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Conserved domains on  [gi|18413950|ref|NP_568102|]
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NAD(P)-binding Rossmann-fold superfamily protein [Arabidopsis thaliana]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10143176)

classical SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase may catalyze isomerization, decarboxylation, epimerization, C=N bond reduction, dehydration, dehalogenation, enoyl-CoA reduction, and/or carbonyl-alcohol oxidoreduction; 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

CATH:  3.40.50.720
EC:  1.-.-.-
Gene Ontology:  GO:0016491
SCOP:  4000029

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
48-309 5.27e-98

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: 290.28  E-value: 5.27e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  48 ETARVLSKRGAHVVIGARNMGAAENAKTEILRQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGVMFCPY 127
Cdd:cd05327  16 ETARELAKRGAHVIIACRNEEKGEEAAAEIKKETGNAKVEVIQLDLSSLASVRQFAEEFLARFPRLDILINNAGIMAPPR 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 128 QLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAktsgvEGRILNVSSVAHIYTyQEGIQFDSINDICSYSDKRAYGQSKL 207
Cdd:cd05327  96 RLTKDGFELQFAVNYLGHFLLTNLLLPVLKASA-----PSRIVNVSSIAHRAG-PIDFNDLDLENNKEYSPYKAYGQSKL 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 208 ANILHANELSRQLqeEGVNITANSVHPGLILTNLFQHTALLMRFLKFFSFYLWKNIPQGAATTCYVALHPSVKGVTGKYF 287
Cdd:cd05327 170 ANILFTRELARRL--EGTGVTVNALHPGVVRTELLRRNGSFFLLYKLLRPFLKKSPEQGAQTALYAATSPELEGVSGKYF 247
                       250       260
                ....*....|....*....|..
gi 18413950 288 ADCNEVTPSKLARDETLAQKLW 309
Cdd:cd05327 248 SDCKIKMSSSEALDEELAEKLW 269
 
Name Accession Description Interval E-value
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
48-309 5.27e-98

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: 290.28  E-value: 5.27e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  48 ETARVLSKRGAHVVIGARNMGAAENAKTEILRQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGVMFCPY 127
Cdd:cd05327  16 ETARELAKRGAHVIIACRNEEKGEEAAAEIKKETGNAKVEVIQLDLSSLASVRQFAEEFLARFPRLDILINNAGIMAPPR 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 128 QLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAktsgvEGRILNVSSVAHIYTyQEGIQFDSINDICSYSDKRAYGQSKL 207
Cdd:cd05327  96 RLTKDGFELQFAVNYLGHFLLTNLLLPVLKASA-----PSRIVNVSSIAHRAG-PIDFNDLDLENNKEYSPYKAYGQSKL 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 208 ANILHANELSRQLqeEGVNITANSVHPGLILTNLFQHTALLMRFLKFFSFYLWKNIPQGAATTCYVALHPSVKGVTGKYF 287
Cdd:cd05327 170 ANILFTRELARRL--EGTGVTVNALHPGVVRTELLRRNGSFFLLYKLLRPFLKKSPEQGAQTALYAATSPELEGVSGKYF 247
                       250       260
                ....*....|....*....|..
gi 18413950 288 ADCNEVTPSKLARDETLAQKLW 309
Cdd:cd05327 248 SDCKIKMSSSEALDEELAEKLW 269
PRK06197 PRK06197
short chain dehydrogenase; Provisional
48-315 2.76e-74

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 231.07  E-value: 2.76e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   48 ETARVLSKRGAHVVIGARNMGAAENAKTEILRQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGVMFCPY 127
Cdd:PRK06197  31 ETAAALAAKGAHVVLAVRNLDKGKAAAARITAATPGADVTLQELDLTSLASVRAAADALRAAYPRIDLLINNAGVMYTPK 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  128 QLSEDGIELQFATNHIGHFLLTNLLLDTMKntaktsGVEG-RILNVSSVAHiyTYQEGIQFDSINDICSYSDKRAYGQSK 206
Cdd:PRK06197 111 QTTADGFELQFGTNHLGHFALTGLLLDRLL------PVPGsRVVTVSSGGH--RIRAAIHFDDLQWERRYNRVAAYGQSK 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  207 LANILHANELSRQLQEEGVNITANSVHPGLILTNLFQHT-ALLMRFLKFFSFYLWKNIPQGAATTCYVALHPSVKGvtGK 285
Cdd:PRK06197 183 LANLLFTYELQRRLAAAGATTIAVAAHPGVSNTELARNLpRALRPVATVLAPLLAQSPEMGALPTLRAATDPAVRG--GQ 260
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 18413950  286 YF--ADCNE-------VTPSKLARDETLAQKLWDFSVKL 315
Cdd:PRK06197 261 YYgpDGFGEqrgypkvVASSAQSHDEDLQRRLWAVSEEL 299
LPOR COG5748
Light-dependent NADPH-protochlorophyllide oxidoreductase [Coenzyme transport and metabolism];
47-316 4.66e-36

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


Pssm-ID: 444458 [Multi-domain]  Cd Length: 324  Bit Score: 132.43  E-value: 4.66e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  47 METARVLSKRGAHVVIGARNMGAAENAKTEILRQNANarVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGVMFcP 126
Cdd:COG5748  20 LYAAKALADRGWHVIMACRDLEKAEAAAQELGIPPDS--YTIIHIDLASLESVRRFVADFRALGRPLDALVCNAAVYY-P 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 127 Y----QLSEDGIELQFATNHIGHFLLTNLLLDTMKntaKTSGVEGRILNVSSVAHIYT-------------------YQE 183
Cdd:COG5748  97 LlkepLRSPDGYELSVATNHLGHFLLCNLLLEDLK---KSPASDPRLVILGTVTANPKelggkipipappdlgdlegFEA 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 184 GIQ--FDSINDICSYSDKrAYGQSKLANILHANELSRQLqEEGVNITANSVHPGLIL-TNLFQHTALLmrFLKFFSFYLw 260
Cdd:COG5748 174 GFKapISMIDGKKFKPGK-AYKDSKLCNVLTMRELHRRY-HESTGIVFSSLYPGCVAdTPLFRNHYPL--FQKLFPLFQ- 248
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18413950 261 KNIPQGAATT-------CYVALHPSVKgVTGKYFADCNEVTP---------SKLARDETLAQKLWDFSVKLI 316
Cdd:COG5748 249 KNITGGYVSQelagervAQVVADPEYA-QSGVYWSWGNRQKKgrksfvqevSPEASDDDKAKRLWELSAKLV 319
LPOR TIGR01289
light-dependent protochlorophyllide reductase; This model represents the light-dependent, ...
49-316 2.34e-29

light-dependent protochlorophyllide reductase; This model represents the light-dependent, NADPH-dependent form of protochlorophyllide reductase. It belongs to the short chain alcohol dehydrogenase family, in contrast to the nitrogenase-related light-independent form. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 200089  Cd Length: 314  Bit Score: 114.58  E-value: 2.34e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950    49 TARVLSKRGA-HVVIGARNMGAAENAKTEILRQNANarVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGVMFCPY 127
Cdd:TIGR01289  19 AAKALAATGEwHVIMACRDFLKAEQAAKSLGMPKDS--YTIMHLDLGSLDSVRQFVQQFRESGRPLDALVCNAAVYFPTA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   128 Q---LSEDGIELQFATNHIGHFLLTNLLLDTMKN--------------TAKTSGVEGRILNVSSVAHIYTYQEGIQ-FDS 189
Cdd:TIGR01289  97 KeprFTADGFELSVGTNHLGHFLLCNLLLDDLKNspnkdkrliivgsiTGNTNTLAGNVPPKANLGDLSGLAAGFKaPIA 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   190 INDICSYSDKRAYGQSKLANILHANELSRQLQEEgVNITANSVHPGLIL-TNLF-QHTALLMRFLKFFSfylwKNIPQGA 267
Cdd:TIGR01289 177 MIDGKEFKGAKAYKDSKVCNMLTVRELHRRFHDE-TGITFASLYPGCIAdTGLFrEHVPLFRTLFPPFQ----KYITKGY 251
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18413950   268 AT-------TCYVALHPSVKGvTGKYFADCNEVTP-----SKLARDETLAQKLWDFSVKLI 316
Cdd:TIGR01289 252 VSeeeagerLAQVVSDPKLKK-SGVYWSWGNRQESfvnqlSEEVSDDSKASKMWDLSEKLV 311
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
42-243 8.51e-25

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 99.22  E-value: 8.51e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950    42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEIlrQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:pfam00106   9 SSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKEL--GALGGKALFIQGDVTDRAQVKALVEQAVERLGRLDILVNNAG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   122 VM-FCP-YQLSEDGIELQFATNHIGHFLLTNLLLDTMKntaktSGVEGRILNVSSVAHIYTYQEGIqfdsindicsysdk 199
Cdd:pfam00106  87 ITgLGPfSELSDEDWERVIDVNLTGVFNLTRAVLPAMI-----KGSGGRIVNISSVAGLVPYPGGS-------------- 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 18413950   200 rAYGQSKLAnilhANELSRQLQEEGV--NITANSVHPGLILTNLFQ 243
Cdd:pfam00106 148 -AYSASKAA----VIGFTRSLALELAphGIRVNAVAPGGVDTDMTK 188
 
Name Accession Description Interval E-value
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
48-309 5.27e-98

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: 290.28  E-value: 5.27e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  48 ETARVLSKRGAHVVIGARNMGAAENAKTEILRQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGVMFCPY 127
Cdd:cd05327  16 ETARELAKRGAHVIIACRNEEKGEEAAAEIKKETGNAKVEVIQLDLSSLASVRQFAEEFLARFPRLDILINNAGIMAPPR 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 128 QLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAktsgvEGRILNVSSVAHIYTyQEGIQFDSINDICSYSDKRAYGQSKL 207
Cdd:cd05327  96 RLTKDGFELQFAVNYLGHFLLTNLLLPVLKASA-----PSRIVNVSSIAHRAG-PIDFNDLDLENNKEYSPYKAYGQSKL 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 208 ANILHANELSRQLqeEGVNITANSVHPGLILTNLFQHTALLMRFLKFFSFYLWKNIPQGAATTCYVALHPSVKGVTGKYF 287
Cdd:cd05327 170 ANILFTRELARRL--EGTGVTVNALHPGVVRTELLRRNGSFFLLYKLLRPFLKKSPEQGAQTALYAATSPELEGVSGKYF 247
                       250       260
                ....*....|....*....|..
gi 18413950 288 ADCNEVTPSKLARDETLAQKLW 309
Cdd:cd05327 248 SDCKIKMSSSEALDEELAEKLW 269
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
48-312 3.23e-90

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: 270.88  E-value: 3.23e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  48 ETARVLSKRGAHVVIGARNMGAAENAKTEILRQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGVMFCPY 127
Cdd:cd09807  16 ETARELARRGARVIMACRDMAKCEEAAAEIRRDTLNHEVIVRHLDLASLKSIRAFAAEFLAEEDRLDVLINNAGVMRCPY 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 128 QLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAKTsgvegRILNVSSVAHIYTYqegIQFDSINDICSYSDKRAYGQSKL 207
Cdd:cd09807  96 SKTEDGFEMQFGVNHLGHFLLTNLLLDLLKKSAPS-----RIVNVSSLAHKAGK---INFDDLNSEKSYNTGFAYCQSKL 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 208 ANILHANELSRQLQeeGVNITANSVHPGLILTNLFQHT----ALLMRFLKFFSFYLWKNIPQGAATTCYVALHPSVKGVT 283
Cdd:cd09807 168 ANVLFTRELARRLQ--GTGVTVNALHPGVVRTELGRHTgihhLFLSTLLNPLFWPFVKTPREGAQTSIYLALAEELEGVS 245
                       250       260
                ....*....|....*....|....*....
gi 18413950 284 GKYFADCNEVTPSKLARDETLAQKLWDFS 312
Cdd:cd09807 246 GKYFSDCKLKEPAPEAMDEETARRLWEIS 274
PRK06197 PRK06197
short chain dehydrogenase; Provisional
48-315 2.76e-74

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 231.07  E-value: 2.76e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   48 ETARVLSKRGAHVVIGARNMGAAENAKTEILRQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGVMFCPY 127
Cdd:PRK06197  31 ETAAALAAKGAHVVLAVRNLDKGKAAAARITAATPGADVTLQELDLTSLASVRAAADALRAAYPRIDLLINNAGVMYTPK 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  128 QLSEDGIELQFATNHIGHFLLTNLLLDTMKntaktsGVEG-RILNVSSVAHiyTYQEGIQFDSINDICSYSDKRAYGQSK 206
Cdd:PRK06197 111 QTTADGFELQFGTNHLGHFALTGLLLDRLL------PVPGsRVVTVSSGGH--RIRAAIHFDDLQWERRYNRVAAYGQSK 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  207 LANILHANELSRQLQEEGVNITANSVHPGLILTNLFQHT-ALLMRFLKFFSFYLWKNIPQGAATTCYVALHPSVKGvtGK 285
Cdd:PRK06197 183 LANLLFTYELQRRLAAAGATTIAVAAHPGVSNTELARNLpRALRPVATVLAPLLAQSPEMGALPTLRAATDPAVRG--GQ 260
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 18413950  286 YF--ADCNE-------VTPSKLARDETLAQKLWDFSVKL 315
Cdd:PRK06197 261 YYgpDGFGEqrgypkvVASSAQSHDEDLQRRLWAVSEEL 299
PRK06196 PRK06196
oxidoreductase; Provisional
14-315 1.01e-68

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 217.24  E-value: 1.01e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   14 SGFGSASTAEEVTQGIDATNLTAIITGGTGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEIlrqnanARVTLLQLDL 93
Cdd:PRK06196   7 SGFGAASTAEEVLAGHDLSGKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALAGI------DGVEVVMLDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   94 SSIKSIKAFVREFHALHLPLNLLINNAGVMFCPYQLSEDGIELQFATNHIGHFLLTNLLLDtmkntAKTSGVEGRILNVS 173
Cdd:PRK06196  81 ADLESVRAFAERFLDSGRRIDILINNAGVMACPETRVGDGWEAQFATNHLGHFALVNLLWP-----ALAAGAGARVVALS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  174 SVAHIYTyqeGIQFDSINDICSYSDKRAYGQSKLANILHANELSRQLQEEGVNitANSVHPGLILTNLFQHTALL-MRFL 252
Cdd:PRK06196 156 SAGHRRS---PIRWDDPHFTRGYDKWLAYGQSKTANALFAVHLDKLGKDQGVR--AFSVHPGGILTPLQRHLPREeQVAL 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  253 KffsfylW------------KNIPQGAATTCYVALHPSVKGVTGKYFADCN--EVTPS--------KLARDETLAQKLWD 310
Cdd:PRK06196 231 G------WvdehgnpidpgfKTPAQGAATQVWAATSPQLAGMGGLYCEDCDiaEPTPKdapwsgvrPHAIDPEAAARLWA 304

