRKSQGNIINLSSLVGSIGQKQAAPYVATK 163
                       170       180       190
                ....*....|....*....|....*....|.
gi 19114010 163 SALAQFTSALRKETIDTRIRIMEVDPGLVET 193
Cdd:cd08933 164 GAITAMTKALAVDESRYGVRVNCISPGNIWT 194
PRK07677 PRK07677
short chain dehydrogenase; Provisional
6-93 3.63e-12

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 64.31  E-value: 3.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    6 GKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESkYEVSVLPLKLDVSDLKSIPGVIESLPKEFAD 85
Cdd:PRK07677   1 EKVVIITGGSSGMGKAMAKRFAE-EGANVVITGRTKEKLEEAKLEIEQ-FPGQVLTVQMDVRNPEDVQKMVEQIDEKFGR 78

                 ....*...
gi 19114010   86 IDVLINNA 93
Cdd:PRK07677  79 IDALINNA 86
PRK08017 PRK08017
SDR family oxidoreductase;
7-230 4.85e-12

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 63.95  E-value: 4.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    7 KTILITGASSGIGKSTAFEIAKvaKVKLILAARRFStvEEIAKELESKYEvsvlPLKLDVSDLKSIpgvieslpkEFADI 86
Cdd:PRK08017   3 KSVLITGCSSGIGLEAALELKR--RGYRVLAACRKP--DDVARMNSLGFT----GILLDLDDPESV---------ERAAD 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   87 DV----------LINNAGLAL-GTdkvidLNIDDAVTM---ITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESY 152
Cdd:PRK08017  66 EVialtdnrlygLFNNAGFGVyGP-----LSTISRQQMeqqFSTNFFGTHQLTMLLLPAMLPHGEGRIVMTSSVMGLIST 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  153 VGGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFS--VVRFHGDKQKADNVYKNSEPLTPEDIAEVILFAL 230
Cdd:PRK08017 141 PGRGAYAASKYALEAWSDALRMELRHSGIKVSLIEPGPIRTRFTdnVNQTQSDKPVENPGIAARFTLGPEAVVPKLRHAL 220
PRK05599 PRK05599
SDR family oxidoreductase;
8-232 7.59e-12

SDR family oxidoreductase;


Pssm-ID: 235527 [Multi-domain]  Cd Length: 246  Bit Score: 63.37  E-value: 7.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    8 TILITGASSGIGKSTAFEIAkvAKVKLILAARRFSTVEEIAKELESKYEVSVLPLKLDVSDLKSIPGVIESLPKEFADID 87
Cdd:PRK05599   2 SILILGGTSDIAGEIATLLC--HGEDVVLAARRPEAAQGLASDLRQRGATSVHVLSFDAQDLDTHRELVKQTQELAGEIS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   88 VLINNAGLaLGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKN-KGDILNVGSIAGRESYVGGSVYCSTKSALA 166
Cdd:PRK05599  80 LAVVAFGI-LGDQERAETDEAHAVEIATVDYTAQVSMLTVLADELRAQTaPAAIVAFSSIAGWRARRANYVYGSTKAGLD 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19114010  167 QFTSALRKETIDTRIRIMEVDPGLVETEFSvvrfHGDKQKADNVYknsepltPEDIAEVILFALTR 232
Cdd:PRK05599 159 AFCQGLADSLHGSHVRLIIARPGFVIGSMT----TGMKPAPMSVY-------PRDVAAAVVSAITS 213
PRK06194 PRK06194
hypothetical protein; Provisional
1-193 7.61e-12

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 63.88  E-value: 7.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAfEIAKVAKVKLILAARRFSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLP 80
Cdd:PRK06194   1 MKDFAGKVAVITGAASGFGLAFA-RIGAALGMKLVLADVQQDALDRAVAELRAQ-GAEVLGVRTDVSDAAQVEALADAAL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   81 KEFADIDVLINNAGLALGtDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNK------GDILNVGSIAGRESYVG 154
Cdd:PRK06194  79 ERFGAVHLLFNNAGVGAG-GLVWENSLADWEWVLGVNLWGVIHGVRAFTPLMLAAAEkdpayeGHIVNTASMAGLLAPPA 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 19114010  155 GSVYCSTKSALAQFTSALRK--ETIDTRIRIMEVDPGLVET 193
Cdd:PRK06194 158 MGIYNVSKHAVVSLTETLYQdlSLVTDQVGASVLCPYFVPT 198
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
6-243 1.49e-11

Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, classical (c) SDRs; This subgroup includes a putative carbohydrate or polyalcohol metabolizing SDR (A3DFK9) from Clostridium thermocellum. Its members have a TGXXXGXG classical-SDR glycine-rich NAD-binding motif, and some have a canonical SDR active site tetrad (A3DFK9 lacks the upstream Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187662 [Multi-domain]  Cd Length: 242  Bit Score: 62.60  E-value: 1.49e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   6 GKTILITGASSGIGKSTAFEIAKvAKVKLILAarrfSTVEEIAKELESKYEVSVLPLKLDVSDLKSIPGVIESLPKEFAD 85
Cdd:cd09761   1 GKVAIVTGGGHGIGKQICLDFLE-AGDKVVFA----DIDEERGADFAEAEGPNLFFVHGDVADETLVKFVVYAMLEKLGR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  86 IDVLINNAglALGTDKVI-DLNIDDAVTMITTNVLGMMAMTRAVLPiFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSA 164
Cdd:cd09761  76 IDVLVNNA--ARGSKGILsSLLLEEWDRILSVNLTGPYELSRYCRD-ELIKNKGRIINIASTRAFQSEPDSEAYAASKGG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010 165 LAQFTSALrKETIDTRIRIMEVDPGLVET----EFSVVRFHGDKQKADNVYKNSeplTPEDIAEVILFALTRRENVVIAD 240
Cdd:cd09761 153 LVALTHAL-AMSLGPDIRVNCISPGWINTteqqEFTAAPLTQEDHAQHPAGRVG---TPKDIANLVLFLCQQDAGFITGE 228

                ...
gi 19114010 241 TLV 243
Cdd:cd09761 229 TFI 231
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
4-143 2.72e-11

human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human HSDL2 and related protens. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 61.69  E-value: 2.72e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   4 LDGKTILITGASSGIGKSTAFEIAKVAkVKLILAARRFS-------TVEEIAKELEsKYEVSVLPLKLDVSDLKSIPGVI 76
Cdd:cd09762   1 LAGKTLFITGASRGIGKAIALKAARDG-ANVVIAAKTAEphpklpgTIYTAAEEIE-AAGGKALPCIVDIRDEDQVRAAV 78
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19114010  77 ESLPKEFADIDVLINNAGlALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNV 143
Cdd:cd09762  79 EKAVEKFGGIDILVNNAS-AISLTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILNL 144
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
4-194 2.86e-11

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This subgroup includes human DHRS1 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187664 [Multi-domain]  Cd Length: 265  Bit Score: 62.08  E-value: 2.86e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   4 LDGKTILITGASSGIGKSTAFEIAKVAKVKLILAARRFSTVEEIAKELESKYEVSVlPLKLDVSDLKSIPGVIESLPKEF 83
Cdd:cd09763   1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTILPQLPGTAEEIEARGGKCI-PVRCDHSDDDEVEALFERVAREQ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  84 -ADIDVLINNAGLALGTDKVID---------LNIDDavtMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGREsYV 153
Cdd:cd09763  80 qGRLDILVNNAYAAVQLILVGVakpfweeppTIWDD---INNVGLRAHYACSVYAAPLMVKAGKGLIVIISSTGGLE-YL 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 19114010 154 GGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETE 194
Cdd:cd09763 156 FNVAYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTE 196
PRK06114 PRK06114
SDR family oxidoreductase;
3-193 2.93e-11

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 61.72  E-value: 2.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    3 RLDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFST-VEEIAKELESKYEVSVLpLKLDVSDLKSIPGVIESLPK 81
Cdd:PRK06114   5 DLDGQVAFVTGAGSGIGQRIAIGLAQ-AGADVALFDLRTDDgLAETAEHIEAAGRRAIQ-IAADVTSKADLRAAVARTEA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   82 EFADIDVLINNAGLAlGTDKVIDLNIDDAVTMITTNVLGMM----AMTRAVLPifysKNKGDILNVGSIAGRESYVG--G 155
Cdd:PRK06114  83 ELGALTLAVNAAGIA-NANPAEEMEEEQWQTVMDINLTGVFlscqAEARAMLE----NGGGSIVNIASMSGIIVNRGllQ 157
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 19114010  156 SVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVET 193
Cdd:PRK06114 158 AHYNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTAT 195
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
4-196 3.99e-11