                 ....*
gi 18413950  311 FSVKL 315
Cdd:PRK06196 305 LSAAL 309
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
48-316 1.61e-60

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: 195.12  E-value: 1.61e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  48 ETARVLSKRGAHVVIGARNMGAAENAKTEILRQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGVMFCPY 127
Cdd:cd09809  16 ETARSFALHGAHVILACRNMSRASAAVSRILEEWHKARVEAMTLDLASLRSVQRFAEAFKAKNSPLHVLVCNAAVFALPW 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 128 QLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAKTsgvegRILNVSSVAHiytyqegiQFDSINDIC------------- 194
Cdd:cd09809  96 TLTEDGLETTFQVNHLGHFYLVQLLEDVLRRSAPA-----RVIVVSSESH--------RFTDLPDSCgnldfsllsppkk 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 195 SYSDKRAYGQSKLANILHANELSRQLQEEGvnITANSVHPGLILTNLFQHTALLMRFLKFFSFYLWKNIPQGAATTCYVA 274
Cdd:cd09809 163 KYWSMLAYNRAKLCNILFSNELHRRLSPRG--ITSNSLHPGNMMYSSIHRNWWVYTLLFTLARPFTKSMQQGAATTVYCA 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 18413950 275 LHPSVKGVTGKYFADCNEVTPSKLARDETLAQKLWDFSVKLI 316
Cdd:cd09809 241 TAPELEGLGGMYFNNCFRCLPSPEAQSEATAQQLWELSERLI 282
PRK05854 PRK05854
SDR family oxidoreductase;
50-315 5.50e-52

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 174.10  E-value: 5.50e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   50 ARVLSKRGAHVVIGARNMGAAENAKTEILRQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGVMFCP-YQ 128
Cdd:PRK05854  31 ARRLAAAGAEVILPVRNRAKGEAAVAAIRTAVPDAKLSLRALDLSSLASVAALGEQLRAEGRPIHLLINNAGVMTPPeRQ 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  129 LSEDGIELQFATNHIGHFLLTNLLLDTMKNTAktsgveGRILNVSSVAhiyTYQEGIQFDSINDICSYSDKRAYGQSKLA 208
Cdd:PRK05854 111 TTADGFELQFGTNHLGHFALTAHLLPLLRAGR------ARVTSQSSIA---ARRGAINWDDLNWERSYAGMRAYSQSKIA 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  209 NILHANELSRQLQEEGVNITANSVHPGLILTNLF--------QHTALLMRFLKFFSF--YLWKNIPQGAATTCYVALHPS 278
Cdd:PRK05854 182 VGLFALELDRRSRAAGWGITSNLAHPGVAPTNLLaarpevgrDKDTLMVRLIRSLSArgFLVGTVESAILPALYAATSPD 261
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 18413950  279 VKGvtGKYF------------ADCNEVTPsklARDETLAQKLWDFSVKL 315
Cdd:PRK05854 262 AEG--GAFYgprgpgelgggpVEQALYPP---LRRNAEAARLWEVSEQL 305
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
47-316 1.69e-43

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: 151.90  E-value: 1.69e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  47 METARVLSKRGA-HVVIGARNMGAAENAKTEILRqnANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGVMF- 124
Cdd:cd09810  15 LAAAKALARRGEwHVVMACRDFLKAEQAAQEVGM--PKDSYSVLHCDLASLDSVRQFVDNFRRTGRPLDALVCNAAVYLp 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 125 --CPYQLSEDGIELQFATNHIGHFLLTNLLLDTMKNtakTSGVEGRILNVSSVAH-----------------IYTYQEGI 185
Cdd:cd09810  93 taKEPRFTADGFELTVGVNHLGHFLLTNLLLEDLQR---SENASPRIVIVGSITHnpntlagnvppratlgdLEGLAGGL 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 186 Q-FDSINDICSYSDKRAYGQSKLANILHANELSRQLQEEgVNITANSVHPGLIL-TNLFQHTALLMR--FLKFFSFylwk 261
Cdd:cd09810 170 KgFNSMIDGGEFEGAKAYKDSKVCNMLTTYELHRRLHEE-TGITFNSLYPGCIAeTGLFREHYPLFRtlFPPFQKY---- 244
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18413950 262 nIPQGAATT-------CYVALHPSVkGVTGKYFADCN-----EVTPSKLARDETLAQKLWDFSVKLI 316
Cdd:cd09810 245 -ITKGYVSEeeagerlAAVIADPSL-GVSGVYWSWGKasgsfENQSSQESSDDEKARKLWEISEKLV 309
LPOR COG5748
Light-dependent NADPH-protochlorophyllide oxidoreductase [Coenzyme transport and metabolism];
47-316 4.66e-36

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


Pssm-ID: 444458 [Multi-domain]  Cd Length: 324  Bit Score: 132.43  E-value: 4.66e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  47 METARVLSKRGAHVVIGARNMGAAENAKTEILRQNANarVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGVMFcP 126
Cdd:COG5748  20 LYAAKALADRGWHVIMACRDLEKAEAAAQELGIPPDS--YTIIHIDLASLESVRRFVADFRALGRPLDALVCNAAVYY-P 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 127 Y----QLSEDGIELQFATNHIGHFLLTNLLLDTMKntaKTSGVEGRILNVSSVAHIYT-------------------YQE 183
Cdd:COG5748  97 LlkepLRSPDGYELSVATNHLGHFLLCNLLLEDLK---KSPASDPRLVILGTVTANPKelggkipipappdlgdlegFEA 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 184 GIQ--FDSINDICSYSDKrAYGQSKLANILHANELSRQLqEEGVNITANSVHPGLIL-TNLFQHTALLmrFLKFFSFYLw 260
Cdd:COG5748 174 GFKapISMIDGKKFKPGK-AYKDSKLCNVLTMRELHRRY-HESTGIVFSSLYPGCVAdTPLFRNHYPL--FQKLFPLFQ- 248
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18413950 261 KNIPQGAATT-------CYVALHPSVKgVTGKYFADCNEVTP---------SKLARDETLAQKLWDFSVKLI 316
Cdd:COG5748 249 KNITGGYVSQelagervAQVVADPEYA-QSGVYWSWGNRQKKgrksfvqevSPEASDDDKAKRLWELSAKLV 319
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
48-250 2.61e-32

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 120.74  E-value: 2.61e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  48 ETARVLSKRGAHVVIGARNMGAAENAKTEIlrQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGVM---- 123
Cdd:COG0300  20 ALARALAARGARVVLVARDAERLEALAAEL--RAAGARVEVVALDVTDPDAVAALAEAVLARFGPIDVLVNNAGVGgggp 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 124 FCpyQLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAKtsgveGRILNVSSVAHIYtyqeGIQFDSindicsysdkrAYG 203
Cdd:COG0300  98 FE--ELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGR-----GRIVNVSSVAGLR----GLPGMA-----------AYA 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 18413950 204 QSKLANILHANELSRQLQEEGVNITAnsVHPGLILTNLFQHTALLMR 250
Cdd:COG0300 156 ASKAALEGFSESLRAELAPTGVRVTA--VCPGPVDTPFTARAGAPAG 200
PLN00015 PLN00015
protochlorophyllide reductase
49-317 4.23e-32

protochlorophyllide reductase


Pssm-ID: 177654  Cd Length: 308  Bit Score: 121.74  E-value: 4.23e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   49 TARVLSKRGA-HVVIGARNMGAAENAKTEILRQNANarVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGVmfcpY 127
Cdd:PLN00015  13 TAKALAETGKwHVVMACRDFLKAERAAKSAGMPKDS--YTVMHLDLASLDSVRQFVDNFRRSGRPLDVLVCNAAV----Y 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  128 Q-------LSEDGIELQFATNHIGHFLLTNLLLDTMKN--------------TAKT----------------SGVEGRIL 170
Cdd:PLN00015  87 LptakeptFTADGFELSVGTNHLGHFLLSRLLLDDLKKsdypskrliivgsiTGNTntlagnvppkanlgdlRGLAGGLN 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  171 NVSSVAHIytyqEGIQFDSindicsysdKRAYGQSKLANILHANELSRQLQEEgVNITANSVHPGLIL-TNLF-QHTALl 248
Cdd:PLN00015 167 GLNSSAMI----DGGEFDG---------AKAYKDSKVCNMLTMQEFHRRYHEE-TGITFASLYPGCIAtTGLFrEHIPL- 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  249 mrFLKFFSFYLwKNIPQGaattcYVALHPSVK-----------GVTGKYFA-----DCNEVTPSKLARDETLAQKLWDFS 312
Cdd:PLN00015 232 --FRLLFPPFQ-KYITKG-----YVSEEEAGKrlaqvvsdpslTKSGVYWSwnggsASFENQLSQEASDAEKAKKVWEIS 303

                 ....*
gi 18413950  313 VKLIN 317
Cdd:PLN00015 304 EKLVG 308
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
48-289 2.07e-31

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: 117.72  E-value: 2.07e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  48 ETARVLSKRGA-HVVIGARNMGAAENAKTEILRQNANARVtlLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGVMF-- 124
Cdd:cd05324  15 EIVRQLAKSGPgTVILTARDVERGQAAVEKLRAEGLSVRF--HQLDVTDDASIEAAADFVEEKYGGLDILVNNAGIAFkg 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 125 -CPYQLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAktsgvEGRILNVSSVAhiytyqeGIQfdsindicsysdKRAYG 203
Cdd:cd05324  93 fDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSP-----AGRIVNVSSGL-------GSL------------TSAYG 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 204 QSKLANILHANELSRQLQEEgvNITANSVHPGLILTNLFQHTAllmrflkffsfylWKNIPQGAATTCYVALHPSVKGVT 283
Cdd:cd05324 149 VSKAALNALTRILAKELKET--GIKVNACCPGWVKTDMGGGKA-------------PKTPEEGAETPVYLALLPPDGEPT 213

                ....*.
gi 18413950 284 GKYFAD 289
Cdd:cd05324 214 GKFFSD 219
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
42-246 1.33e-29

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: 113.34  E-value: 1.33e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEIlrQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:COG1028  15 SSGIGRAIARALAAEGARVVITDRDAEALEAAAAEL--RAAGGRALAVAADVTDEAAVEALVAAAVAAFGRLDILVNNAG 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 122 VMFCP--YQLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAKtsgveGRILNVSSVAHIYtyqegiqfdsindicSYSDK 199
Cdd:COG1028  93 ITPPGplEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGG-----GRIVNISSIAGLR---------------GSPGQ 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 18413950 200 RAYGQSKLANILHANELSRQLQEEGvnITANSVHPGLILTNLFQHTA 246
Cdd:COG1028 153 AAYAASKAAVVGLTRSLALELAPRG--IRVNAVAPGPIDTPMTRALL 197
LPOR TIGR01289
light-dependent protochlorophyllide reductase; This model represents the light-dependent, ...
49-316 2.34e-29

light-dependent protochlorophyllide reductase; This model represents the light-dependent, NADPH-dependent form of protochlorophyllide reductase. It belongs to the short chain alcohol dehydrogenase family, in contrast to the nitrogenase-related light-independent form. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 200089  Cd Length: 314  Bit Score: 114.58  E-value: 2.34e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950    49 TARVLSKRGA-HVVIGARNMGAAENAKTEILRQNANarVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGVMFCPY 127
Cdd:TIGR01289  19 AAKALAATGEwHVIMACRDFLKAEQAAKSLGMPKDS--YTIMHLDLGSLDSVRQFVQQFRESGRPLDALVCNAAVYFPTA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   128 Q---LSEDGIELQFATNHIGHFLLTNLLLDTMKN--------------TAKTSGVEGRILNVSSVAHIYTYQEGIQ-FDS 189
Cdd:TIGR01289  97 KeprFTADGFELSVGTNHLGHFLLCNLLLDDLKNspnkdkrliivgsiTGNTNTLAGNVPPKANLGDLSGLAAGFKaPIA 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   190 INDICSYSDKRAYGQSKLANILHANELSRQLQEEgVNITANSVHPGLIL-TNLF-QHTALLMRFLKFFSfylwKNIPQGA 267
Cdd:TIGR01289 177 MIDGKEFKGAKAYKDSKVCNMLTVRELHRRFHDE-TGITFASLYPGCIAdTGLFrEHVPLFRTLFPPFQ----KYITKGY 251
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18413950   268 AT-------TCYVALHPSVKGvTGKYFADCNEVTP-----SKLARDETLAQKLWDFSVKLI 316
Cdd:TIGR01289 252 VSeeeagerLAQVVSDPKLKK-SGVYWSWGNRQESfvnqlSEEVSDDSKASKMWDLSEKLV 311
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
42-270 4.05e-27

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: 106.60  E-value: 4.05e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGARNmgaAENAKTEILRQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:cd05233   7 SSGIGRAIARRLAREGAKVVLADRN---EEALAELAAIEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILVNNAG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 122 VM--FCPYQLSEDGIELQFATNHIGHFLLTNLLLDTMKntaktSGVEGRILNVSSVAHIYTYQEGIqfdsindicsysdk 199
Cdd:cd05233  84 IArpGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMK-----KQGGGRIVNISSVAGLRPLPGQA-------------- 144
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18413950 200 rAYGQSKLANILHANELSRQLQEEGvnITANSVHPGLILTNLFQHTALLMRFLKFFsfylwKNIPQGAATT 270
Cdd:cd05233 145 -AYAASKAALEGLTRSLALELAPYG--IRVNAVAPGLVDTPMLAKLGPEEAEKELA-----AAIPLGRLGT 207
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
42-243 8.51e-25

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 99.22  E-value: 8.51e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950    42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEIlrQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:pfam00106   9 SSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKEL--GALGGKALFIQGDVTDRAQVKALVEQAVERLGRLDILVNNAG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   122 VM-FCP-YQLSEDGIELQFATNHIGHFLLTNLLLDTMKntaktSGVEGRILNVSSVAHIYTYQEGIqfdsindicsysdk 199
Cdd:pfam00106  87 ITgLGPfSELSDEDWERVIDVNLTGVFNLTRAVLPAMI-----KGSGGRIVNISSVAGLVPYPGGS-------------- 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 18413950   200 rAYGQSKLAnilhANELSRQLQEEGV--NITANSVHPGLILTNLFQ 243
Cdd:pfam00106 148 -AYSASKAA----VIGFTRSLALELAphGIRVNAVAPGGVDTDMTK 188
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
42-244 2.21e-24

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: 99.10  E-value: 2.21e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEIlrqnaNARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:COG4221  14 SSGIGAATARALAAAGARVVLAARRAERLEALAAEL-----GGRALAVPLDVTDEAAVEAAVAAAVAEFGRLDVLVNNAG 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 122 VM-FCP-YQLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAKtsgveGRILNVSSVAHIYTYQEGIqfdsindicsysdk 199
Cdd:COG4221  89 VAlLGPlEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGS-----GHIVNISSIAGLRPYPGGA-------------- 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 18413950 200 rAYGQSKLAniLHAneLSRQLQEE--GVNITANSVHPGLILTNLFQH 244
Cdd:COG4221 150 -VYAATKAA--VRG--LSESLRAElrPTGIRVTVIEPGAVDTEFLDS 191
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
49-289 2.59e-21

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: 91.12  E-value: 2.59e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  49 TARVLSKRGAHVVIGARNMGAAENAKTEILRQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGVMFCPYQ 128
Cdd:cd09808  17 AALAIAKRGGTVHMVCRNQTRAEEARKEIETESGNQNIFLHIVDMSDPKQVWEFVEEFKEEGKKLHVLINNAGCMVNKRE 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 129 LSEDGIELQFATNHIGHFLLTNLLLDTMKNTAktsgvEGRILNVSSVAHIytyqegIQFDSINDICS----YSDKRAYGQ 204
Cdd:cd09808  97 LTEDGLEKNFATNTLGTYILTTHLIPVLEKEE-----DPRVITVSSGGML------VQKLNTNNLQSertaFDGTMVYAQ 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 205 SKLANILhaneLSRQLQEEGVNITANSVHPGLILTNLFQHTalLMRFLKFFSFYLwKNIPQGAATTCYVALHPS-VKGVT 283
Cdd:cd09808 166 NKRQQVI----MTEQWAKKHPEIHFSVMHPGWADTPAVRNS--MPDFHARFKDRL-RSEEQGADTVVWLALSSAaAKAPS 238

                ....*.
gi 18413950 284 GKYFAD 289
Cdd:cd09808 239 GRFYQD 244
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
44-241 5.86e-20

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: 86.97  E-value: 5.86e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  44 GIGMETARVLSKRGAHVVIGA-RNMGAAENAKTEIlrqNANARVTLLQLDLSS--IKSIKAFVREFHALHlpLNLLINNA 120
Cdd:cd05325   9 GIGLELVRQLLARGNNTVIATcRDPSAATELAALG---ASHSRLHILELDVTDeiAESAEAVAERLGDAG--LDVLINNA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 121 GV--MFCPY-QLSEDGIELQFATNHIGHFLLTNLLLDTMKNtaktsGVEGRILNVSSVAhiytyqeGiqfdSINDI---C 194
Cdd:cd05325  84 GIlhSYGPAsEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLK-----GARAKIINISSRV-------G----SIGDNtsgG 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 18413950 195 SYSdkraYGQSKLA-NILHANeLSRQLQEEGvnITANSVHPGLILTNL 241
Cdd:cd05325 148 WYS----YRASKAAlNMLTKS-LAVELKRDG--ITVVSLHPGWVRTDM 188
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
48-259 3.10e-18

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: 82.66  E-value: 3.10e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  48 ETARVLSKRGAHVVIGARNMGAAENAKTEilrqnANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGVM-FCP 126
Cdd:cd05374  15 ALALALAAQGYRVIATARNPDKLESLGEL-----LNDNLEVLELDVTDEESIKAAVKEVIERFGRIDVLVNNAGYGlFGP 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 127 Y-QLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAKtsgveGRILNVSSVAhiytyqeGIQFDSINDicsysdkrAYGQS 205
Cdd:cd05374  90 LeETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGS-----GRIVNVSSVA-------GLVPTPFLG--------PYCAS 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 18413950 206 KLAniLHA--NELSRQLQEEGVNITanSVHPGLILTNLFQHTALLMRFLKFFSFYL 259
Cdd:cd05374 150 KAA--LEAlsESLRLELAPFGIKVT--IIEPGPVRTGFADNAAGSALEDPEISPYA 201
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
48-245 1.42e-17

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: 80.71  E-value: 1.42e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  48 ETARVLSKRGAHVVIGARNMGAAENAKTEILrQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGV-MFCP 126
Cdd:cd05332  18 ELAYHLARLGARLVLSARREERLEEVKSECL-ELGAPSPHVVPLDMSDLEDAEQVVEEALKLFGGLDILINNAGIsMRSL 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 127 YQ-LSEDGIELQFATNHIGHFLLTNLLLDTMKNTAKtsgveGRILNVSSVAHIYtyqeGIQFDSindicsysdkrAYGQS 205
Cdd:cd05332  97 FHdTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQ-----GSIVVVSSIAGKI----GVPFRT-----------AYAAS 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 18413950 206 KLAniLHA--NELSRQLQEEGVNITanSVHPGLILTNLFQHT 245
Cdd:cd05332 157 KHA--LQGffDSLRAELSEPNISVT--VVCPGLIDTNIAMNA 194
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
49-240 3.38e-17

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 79.43  E-value: 3.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   49 TARVLSKRGAHVVIGARNMGAAENAKTEIlrQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGVmFCP-- 126
Cdd:PRK05653  21 IALRLAADGAKVVIYDSNEEAAEALAAEL--RAAGGEARVLVFDVSDEAAVRALIEAAVEAFGALDILVNNAGI-TRDal 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  127 -YQLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAKtsgveGRILNVSSVAhiytyqeGIQfdsindicSYSDKRAYGQS 205
Cdd:PRK05653  98 lPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARY-----GRIVNISSVS-------GVT--------GNPGQTNYSAA 157
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 18413950  206 KLAniLHAneLSRQLQEE--GVNITANSVHPGLILTN 240
Cdd:PRK05653 158 KAG--VIG--FTKALALElaSRGITVNAVAPGFIDTD 190
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
44-174 2.69e-14

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: 71.35  E-value: 2.69e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  44 GIGMETARVLSKRGAHVVIGARNMGAAENAKteilrqNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGVM 123
Cdd:COG3967  16 GIGLALAKRLHARGNTVIITGRREEKLEEAA------AANPGLHTIVLDVADPASIAALAEQVTAEFPDLNVLINNAGIM 89
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 18413950 124 FcPYQLSEDGIELQ-----FATNHIGHFLLTNLLLDTMKNTAktsgvEGRILNVSS 174
Cdd:COG3967  90 R-AEDLLDEAEDLAdaereITTNLLGPIRLTAAFLPHLKAQP-----EAAIVNVSS 139
PRK12826 PRK12826
SDR family oxidoreductase;
42-243 8.04e-14

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 69.95  E-value: 8.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIGARNMGAAEnAKTEILRQnANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:PRK12826  15 ARGIGRAIAVRLAADGAEVIVVDICGDDAA-ATAELVEA-AGGKARARQVDVRDRAALKAAVAAGVEDFGRLDILVANAG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  122 VmfCP----YQLSEDGIELQFATNHIGHFLLTNLLLDTMKntaKTSGveGRILNVSSVAhiytyqeGIQFDSINDIcsys 197
Cdd:PRK12826  93 I--FPltpfAEMDDEQWERVIDVNLTGTFLLTQAALPALI---RAGG--GRIVLTSSVA-------GPRVGYPGLA---- 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 18413950  198 dkrAYGQSK-----LANILhANELSRQlqeegvNITANSVHPGLILT----NLFQ 243
Cdd:PRK12826 155 ---HYAASKaglvgFTRAL-ALELAAR------NITVNSVHPGGVDTpmagNLGD 199
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
50-239 2.60e-13

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 68.74  E-value: 2.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   50 ARVLSKRGAHVVIGAR-NMGAAENAKTEIlrQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGVM----F 124
Cdd:PRK12825  23 ALRLARAGADVVVHYRsDEEAAEELVEAV--EALGRRAQAVQADVTDKAALEAAVAAAVERFGRIDILVNNAGIFedkpL 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  125 CPYqlSEDGIELQFATNHIGHFLLTNLLLDTMKntaKTSGveGRILNVSSVAhiytyqegiqfdsindicsySDKR---- 200
Cdd:PRK12825 101 ADM--SDDEWDEVIDVNLSGVFHLLRAVVPPMR---KQRG--GRIVNISSVA--------------------GLPGwpgr 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 18413950  201 -AYGQSKLANILHANELSRQLQEEGvnITANSVHPGLILT 239
Cdd:PRK12825 154 sNYAAAKAGLVGLTKALARELAEYG--ITVNMVAPGDIDT 191
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
59-276 4.54e-13

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: 68.57  E-value: 4.54e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  59 HVVIGARNMGAAENAKTEILRQNANARVTL--LQLDLSSIKSIKAFVREFHALHLPLNLLINNAGVMFCP---------- 126
Cdd:cd08941  32 TLILACRNLQRAEAACRALLASHPDARVVFdyVLVDLSNMVSVFAAAKELKKRYPRLDYLYLNAGIMPNPgidwigaike 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 127 -------------------------YQLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAKTSGVegrILNVSSVAHIYTY 181
Cdd:cd08941 112 vltnplfavtnptykiqaegllsqgDKATEDGLGEVFQTNVFGHYYLIRELEPLLCRSDGGSQI---IWTSSLNASPKYF 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 182 qegiqfdSINDICSYSDKRAYGQSKLANILHANELSRQLQEEGVNitANSVHPGLILTNLF-QHTALLMRFLKFFSFYL- 259
Cdd:cd08941 189 -------SLEDIQHLKGPAPYSSSKYLVDLLSLALNRKFNKLGVY--SYVVHPGICTTNLTyGILPPFTWTLALPLFYLl 259
                       250       260
                ....*....|....*....|....*
gi 18413950 260 ------WKNIP--QGAATTCYVALH 276
Cdd:cd08941 260 rrlgspWHTISpyNGAEALVWLALQ 284
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
42-247 1.48e-12

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: 65.85  E-value: 1.48e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTeilrqnANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:cd08932   9 SRGIGIEIARALARDGYRVSLGLRNPEDLAALSA------SGGDVEAVPYDARDPEDARALVDALRDRFGRIDVLVHNAG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 122 VM----FCPYQLSEdgIELQFATNHIGHFLLTNLLLDTMKNTAKtsgveGRILNVSSVAHiytyQEGIQFDSIndicsys 197
Cdd:cd08932  83 IGrpttLREGSDAE--LEAHFSINVIAPAELTRALLPALREAGS-----GRVVFLNSLSG----KRVLAGNAG------- 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 18413950 198 dkraYGQSKLANILHANELSRQLQEEGVNITAnsVHPGLILTNLFQHTAL 247
Cdd:cd08932 145 ----YSASKFALRALAHALRQEGWDHGVRVSA--VCPGFVDTPMAQGLTL 188
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
49-284 2.21e-12

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: 65.53  E-value: 2.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950    49 TARVLSKRGAHVVIGARNMGAAENAKTEILRQNANArvtlLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGV---MFC 125
Cdd:pfam13561  12 IARALAEEGAEVVLTDLNEALAKRVEELAEELGAAV----LPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGFapkLKG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   126 PY-QLSEDGIELQFATNHIGHFLLTNLLLDTMKNTaktsgveGRILNVSSVAHIYTyqegiqFDSINdicsysdkrAYGQ 204
Cdd:pfam13561  88 PFlDTSREDFDRALDVNLYSLFLLAKAALPLMKEG-------GSIVNLSSIGAERV------VPNYN---------AYGA 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   205 SKlANILH-----ANELSRQlqeegvNITANSVHPGLILTNLFQHTALLMRFLKFFSfylwKNIPQG--------AATTC 271
Cdd:pfam13561 146 AK-AALEAltrylAVELGPR------GIRVNAISPGPIKTLAASGIPGFDELLAAAE----ARAPLGrlgtpeevANAAA 214
                         250
                  ....*....|...
gi 18413950   272 YVAlHPSVKGVTG 284
Cdd:pfam13561 215 FLA-SDLASYITG 226
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
44-244 2.81e-12

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: 65.34  E-value: 2.81e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  44 GIGMETARVLSKRGAHVVIGARNMGAAENAKTEILRqnANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGVM 123
Cdd:cd05339  10 GIGRLLALEFAKRGAKVVILDINEKGAEETANNVRK--AGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTILINNAGVV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 124 --FCPYQLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAKtsgveGRILNVSSVA-HIYTyqegiqfdsindiCSYSDkr 200
Cdd:cd05339  88 sgKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNH-----GHIVTIASVAgLISP-------------AGLAD-- 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 18413950 201 aYGQSKLANILHANELSRQLQEEGV-NITANSVHPGLILTNLFQH 244
Cdd:cd05339 148 -YCASKAAAVGFHESLRLELKAYGKpGIKTTLVCPYFINTGMFQG 191
PRK06914 PRK06914
SDR family oxidoreductase;
42-175 3.04e-12

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 65.82  E-value: 3.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEILRQNANARVTLLQLDLS---SIKSIKAFVREFHalhlPLNLLIN 118
Cdd:PRK06914  12 SSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQATQLNLQQNIKVQQLDVTdqnSIHNFQLVLKEIG----RIDLLVN 87
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18413950  119 NAGVMFCPY--QLSEDGIELQFATNHIGHFLLTNLLLDTMKntaKTSGveGRILNVSSV 175
Cdd:PRK06914  88 NAGYANGGFveEIPVEEYRKQFETNVFGAISVTQAVLPYMR---KQKS--GKIINISSI 141
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
51-241 3.45e-12

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: 65.12  E-value: 3.45e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  51 RVLSKRGA-HVVIGARNMGAAENakteiLRQNANARVTLLQLDLSSIKSIKAFVREFHalhlPLNLLINNAGVmFCPYQL 129
Cdd:cd05354  21 ESLLAHGAkKVYAAVRDPGSAAH-----LVAKYGDKVVPLRLDVTDPESIKAAAAQAK----DVDVVINNAGV-LKPATL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 130 SE----DGIELQFATNHIGHFLLTNLLLDTMKNTAKtsgveGRILNVSSVAhiytyqegiqfdsinDICSYSDKRAYGQS 205
Cdd:cd05354  91 LEegalEALKQEMDVNVFGLLRLAQAFAPVLKANGG-----GAIVNLNSVA---------------SLKNFPAMGTYSAS 150
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 18413950 206 KLANILHANELSRQLQEEGVNITanSVHPGLILTNL 241
Cdd:cd05354 151 KSAAYSLTQGLRAELAAQGTLVL--SVHPGPIDTRM 184
PRK09730 PRK09730
SDR family oxidoreductase;
42-241 2.36e-11

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 62.95  E-value: 2.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIG-ARNMGAAENAKTEILRQNANArvTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNA 120
Cdd:PRK09730  10 SRGIGRATALLLAQEGYTVAVNyQQNLHAAQEVVNLITQAGGKA--FVLQADISDENQVVAMFTAIDQHDEPLAALVNNA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  121 GVMFCPY---QLSEDGIELQFATNHIGHFLLTNlllDTMKNTA-KTSGVEGRILNVSSVAhiytyqegiqfDSINDICSY 196
Cdd:PRK09730  88 GILFTQCtveNLTAERINRVLSTNVTGYFLCCR---EAVKRMAlKHGGSGGAIVNVSSAA-----------SRLGAPGEY 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 18413950  197 SDkraYGQSKLANILHANELSRQLQEEGVNItaNSVHPGLILTNL 241
Cdd:PRK09730 154 VD---YAASKGAIDTLTTGLSLEVAAQGIRV--NCVRPGFIYTEM 193
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
42-242 4.57e-11