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 61.31  E-value: 3.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    4 LDGKTILITGASSGIGKSTAFEIAKVAkVKLILAARRFSTVEEIAKELESKYEVSVlPLKLDVSDLKSIPGVIESLPKEF 83
Cdd:PRK08085   7 LAGKNILITGSAQGIGFLLATGLAEYG-AEIIINDITAERAELAVAKLRQEGIKAH-AAPFNVTHKQEVEAAIEHIEKDI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   84 ADIDVLINNAGLALgTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIA---GRESYvggSVYCS 160
Cdd:PRK08085  85 GPIDVLINNAGIQR-RHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMQselGRDTI---TPYAA 160
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 19114010  161 TKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFS 196
Cdd:PRK08085 161 SKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMT 196
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
4-169 4.31e-11

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 61.32  E-value: 4.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    4 LDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLPKEF 83
Cdd:PRK07523   8 LTGRRALVTGSSQGIGYALAEGLAQ-AGAEVILNGRDPAKLAAAAESLKGQ-GLSAHALAFDVTDHDAVRAAIDAFEAEI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   84 ADIDVLINNAGLALGTdKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKS 163
Cdd:PRK07523  86 GPIDILVNNAGMQFRT-PLEDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVQSALARPGIAPYTATKG 164

                 ....*.
gi 19114010  164 ALAQFT 169
Cdd:PRK07523 165 AVGNLT 170
PRK12742 PRK12742
SDR family oxidoreductase;
1-194 5.53e-11

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 60.93  E-value: 5.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFEIAKV-AKVKLILAARRfSTVEEIAKELESKyevsvlPLKLDVSDLKSIPGVIesl 79
Cdd:PRK12742   1 MGAFTGKKVLVLGGSRGIGAAIVRRFVTDgANVRFTYAGSK-DAAERLAQETGAT------AVQTDSADRDAVIDVV--- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   80 pKEFADIDVLINNAGLALGTDKvIDLNIDDAVTMITTNVLGmmAMTRAVLPIFYSKNKGDILNVGSIAG-RESYVGGSVY 158
Cdd:PRK12742  71 -RKSGALDILVVNAGIAVFGDA-LELDADDIDRLFKINIHA--PYHASVEAARQMPEGGRIIIIGSVNGdRMPVAGMAAY 146
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 19114010  159 CSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETE 194
Cdd:PRK12742 147 AASKSALQGMARGLARDFGPRGITINVVQPGPIDTD 182
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
4-228 9.71e-11

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 60.27  E-value: 9.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    4 LDGKTILITGASSGIGKSTAFEIAKV-AKVklILAARRFSTVEEIAKELES--KYEVSVLPLKLDVSDLKSIPGVIESLP 80
Cdd:PRK08945  10 LKDRIILVTGAGDGIGREAALTYARHgATV--ILLGRTEEKLEAVYDEIEAagGPQPAIIPLDLLTATPQNYQQLADTIE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   81 KEFADIDVLINNAGLaLGTDKVID-LNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYC 159
Cdd:PRK08945  88 EQFGRLDGVLHNAGL-LGELGPMEqQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSSSVGRQGRANWGAYA 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19114010  160 STKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFsvvrfhgdKQKAdnvYKNSEPL---TPEDIAEVILF 228
Cdd:PRK08945 167 VSKFATEGMMQVLADEYQGTNLRVNCINPGGTRTAM--------RASA---FPGEDPQklkTPEDIMPLYLY 227
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
10-232 1.25e-10

Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a classical SDR which binds NADP. Members of this subgroup contain the YXXXK active site characteristic of SDRs. Also, an upstream Asn residue of the canonical catalytic tetrad is partially conserved in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 59.46  E-value: 1.25e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  10 LITGASSGIGKSTAfEIAKVAKVKLILAARRFSTVEEIAKELESKyevsvlplkLDVSDLKSIPGViESLPKEFADIDVL 89
Cdd:cd11730   2 LILGATGGIGRALA-RALAGRGWRLLLSGRDAGALAGLAAEVGAL---------ARPADVAAELEV-WALAQELGPLDLL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  90 INNAGLALGTdKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILnvGSIAGRESYVGGSVYCSTKSALAQFT 169
Cdd:cd11730  71 VYAAGAILGK-PLARTKPAAWRRILDANLTGAALVLKHALALLAAGARLVFL--GAYPELVMLPGLSAYAAAKAALEAYV 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19114010 170 SALRKETIDTRIRImeVDPGLVETEFSVVRFHGDKqkadnvyknsEPLTPEDIAEVILFALTR 232
Cdd:cd11730 148 EVARKEVRGLRLTL--VRPPAVDTGLWAPPGRLPK----------GALSPEDVAAAILEAHQG 198
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
3-243 2.89e-10

cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB) is a classical SDR, it is of particular importance for its role in the degradation of biphenyl/polychlorinated biphenyls(PCBs); PCBs are a significant source of environmental contamination. This subgroup also includes Pseudomonas putida F1 cis-biphenyl-1,2-dihydrodiol-1,2-dehydrogenase (aka cis-benzene glycol dehydrogenase, encoded by the bnzE gene), which participates in benzene metabolism. In addition it includes Pseudomonas sp. C18 putative 1,2-dihydroxy-1,2-dihydronaphthalene dehydrogenase (aka dibenzothiophene dihydrodiol dehydrogenase, encoded by the doxE gene) which participates in an upper naphthalene catabolic pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187606 [Multi-domain]  Cd Length: 257  Bit Score: 58.90  E-value: 2.89e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   3 RLDGKTILITGASSGIGKST--AF--EIAKVAKVKLilaarrfstVEEIAKELESKYEVSVLPLKLDVSDLKSIPGVIES 78
Cdd:cd05348   1 WLKGEVALITGGGSGLGRALveRFvaEGAKVAVLDR---------SAEKVAELRADFGDAVVGVEGDVRSLADNERAVAR 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  79 LPKEFADIDVLINNAGLALGTDKVIDL---NIDDAV-TMITTNVLGMMAMTRAVLPIFYsKNKGDILNVGSIAGRESYVG 154
Cdd:cd05348  72 CVERFGKLDCFIGNAGIWDYSTSLVDIpeeKLDEAFdELFHINVKGYILGAKAALPALY-ATEGSVIFTVSNAGFYPGGG 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010 155 GSVYCSTKSALAQFTSALRKEtIDTRIRIMEVDPGLVETEFSVVRFHGDKQKA------DNVYKNSEPL----TPEDIAE 224
Cdd:cd05348 151 GPLYTASKHAVVGLVKQLAYE-LAPHIRVNGVAPGGMVTDLRGPASLGQGETSistpplDDMLKSILPLgfapEPEDYTG 229
                       250
                ....*....|....*....
gi 19114010 225 VILFALTRRENVVIADTLV 243
Cdd:cd05348 230 AYVFLASRGDNRPATGTVI 248
PRK06197 PRK06197
short chain dehydrogenase; Provisional
5-94 5.69e-10

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 58.50  E-value: 5.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    5 DGKTILITGASSGIGKSTAFEIA-KVAKVklILAARRFSTVEEIAKELESKY---EVSVLplKLDVSDLKSIPGVIESLP 80
Cdd:PRK06197  15 SGRVAVVTGANTGLGYETAAALAaKGAHV--VLAVRNLDKGKAAAARITAATpgaDVTLQ--ELDLTSLASVRAAADALR 90
                         90
                 ....*....|....
gi 19114010   81 KEFADIDVLINNAG 94
Cdd:PRK06197  91 AAYPRIDLLINNAG 104
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-193 6.15e-10

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 57.87  E-value: 6.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGAS--SGIGKSTAFEIAKVAkvklilaARRFST------------VEE-----IAKELESkYEVSVLP 61
Cdd:PRK12859   1 MNQLKNKVAVVTGVSrlDGIGAAICKELAEAG-------ADIFFTywtaydkempwgVDQdeqiqLQEELLK-NGVKVSS 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   62 LKLDVSDLKSIPGVIESLPKEFADIDVLINNAGLALGTD-KVIDLNIDDAVTMIttNVLGMMAMTRAVLPIFYSKNKGDI 140
Cdd:PRK12859  73 MELDLTQNDAPKELLNKVTEQLGYPHILVNNAAYSTNNDfSNLTAEELDKHYMV--NVRATTLLSSQFARGFDKKSGGRI 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 19114010  141 LNVGSIAGRESYVGGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVET 193
Cdd:PRK12859 151 INMTSGQFQGPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDT 203
PRK07577 PRK07577
SDR family oxidoreductase;
7-231 7.12e-10

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 57.43  E-value: 7.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    7 KTILITGASSGIGKSTAFEIAKVAKvKLILAARrfSTVEEIAKELeskyevsvlpLKLDVSDLKSIPGVIESLPKEFAdI 86
Cdd:PRK07577   4 RTVLVTGATKGIGLALSLRLANLGH-QVIGIAR--SAIDDFPGEL----------FACDLADIEQTAATLAQINEIHP-V 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   87 DVLINNAGLALgTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSvYCSTKSALA 166
Cdd:PRK07577  70 DAIVNNVGIAL-PQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNICSRAIFGALDRTS-YSAAKSALV 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  167 QFTSALRKETIDTRIRIMEVDPGLVETE-FSVVRFHGdkQKADNVYKNSEPL----TPEDIAEVILFALT 231
Cdd:PRK07577 148 GCTRTWALELAEYGITVNAVAPGPIETElFRQTRPVG--SEEEKRVLASIPMrrlgTPEEVAAAIAFLLS 215
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
4-194 8.35e-10

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 57.61  E-value: 8.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    4 LDGKTILITGASSGIGKSTAFEIAKVAKVKLILAARRFSTVEEIAKELESKYEVsvlpLKLDVSDLKSIPGVIESLPKEF 83
Cdd:PRK12481   6 LNGKVAIITGCNTGLGQGMAIGLAKAGADIVGVGVAEAPETQAQVEALGRKFHF----ITADLIQQKDIDSIVSQAVEVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   84 ADIDVLINNAGLALGTDkVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSK-NKGDILNVGSIAgreSYVGG---SVYC 159
Cdd:PRK12481  82 GHIDILINNAGIIRRQD-LLEFGNKDWDDVININQKTVFFLSQAVAKQFVKQgNGGKIINIASML---SFQGGirvPSYT 157
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 19114010  160 STKSALAQFTSALRKETIDTRIRIMEVDPGLVETE 194
Cdd:PRK12481 158 ASKSAVMGLTRALATELSQYNINVNAIAPGYMATD 192
PRK07904 PRK07904
decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;
7-239 8.77e-10

decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;


Pssm-ID: 181162 [Multi-domain]  Cd Length: 253  Bit Score: 57.41  E-value: 8.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    7 KTILITGASSGIGKSTAFEIAKVAKVKLILAARRFSTVEEIA-KELESKYEVSVLPLKLDVSDLKSIPGVIEslpKEFA- 84
Cdd:PRK07904   9 QTILLLGGTSEIGLAICERYLKNAPARVVLAALPDDPRRDAAvAQMKAAGASSVEVIDFDALDTDSHPKVID---AAFAg 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   85 -DIDVLINNAGLaLGTDKVIDLNIDDAVTMITTNVLGmmAMTRAVL--PIFYSKNKGDILNVGSIAGRESYVGGSVYCST 161
Cdd:PRK07904  86 gDVDVAIVAFGL-LGDAEELWQNQRKAVQIAEINYTA--AVSVGVLlgEKMRAQGFGQIIAMSSVAGERVRRSNFVYGST 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  162 KSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVvrfhgDKQKAdnvyknsePLT--PEDIAEVILFALTRRENVVIA 239
Cdd:PRK07904 163 KAGLDGFYLGLGEALREYGVRVLVVRPGQVRTRMSA-----HAKEA--------PLTvdKEDVAKLAVTAVAKGKELVWA 229
PRK07062 PRK07062
SDR family oxidoreductase;
4-193 1.03e-09

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 57.36  E-value: 1.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    4 LDGKTILITGASSGIGKSTA----FEIAKVAkvkliLAARRFSTVEEIAKELESKY-EVSVLPLKLDVSDLKSIPGVIES 78
Cdd:PRK07062   6 LEGRVAVVTGGSSGIGLATVelllEAGASVA-----ICGRDEERLASAEARLREKFpGARLLAARCDVLDEADVAAFAAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   79 LPKEFADIDVLINNAG------LALGTDkvidlniDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGR--- 149
Cdd:PRK07062  81 VEARFGGVDMLVNNAGqgrvstFADTTD-------DAWRDELELKYFSVINPTRAFLPLLRASAAASIVCVNSLLALqpe 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 19114010  150 ESYVGGSvycSTKSALAQFTSALRKETIDTRIRIMEVDPGLVET 193
Cdd:PRK07062 154 PHMVATS---AARAGLLNLVKSLATELAPKGVRVNSILLGLVES 194
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
7-160 1.38e-09

3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other enzymes) catalyzes NADP-dependent sterol C-4 demethylation, as part of steroid biosynthesis. 3-keto reductase is a classical SDR, with a well conserved canonical active site tetrad and fairly well conserved characteristic NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187645 [Multi-domain]  Cd Length: 290  Bit Score: 57.40  E-value: 1.38e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   7 KTILITGASSGIGKSTAF----EIAKVAKVKLILAARRFSTVEEIAKELESKY---EVSVLPLKLDVSDLKSIPGVIESL 79
Cdd:cd08941   2 KVVLVTGANSGLGLAICErllaEDDENPELTLILACRNLQRAEAACRALLASHpdaRVVFDYVLVDLSNMVSVFAAAKEL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  80 PKEFADIDVLINNAGLA-LGTdkvidLNIDDAVTMITTNvlGMMAMTravLPIFYSKNKGdILNVGSIAGRESYvgGSVY 158
Cdd:cd08941  82 KKRYPRLDYLYLNAGIMpNPG-----IDWIGAIKEVLTN--PLFAVT---NPTYKIQAEG-LLSQGDKATEDGL--GEVF 148

                ..
gi 19114010 159 CS 160
Cdd:cd08941 149 QT 150
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
63-228 2.17e-09

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 56.16  E-value: 2.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   63 KLDVSDLKSIPGVIESLPkefADIDVLINNAGLAlgtdkvidlNIDDAVTMITTNVLGMMAMTRAVLPIFysKNKGDILN 142
Cdd:PRK12428  29 QADLGDPASIDAAVAALP---GRIDALFNIAGVP---------GTAPVELVARVNFLGLRHLTEALLPRM--APGGAIVN 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  143 VGSIAGRE---------------SYVGGSVYCS------------TKSALAQFTSALRKETIDTR-IRIMEVDPGLVET- 193
Cdd:PRK12428  95 VASLAGAEwpqrlelhkalaataSFDEGAAWLAahpvalatgyqlSKEALILWTMRQAQPWFGARgIRVNCVAPGPVFTp 174
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 19114010  194 ---EFsvVRFHGDKQKADNVYKNSEPLTPEDIAEVILF 228
Cdd:PRK12428 175 ilgDF--RSMLGQERVDSDAKRMGRPATADEQAAVLVF 210
PRK07889 PRK07889
enoyl-[acyl-carrier-protein] reductase FabI;
1-148 4.41e-09

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 236124 [Multi-domain]  Cd Length: 256  Bit Score: 55.33  E-value: 4.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSgiGKSTAFEIAKVAK---VKLILAA--RRFSTVEEIAKELESKYEVsvlpLKLDVSDLKSIPGV 75
Cdd:PRK07889   2 MGLLEGKRILVTGVIT--DSSIAFHVARVAQeqgAEVVLTGfgRALRLTERIAKRLPEPAPV----LELDVTNEEHLASL 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19114010   76 IESLPKEFADIDVLINNAGLA----LGTdKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFyskNKGdilnvGSIAG 148
Cdd:PRK07889  76 ADRVREHVDGLDGVVHSIGFApqsaLGG-NFLDAPWEDVATALHVSAYSLKSLAKALLPLM---NEG-----GSIVG 143
PRK12747 PRK12747
short chain dehydrogenase; Provisional
4-228 4.62e-09

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 55.47  E-value: 4.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    4 LDGKTILITGASSGIGKSTAFEIAKVAKVKLILAARRFSTVEEIAKELESKYEvSVLPLKLDVSDLKSIPGVIESLPKEF 83
Cdd:PRK12747   2 LKGKVALVTGASRGIGRAIAKRLANDGALVAIHYGNRKEEAEETVYEIQSNGG-SAFSIGANLESLHGVEALYSSLDNEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   84 AD------IDVLINNAGLALG------TDKVIDlniddavTMITTNVLGMMAMTRAVLPIFysKNKGDILNVGSIAGRES 151
Cdd:PRK12747  81 QNrtgstkFDILINNAGIGPGafieetTEQFFD-------RMVSVNAKAPFFIIQQALSRL--RDNSRIINISSAATRIS 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19114010  152 YVGGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGD--KQKADNVYKNSEPLTPEDIAEVILF 228
Cdd:PRK12747 152 LPDFIAYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMNAELLSDPmmKQYATTISAFNRLGEVEDIADTAAF 230
PRK05876 PRK05876
short chain dehydrogenase; Provisional
1-195 6.95e-09