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: 61.91  E-value: 4.57e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIG-ARNMGAAENAKTEIlrQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNA 120
Cdd:cd05362  12 SRGIGRAIAKRLARDGASVVVNyASSKAAAEEVVAEI--EAAGGKAIAVQADVSDPSQVARLFDAAEKAFGGVDILVNNA 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 121 GVM-FCPY-QLSEDGIELQFATNHIGHFLltnllldTMKNTAKTSGVEGRILNVSSVAhIYTYQEGiqfdsindicsYSd 198
Cdd:cd05362  90 GVMlKKPIaETSEEEFDRMFTVNTKGAFF-------VLQEAAKRLRDGGRIINISSSL-TAAYTPN-----------YG- 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 18413950 199 krAYGQSKLANILHANELSRQLQEEGvnITANSVHPGLILTNLF 242
Cdd:cd05362 150 --AYAGSKAAVEAFTRVLAKELGGRG--ITVNAVAPGPVDTDMF 189
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
50-243 5.01e-11

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: 61.92  E-value: 5.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  50 ARVLSKRGAH--VVIGARNMGAAENAKTEIlrqNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGVM--FC 125
Cdd:cd05367  16 AEELLKRGSPsvVVLLARSEEPLQELKEEL---RPGLRVTTVKADLSDAAGVEQLLEAIRKLDGERDLLINNAGSLgpVS 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 126 PY-QLSEDGIELQFATNHIGHFLLTNLLLdtmkNTAKTSGVEGRILNVSSVAhiytyqegiqfdSINDICSYSdkrAYGQ 204
Cdd:cd05367  93 KIeFIDLDELQKYFDLNLTSPVCLTSTLL----RAFKKRGLKKTVVNVSSGA------------AVNPFKGWG---LYCS 153
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 18413950 205 SKLAnilhANELSRQLQEEGVNITANSVHPGLILTNLFQ 243
Cdd:cd05367 154 SKAA----RDMFFRVLAAEEPDVRVLSYAPGVVDTDMQR 188
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
42-241 5.45e-11

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: 61.79  E-value: 5.45e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEILRQNANARVtlLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:cd05333   9 SRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEIKALGGNAAA--LEADVSDREAVEALVEKVEAEFGPVDILVNNAG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 122 V----MFcpYQLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAKtsgveGRILNVSSVAHIYtyqeGiQFDSINdicsYS 197
Cdd:cd05333  87 ItrdnLL--MRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRS-----GRIINISSVVGLI----G-NPGQAN----YA 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 18413950 198 DKRA--YGQSKLAnilhANELSRQlqeegvNITANSVHPGLILTNL 241
Cdd:cd05333 151 ASKAgvIGFTKSL----AKELASR------GITVNAVAPGFIDTDM 186
PRK06500 PRK06500
SDR family oxidoreductase;
44-243 6.99e-11

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 61.51  E-value: 6.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   44 GIGMETARVLSKRGAHVVIGARNMGAAENAKTEIlrqnaNARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGV- 122
Cdd:PRK06500  17 GIGLETARQFLAEGARVAITGRDPASLEAARAEL-----GESALVIRADAGDVAAQKALAQALAEAFGRLDAVFINAGVa 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  123 MFCPY-QLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAKTsgvegrILNVSSVAHIytyqeGIQFDSIndicsysdkra 201
Cdd:PRK06500  92 KFAPLeDWDEAMFDRSFNTNVKGPYFLIQALLPLLANPASI------VLNGSINAHI-----GMPNSSV----------- 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 18413950  202 YGQSKLANILHANELSRQLQEEGVNItaNSVHPGLILTNLFQ 243
Cdd:PRK06500 150 YAASKAALLSLAKTLSGELLPRGIRV--NAVSPGPVQTPLYG 189
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
42-239 9.80e-11

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: 61.14  E-value: 9.80e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEiLRQNANARVTLLQLDLSSIKSIKAFVREfhalhLP-----LNLL 116
Cdd:cd05346   9 SSGIGEATARRFAKAGAKLILTGRRAERLQELADE-LGAKFPVKVLPLQLDVSDRESIEAALEN-----LPeefrdIDIL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 117 INNAGV---MFCPYQLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAKtsgveGRILNVSSVAHIYTYQEGiqfdSIndi 193
Cdd:cd05346  83 VNNAGLalgLDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQ-----GHIINLGSIAGRYPYAGG----NV--- 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 18413950 194 csysdkraYGQSKLAnilhANELSRQLQEE--GVNITANSVHPGLILT 239
Cdd:cd05346 151 --------YCATKAA----VRQFSLNLRKDliGTGIRVTNIEPGLVET 186
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
42-243 2.31e-10

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: 60.01  E-value: 2.31e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGARNmgAAENAKTEILRQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:cd05323   9 ASGIGLATAKLLLKKGAKVAILDRN--ENPGAAAELQAINPKVKATFVQCDVTSWEQLAAAFKKAIEKFGRVDILINNAG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 122 V-----MFCPYQLSEDgIELQFATNHIGHFLLTNLLLDTMKNTAKTSGveGRILNVSSVAHIYtyqEGIQFDsindicsy 196
Cdd:cd05323  87 IldeksYLFAGKLPPP-WEKTIDVNLTGVINTTYLALHYMDKNKGGKG--GVIVNIGSVAGLY---PAPQFP-------- 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 18413950 197 sdkrAYGQSKLAnILHaneLSRQL---QEEGVNITANSVHPGLILTNLFQ 243
Cdd:cd05323 153 ----VYSASKHG-VVG---FTRSLadlLEYKTGVRVNAICPGFTNTPLLP 194
PRK07825 PRK07825
short chain dehydrogenase; Provisional
48-176 2.62e-10

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 59.95  E-value: 2.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   48 ETARVLSKRGAHVVIGARNMGAAENAKTEIlrqnanARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGVMFCPY 127
Cdd:PRK07825  20 ATARALAALGARVAIGDLDEALAKETAAEL------GLVVGGPLDVTDPASFAAFLDAVEADLGPIDVLVNNAGVMPVGP 93
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 18413950  128 QL--SEDGIELQFATNHIGHFLLTNLLLDTMkntaktsgVE---GRILNVSSVA 176
Cdd:PRK07825  94 FLdePDAVTRRILDVNVYGVILGSKLAAPRM--------VPrgrGHVVNVASLA 139
PRK12827 PRK12827
short chain dehydrogenase; Provisional
50-288 4.19e-10

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 59.35  E-value: 4.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   50 ARVLSKRGAHVVI--GARNMGAAENAKTEILRQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGVM-FCP 126
Cdd:PRK12827  23 AVRLAADGADVIVldIHPMRGRAEADAVAAGIEAAGGKALGLAFDVRDFAATRAALDAGVEEFGRLDILVNNAGIAtDAA 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  127 Y-QLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAKTsgveGRILNVSSVAhIYTYQEGiqfdsindicsysdKRAYGQS 205
Cdd:PRK12827 103 FaELSIEEWDDVIDVNLDGFFNVTQAALPPMIRARRG----GRIVNIASVA-GVRGNRG--------------QVNYAAS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  206 KLANILHANELSRQLQEEGvnITANSVHPGLILTNLFQHTALLMRFLKFFSFYLWKNIPQGAATTCYVAlHPSVKGVTGK 285
Cdd:PRK12827 164 KAGLIGLTKTLANELAPRG--ITVNAVAPGAINTPMADNAAPTEHLLNPVPVQRLGEPDEVAALVAFLV-SDAASYVTGQ 240

                 ...
gi 18413950  286 YFA 288
Cdd:PRK12827 241 VIP 243
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
42-235 5.99e-10

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: 58.65  E-value: 5.99e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEIlrqNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:cd08942  15 SRGIGRMIAQGFLEAGARVIISARKAEACADAAEEL---SAYGECIAIPADLSSEEGIEALVARVAERSDRLDVLVNNAG 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 122 VMF-CPY-QLSEDGIELQFATNHIGHFLLTNLLLDTMKnTAKTSGVEGRILNVSSVAHIytyqegiqfdsindICSYSDK 199
Cdd:cd08942  92 ATWgAPLeAFPESGWDKVMDINVKSVFFLTQALLPLLR-AAATAENPARVINIGSIAGI--------------VVSGLEN 156
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 18413950 200 RAYGQSKLAniLHanELSRQLQEE--GVNITANSVHPG 235
Cdd:cd08942 157 YSYGASKAA--VH--QLTRKLAKElaGEHITVNAIAPG 190
PRK07063 PRK07063
SDR family oxidoreductase;
49-132 2.26e-09

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 57.37  E-value: 2.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   49 TARVLSKRGAHVVIGARNMGAAENAKTEILRQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGV-MFC-P 126
Cdd:PRK07063  23 IARAFAREGAAVALADLDAALAERAAAAIARDVAGARVLAVPADVTDAASVAAAVAAAEEAFGPLDVLVNNAGInVFAdP 102

                 ....*.
gi 18413950  127 YQLSED 132
Cdd:PRK07063 103 LAMTDE 108
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
42-243 2.50e-09

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 57.08  E-value: 2.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVigARNMGAAENAK-TEILRQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNA 120
Cdd:PRK12824  11 KRGIGSAIARELLNDGYRVI--ATYFSGNDCAKdWFEEYGFTEDQVRLKELDVTDTEECAEALAEIEEEEGPVDILVNNA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  121 GV----MF--CPYQLSEDGIElqfaTNHIGHFLLTNLLLDTMKNTAktsgvEGRILNVSSVAHiytyQEGiQFDSINdic 194
Cdd:PRK12824  89 GItrdsVFkrMSHQEWNDVIN----TNLNSVFNVTQPLFAAMCEQG-----YGRIINISSVNG----LKG-QFGQTN--- 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18413950  195 sysdkraYGQSKLANIlhanELSRQLQEEGV--NITANSVHPGLILTNLFQ 243
Cdd:PRK12824 152 -------YSAAKAGMI----GFTKALASEGAryGITVNCIAPGYIATPMVE 191
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
42-243 2.62e-09

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 56.77  E-value: 2.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIG-ARNMGAAENAKTEIlrQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNA 120
Cdd:PRK05565  14 SGGIGRAIAELLAKEGAKVVIAyDINEEAAQELLEEI--KEEGGDAIAVKADVSSEEDVENLVEQIVEKFGKIDILVNNA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  121 GVM-FCP-YQLSEDGIELQFATNHIGHFLLTNLLLDTMKNtaKTSGVegrILNVSsvahiytyqegiqfdSINDICSYSD 198
Cdd:PRK05565  92 GISnFGLvTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIK--RKSGV---IVNIS---------------SIWGLIGASC 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 18413950  199 KRAYGQSKLANILHANELSRQLQEEGvnITANSVHPGLILTNLFQ 243
Cdd:PRK05565 152 EVLYSASKGAVNAFTKALAKELAPSG--IRVNAVAPGAIDTEMWS 194
PRK06124 PRK06124
SDR family oxidoreductase;
48-176 6.96e-09

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 55.87  E-value: 6.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   48 ETARVLSKRGAHVVIGARNMGAAENAKTEILRQNANARVtlLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGV----- 122
Cdd:PRK06124  26 EIARALAGAGAHVLVNGRNAATLEAAVAALRAAGGAAEA--LAFDIADEEAVAAAFARIDAEHGRLDILVNNVGArdrrp 103
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 18413950  123 MfcpYQLSEDGIELQFATNHIGHFLLTNLLLDTMKntaktSGVEGRILNVSSVA 176
Cdd:PRK06124 104 L---AELDDAAIRALLETDLVAPILLSRLAAQRMK-----RQGYGRIIAITSIA 149
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
42-241 7.76e-09

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: 55.55  E-value: 7.76e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGARNmgaaeNAKTEILRQNANArVTLLQLDLSSIKSikafVREFHALHLPLNLLINNAG 121
Cdd:cd05351  16 GKGIGRATVKALAKAGARVVAVSRT-----QADLDSLVRECPG-IEPVCVDLSDWDA----TEEALGSVGPVDLLVNNAA 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 122 V-MFCPY-QLSEDGIELQFATNHIGHFLLTNLLLDTMKNtaktSGVEGRILNVSSVAhiytyqegiqfdsinDICSYSDK 199
Cdd:cd05351  86 VaILQPFlEVTKEAFDRSFDVNVRAVIHVSQIVARGMIA----RGVPGSIVNVSSQA---------------SQRALTNH 146
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 18413950 200 RAYGQSKLA----NILHANELSRQlqeegvNITANSVHPGLILTNL 241
Cdd:cd05351 147 TVYCSTKAAldmlTKVMALELGPH------KIRVNSVNPTVVMTDM 186
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
42-244 1.03e-08

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: 55.05  E-value: 1.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIG-ARNMGAAENAKTEIlrQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNA 120
Cdd:cd05359   7 SRGIGKAIALRLAERGADVVINyRKSKDAAAEVAAEI--EELGGKAVVVRADVSQPQDVEEMFAAVKERFGRLDVLVSNA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 121 --GVMFCPYQLSEDGIELQFATNHIGHFLLTNLLLDTMkntAKTSGveGRILNVSSVAHIYTYQegiqfdsindicSYSd 198
Cdd:cd05359  85 aaGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLM---RERGG--GRIVAISSLGSIRALP------------NYL- 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 18413950 199 krAYGQSKLAniLHAneLSRQLQEE----GvnITANSVHPGLILTNLFQH 244
Cdd:cd05359 147 --AVGTAKAA--LEA--LVRYLAVElgprG--IRVNAVSPGVIDTDALAH 188
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
42-239 1.45e-08

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: 54.59  E-value: 1.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEILRqnANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:cd05344  10 SSGIGLAIARALAREGARVAICARNRENLERAASELRA--GGAGVLAVVADLTDPEDIDRLVEKAGDAFGRVDILVNNAG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 122 ----VMFcpYQLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAKtsgveGRILNVSSVAhiytyqegIQFDSINDICSyS 197
Cdd:cd05344  88 gpppGPF--AELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGW-----GRIVNISSLT--------VKEPEPNLVLS-N 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 18413950 198 DKRAygqsklANILHANELSRQLQEEgvNITANSVHPGLILT 239
Cdd:cd05344 152 VARA------GLIGLVKTLSRELAPD--GVTVNSVLPGYIDT 185
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
42-243 2.74e-08