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 54.96  E-value: 6.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFEIAKVAkVKLILAARRFSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLP 80
Cdd:PRK05876   1 MDGFPGRGAVITGGASGIGLATGTEFARRG-ARVVLGDVDKPGLRQAVNHLRAE-GFDVHGVMCDVRHREEVTHLADEAF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   81 KEFADIDVLINNAGLALGtDKVIDLNIDDAVTMITTNVLGMMAMTRAVLP-IFYSKNKGDILNVGSIAGRESYVGGSVYC 159
Cdd:PRK05876  79 RLLGHVDVVFSNAGIVVG-GPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPrLLEQGTGGHVVFTASFAGLVPNAGLGAYG 157
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 19114010  160 STKSALAQFTSALRKETIDTRIRIMEVDPGLVETEF 195
Cdd:PRK05876 158 VAKYGVVGLAETLAREVTADGIGVSVLCPMVVETNL 193
PRK05854 PRK05854
SDR family oxidoreductase;
4-168 8.29e-09

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 55.07  E-value: 8.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    4 LDGKTILITGASSGIGKSTAFEIAkVAKVKLILAARRFSTVEEIAKELESKYEVSVLPLK-LDVSDLKSIPGVIESLPKE 82
Cdd:PRK05854  12 LSGKRAVVTGASDGLGLGLARRLA-AAGAEVILPVRNRAKGEAAVAAIRTAVPDAKLSLRaLDLSSLASVAALGEQLRAE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   83 FADIDVLINNAGLALGTDKviDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSkNKGDILNVGSIAGRE------------ 150
Cdd:PRK05854  91 GRPIHLLINNAGVMTPPER--QTTADGFELQFGTNHLGHFALTAHLLPLLRA-GRARVTSQSSIAARRgainwddlnwer 167
                        170
                 ....*....|....*...
gi 19114010  151 SYVGGSVYCSTKSALAQF 168
Cdd:PRK05854 168 SYAGMRAYSQSKIAVGLF 185
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
1-189 1.29e-08

2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 54.19  E-value: 1.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKST--AF--EIAKVAKVKLilaarrfstVEEIAKELESKYEVSVLPLKLDVSDLKSIPGVI 76
Cdd:PRK06200   1 MGWLHGQVALITGGGSGIGRALveRFlaEGARVAVLER---------SAEKLASLRQRFGDHVLVVEGDVTSYADNQRAV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   77 ESLPKEFADIDVLINNAGLALGTDKVIDL---NIDDAV-TMITTNVLGMMAMTRAVLPIFYsKNKGDILNVGSIAGRESY 152
Cdd:PRK06200  72 DQTVDAFGKLDCFVGNAGIWDYNTSLVDIpaeTLDTAFdEIFNVNVKGYLLGAKAALPALK-ASGGSMIFTLSNSSFYPG 150
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 19114010  153 VGGSVYCSTKSALAQFTSALRKEtIDTRIRIMEVDPG 189
Cdd:PRK06200 151 GGGPLYTASKHAVVGLVRQLAYE-LAPKIRVNGVAPG 186
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
4-194 1.47e-08

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 54.84  E-value: 1.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    4 LDGKTILITGASSGIGKStafeIAKV-----AKVKL--ILAARRfsTVEEIAKELESKyevsvlPLKLDVSDLKSIPGVI 76
Cdd:PRK08261 208 LAGKVALVTGAARGIGAA----IAEVlardgAHVVCldVPAAGE--ALAAVANRVGGT------ALALDITAPDAPARIA 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   77 ESLPKEFADIDVLINNAGLalgT-DKVIdLNID----DAVtmITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRES 151
Cdd:PRK08261 276 EHLAERHGGLDIVVHNAGI---TrDKTL-ANMDearwDSV--LAVNLLAPLRITEALLAAGALGDGGRIVGVSSISGIAG 349
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 19114010  152 YVGGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETE 194
Cdd:PRK08261 350 NRGQTNYAASKAGVIGLVQALAPLLAERGITINAVAPGFIETQ 392
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
9-230 1.79e-08

Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a classical SDR, it contains a glycine-rich motif similar to the canonical motif of the SDR NAD(P)-binding site. However, the typical SDR active site residues are absent in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 52.97  E-value: 1.79e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   9 ILITGASSGIGKSTAFEIAKvaKVKLILAARRfstveeiakeleSKYEVSVlplklDVSDLKSipgvIESLPKEFADIDV 88
Cdd:cd11731   1 IIVIGATGTIGLAVAQLLSA--HGHEVITAGR------------SSGDYQV-----DITDEAS----IKALFEKVGHFDA 57
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  89 LINNAGLALGTdKVIDLNIDDAVTMITTNVLGMMAMTRAVLPifYSKNKGDILNVGSIAGRESYVGGSVYCSTKSALAQF 168
Cdd:cd11731  58 IVSTAGDAEFA-PLAELTDADFQRGLNSKLLGQINLVRHGLP--YLNDGGSITLTSGILAQRPIPGGAAAATVNGALEGF 134
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19114010 169 TSALRKETIDtRIRIMEVDPGLVET--EFSVVRFHGDkqkadnvyknsEPLTPEDIAEVILFAL 230
Cdd:cd11731 135 VRAAAIELPR-GIRINAVSPGVVEEslEAYGDFFPGF-----------EPVPAEDVAKAYVRSV 186
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
6-140 3.37e-08

UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; UDP-Glcnac inverting 4,6-dehydratase was identified in Helicobacter pylori as the hexameric flaA1 gene product (FlaA1). FlaA1 is hexameric, possesses UDP-GlcNAc-inverting 4,6-dehydratase activity, and catalyzes the first step in the creation of a pseudaminic acid derivative in protein glycosylation. Although this subgroup has the NADP-binding motif characteristic of extended SDRs, its members tend to have a Met substituted for the active site Tyr found in most SDR families. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187548 [Multi-domain]  Cd Length: 287  Bit Score: 53.01  E-value: 3.37e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   6 GKTILITGASSGIGKSTAFEIAKVAKVKLILAARRFSTVEEIAKELESKY-EVSVLPLKLDVSDLKSIPGVIeslpkEFA 84
Cdd:cd05237   2 GKTILVTGGAGSIGSELVRQILKFGPKKLIVFDRDENKLHELVRELRSRFpHDKLRFIIGDVRDKERLRRAF-----KER 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  85 DIDVLINNAGL-----------------ALGTDKVIDLNIDDAVT---MITT----NVLGMMAMTRAV---LPIFYSKNK 137
Cdd:cd05237  77 GPDIVFHAAALkhvpsmednpeeaiktnVLGTKNVIDAAIENGVEkfvCISTdkavNPVNVMGATKRVaekLLLAKNEYS 156

                ...
gi 19114010 138 GDI 140
Cdd:cd05237 157 SST 159
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
8-224 4.00e-08

classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an incomplete match to the canonical glycine rich NAD-binding motif and lacks the typical active site tetrad (instead of the critical active site Tyr, it has Phe, but contains the nearby Lys). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187631 [Multi-domain]  Cd Length: 238  Bit Score: 52.38  E-value: 4.00e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   8 TILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKYEVSVLPLKLDVSDLKSIPGVIESLPKEFADID 87
Cdd:cd05373   1 VAAVVGAGDGLGAAIARRFAA-EGFSVALAARREAKLEALLVDIIRDAGGSAKAVPTDARDEDEVIALFDLIEEEIGPLE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  88 VLINNAGlALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSALAQ 167
Cdd:cd05373  80 VLVYNAG-ANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASLRGRAGFAAFAGAKFALRA 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19114010 168 FTSALRKETIDTRIRIMEV--DpGLVETEFSVVRFhgdkqkaDNVYKNSEP---LTPEDIAE 224
Cdd:cd05373 159 LAQSMARELGPKGIHVAHViiD-GGIDTDFIRERF-------PKRDERKEEdgiLDPDAIAE 212
LPOR COG5748
Light-dependent NADPH-protochlorophyllide oxidoreductase [Coenzyme transport and metabolism];
1-130 5.52e-08

Light-dependent NADPH-protochlorophyllide oxidoreductase [Coenzyme transport and metabolism];


Pssm-ID: 444458 [Multi-domain]  Cd Length: 324  Bit Score: 52.69  E-value: 5.52e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   1 MSRLDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKEL-ESKYEVSVLPlkLDVSDLKSIPGVIESL 79
Cdd:COG5748   1 MSQDQKSTVIITGASSGVGLYAAKALAD-RGWHVIMACRDLEKAEAAAQELgIPPDSYTIIH--IDLASLESVRRFVADF 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 19114010  80 PKEFADIDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLP 130
Cdd:COG5748  78 RALGRPLDALVCNAAVYYPLLKEPLRSPDGYELSVATNHLGHFLLCNLLLE 128
PRK05717 PRK05717
SDR family oxidoreductase;
5-244 6.81e-08