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: 54.03  E-value: 2.74e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEILRQNANARVtllqlDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:cd08944  12 GAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALRV-----DVTDEQQVAALFERAVEEFGGLDLLVNNAG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 122 VMFCPYQLSEDGIEL---QFATNHIGHFLLTNLLLDTMKNTAKtsgveGRILNVSSVAHiytyQEGIQFDSindicsysd 198
Cdd:cd08944  87 AMHLTPAIIDTDLAVwdqTMAINLRGTFLCCRHAAPRMIARGG-----GSIVNLSSIAG----QSGDPGYG--------- 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 18413950 199 krAYGQSKLANILHANELSRQLQEEGvnITANSVHPGLILTNLFQ 243
Cdd:cd08944 149 --AYGASKAAIRNLTRTLAAELRHAG--IRCNALAPGLIDTPLLL 189
PRK06949 PRK06949
SDR family oxidoreductase;
42-244 3.76e-08

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 53.61  E-value: 3.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEILRQNANARVtlLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:PRK06949  18 SSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIEAEGGAAHV--VSLDVTDYQSIKAAVAHAETEAGTIDILVNNSG 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  122 V--MFCPYQLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAKTSG---VEGRILNVSSVAHIYTY-QEGIqfdsindics 195
Cdd:PRK06949  96 VstTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIARAKGAGntkPGGRIINIASVAGLRVLpQIGL---------- 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 18413950  196 ysdkraYGQSKLANILHANELSRQLQEEGVNItaNSVHPGLILTNLFQH 244
Cdd:PRK06949 166 ------YCMSKAAVVHMTRAMALEWGRHGINV--NAICPGYIDTEINHH 206
PRK09072 PRK09072
SDR family oxidoreductase;
43-227 4.30e-08

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 53.41  E-value: 4.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   43 GGIGMETARVLSKRGAHVVIGARNMGAAENAKTEIlrqNANARVTLLQLDLSSIKSIKAfVREFHALHLPLNLLINNAGV 122
Cdd:PRK09072  15 GGIGQALAEALAAAGARLLLVGRNAEKLEALAARL---PYPGRHRWVVADLTSEAGREA-VLARAREMGGINVLINNAGV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  123 -MFCPY-QLSEDGIELQFATNHIGHFLLTNLLLDTMKntAKTSGVegrILNVSSVahiytyqegiqFDSIndicSYSDKR 200
Cdd:PRK09072  91 nHFALLeDQDPEAIERLLALNLTAPMQLTRALLPLLR--AQPSAM---VVNVGST-----------FGSI----GYPGYA 150
                        170       180
                 ....*....|....*....|....*....
gi 18413950  201 AYGQSKLAniLH--ANELSRQLQEEGVNI 227
Cdd:PRK09072 151 SYCASKFA--LRgfSEALRRELADTGVRV 177
PRK06123 PRK06123
SDR family oxidoreductase;
48-241 5.67e-08

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 52.86  E-value: 5.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   48 ETARVLSKRGAHVVIGARNMGAAENAKTEILRQnANARVTLLQLDLSS----IKSIKAFVREFHalhlPLNLLINNAGVM 123
Cdd:PRK06123  17 ATALLAAERGYAVCLNYLRNRDAAEAVVQAIRR-QGGEALAVAADVADeadvLRLFEAVDRELG----RLDALVNNAGIL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  124 FCPYQLSE-DGIELQ--FATNHIGHFLLTNLLLDTMknTAKTSGVEGRILNVSSVAHiytyqegiQFDSINDicsYSDkr 200
Cdd:PRK06123  92 EAQMRLEQmDAARLTriFATNVVGSFLCAREAVKRM--STRHGGRGGAIVNVSSMAA--------RLGSPGE---YID-- 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 18413950  201 aYGQSKLANILHANELSRQLQEEGVNItaNSVHPGLILTNL 241
Cdd:PRK06123 157 -YAASKGAIDTMTIGLAKEVAAEGIRV--NAVRPGVIYTEI 194
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
43-265 8.09e-08

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: 52.67  E-value: 8.09e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  43 GGIGMETARVLSKRGAHVVIGARNMgaaENAKTEILRQNANARVTLLQLDLSSIKSIKAfVREFHALHLP---LNLLINN 119
Cdd:cd09805  10 SGFGNLLAKKLDSLGFTVLAGCLTK---NGPGAKELRRVCSDRLRTLQLDVTKPEQIKR-AAQWVKEHVGekgLWGLVNN 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 120 AGVMfcpyQLSEDGIELQFAT-------NHIGHFLLTNLLLDTMKNtAKtsgveGRILNVSSVAhiytyqegiqfdsiND 192
Cdd:cd09805  86 AGIL----GFGGDEELLPMDDyrkcmevNLFGTVEVTKAFLPLLRR-AK-----GRVVNVSSMG--------------GR 141
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18413950 193 IcSYSDKRAYGQSKLANILHANELSRQLQEEGVNITAnsVHPGLILTNLFQHTALLMRFLKffsfYLWKNIPQ 265
Cdd:cd09805 142 V-PFPAGGAYCASKAAVEAFSDSLRRELQPWGVKVSI--IEPGNFKTGITGNSELWEKQAK----KLWERLPP 207
FabG-like PRK07231
SDR family oxidoreductase;
42-241 1.43e-07

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 51.75  E-value: 1.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEIlrqNANARVTLLQLDLSSIKSIKAFVR----EFHALHlplnLLI 117
Cdd:PRK07231  14 SSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEI---LAGGRAIAVAADVSDEADVEAAVAaaleRFGSVD----ILV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  118 NNAGV--MFCP-YQLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAKtsgveGRILNVSSVAhiytyqeGIQF-DSINdi 193
Cdd:PRK07231  87 NNAGTthRNGPlLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGG-----GAIVNVASTA-------GLRPrPGLG-- 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 18413950  194 csysdkrAYGQSKLANILhaneLSRQLQEE--GVNITANSVHPGLILTNL 241
Cdd:PRK07231 153 -------WYNASKGAVIT----LTKALAAElgPDKIRVNAVAPVVVETGL 191
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
44-241 1.80e-07

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: 51.72  E-value: 1.80e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  44 GIGMETARVLSKRGAHVVIGARNMGAAENAKTEIlrqnaNARVTLLQLDLSSIKSIKAFVREFHALHlPLNLLINNAGVM 123
Cdd:cd08951  18 GLGLAAARTLLHQGHEVVLHARSQKRAADAKAAC-----PGAAGVLIGDLSSLAETRKLADQVNAIG-RFDAVIHNAGIL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 124 FCPYQLSED-GIELQFATNHIGHFLLTNLLLDTMkntaktsgvegRILNVSSVAHiytyqEGIQfDSINDIC----SYSD 198
Cdd:cd08951  92 SGPNRKTPDtGIPAMVAVNVLAPYVLTALIRRPK-----------RLIYLSSGMH-----RGGN-ASLDDIDwfnrGEND 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 18413950 199 KRAYGQSKLANILHANELSRQLQeegvNITANSVHPGLILTNL 241
Cdd:cd08951 155 SPAYSDSKLHVLTLAAAVARRWK----DVSSNAVHPGWVPTKM 193
PRK06947 PRK06947
SDR family oxidoreductase;
42-241 2.07e-07

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 51.34  E-value: 2.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIG-ARNMGAAENAKTEIlrQNANARVTLLQLDLSS----IKSIKAFVREFHALHlplnLL 116
Cdd:PRK06947  11 SRGIGRATAVLAAARGWSVGINyARDAAAAEETADAV--RAAGGRACVVAGDVANeadvIAMFDAVQSAFGRLD----AL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  117 INNAGVMFCPYQLSE---DGIELQFATNHIGHFLLTNLLLDTMknTAKTSGVEGRILNVSSVAHiytyqegiQFDSINDi 193
Cdd:PRK06947  85 VNNAGIVAPSMPLADmdaARLRRMFDTNVLGAYLCAREAARRL--STDRGGRGGAIVNVSSIAS--------RLGSPNE- 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 18413950  194 csYSDkraYGQSKLANILHANELSRQLQEEGVNItaNSVHPGLILTNL 241
Cdd:PRK06947 154 --YVD---YAGSKGAVDTLTLGLAKELGPHGVRV--NAVRPGLIETEI 194
PRK12829 PRK12829
short chain dehydrogenase; Provisional
42-237 2.34e-07

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 51.21  E-value: 2.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIGARNMGAAEnaktEILRQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:PRK12829  20 ASGIGRAIAEAFAEAGARVHVCDVSEAALA----ATAARLPGAKVTATVADVADPAQVERVFDTAVERFGGLDVLVNNAG 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  122 VmFCPY----QLSEDGIELQFATNHIGHFLLTNLLLDTMkntaKTSGVEGRILNVSSVAhiytyqegiqfdsinDICSYS 197
Cdd:PRK12829  96 I-AGPTggidEITPEQWEQTLAVNLNGQFYFARAAVPLL----KASGHGGVIIALSSVA---------------GRLGYP 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 18413950  198 DKRAYGQSKLANILHANELSRQLQEEGvnITANSVHPGLI 237
Cdd:PRK12829 156 GRTPYAASKWAVVGLVKSLAIELGPLG--IRVNAILPGIV 193
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
42-243 2.51e-07

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: 50.84  E-value: 2.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEILRqnanaRVTLLQLDLSS----IKSIKAFVREFHalhlPLNLLI 117
Cdd:cd05341  14 ARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGD-----AARFFHLDVTDedgwTAVVDTAREAFG----RLDVLV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 118 NNAGVMFCPYQLSEDGIELQ--FATNHIGHFLLTNLLLDTMKNTAKtsgveGRILNVSSVAhiytyqegiqfdSINDICS 195
Cdd:cd05341  85 NNAGILTGGTVETTTLEEWRrlLDINLTGVFLGTRAVIPPMKEAGG-----GSIINMSSIE------------GLVGDPA 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 18413950 196 YSdkrAYGQSKLANILHANELSRQLQEEGVNITANSVHPGLILTNLFQ 243
Cdd:cd05341 148 LA---AYNASKGAVRGLTKSAALECATQGYGIRVNSVHPGYIYTPMTD 192
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
42-238 2.79e-07

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 52.16  E-value: 2.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEILRQNanaRVTLLQLDLSSIKSIKA----FVREFHAlhlpLNLLI 117
Cdd:PRK08324 431 AGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGPD---RALGVACDVTDEAAVQAafeeAALAFGG----VDIVV 503
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  118 NNAGVMF--CPYQLSEDGIELQFATNHIGHFLLTNLLLDTMKNtaktSGVEGRILNVSSVahiytyqegiqfdsiNDICS 195
Cdd:PRK08324 504 SNAGIAIsgPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKA----QGLGGSIVFIASK---------------NAVNP 564
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 18413950  196 YSDKRAYGQSKLAnilhANELSRQLQEEG--VNITANSVHPGLIL 238
Cdd:PRK08324 565 GPNFGAYGAAKAA----ELHLVRQLALELgpDGIRVNGVNPDAVV 605
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
44-175 3.56e-07

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: 50.38  E-value: 3.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  44 GIGMETARVLSKRGAHVVIGARNMGAAENAKTEIlrQNANARVtllqLDLSSIKSIKAFVREFHALHLPLNLLINNAGVM 123
Cdd:cd05370  16 GIGLALARKFLEAGNTVIITGRREERLAEAKKEL--PNIHTIV----LDVGDAESVEALAEALLSEYPNLDILINNAGIQ 89
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18413950 124 FcPYQLSE-----DGIELQFATNHIGHFLLTNLLLDTMKNTAktsgvEGRILNVSSV 175
Cdd:cd05370  90 R-PIDLRDpasdlDKADTEIDTNLIGPIRLIKAFLPHLKKQP-----EATIVNVSSG 140
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
42-242 3.66e-07

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 50.58  E-value: 3.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVI-GARNMGAAENAKTEIlrQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNA 120
Cdd:PRK05557  14 SRGIGRAIAERLAAQGANVVInYASSEAGAEALVAEI--GALGGKALAVQGDVSDAESVERAVDEAKAEFGGVDILVNNA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  121 GVM----FcpYQLSEDGIELQFATNHIGHFLLTNLLLDTMkntakTSGVEGRILNVSSVAHIYTyqegiQFDSINdicsy 196
Cdd:PRK05557  92 GITrdnlL--MRMKEEDWDRVIDTNLTGVFNLTKAVARPM-----MKQRSGRIINISSVVGLMG-----NPGQAN----- 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 18413950  197 sdkraYGQSKLAniLH------ANEL-SRqlqeegvNITANSVHPGLILTNLF 242
Cdd:PRK05557 155 -----YAASKAG--VIgftkslARELaSR-------GITVNAVAPGFIETDMT 193
PRK06182 PRK06182
short chain dehydrogenase; Validated
42-181 5.52e-07

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 50.34  E-value: 5.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIGARNMGaaenaKTEILrqnANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:PRK06182  12 SSGIGKATARRLAAQGYTVYGAARRVD-----KMEDL---ASLGVHPLSLDVTDEASIKAAVDTIIAEEGRIDVLVNNAG 83
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18413950  122 vmFCPYQLSED-GIE---LQFATNHIGHFLLTNLLLDTMKntAKTSgveGRILNVSSVA-HIYTY 181
Cdd:PRK06182  84 --YGSYGAIEDvPIDearRQFEVNLFGAARLTQLVLPHMR--AQRS---GRIINISSMGgKIYTP 141
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
42-176 5.61e-07

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: 49.94  E-value: 5.61e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEIL--RQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINN 119
Cdd:cd08939  10 SSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIEaeANASGQKVSYISADLSDYEEVEQAFAQAVEKGGPPDLVVNC 89
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18413950 120 AGVMFCPY--QLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAKtsgveGRILNVSSVA 176
Cdd:cd08939  90 AGISIPGLfeDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRP-----GHIVFVSSQA 143
PRK12939 PRK12939
short chain dehydrogenase; Provisional
42-242 7.14e-07

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 49.58  E-value: 7.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEIlrQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:PRK12939  16 ARGLGAAFAEALAEAGATVAFNDGLAAEARELAAAL--EAAGGRAHAIAADLADPASVQRFFDAAAAALGGLDGLVNNAG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  122 VMFCPY--QLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAKtsgveGRILNVSSVAHIYTYQEGIqfdsindicsysdk 199
Cdd:PRK12939  94 ITNSKSatELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGR-----GRIVNLASDTALWGAPKLG-------------- 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 18413950  200 rAYGQSKLANILHANELSRQLQEEGvnITANSVHPGLILTNLF 242
Cdd:PRK12939 155 -AYVASKGAVIGMTRSLARELGGRG--ITVNAIAPGLTATEAT 194
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
42-178 7.98e-07

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: 49.31  E-value: 7.98e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGARNMGAAEnaktEILRQNANARVTlLQLDLSSIKSIKAFVRefHALHL--PLNLLINN 119
Cdd:cd05345  14 GSGFGEGIARRFAQEGARVVIADINADGAE----RVAADIGEAAIA-IQADVTKRADVEAMVE--AALSKfgRLDILVNN 86
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18413950 120 AGVMFCP---YQLSEDGIELQFATNHIGHFLLTNLLLDTMKntaktSGVEGRILNVSSVAHI 178
Cdd:cd05345  87 AGITHRNkpmLEVDEEEFDRVFAVNVKSIYLSAQALVPHME-----EQGGGVIINIASTAGL 143
PRK12937 PRK12937
short chain dehydrogenase; Provisional
42-242 1.11e-06