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 52.20  E-value: 6.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    5 DGKTILITGASSGIGKS-TAFEIAKVAKVKLI-LAARRFSTVEEIAKEleskyevSVLPLKLDVSDLKSIP-GVIESLpK 81
Cdd:PRK05717   9 NGRVALVTGAARGIGLGiAAWLIAEGWQVVLAdLDRERGSKVAKALGE-------NAWFIAMDVADEAQVAaGVAEVL-G 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   82 EFADIDVLINNAGLALGTDKVID-LNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNkGDILNVGSIAGRESYVGGSVYCS 160
Cdd:PRK05717  81 QFGRLDALVCNAAIADPHNTTLEsLSLAHWNRVLAVNLTGPMLLAKHCAPYLRAHN-GAIVNLASTRARQSEPDTEAYAA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  161 TKSALAQFTSALrKETIDTRIRIMEVDPGLVETEFSVVRFHGDKQKADNVYKNSEPL-TPEDIAEVILFALTRRENVVIA 239
Cdd:PRK05717 160 SKGGLLALTHAL-AISLGPEIRVNAVSPGWIDARDPSQRRAEPLSEADHAQHPAGRVgTVEDVAAMVAWLLSRQAGFVTG 238

                 ....*
gi 19114010  240 DTLVF 244
Cdd:PRK05717 239 QEFVV 243
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
6-95 7.83e-08

human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like SDR domain of human WWOX and related proteins. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 52.21  E-value: 7.83e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   6 GKTILITGASSGIGKSTAFEIAkVAKVKLILAARRFS----TVEEIAKELeSKYEVSVLPlkLDVSDLKSIPGVIESLPK 81
Cdd:cd09809   1 GKVIIITGANSGIGFETARSFA-LHGAHVILACRNMSrasaAVSRILEEW-HKARVEAMT--LDLASLRSVQRFAEAFKA 76
                        90
                ....*....|....
gi 19114010  82 EFADIDVLINNAGL 95
Cdd:cd09809  77 KNSPLHVLVCNAAV 90
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
6-189 9.76e-08

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 51.57  E-value: 9.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    6 GKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKY-EVSVLPLKLDVSDLKSIPGVIESLPKEFA 84
Cdd:PRK12384   2 NQVAVVIGGGQTLGAFLCHGLAE-EGYRVAVADINSEKAANVAQEINAEYgEGMAYGFGADATSEQSVLALSRGVDEIFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   85 DIDVLINNAGLALGTdKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKN-KGDILNVGSIAGRESYVGGSVYCSTKS 163
Cdd:PRK12384  81 RVDLLVYNAGIAKAA-FITDFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDGiQGRIIQINSKSGKVGSKHNSGYSAAKF 159
                        170       180
                 ....*....|....*....|....*.
gi 19114010  164 ALAQFTSALRKETIDTRIRIMEVDPG 189
Cdd:PRK12384 160 GGVGLTQSLALDLAEYGITVHSLMLG 185
PRK08703 PRK08703
SDR family oxidoreductase;
1-169 1.47e-07

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 51.09  E-value: 1.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFEIAKVAKVkLILAARRfstveeiAKELESKY---------EVSVLPLKLDVSDLKS 71
Cdd:PRK08703   1 MATLSDKTILVTGASQGLGEQVAKAYAAAGAT-VILVARH-------QKKLEKVYdaiveaghpEPFAIRFDLMSAEEKE 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   72 IPGVIESLPKEF-ADIDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGR- 149
Cdd:PRK08703  73 FEQFAATIAEATqGKLDGIVHCAGYFYALSPLDFQTVAEWVNQYRINTVAPMGLTRALFPLLKQSPDASVIFVGESHGEt 152
                        170       180
                 ....*....|....*....|.
gi 19114010  150 -ESYVGGsvYCSTKSALAQFT 169
Cdd:PRK08703 153 pKAYWGG--FGASKAALNYLC 171
PRK07806 PRK07806
SDR family oxidoreductase;
1-128 1.91e-07

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 50.49  E-value: 1.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGkstafeiAKVAKvklILAARRFSTV----------EEIAKELESKyEVSVLPLKLDVSDLK 70
Cdd:PRK07806   1 MGDLPGKTALVTGSSRGIG-------ADTAK---ILAGAGAHVVvnyrqkapraNKVVAEIEAA-GGRASAVGADLTDEE 69
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19114010   71 SIPGVIESLPKEFADIDVLINNAG----LALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAV 128
Cdd:PRK07806  70 SVAALMDTAREEFGGLDALVLNASggmeSGMDEDYAMRLNRDAQRNLARAALPLMPAGSRVV 131
PRK06057 PRK06057
short chain dehydrogenase; Provisional
3-207 1.93e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 50.88  E-value: 1.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    3 RLDGKTILITGASSGIGKSTAFEIAKVAkVKLILAARRFSTVEEIAKeleskyEVSVLPLKLDVSDLKSIPGVIESLPKE 82
Cdd:PRK06057   4 RLAGRVAVITGGGSGIGLATARRLAAEG-ATVVVGDIDPEAGKAAAD------EVGGLFVPTDVTDEDAVNALFDTAAET 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   83 FADIDVLINNAGLALGTDKVI-DLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGresyVGGSV---- 157
Cdd:PRK06057  77 YGSVDIAFNNAGISPPEDDSIlNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASFVA----VMGSAtsqi 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 19114010  158 -YCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGDKQKA 207
Cdd:PRK06057 153 sYTASKGGVLAMSRELGVQFARQGIRVNALCPGPVNTPLLQELFAKDPERA 203
PRK06953 PRK06953
SDR family oxidoreductase;
7-194 2.06e-07

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 50.46  E-value: 2.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    7 KTILITGASSGIGKSTAFEIAKvAKVKLILAARRfstvEEIAKELEskyEVSVLPLKLDVSDLKSIPGVIESLPKEfaDI 86
Cdd:PRK06953   2 KTVLIVGASRGIGREFVRQYRA-DGWRVIATARD----AAALAALQ---ALGAEALALDVADPASVAGLAWKLDGE--AL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   87 DVLINNAGLALG-TDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPifYSKNKGDILNV-----GSIAGRESyVGGSVYCS 160
Cdd:PRK06953  72 DAAVYVAGVYGPrTEGVEPITREDFDAVMHTNVLGPMQLLPILLP--LVEAAGGVLAVlssrmGSIGDATG-TTGWLYRA 148
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 19114010  161 TKSALaqfTSALRKETIDTRIRI-MEVDPGLVETE 194
Cdd:PRK06953 149 SKAAL---NDALRAASLQARHATcIALHPGWVRTD 180
PRK08416 PRK08416
enoyl-ACP reductase;
1-93 4.68e-07

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 49.77  E-value: 4.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFEIAKVAKVKLILAARRFSTVEEIAKELESKYEVSVLPLKLDVSDLKSIPGVIESLP 80
Cdd:PRK08416   3 SNEMKGKTLVISGGTRGIGKAIVYEFAQSGVNIAFTYNSNVEEANKIAEDLEQKYGIKAKAYPLNILEPETYKELFKKID 82
                         90
                 ....*....|...
gi 19114010   81 KEFADIDVLINNA 93
Cdd:PRK08416  83 EDFDRVDFFISNA 95
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
6-228 7.68e-07

Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate dehydrogenase (SDH, aka glucitol 6-phosphate dehydrogenase) catalyzes the NAD-dependent interconversion of D-fructose 6-phosphate to D-sorbitol 6-phosphate. SDH is a member of the classical SDRs, with the characteristic catalytic tetrad, but without a complete match to the typical NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187583 [Multi-domain]  Cd Length: 257  Bit Score: 49.00  E-value: 7.68e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   6 GKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKYEVSVLPLKLDVSDLKSIPGVIESLPKEFAD 85
Cdd:cd05322   2 NQVAVVIGGGQTLGEFLCHGLAE-AGYDVAVADINSENAEKVADEINAEYGEKAYGFGADATNEQSVIALSKGVDEIFKR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  86 IDVLINNAGLALgTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKN-KGDILNVGSIAGRESYVGGSVYCSTKSA 164
Cdd:cd05322  81 VDLLVYSAGIAK-SAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDGiQGRIIQINSKSGKVGSKHNSGYSAAKFG 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19114010 165 LAQFTSALRKETIDTRIRIMEVDPG-LVETEF-------SVVRFHGDKQKADNVYKNSEPL----TPEDIAEVILF 228
Cdd:cd05322 160 GVGLTQSLALDLAEHGITVNSLMLGnLLKSPMfqsllpqYAKKLGIKESEVEQYYIDKVPLkrgcDYQDVLNMLLF 235
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
5-128 8.46e-07

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 49.29  E-value: 8.46e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   5 DGKTILITGASSGIGKSTAFEIAKVAKVKLILAARR-FSTVEEIAKELESKYE---VSVLPLKLDVSDLKSIPGVIESLP 80
Cdd:cd08953 204 PGGVYLVTGGAGGIGRALARALARRYGARLVLLGRSpLPPEEEWKAQTLAALEalgARVLYISADVTDAAAVRRLLEKVR 283
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 19114010  81 KEFADIDVLINNAGlALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAV 128
Cdd:cd08953 284 ERYGAIDGVIHAAG-VLRDALLAQKTAEDFEAVLAPKVDGLLNLAQAL 330
PRK07069 PRK07069
short chain dehydrogenase; Validated
10-193 2.85e-06

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 47.01  E-value: 2.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   10 LITGASSGIGKSTAFEIAKV-AKVKLILAARrFSTVEEIAKELESKYEVSV-LPLKLDVSDLKSIPGVIESLPKEFADID 87
Cdd:PRK07069   3 FITGAAGGLGRAIARRMAEQgAKVFLTDIND-AAGLDAFAAEINAAHGEGVaFAAVQDVTDEAQWQALLAQAADAMGGLS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   88 VLINNAGLALGTDkVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSALAQ 167
Cdd:PRK07069  82 VLVNNAGVGSFGA-IEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKAEPDYTAYNASKAAVAS 160
                        170       180
                 ....*....|....*....|....*...
gi 19114010  168 FTS--ALRKETIDTRIRIMEVDPGLVET 193
Cdd:PRK07069 161 LTKsiALDCARRGLDVRCNSIHPTFIRT 188
PRK05875 PRK05875
short chain dehydrogenase; Provisional
4-231 5.44e-06

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 46.33  E-value: 5.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    4 LDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKY---EVSVLPlkLDVSDLKSIPGVIESLP 80
Cdd:PRK05875   5 FQDRTYLVTGGGSGIGKGVAAGLVA-AGAAVMIVGRNPDKLAAAAEEIEALKgagAVRYEP--ADVTDEDQVARAVDAAT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   81 KEFADIDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCS 160
Cdd:PRK05875  82 AWHGRLHGVVHCAGGSETIGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGISSIAASNTHRWFGAYGV 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19114010  161 TKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGDKQKADnvYKNSEPLTP----EDIAEVILFALT 231
Cdd:PRK05875 162 TKSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDLVAPITESPELSAD--YRACTPLPRvgevEDVANLAMFLLS 234
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
4-90 5.56e-06

Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl-[acyl-carrier-protein] reductase FabI is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440388 [Multi-domain]  Cd Length: 254  Bit Score: 46.17  E-value: 5.56e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   4 LDGKTILITGASSgiGKSTAFEIAKVAK---VKLIL-----AARRFstVEEIAKELESKYevsVLPlkLDVSDLKSIPGV 75
Cdd:COG0623   3 LKGKRGLITGVAN--DRSIAWGIAKALHeegAELAFtyqgeALKKR--VEPLAEELGSAL---VLP--CDVTDDEQIDAL 73
                        90
                ....*....|....*
gi 19114010  76 IESLPKEFADIDVLI 90
Cdd:COG0623  74 FDEIKEKWGKLDFLV 88
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
6-229 7.72e-06

SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are putative oxidoreductases belonging to the larger SDR family. All members occur in genomes that encode a cassette for the biosynthesis of mycofactocin, a proposed electron carrier of a novel redox pool. Characterized members of this family are described as NDMA-dependent, meaning that a blue aniline dye serving as an artificial electron acceptor is required for members of this family to cycle in vitro, since the bound NAD residue is not exchangeable. This family resembles TIGR03971 most closely in the N-terminal region, consistent with the published hypothesis of NAD interaction with mycofactocin. See EC 1.1.99.36. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275297 [Multi-domain]  Cd Length: 259  Bit Score: 45.78  E-value: 7.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010     6 GKTILITGASSGIGKSTAFEIAKvAKVKLILAAR---------RFSTVEEIAkELESKYEVSVLPLKLDVSDLKSIPGVI 76
Cdd:TIGR04504   1 GRVALVTGAARGIGAATVRRLAA-DGWRVVAVDLcaddpavgyPLATRAELD-AVAAACPDQVLPVIADVRDPAALAAAV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    77 ESLPKEFADIDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNK---GDILNVGSIAGRESYV 153
Cdd:TIGR04504  79 ALAVERWGRLDAAVAAAGVIAGGRPLWETTDAELDLLLDVNLRGVWNLARAAVPAMLARPDprgGRFVAVASAAATRGLP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   154 GGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEF-----------SVVRFhGDKQKADnvyknsEPLTPEDI 222
Cdd:TIGR04504 159 HLAAYCAAKHAVVGLVRGLAADLGGTGVTANAVSPGSTRTAMlaatarlygltDVEEF-AGHQLLG------RLLEPEEV 231

                  ....*..
gi 19114010   223 AEVILFA 229
Cdd:TIGR04504 232 AAAVAWL 238
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
8-120 9.11e-06

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 44.86  E-value: 9.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010     8 TILITGASSGIGKSTAFEIAKVAKVKLILAARRFST---VEEIAKELESkYEVSVLPLKLDVSDLKSIPGVIESLPKEFA 84
Cdd:pfam08659   2 TYLITGGLGGLGRELARWLAERGARHLVLLSRSAAPrpdAQALIAELEA-RGVEVVVVACDVSDPDAVAALLAEIKAEGP 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 19114010    85 DIDVLINNAGlALGTDKVIDLNIDDAVTMITTNVLG 120
Cdd:pfam08659  81 PIRGVIHAAG-VLRDALLENMTDEDWRRVLAPKVTG 115
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
4-158 1.11e-05

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 45.50  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    4 LDGKTILITGASSGigKSTAFEIAKVAKVKLILAARRF------STVEEIAKELESKYevsVLPLklDVSDLKSIPGVIE 77
Cdd:PRK08415   3 MKGKKGLIVGVANN--KSIAYGIAKACFEQGAELAFTYlnealkKRVEPIAQELGSDY---VYEL--DVSKPEHFKSLAE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   78 SLPKEFADIDVLINNAGLALG---TDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFysKNKGDILNVgsiagreSYVG 154
Cdd:PRK08415  76 SLKKDLGKIDFIVHSVAFAPKealEGSFLETSKEAFNIAMEISVYSLIELTRALLPLL--NDGASVLTL-------SYLG 146

                 ....
gi 19114010  155 GSVY 158
Cdd:PRK08415 147 GVKY 150
PRK07576 PRK07576
short chain dehydrogenase; Provisional
1-228 1.13e-05

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 45.33  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVIESLP 80
Cdd:PRK07576   4 MFDFAGKNVVVVGGTSGINLGIAQAFAR-AGANVAVASRSQEKVDAAVAQLQQA-GPEGLGVSADVRDYAAVEAAFAQIA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   81 KEFADIDVLINNAG---LALgtdkVIDLNIDDAVTMITTNVLGMMAMTRAVLPiFYSKNKGDILNvgsIAGRESYV---G 154
Cdd:PRK07576  82 DEFGPIDVLVSGAAgnfPAP----AAGMSANGFKTVVDIDLLGTFNVLKAAYP-LLRRPGASIIQ---ISAPQAFVpmpM 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  155 GSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVE-TE-FSVVRFHGDKQKAdnvYKNSEPL----TPEDIAEVILF 228
Cdd:PRK07576 154 QAHVCAAKAGVDMLTRTLALEWGPEGIRVNSIVPGPIAgTEgMARLAPSPELQAA---VAQSVPLkrngTKQDIANAALF 230
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
4-173 2.59e-05

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 44.77  E-value: 2.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    4 LDGKTILITGASSGIGKSTAFEIAKVAK---VKLILAARRFSTVEEIAKELESKYEVSVlplkLDVSDLKSIPGVIEsLP 80
Cdd:PRK07792  10 LSGKVAVVTGAAAGLGRAEALGLARLGAtvvVNDVASALDASDVLDEIRAAGAKAVAVA----GDISQRATADELVA-TA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   81 KEFADIDVLINNAGLAlgTDKVI-DLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNK-------GDILNVGSIAGRESY 152
Cdd:PRK07792  85 VGLGGLDIVVNNAGIT--RDRMLfNMSDEEWDAVIAVHLRGHFLLTRNAAAYWRAKAKaaggpvyGRIVNTSSEAGLVGP 162
                        170       180
                 ....*....|....*....|..
gi 19114010  153 VGGSVYCSTKSALAQFT-SALR 173
Cdd:PRK07792 163 VGQANYGAAKAGITALTlSAAR 184
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
6-165 3.74e-05

Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ENRs includes Escherichia coli ENR. ENR catalyzes the NAD(P)H-dependent reduction of enoyl-ACP in the last step of fatty acid biosynthesis. De novo fatty acid biosynthesis is catalyzed by the fatty acid synthetase complex, through the serial addition of 2-carbon subunits. In bacteria and plants,ENR catalyzes one of six synthetic steps in this process. Oilseed rape ENR, and also apparently the NADH-specific form of Escherichia coli ENR, is tetrameric. Although similar to the classical SDRs, this group does not have the canonical catalytic tetrad, nor does it have the typical Gly-rich NAD-binding pattern. Such so-called divergent SDRs have a GXXXXXSXA NAD-binding motif and a YXXMXXXK (or YXXXMXXXK) active site motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187630 [Multi-domain]  Cd Length: 250  Bit Score: 43.72  E-value: 3.74e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   6 GKTILITGASSGigKSTAFEIAKVAK---VKLIL---AARRFSTVEEIAKELESKYEVsvlpLKLDVSDLKSIPGVIESL 79
Cdd:cd05372   1 GKRILITGIAND--RSIAWGIAKALHeagAELAFtyqPEALRKRVEKLAERLGESALV----LPCDVSNDEEIKELFAEV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  80 PKEFADIDVLINNAGLALGTDKV---IDLNIDDAVTMITTNVLGMMAMTRAVLPIFysKNKGDILNVGSIAGRESYVGGS 156
Cdd:cd05372  75 KKDWGKLDGLVHSIAFAPKVQLKgpfLDTSRKGFLKALDISAYSLVSLAKAALPIM--NPGGSIVTLSYLGSERVVPGYN 152

                ....*....
gi 19114010 157 VYCSTKSAL 165
Cdd:cd05372 153 VMGVAKAAL 161
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
72-233 9.26e-05

haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. Haloalcohol dehalogenase show low sequence similarity to short-chain dehydrogenases/reductases (SDRs). Like the SDRs, haloalcohol dehalogenases have a conserved catalytic triad (Ser-Tyr-Lys/Arg), and form a Rossmann fold. However, the normal classical SDR NAD(P)-binding motif (TGXXGXG) and NAD-binding function is replaced with a halide binding site, allowing the enzyme to catalyze a dehalogenation reaction. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 42.56  E-value: 9.26e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  72 IPGVI---ESLPKEFAD--------IDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDI 140
Cdd:cd05361  48 NPGTKalsEQKPEELVDavlqaggaIDVLVSNDYIPRPMNPIDGTSEADIRQAFEALSIFPFALLQAAIAQMKKAGGGSI 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010 141 LNVGSIAGRESYVGGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETE--FSVVRFHGDKQKADNVYKNSePL- 217
Cdd:cd05361 128 IFITSAVPKKPLAYNSLYGPARAAAVALAESLAKELSRDNILVYAIGPNFFNSPtyFPTSDWENNPELRERVKRDV-PLg 206
                       170
                ....*....|....*....
gi 19114010 218 ---TPEDIAEVILFALTRR 233
Cdd:cd05361 207 rlgRPDEMGALVAFLASRR 225
PRK12744 PRK12744
SDR family oxidoreductase;
1-231 9.45e-05

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 42.80  E-value: 9.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSGIG----KSTAFEIAKVAKVKLILAARRfSTVEEIAKELESKyEVSVLPLKLDVSDLKSIPGVI 76
Cdd:PRK12744   3 DHSLKGKVVLIAGGAKNLGgliaRDLAAQGAKAVAIHYNSAASK-ADAEETVAAVKAA-GAKAVAFQADLTTAAAVEKLF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   77 ESLPKEFADIDVLINNAGlalgtdKVIDLNIDDavtmITTNVLGMMAMTRAVLPIFYSKNKGDILN--------VGSIAG 148
Cdd:PRK12744  81 DDAKAAFGRPDIAINTVG------KVLKKPIVE----ISEAEYDEMFAVNSKSAFFFIKEAGRHLNdngkivtlVTSLLG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  149 reSYVGG-SVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEF-------SVVRFHgdKQKADNVYKNSEPLT-P 219
Cdd:PRK12744 151 --AFTPFySAYAGSKAPVEHFTRAASKEFGARGISVTAVGPGPMDTPFfypqegaEAVAYH--KTAAALSPFSKTGLTdI 226
                        250
                 ....*....|..
gi 19114010  220 EDIAEVILFALT 231
Cdd:PRK12744 227 EDIVPFIRFLVT 238
PRK08862 PRK08862
SDR family oxidoreductase;
8-215 1.37e-04

SDR family oxidoreductase;


Pssm-ID: 236342 [Multi-domain]  Cd Length: 227  Bit Score: 42.02  E-value: 1.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    8 TILITGASSGIGKSTAFEIAKVAkVKLILAARRFSTVEEIAKELeSKYEVSVLPLKLDVSDLKSIPGVIESLPKEF-ADI 86
Cdd:PRK08862   7 IILITSAGSVLGRTISCHFARLG-ATLILCDQDQSALKDTYEQC-SALTDNVYSFQLKDFSQESIRHLFDAIEQQFnRAP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   87 DVLINN---AGL-ALGTDKVIDLNIDDAVTMITT-NVLGMMAMTRavlpiFYSKN-KGDILNVGSIAGRESYVGGSvycS 160
Cdd:PRK08862  85 DVLVNNwtsSPLpSLFDEQPSESFIQQLSSLASTlFTYGQVAAER-----MRKRNkKGVIVNVISHDDHQDLTGVE---S 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 19114010  161 TKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGdKQKADNVYKNSE 215
Cdd:PRK08862 157 SNALVSGFTHSWAKELTPFNIRVGGVVPSIFSANGELDAVHW-AEIQDELIRNTE 210
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
7-94 1.51e-04

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 41.31  E-value: 1.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010      7 KTILITGASSGIGKSTAFEIAKVAKVKLILAARR---FSTVEEIAKELESkYEVSVLPLKLDVSDLKSIPGVIESLPKEF 83
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGARRLVLLSRSgpdAPGAAALLAELEA-AGARVTVVACDVADRDALAAVLAAIPAVE 79
                           90
                   ....*....|.
gi 19114010     84 ADIDVLINNAG 94
Cdd:smart00822  80 GPLTGVIHAAG 90
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
10-242 2.00e-04

pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including Trypanosoma cruzi and Leishmania major) to obtain reduced pteridines by salvage rather than biosynthetic pathways. Enzymes in T. cruzi described as pteridine reductase 1 (PTR1) and pteridine reductase 2 (PTR2) have different activity profiles. PTR1 is more active with with fully oxidized biopterin and folate than with reduced forms, while PTR2 reduces dihydrobiopterin and dihydrofolate but not oxidized pteridines. T. cruzi PTR1 and PTR2 are more similar to each other in sequence than either is to the pteridine reductase of Leishmania major, and all are included in this family.


Pssm-ID: 131732 [Multi-domain]  Cd Length: 267  Bit Score: 41.84  E-value: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    10 LITGASSGIGKSTAFEIAKVAKVKLILAARRFSTVEEIAKELESKYEVSVLPLKLDVSDLKSIPG----VIESLPKEFAD 85
Cdd:TIGR02685   5 VVTGAAKRIGSSIAVALHQEGYRVVLHYHRSAAAASTLAAELNARRPNSAVTCQADLSNSATLFSrceaIIDACFRAFGR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    86 IDVLINNA-------------GLALGTDKVIDLNIDDavtMITTNVLGMMAMTRAvlpiFYSKNKGD----------ILN 142
Cdd:TIGR02685  85 CDVLVNNAsafyptpllrgdaGEGVGDKKSLEVQVAE---LFGSNAIAPYFLIKA----FAQRQAGTraeqrstnlsIVN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   143 VGSIAGRESYVGGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLvetefSVVRFHGDKQKADNvYKNSEPL----- 217
Cdd:TIGR02685 158 LCDAMTDQPLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGL-----SLLPDAMPFEVQED-YRRKVPLgqrea 231
                         250       260
                  ....*....|....*....|....*
gi 19114010   218 TPEDIAEVILFALTRRENVVIADTL 242
Cdd:TIGR02685 232 SAEQIADVVIFLVSPKAKYITGTCI 256
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
8-127 3.67e-04

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 41.12  E-value: 3.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   8 TILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELeskyevSVLPLKLDVSDLksipgviESLPKEFADID 87
Cdd:COG0451   1 RILVTGGAGFIGSHLARRLLA-RGHEVVGLDRSPPGAANLAALP------GVEFVRGDLRDP-------EALAAALAGVD 66
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 19114010  88 VLINNAGLAlgtdkviDLNIDDAVTMITTNVLGMMAMTRA 127
Cdd:COG0451  67 AVVHLAAPA-------GVGEEDPDETLEVNVEGTLNLLEA 99
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
4-244 4.02e-04

Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase [Carbohydrate transport and metabolism];


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 41.44  E-value: 4.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   4 LDGKTILITGASSGIGKSTAFEIAKV-AKVklILAARRFSTVEEIAKELESKY-EVSVLPLKLDVSDLKSIPGVIESLPK 81
Cdd:COG3347 423 LAGRVALVTGGAGGIGRATAARLAAEgAAV--VVADLDGEAAEAAAAELGGGYgADAVDATDVDVTAEAAVAAAFGFAGL 500
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  82 EFADIDVLINNAGLALG---TDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGreSYVGGSvY 158
Cdd:COG3347 501 DIGGSDIGVANAGIASSspeEETRLSFWLNNFAHLSTGQFLVARAAFQGTGGQGLGGSSVFAVSKNAAAA--AYGAAA-A 577
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010 159 CSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGDKQKADnvYKNSEPLTPEDIAEVILFALTRRENVVI 238
Cdd:COG3347 578 ATAKAAAQHLLRALAAEGGANGINANRVNPDAVLDGSAIWASAARAERAA--AYGIGNLLLEEVYRKRVALAVLVLAEDI 655

                ....*.
gi 19114010 239 ADTLVF 244
Cdd:COG3347 656 AEAAAF 661
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
7-196 1.07e-03

daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically important therapeutic compound used in some cancer treatments. Daunorubicin C-13 ketoreductase is member of the classical SDR family with a canonical glycine-rich NAD(P)-binding motif, but lacking a complete match to the active site tetrad characteristic of this group. The critical Tyr, plus the Lys and upstream Asn are present, but the catalytic Ser is replaced, generally by Gln. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 39.40  E-value: 1.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   7 KTILITGASSGIGKSTAFE-IAKVAKVklILAARRFSTVEEIAKELESKYEVSVlplkLDVSDLKSIPGVIESLpKEFAD 85
Cdd:cd08951   8 KRIFITGSSDGLGLAAARTlLHQGHEV--VLHARSQKRAADAKAACPGAAGVLI----GDLSSLAETRKLADQV-NAIGR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  86 IDVLINNAGLALGTD-KVIDlniDDAVTMITTNVLGMMAMTRAVLP----IFYSKN--KGDILNVGSI-AGRESYVGGSV 157
Cdd:cd08951  81 FDAVIHNAGILSGPNrKTPD---TGIPAMVAVNVLAPYVLTALIRRpkrlIYLSSGmhRGGNASLDDIdWFNRGENDSPA 157
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 19114010 158 YCSTKSALAQFTSALRKETIDTRIRimEVDPGLVETEFS 196
Cdd:cd08951 158 YSDSKLHVLTLAAAVARRWKDVSSN--AVHPGWVPTKMG 194
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
6-231 1.25e-03

dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an NAD-binding protein related to the SDRs. It converts dihydrobiopterin into tetrahydrobiopterin, a cofactor necessary in catecholamines synthesis. Dihydropteridine reductase has the YXXXK of these tyrosine-dependent oxidoreductases, but lacks the typical upstream Asn and Ser catalytic residues. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 39.23  E-value: 1.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   6 GKTILITGASSGIGKSTAfeiAKVAKVKLILAARRFSTVEEiakeleSKYEVSVLPLKLDVSDLKSipgVIESLPKEFAD 85
Cdd:cd05334   1 ARVVLVYGGRGALGSAVV---QAFKSRGWWVASIDLAENEE------ADASIIVLDSDSFTEQAKQ---VVASVARLSGK 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010  86 IDVLINNAG-LALGTDKVIDL--NIDdavTMITTNVLGMMAMTRAVLPifYSKNKGDILNVGSIAGRESYVGGSVYCSTK 162
Cdd:cd05334  69 VDALICVAGgWAGGSAKSKSFvkNWD---LMWKQNLWTSFIASHLATK--HLLSGGLLVLTGAKAALEPTPGMIGYGAAK 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19114010 163 SALAQFTSALRKETIDTR--IRIMEVDPGLVETEfsvvrfhGDKQ---KADnvykNSEPLTPEDIAEVILFALT 231
Cdd:cd05334 144 AAVHQLTQSLAAENSGLPagSTANAILPVTLDTP-------ANRKampDAD----FSSWTPLEFIAELILFWAS 206
PRK08340 PRK08340
SDR family oxidoreductase;
9-94 1.59e-03

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 39.02  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    9 ILITGASSGIGKSTAFEIAKVAKvKLILAARRFSTVEEIAKELESKYEVSvlPLKLDVSDLKSIPGVIESLPKEFADIDV 88
Cdd:PRK08340   3 VLVTASSRGIGFNVARELLKKGA-RVVISSRNEENLEKALKELKEYGEVY--AVKADLSDKDDLKNLVKEAWELLGGIDA 79

                 ....*.
gi 19114010   89 LINNAG 94
Cdd:PRK08340  80 LVWNAG 85
PRK08177 PRK08177
SDR family oxidoreductase;
7-194 1.97e-03

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 38.47  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    7 KTILITGASSGIGKSTAFEIAKVakvklilAARRFSTVEEIAKE--LESKYEVSVlpLKLDVSDLKSIPGVIESLPKEfa 84
Cdd:PRK08177   2 RTALIIGASRGLGLGLVDRLLER-------GWQVTATVRGPQQDtaLQALPGVHI--EKLDMNDPASLDQLLQRLQGQ-- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   85 DIDVLINNAGLAlGTDkvidlniDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGS-IAGRESYVGGSV------ 157
Cdd:PRK08177  71 RFDLLFVNAGIS-GPA-------HQSAADATAAEIGQLFLTNAIAPIRLARRLLGQVRPGQgVLAFMSSQLGSVelpdgg 142
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 19114010  158 ----YCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETE 194
Cdd:PRK08177 143 emplYKASKAALNSMTRSFVAELGEPTLTVLSMHPGWVKTD 183
PRK07984 PRK07984
enoyl-ACP reductase FabI;
1-112 3.99e-03

enoyl-ACP reductase FabI;


Pssm-ID: 181187 [Multi-domain]  Cd Length: 262  Bit Score: 37.96  E-value: 3.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASS------GIGKSTAFEIAKVA------KVKlilaarrfSTVEEIAKELESKYevsVLPlkLDVSD 68
Cdd:PRK07984   1 MGFLSGKRILVTGVASklsiayGIAQAMHREGAELAftyqndKLK--------GRVEEFAAQLGSDI---VLP--CDVAE 67
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 19114010   69 LKSIPGVIESLPKEFADIDVLINNAGLALGTDkvIDLNIDDAVT 112
Cdd:PRK07984  68 DASIDAMFAELGKVWPKFDGFVHSIGFAPGDQ--LDGDYVNAVT 109
PRK06997 PRK06997
enoyl-[acyl-carrier-protein] reductase FabI;
1-96 6.42e-03

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 180789 [Multi-domain]  Cd Length: 260  Bit Score: 37.11  E-value: 6.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    1 MSRLDGKTILITGASSgiGKSTAFEIAKV-----AKVKLILAARRFST-VEEIAKELESKyevsvLPLKLDVSDLKSIPG 74
Cdd:PRK06997   1 MGFLAGKRILITGLLS--NRSIAYGIAKAckregAELAFTYVGDRFKDrITEFAAEFGSD-----LVFPCDVASDEQIDA 73
                         90       100
                 ....*....|....*....|..
gi 19114010   75 VIESLPKEFADIDVLINNAGLA 96
Cdd:PRK06997  74 LFASLGQHWDGLDGLVHSIGFA 95
PRK08339 PRK08339
short chain dehydrogenase; Provisional
4-206 9.10e-03

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 36.76  E-value: 9.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010    4 LDGKTILITGASSGIGKSTAFEIAKvAKVKLILAARRFSTVEEIAKELESKYEVSVLPLKLDVSDLKSIPGVIESLpKEF 83
Cdd:PRK08339   6 LSGKLAFTTASSKGIGFGVARVLAR-AGADVILLSRNEENLKKAREKIKSESNVDVSYIVADLTKREDLERTVKEL-KNI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114010   84 ADIDVLINNAGlALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKS 163
Cdd:PRK08339  84 GEPDIFFFSTG-GPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSVAIKEPIPNIALSNVVRI 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 19114010  164 ALAQFTSALRKETIDTRIRIMEVDPGLVETEfSVVRFHGDKQK 206
Cdd:PRK08339 163 SMAGLVRTLAKELGPKGITVNGIMPGIIRTD-RVIQLAQDRAK 204
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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