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 48.97  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIG-ARNMGAAENAKTEIlrQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNA 120
Cdd:PRK12937  14 SRGIGAAIARRLAADGFAVAVNyAGSAAAADELVAEI--EAAGGRAIAVQADVADAAAVTRLFDAAETAFGRIDVLVNNA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  121 GVMFCPY--QLSEDGIELQFATNHIGHFLltnllldTMKNTAKTSGVEGRILNVSsvahiyTYQEGIQFDsindicSYSd 198
Cdd:PRK12937  92 GVMPLGTiaDFDLEDFDRTIATNLRGAFV-------VLREAARHLGQGGRIINLS------TSVIALPLP------GYG- 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 18413950  199 krAYGQSK--LANILHAneLSRQLQeeGVNITANSVHPGLILTNLF 242
Cdd:PRK12937 152 --PYAASKaaVEGLVHV--LANELR--GRGITVNAVAPGPVATELF 191
PRK09242 PRK09242
SDR family oxidoreductase;
42-241 1.37e-06

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 48.98  E-value: 1.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEILRQNANARVTLLQLDLSS---IKSIKAFVRE-FHALHlplnLLI 117
Cdd:PRK09242  18 SKGIGLAIAREFLGLGADVLIVARDADALAQARDELAEEFPEREVHGLAADVSDdedRRAILDWVEDhWDGLH----ILV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  118 NNAGVMFCPYQL--SEDGIELQFATNHIGHFLLTNLLLDTMKNTAKTSgvegrILNVSSVAHIYTYQEGIqfdsindics 195
Cdd:PRK09242  94 NNAGGNIRKAAIdyTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSA-----IVNIGSVSGLTHVRSGA---------- 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 18413950  196 ysdkrAYGQSKLAnilhANELSRQLQEE--GVNITANSVHPGLILTNL 241
Cdd:PRK09242 159 -----PYGMTKAA----LLQMTRNLAVEwaEDGIRVNAVAPWYIRTPL 197
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
42-241 2.25e-06

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: 48.23  E-value: 2.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGA-RNMGAAENAKTEILRQNANARVtlLQLDLSSIKS----IKAFVREFHALHlplnLL 116
Cdd:cd05337  10 SRGIGRAIATELAARGFDIAINDlPDDDQATEVVAEVLAAGRRAIY--FQADIGELSDhealLDQAWEDFGRLD----CL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 117 INNAGVMFCP----YQLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAKT-SGVEGRILNVSsvahiytyqegiqfdSIN 191
Cdd:cd05337  84 VNNAGIAVRPrgdlLDLTEDSFDRLIAINLRGPFFLTQAVARRMVEQPDRfDGPHRSIIFVT---------------SIN 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 18413950 192 DICSYSDKRAYGQSKLANILHANELSRQLQEEGvnITANSVHPGLILTNL 241
Cdd:cd05337 149 AYLVSPNRGEYCISKAGLSMATRLLAYRLADEG--IAVHEIRPGLIHTDM 196
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
49-244 2.81e-06

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: 47.76  E-value: 2.81e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  49 TARVLSKRGAHVVIGARNMGAAENAKTEILRQNANARVtllqldlssiksIKAFVREFHALHL----------PLNLLIN 118
Cdd:cd05360  16 TALAFAERGAKVVLAARSAEALHELAREVRELGGEAIA------------VVADVADAAQVERaadtaverfgRIDTWVN 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 119 NAGVMFcpYQLSEDGIELQFA----TNHIGHFLLTNLLLDTMKntaktSGVEGRILNVSSVAHiytyQEGIQFDSindic 194
Cdd:cd05360  84 NAGVAV--FGRFEDVTPEEFRrvfdVNYLGHVYGTLAALPHLR-----RRGGGALINVGSLLG----YRSAPLQA----- 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 18413950 195 sysdkrAYGQSKLANILHANELSRQLQEEGVNITANSVHPGLILTNLFQH 244
Cdd:cd05360 148 ------AYSASKHAVRGFTESLRAELAHDGAPISVTLVQPTAMNTPFFGH 191
PRK07060 PRK07060
short chain dehydrogenase; Provisional
42-241 2.83e-06

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 47.79  E-value: 2.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEIlrqnaNARVtlLQLDLSSIKSIKAFVrefhALHLPLNLLINNAG 121
Cdd:PRK07060  18 SSGIGRACAVALAQRGARVVAAARNAAALDRLAGET-----GCEP--LRLDVGDDAAIRAAL----AAAGAFDGLVNCAG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  122 --VMFCPYQLSEDGIELQFATNHIGHFLltnllldTMKNTAK---TSGVEGRILNVSSVAHIYTYQegiqfdsindicsy 196
Cdd:PRK07060  87 iaSLESALDMTAEGFDRVMAVNARGAAL-------VARHVARamiAAGRGGSIVNVSSQAALVGLP-------------- 145
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 18413950  197 sDKRAYGQSKLANILHANELSRQLQEEGvnITANSVHPGLILTNL 241
Cdd:PRK07060 146 -DHLAYCASKAALDAITRVLCVELGPHG--IRVNSVNPTVTLTPM 187
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
42-242 3.75e-06

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: 47.39  E-value: 3.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEilrQNANARVTLLQLDLSSIKSIKA----FVREFHAlhlpLNLLI 117
Cdd:cd08943  10 ASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEA---AQGGPRALGVQCDVTSEAQVQSafeqAVLEFGG----LDIVV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 118 NNAGVmFCPYQLSEDGIEL---QFATNHIGHFLLTNLLLDTMkntaKTSGVEGRILNVSSVahiytyqegiqfdsiNDIC 194
Cdd:cd08943  83 SNAGI-ATSSPIAETSLEDwnrSMDINLTGHFLVSREAFRIM----KSQGIGGNIVFNASK---------------NAVA 142
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 18413950 195 SYSDKRAYGQSKLAnilhANELSRQLQEEG--VNITANSVHPGLILTNLF 242
Cdd:cd08943 143 PGPNAAAYSAAKAA----EAHLARCLALEGgeDGIRVNTVNPDAVFRGSK 188
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
42-239 3.92e-06

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: 47.18  E-value: 3.92e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEIlrQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:cd05365   8 AAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAI--QQAGGQAIGLECNVTSEQDLEAVVKATVSQFGGITILVNNAG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 122 ----VMFCPYQLSEDgIELQFATNHIGHFLLTNLLLDTMKntaKTSGveGRILNVSSVAHIYTyqegiqfdsindicSYs 197
Cdd:cd05365  86 gggpKPFDMPMTEED-FEWAFKLNLFSAFRLSQLCAPHMQ---KAGG--GAILNISSMSSENK--------------NV- 144
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 18413950 198 DKRAYGQSKLAnilhANELSRQLQEE--GVNITANSVHPGLILT 239
Cdd:cd05365 145 RIAAYGSSKAA----VNHMTRNLAFDlgPKGIRVNAVAPGAVKT 184
PRK08017 PRK08017
SDR family oxidoreductase;
44-239 4.08e-06

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 47.39  E-value: 4.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   44 GIGMETARVLSKRGAHVVIGARnmgaaenaKTEILRQNANARVTLLQLDLSSIKSIKAFVREFHAL-HLPLNLLINNAGV 122
Cdd:PRK08017  13 GIGLEAALELKRRGYRVLAACR--------KPDDVARMNSLGFTGILLDLDDPESVERAADEVIALtDNRLYGLFNNAGF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  123 -MFCPYQ-LSEDGIELQFATNHIGHFLLTNLLLDTMKNTAktsgvEGRILNVSSVAhiytyqegiqfdsinDICSYSDKR 200
Cdd:PRK08017  85 gVYGPLStISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHG-----EGRIVMTSSVM---------------GLISTPGRG 144
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 18413950  201 AYGQSKLANILHANELSRQLQEEGVNITAnsVHPGLILT 239
Cdd:PRK08017 145 AYAASKYALEAWSDALRMELRHSGIKVSL--IEPGPIRT 181
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
42-244 5.39e-06

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 47.02  E-value: 5.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIG-ARNMGAAENAKTEIlrQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNA 120
Cdd:PRK08063  13 SRGIGKAIALRLAEEGYDIAVNyARSRKAAEETAEEI--EALGRKALAVKANVGDVEKIKEMFAQIDEEFGRLDVFVNNA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  121 --GVMFCPYQLSEDGIELQFATNHIGhflLTNLLLDTMKNTAKTSGveGRILNVSSvahiytyqegiqFDSINDICSYSd 198
Cdd:PRK08063  91 asGVLRPAMELEESHWDWTMNINAKA---LLFCAQEAAKLMEKVGG--GKIISLSS------------LGSIRYLENYT- 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 18413950  199 krAYGQSKLAniLHAneLSRQLQEE--GVNITANSVHPGLILTNLFQH 244
Cdd:PRK08063 153 --TVGVSKAA--LEA--LTRYLAVElaPKGIAVNAVSGGAVDTDALKH 194
PRK08264 PRK08264
SDR family oxidoreductase;
42-241 5.51e-06

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 46.81  E-value: 5.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAH-VVIGARNMGAAEnakteilrqNANARVTLLQLDLSSIKSIKAFVRefHAlhLPLNLLINNA 120
Cdd:PRK08264  15 NRGIGRAFVEQLLARGAAkVYAAARDPESVT---------DLGPRVVPLQLDVTDPASVAAAAE--AA--SDVTILVNNA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  121 GVMFCPYQL---SEDGIELQFATNHIGHFLLTNLLLDTMKNTAKtsgveGRILNVSSVAHIYTYQEGiqfdsindicsys 197
Cdd:PRK08264  82 GIFRTGSLLlegDEDALRAEMETNYFGPLAMARAFAPVLAANGG-----GAIVNVLSVLSWVNFPNL------------- 143
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 18413950  198 dkRAYGQSKLA-----NILHAnELSRQlqeegvNITANSVHPGLILTNL 241
Cdd:PRK08264 144 --GTYSASKAAawsltQALRA-ELAPQ------GTRVLGVHPGPIDTDM 183
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
42-241 7.85e-06

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: 46.67  E-value: 7.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGARNmgaaENAKTEILRQ--NANARVTLLQLDLSSI---KSIKAFVreFHALHLPLNLL 116
Cdd:cd05329  15 TKGIGYAIVEELAGLGAEVYTCARN----QKELDECLTEwrEKGFKVEGSVCDVSSRserQELMDTV--ASHFGGKLNIL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 117 INNAGVMFCPYQL--SEDGIELQFATNHIGHFLLTNLLLDTMKNTAKTSgvegrILNVSSVAhiytyqeGIQfdsindic 194
Cdd:cd05329  89 VNNAGTNIRKEAKdyTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGN-----IVFISSVA-------GVI-------- 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 18413950 195 SYSDKRAYGQSKLAnilhANELSRQLQEEGV--NITANSVHPGLILTNL 241
Cdd:cd05329 149 AVPSGAPYGATKGA----LNQLTRSLACEWAkdNIRVNAVAPWVIATPL 193
PRK08589 PRK08589
SDR family oxidoreductase;
42-241 8.06e-06

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 46.70  E-value: 8.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKtEIlrQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:PRK08589  15 STGIGQASAIALAQEGAYVLAVDIAEAVSETVD-KI--KSNGGKAKAYHVDISDEQQVKDFASEIKEQFGRVDVLFNNAG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  122 VMFCPYQLSEDGIELQ---FATNHIGHFLLTNLLLDTMKNTAktsgveGRILNVSSVAhiytyqeGIQFDsindicsySD 198
Cdd:PRK08589  92 VDNAAGRIHEYPVDVFdkiMAVDMRGTFLMTKMLLPLMMEQG------GSIINTSSFS-------GQAAD--------LY 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 18413950  199 KRAYGQSKLANILHANELSRQLQEEGvnITANSVHPGLILTNL 241
Cdd:PRK08589 151 RSGYNAAKGAVINFTKSIAIEYGRDG--IRANAIAPGTIETPL 191
PRK06179 PRK06179
short chain dehydrogenase; Provisional
42-175 1.21e-05

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 46.05  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIGARNMGAAEnakteilrqnANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:PRK06179  13 SSGIGRATAEKLARAGYRVFGTSRNPARAA----------PIPGVELLELDVTDDASVQAAVDEVIARAGRIDVLVNNAG 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 18413950  122 VMFCPyQLSEDGIElQ----FATNHIGHFLLTNLLLDTMKntAKTSgveGRILNVSSV 175
Cdd:PRK06179  83 VGLAG-AAEESSIA-QaqalFDTNVFGILRMTRAVLPHMR--AQGS---GRIINISSV 133
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
42-174 1.30e-05

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: 45.66  E-value: 1.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEIlRQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:cd05369  12 GTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEI-SSATGGRAHPIQCDVRDPEAVEAAVDETLKEFGKIDILINNAA 90
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18413950 122 VMF-CPY-QLSEDGIELQFATNHIGHFLLTNLLLDTMKNtaktSGVEGRILNVSS 174
Cdd:cd05369  91 GNFlAPAeSLSPNGFKTVIDIDLNGTFNTTKAVGKRLIE----AKHGGSILNISA 141
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
42-257 1.41e-05

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: 45.86  E-value: 1.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEIL-RQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNA 120
Cdd:cd05364  12 SSGIGAGTAILFARLGARLALTGRDAERLEETRQSCLqAGVSEKKILLVVADLTEEEGQDRIISTTLAKFGRLDILVNNA 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 121 GVMfcpyqlSEDGIELQ--------FATNHIGHFLLTNLLLDTMKNTaktsgvEGRILNVSSVAHIYtyqegiqfdsind 192
Cdd:cd05364  92 GIL------AKGGGEDQdieeydkvMNLNLRAVIYLTKLAVPHLIKT------KGEIVNVSSVAGGR------------- 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18413950 193 icSYSDKRAYGQSKLANILHANELSRQLQEEGVNItaNSVHPGLILTNLfqHTALLM---RFLKFFSF 257
Cdd:cd05364 147 --SFPGVLYYCISKAALDQFTRCTALELAPKGVRV--NSVSPGVIVTGF--HRRMGMpeeQYIKFLSR 208
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
42-243 1.75e-05

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 45.65  E-value: 1.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIGARNMGAAenAKTEILRQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:PRK12429  13 ASGIGLEIALALAKEGAKVVIADLNDEAA--AAAAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVETFGGVDILVNNAG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  122 VMFCP--YQLSEDGIELQFATNHIGHFLLTNLLLDTMKntaKTSGveGRILNVSSVahiytyqegiqfdsiNDICSYSDK 199
Cdd:PRK12429  91 IQHVApiEDFPTEKWKKMIAIMLDGAFLTTKAALPIMK---AQGG--GRIINMASV---------------HGLVGSAGK 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 18413950  200 RAYGQSKLANIlhanELSRQLQEEGV--NITANSVHPGLILTNLFQ 243
Cdd:PRK12429 151 AAYVSAKHGLI----GLTKVVALEGAthGVTVNAICPGYVDTPLVR 192
PRK05855 PRK05855
SDR family oxidoreductase;
45-245 1.99e-05

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 46.13  E-value: 1.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   45 IGMETARVLSKRGAHVVIGARNMGAAENAKTEIlrQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGVmf 124
Cdd:PRK05855 327 IGRETALAFAREGAEVVASDIDEAAAERTAELI--RAAGAVAHAYRVDVSDADAMEAFAEWVRAEHGVPDIVVNNAGI-- 402
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  125 cpyqlSEDGIELQFATNHIGHFLLTNL-------------LLDtmkntaktSGVEGRILNVSSVAhiytyqegiqfdsin 191
Cdd:PRK05855 403 -----GMAGGFLDTSAEDWDRVLDVNLwgvihgcrlfgrqMVE--------RGTGGHIVNVASAA--------------- 454
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18413950  192 dicSYSDKR---AYGQSKLANILHANELSRQLQEEGVNITAnsVHPGLILTNLFQHT 245
Cdd:PRK05855 455 ---AYAPSRslpAYATSKAAVLMLSECLRAELAAAGIGVTA--ICPGFVDTNIVATT 506
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
42-241 2.67e-05

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: 44.63  E-value: 2.67e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEILRQNANarVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:cd05350   7 SSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNPNPS--VEVEILDVTDEERNQLVIAELEAELGGLDLVIINAG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 122 VMFcpyqlSEDGIELQFA-------TNHIGHFLLTNLLLDTMKntAKTSgveGRILNVSSVAHIYtyqegiqfdsindic 194
Cdd:cd05350  85 VGK-----GTSLGDLSFKafretidTNLLGAAAILEAALPQFR--AKGR---GHLVLISSVAALR--------------- 139
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 18413950 195 SYSDKRAYGQSKLANILHANELSRQLQEEGVNITanSVHPGLILTNL 241
Cdd:cd05350 140 GLPGAAAYSASKAALSSLAESLRYDVKKRGIRVT--VINPGFIDTPL 184
PRK07201 PRK07201
SDR family oxidoreductase;
43-176 2.97e-05

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 45.71  E-value: 2.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   43 GGIGMETARVLSKRGAHVVIGARNMGAAENAKTEILRQNANARVtlLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG- 121
Cdd:PRK07201 381 SGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAKGGTAHA--YTCDLTDSAAVDHTVKDILAEHGHVDYLVNNAGr 458
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18413950  122 -----VMfcpyqLSED---GIELQFATNHIGHFLLTNLLLDTMknTAKTSgveGRILNVSSVA 176
Cdd:PRK07201 459 sirrsVE-----NSTDrfhDYERTMAVNYFGAVRLILGLLPHM--RERRF---GHVVNVSSIG 511
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
42-243 3.34e-05

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: 44.75  E-value: 3.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGarNMGAAENAKTEILRQNANARVTLLQL--DLSSIKSIKAFVREFHALHLPLNLLINN 119
Cdd:cd08940  11 TSGIGLGIARALAAAGANIVLN--GFGDAAEIEAVRAGLAAKHGVKVLYHgaDLSKPAAIEDMVAYAQRQFGGVDILVNN 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 120 AGVMFCP--YQLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAktsgvEGRILNVSSVahiytyqegiqfdsiNDICSYS 197
Cdd:cd08940  89 AGIQHVApiEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQG-----WGRIINIASV---------------HGLVASA 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 18413950 198 DKRAYGQSKLANIlhanELSR--QLQEEGVNITANSVHPGLILTNLFQ 243
Cdd:cd08940 149 NKSAYVAAKHGVV----GLTKvvALETAGTGVTCNAICPGWVLTPLVE 192
PRK07326 PRK07326
SDR family oxidoreductase;
42-176 5.01e-05

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 43.85  E-value: 5.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEIlrqNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:PRK07326  15 SKGIGFAIAEALLAEGYKVAITARDQKELEEAAAEL---NNKGNVLGLAADVRDEADVQRAVDAIVAAFGGLDVLIANAG 91
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18413950  122 V-MFCPYQ-LSEDGIELQFATNHIGHFLLTNLLLDTMKNTaktsgvEGRILNVSSVA 176
Cdd:PRK07326  92 VgHFAPVEeLTPEEWRLVIDTNLTGAFYTIKAAVPALKRG------GGYIINISSLA 142
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
42-270 5.73e-05

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: 44.04  E-value: 5.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEIlrQNANARVTL-LQLDLSSIKSIKAFVREFHALHLPLNLLINNA 120
Cdd:cd05343  15 SVGIGAAVARALVQHGMKVVGCARRVDKIEALAAEC--QSAGYPTLFpYQCDLSNEEQILSMFSAIRTQHQGVDVCINNA 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 121 GVMFcPYQLSE---DGIELQFATNHIGHFLLTNLLLDTMKntaKTSGVEGRILNVSSV-AHIYTYQEGIQFdsindicsy 196
Cdd:cd05343  93 GLAR-PEPLLSgktEGWKEMFDVNVLALSICTREAYQSMK---ERNVDDGHIININSMsGHRVPPVSVFHF--------- 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18413950 197 sdkraYGQSKLANILHANELSRQLQEEGVNITANSVHPGLILTNlfqhtallmrflkfFSFYLWKNIPQGAATT 270
Cdd:cd05343 160 -----YAATKHAVTALTEGLRQELREAKTHIRATSISPGLVETE--------------FAFKLHDNDPEKAAAT 214
PRK07109 PRK07109
short chain dehydrogenase; Provisional
48-244 6.22e-05

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 44.14  E-value: 6.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   48 ETARVLSKRGAHVVIGARNMGAAENAKTEIlrQNANARVTLLQLDLSSIKSIKA----FVREFHalhlPLNLLINNAGV- 122
Cdd:PRK07109  23 ATARAFARRGAKVVLLARGEEGLEALAAEI--RAAGGEALAVVADVADAEAVQAaadrAEEELG----PIDTWVNNAMVt 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  123 MFCPY-QLSEDGIELQFATNHIGHFLLTNLLLDTMKNTaktsgVEGRILNVSSVAhiyTYQeGIQFDSindicsysdkrA 201
Cdd:PRK07109  97 VFGPFeDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPR-----DRGAIIQVGSAL---AYR-SIPLQS-----------A 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 18413950  202 YGQSKlanilHANE-----LSRQLQEEGVNITANSVHPGLILTNLFQH 244
Cdd:PRK07109 157 YCAAK-----HAIRgftdsLRCELLHDGSPVSVTMVQPPAVNTPQFDW 199
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
42-235 6.74e-05

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 43.78  E-value: 6.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEIlrQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:PRK08213  21 SRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHL--EALGIDALWIAADVADEADIERLAEETLERFGHVDILVNNAG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  122 VMF------CPYQLSEDGIELqfatNHIGHFLLTnllldtmKNTAKTSGVE---GRILNVSSVAhiytyqeGIQFDSInd 192
Cdd:PRK08213  99 ATWgapaedHPVEAWDKVMNL----NVRGLFLLS-------QAVAKRSMIPrgyGRIINVASVA-------GLGGNPP-- 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 18413950  193 icSYSDKRAYGQSKLANIlhanELSRQLQEE-GV-NITANSVHPG 235
Cdd:PRK08213 159 --EVMDTIAYNTSKGAVI----NFTRALAAEwGPhGIRVNAIAPG 197
PRK07774 PRK07774
SDR family oxidoreductase;
42-239 7.44e-05

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 43.58  E-value: 7.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEILRQNANARVtlLQLDLSSIKSIKAF----VREFHALHlplnLLI 117
Cdd:PRK07774  15 AGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGGTAIA--VQVDVSDPDSAKAMadatVSAFGGID----YLV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  118 NNAGVM--FCPYQLSE---DGIELQFATNHIGHFLLTNLLLDTMkntAKTSGveGRILNVSSVAhIYTYQeGIqfdsind 192
Cdd:PRK07774  89 NNAAIYggMKLDLLITvpwDYYKKFMSVNLDGALVCTRAVYKHM---AKRGG--GAIVNQSSTA-AWLYS-NF------- 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 18413950  193 icsysdkraYGQSKLAnilhANELSRQLQEE--GVNITANSVHPGLILT 239
Cdd:PRK07774 155 ---------YGLAKVG----LNGLTQQLARElgGMNIRVNAIAPGPIDT 190
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
42-240 7.99e-05

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: 43.48  E-value: 7.99e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEILRQNANaRVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:cd08930  11 AGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKN-RVIALELDITSKESIKELIESYLEKFGRIDILINNAY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 122 VMFCPY-----QLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAKtsgveGRILNVSSVAHI-----YTYQEGIQFDSIN 191
Cdd:cd08930  90 PSPKVWgsrfeEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGK-----GSIINIASIYGViapdfRIYENTQMYSPVE 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 18413950 192 dicsysdkraYGQSKlANILHaneLSRQLQEE--GVNITANSVHPGLILTN 240
Cdd:cd08930 165 ----------YSVIK-AGIIH---LTKYLAKYyaDTGIRVNAISPGGILNN 201
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
42-244 8.01e-05

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: 43.30  E-value: 8.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEIlrQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:cd08934  12 SSGIGEATARALAAEGAAVAIAARRVDRLEALADEL--EAEGGKALVLELDVTDEQQVDAAVERTVEALGRLDILVNNAG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 122 VMFCPYQLSEDGIELQ--FATNHIGHFLLTNLLLDTMKNTAKtsgveGRILNVSSVAhiytyQEGIQFDSIndicsysdk 199
Cdd:cd08934  90 IMLLGPVEDADTTDWTrmIDTNLLGLMYTTHAALPHHLLRNK-----GTIVNISSVA-----GRVAVRNSA--------- 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 18413950 200 rAYGQSKLANILHANELSRQLQEEGVNITAnsVHPGLILTNLFQH 244
Cdd:cd08934 151 -VYNATKFGVNAFSEGLRQEVTERGVRVVV--IEPGTVDTELRDH 192
PRK06940 PRK06940
short chain dehydrogenase; Provisional
47-243 1.04e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 43.08  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   47 METARVLSKrGAHVVIGARNMGAAENAkTEILRQnANARVTLLQLDLSSIKSIKAFVREFHALHlPLNLLINNAGVmfCP 126
Cdd:PRK06940  15 QAIARRVGA-GKKVLLADYNEENLEAA-AKTLRE-AGFDVSTQEVDVSSRESVKALAATAQTLG-PVTGLVHTAGV--SP 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  127 YQLSedgIELQFATNHIGhfllTNLLLDTMKNTAKTSGVEGRILNVSS-------------VAHIYTYQ----EGIQFDS 189
Cdd:PRK06940  89 SQAS---PEAILKVDLYG----TALVLEEFGKVIAPGGAGVVIASQSGhrlpaltaeqeraLATTPTEEllslPFLQPDA 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 18413950  190 INDicsysDKRAYGQSKLANILHANELSRQLQEEGVNItaNSVHPGLILTNLFQ 243
Cdd:PRK06940 162 IED-----SLHAYQIAKRANALRVMAEAVKWGERGARI--NSISPGIISTPLAQ 208
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
42-246 1.07e-04

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 43.25  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTeiLRQNAnARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:PRK08226  15 LQGIGEGIARVFARHGANLILLDISPEIEKLADE--LCGRG-HRCTAVVADVRDPASVAAAIKRAKEKEGRIDILVNNAG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  122 VM-FCPY-QLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAktsgvEGRILNVSSVAhiytyqegiqfdsiNDICSYSDK 199
Cdd:PRK08226  92 VCrLGSFlDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARK-----DGRIVMMSSVT--------------GDMVADPGE 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 18413950  200 RAYGQSKLANILHANELSRQLQEEgvNITANSVHPGLILTNLFQHTA 246
Cdd:PRK08226 153 TAYALTKAAIVGLTKSLAVEYAQS--GIRVNAICPGYVRTPMAESIA 197
PRK08263 PRK08263
short chain dehydrogenase; Provisional
48-181 1.20e-04

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 43.10  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   48 ETARVLSKRGAHVVIGARNMgaaenAKTEILRQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGVM-FCP 126
Cdd:PRK08263  18 AWTEAALERGDRVVATARDT-----ATLADLAEKYGDRLLPLALDVTDRAAVFAAVETAVEHFGRLDIVVNNAGYGlFGM 92
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18413950  127 Y-QLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAKtsgveGRILNVSSVAHIYTY 181
Cdd:PRK08263  93 IeEVTESEARAQIDTNFFGALWVTQAVLPYLREQRS-----GHIIQISSIGGISAF 143
PRK08340 PRK08340
SDR family oxidoreductase;
50-176 1.22e-04

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 42.87  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   50 ARVLSKRGAHVVIGARNMGAAENAKTEILRQnanARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGVMFC-PYQ 128
Cdd:PRK08340  17 ARELLKKGARVVISSRNEENLEKALKELKEY---GEVYAVKADLSDKDDLKNLVKEAWELLGGIDALVWNAGNVRCePCM 93
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 18413950  129 LSEDGIE--LQFATNHI---GHflLTNLLLDT-MKNtaKTSGVegrILNVSSVA 176
Cdd:PRK08340  94 LHEAGYSdwLEAALLHLvapGY--LTTLLIQAwLEK--KMKGV---LVYLSSVS 140
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
44-239 1.27e-04

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: 42.83  E-value: 1.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  44 GIGMETARVLS---KRGAHVVIGARNMGAAENAkTEILRQNANARVTLLQLDLSSIKSIKAFVREFHALHlpLNLLINNA 120
Cdd:cd09806  11 GIGLHLAVRLAsdpSKRFKVYATMRDLKKKGRL-WEAAGALAGGTLETLQLDVCDSKSVAAAVERVTERH--VDVLVCNA 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 121 GV-MFCPYQ-LSEDGIELQFATNHIGHFLLTNLLLDTMKNTAktsgvEGRILNVSSVAHIytyqEGIQFdsiNDIcsysd 198
Cdd:cd09806  88 GVgLLGPLEaLSEDAMASVFDVNVFGTVRMLQAFLPDMKRRG-----SGRILVTSSVGGL----QGLPF---NDV----- 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 18413950 199 kraYGQSKLANILHANELSRQLQEEGVNITAnsVHPGLILT 239
Cdd:cd09806 151 ---YCASKFALEGLCESLAVQLLPFNVHLSL--IECGPVHT 186
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
50-240 1.37e-04

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 42.80  E-value: 1.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   50 ARVLSKRGAHVVIGARNMGAAEnakTEILRQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGVMFCPYQL 129
Cdd:PRK06935  32 AVALAKAGADIIITTHGTNWDE---TRRLIEKEGRKVTFVQVDLTKPESAEKVVKEALEEFGKIDILVNNAGTIRRAPLL 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  130 --SEDGIELQFATNHIGHFLLTNLLLDTMKNTAktsgvEGRILNVSSvahIYTYQEGIQFDsindicsysdkrAYGQSK- 206
Cdd:PRK06935 109 eyKDEDWNAVMDINLNSVYHLSQAVAKVMAKQG-----SGKIINIAS---MLSFQGGKFVP------------AYTASKh 168
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 18413950  207 -LANILH--ANELSRQlqeegvNITANSVHPGLILTN 240
Cdd:PRK06935 169 gVAGLTKafANELAAY------NIQVNAIAPGYIKTA 199
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
50-246 1.40e-04

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 43.29  E-value: 1.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   50 ARVLSKRGAHVVigARNMGAAENAkteiLRQNANA-RVTLLQLDLSSIKS---IKAFVREFHAlhlPLNLLINNAGV--- 122
Cdd:PRK08261 227 AEVLARDGAHVV--CLDVPAAGEA----LAAVANRvGGTALALDITAPDAparIAEHLAERHG---GLDIVVHNAGItrd 297
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  123 -----MfcpyqlSEDGIELQFATNHIGHFLLTNLLLDtmkntAKTSGVEGRILNVSSVAhiytyqeGI--QFDSINdics 195
Cdd:PRK08261 298 ktlanM------DEARWDSVLAVNLLAPLRITEALLA-----AGALGDGGRIVGVSSIS-------GIagNRGQTN---- 355
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18413950  196 ysdkraYGQSKLANILHANELSRQLQEEGvnITANSVHPGLILTnlfQHTA 246
Cdd:PRK08261 356 ------YAASKAGVIGLVQALAPLLAERG--ITINAVAPGFIET---QMTA 395
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
42-175 1.59e-04

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: 42.38  E-value: 1.59e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEILR----------QNANARVTLLQLDLSSIKSIKAFVREFHALHL 111
Cdd:cd05338  12 SRGIGRAIALRLAKAGATVVVAAKTASEGDNGSAKSLPgtieetaeeiEAAGGQALPIVVDVRDEDQVRALVEATVDQFG 91
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18413950 112 PLNLLINNAGVMFcpYQLSEDGIELQF----ATNHIGHFLLTNLLLDTMKNTAKtsgveGRILNVSSV 175
Cdd:cd05338  92 RLDILVNNAGAIW--LSLVEDTPAKRFdlmqRVNLRGTYLLSQAALPHMVKAGQ-----GHILNISPP 152
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
48-178 1.67e-04

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: 42.59  E-value: 1.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950    48 ETARVLSKRGAHVVIGARNMGAAENAKTEILRQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLN----LLINNAGVM 123
Cdd:TIGR01500  19 ELAKCLKSPGSVLVLSARNDEALRQLKAEIGAERSGLRVVRVSLDLGAEAGLEQLLKALRELPRPKGlqrlLLINNAGTL 98
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18413950   124 fcpYQLSE--------DGIELQFATNHIGHFLLTNLLLDTMKNtakTSGVEGRILNVSSVAHI 178
Cdd:TIGR01500  99 ---GDVSKgfvdlsdsTQVQNYWALNLTSMLCLTSSVLKAFKD---SPGLNRTVVNISSLCAI 155
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
42-239 1.84e-04

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: 42.53  E-value: 1.84e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGARNmgaAENAKTEILR-QNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNA 120
Cdd:cd08945  12 TSGIGLAIARRLGKEGLRVFVCARG---EEGLATTVKElREAGVEADGRTCDVRSVPEIEALVAAAVARYGPIDVLVNNA 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 121 GVM--FCPYQLSEDGIELQFATNHIGHFLLTNLLLdtmKNTAKTSGVEGRILNVSSVAHiytyQEGIQFDSindicsysd 198
Cdd:cd08945  89 GRSggGATAELADELWLDVVETNLTGVFRVTKEVL---KAGGMLERGTGRIINIASTGG----KQGVVHAA--------- 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 18413950 199 krAYGQSKLANILHANELSRQLQEEGvnITANSVHPGLILT 239
Cdd:cd08945 153 --PYSASKHGVVGFTKALGLELARTG--ITVNAVCPGFVET 189
PRK07890 PRK07890
short chain dehydrogenase; Provisional
57-246 1.94e-04

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 42.25  E-value: 1.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   57 GAHVVIGARNMGAAENAKTEIlrQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGVMfcPYQLSEDGIEL 136
Cdd:PRK07890  29 GADVVLAARTAERLDEVAAEI--DDLGRRALAVPTDITDEDQCANLVALALERFGRVDALVNNAFRV--PSMKPLADADF 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  137 Q-----FATNHIGHFLLTNLLLDTMKntaKTSGVegrILNVSS--VAHiytyqegiqfdsindicsySDKR--AYGQSKL 207
Cdd:PRK07890 105 AhwravIELNVLGTLRLTQAFTPALA---ESGGS---IVMINSmvLRH-------------------SQPKygAYKMAKG 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 18413950  208 ANILHANELSRQLQEEGvnITANSVHPGLI----LTNLFQHTA 246
Cdd:PRK07890 160 ALLAASQSLATELGPQG--IRVNSVAPGYIwgdpLKGYFRHQA 200
PRK05993 PRK05993
SDR family oxidoreductase;
43-247 2.26e-04

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 42.32  E-value: 2.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   43 GGIGMETARVLSKRGAHVVIGARnmgaaenaKTEILRQNANARVTLLQLDLSSIKSIKAFVREfhALHLP---LNLLINN 119
Cdd:PRK05993  14 SGIGAYCARALQSDGWRVFATCR--------KEEDVAALEAEGLEAFQLDYAEPESIAALVAQ--VLELSggrLDALFNN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  120 -----AGVMfcpYQLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAktsgvEGRILNVSSVAHIYTYQegiqfdsindic 194
Cdd:PRK05993  84 gaygqPGAV---EDLPTEALRAQFEANFFGWHDLTRRVIPVMRKQG-----QGRIVQCSSILGLVPMK------------ 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 18413950  195 sYsdKRAYGQSKLAniLHANELSRQLQEEGVNITANSVHPGLILTNlFQHTAL 247
Cdd:PRK05993 144 -Y--RGAYNASKFA--IEGLSLTLRMELQGSGIHVSLIEPGPIETR-FRANAL 190
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
42-241 2.52e-04

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: 41.93  E-value: 2.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGARNMGAAEnAKTEILRQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:cd05352  17 SRGIGLAIARALAEAGADVAIIYNSAPRAE-EKAEELAKKYGVKTKAYKCDVSSQESVEKTFKQIQKDFGKIDILIANAG 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 122 VmfCPYQLSEDGIELQFATnhighflLTNLLLDTMKNTAKtsgvegrilnvsSVAHIYTYQegiQFDSINDICSYSDKR- 200
Cdd:cd05352  96 I--TVHKPALDYTYEQWNK-------VIDVNLNGVFNCAQ------------AAAKIFKKQ---GKGSLIITASMSGTIv 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 18413950 201 -------AYGQSKLANILHANELSRQLQEEGvnITANSVHPGLILTNL 241
Cdd:cd05352 152 nrpqpqaAYNASKAAVIHLAKSLAVEWAKYF--IRVNSISPGYIDTDL 197
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
42-241 2.91e-04

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 41.69  E-value: 2.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIgarNMGAAENAKTEILRQNanarVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:PRK06463  16 TRGIGRAIAEAFLREGAKVAV---LYNSAENEAKELREKG----VFTIKCDVGNRDQVKKSKEVVEKEFGRVDVLVNNAG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  122 VMFC-PY-QLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAKtsgveGRILNVSSVAHIYTYQEGIQFDSIndicsysdk 199
Cdd:PRK06463  89 IMYLmPFeEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKN-----GAIVNIASNAGIGTAAEGTTFYAI--------- 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 18413950  200 raygqSKLANILHANELSRQLQEegVNITANSVHPGLILTNL 241
Cdd:PRK06463 155 -----TKAGIIILTRRLAFELGK--YGIRVNAVAPGWVETDM 189
PRK06484 PRK06484
short chain dehydrogenase; Validated
50-243 3.88e-04

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 42.14  E-value: 3.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   50 ARVLSKRGAHVVIGARNMGAAENakteiLRQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGV----MFC 125
Cdd:PRK06484  22 CQRFARAGDQVVVADRNVERARE-----RADSLGPDHHALAMDVSDEAQIREGFEQLHREFGRIDVLVNNAGVtdptMTA 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  126 PYQLSEDGIELQFATNHIGHFLLTNLLLDTMkntakTSGVEGR-ILNVSSVAhiytyqegiqfdsinDICSYSDKRAYGQ 204
Cdd:PRK06484  97 TLDTTLEEFARLQAINLTGAYLVAREALRLM-----IEQGHGAaIVNVASGA---------------GLVALPKRTAYSA 156
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 18413950  205 SKLANILHANELSRQLQEEGVNITAnsVHPGLILTNLFQ 243
Cdd:PRK06484 157 SKAAVISLTRSLACEWAAKGIRVNA--VLPGYVRTQMVA 193
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
43-239 3.98e-04

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: 41.35  E-value: 3.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  43 GGIGMETARVLSKRGAHVVIGARNMGAAENAKTEILRQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGV 122
Cdd:cd05330  13 SGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEIAPDAEVLLIKADVSDEAQVEAYVDATVEQFGRIDGFFNNAGI 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 123 MfCPYQLSEDGIELQF----ATNHIGHFLLTNLLLDTMKNTAktsgvEGRILNVSSVAHIytyqEGIqfdsindicsySD 198
Cdd:cd05330  93 E-GKQNLTEDFGADEFdkvvSINLRGVFYGLEKVLKVMREQG-----SGMIVNTASVGGI----RGV-----------GN 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 18413950 199 KRAYGQSKLANILHANELSRQLQEEGVNItaNSVHPGLILT 239
Cdd:cd05330 152 QSGYAAAKHGVVGLTRNSAVEYGQYGIRI--NAIAPGAILT 190
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
42-248 4.25e-04

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: 41.29  E-value: 4.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEILRQNANA-RVTLLQLDLSSIKSIK-AFVREFHALHlplnLLINN 119
Cdd:cd08935  14 TGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGGRAiALAADVLDRASLERAReEIVAQFGTVD----ILING 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 120 AG----------------VMFCPYQLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAKtsgveGRILNVSSVAhiytyqe 183
Cdd:cd08935  90 AGgnhpdattdpehyepeTEQNFFDLDEEGWEFVFDLNLNGSFLPSQVFGKDMLEQKG-----GSIINISSMN------- 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18413950 184 giQFDSINDICSYSdkraygQSKLANILHANELSRQLQEEGVNItaNSVHPGLILTNlfQHTALL 248
Cdd:cd08935 158 --AFSPLTKVPAYS------AAKAAVSNFTQWLAVEFATTGVRV--NAIAPGFFVTP--QNRKLL 210
PRK06484 PRK06484
short chain dehydrogenase; Validated
50-239 5.23e-04

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 41.76  E-value: 5.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   50 ARVLSKRGAHVVIGARNMGAAENakteiLRQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGV--MFCP- 126
Cdd:PRK06484 286 ADRFAAAGDRLLIIDRDAEGAKK-----LAEALGDEHLSVQADITDEAAVESAFAQIQARWGRLDVLVNNAGIaeVFKPs 360
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  127 YQLSEDGIELQFATNHIGHFLltnllldTMKNTAKTSGVEGRILNVSsvahiytyqegiqfdSINDICSYSDKRAYGQSK 206
Cdd:PRK06484 361 LEQSAEDFTRVYDVNLSGAFA-------CARAAARLMSQGGVIVNLG---------------SIASLLALPPRNAYCASK 418
                        170       180       190
                 ....*....|....*....|....*....|...
gi 18413950  207 LANILHANELSRQLQEEGvnITANSVHPGLILT 239
Cdd:PRK06484 419 AAVTMLSRSLACEWAPAG--IRVNTVAPGYIET 449
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
50-239 5.70e-04

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 40.72  E-value: 5.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   50 ARVLSKRGAHV-VIGARNMGAAENAKTEILRqnANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAGV------ 122
Cdd:PRK12745  19 ARALAAAGFDLaINDRPDDEELAATQQELRA--LGVEVIFFPADVADLSAHEAMLDAAQAAWGRIDCLVNNAGVgvkvrg 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  123 -MFcpyQLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAKTS-GVEGRILNVSSVAHIYTyqegiqfdSINdicsysdkR 200
Cdd:PRK12745  97 dLL---DLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEPEeLPHRSIVFVSSVNAIMV--------SPN--------R 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 18413950  201 A-YGQSKLANILHANELSRQLQEEGvnITANSVHPGLILT 239
Cdd:PRK12745 158 GeYCISKAGLSMAAQLFAARLAEEG--IGVYEVRPGLIKT 195
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
42-239 5.93e-04

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: 40.82  E-value: 5.93e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGARNM-GAAENAKTEILRQNANArvTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNA 120
Cdd:cd05366  11 AQGIGRAIAERLAADGFNIVLADLNLeEAAKSTIQEISEAGYNA--VAVGADVTDKDDVEALIDQAVEKFGSFDVMVNNA 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 121 GVmfCPYQ----LSEDGIELQFATNHIGHFLLTNLLLDTMKNTaktsGVEGRILNVSSVAhiytyqeGIQfdsindicSY 196
Cdd:cd05366  89 GI--APITplltITEEDLKKVYAVNVFGVLFGIQAAARQFKKL----GHGGKIINASSIA-------GVQ--------GF 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 18413950 197 SDKRAYGQSKLANILHANELSRQLQEEGvnITANSVHPGLILT 239
Cdd:cd05366 148 PNLGAYSASKFAVRGLTQTAAQELAPKG--ITVNAYAPGIVKT 188
PRK07577 PRK07577
SDR family oxidoreductase;
42-245 6.75e-04

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 40.48  E-value: 6.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIGARNmgAAENAKTEilrqnanarvtLLQLDLSSIKSIKAFVREFHALHlPLNLLINNAG 121
Cdd:PRK07577  12 TKGIGLALSLRLANLGHQVIGIARS--AIDDFPGE-----------LFACDLADIEQTAATLAQINEIH-PVDAIVNNVG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  122 VMFcPYQLSEdgIELQ-----FATNHIGHFLLTNLLLDTMKNTAktsgvEGRILNVSSVAhiytyqegiqfdsindICSY 196
Cdd:PRK07577  78 IAL-PQPLGK--IDLAalqdvYDLNVRAAVQVTQAFLEGMKLRE-----QGRIVNICSRA----------------IFGA 133
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 18413950  197 SDKRAYGQSKLANILHANELSRQLQEEGvnITANSVHPGLILTNLFQHT 245
Cdd:PRK07577 134 LDRTSYSAAKSALVGCTRTWALELAEYG--ITVNAVAPGPIETELFRQT 180
PRK06180 PRK06180
short chain dehydrogenase; Provisional
48-175 7.33e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 40.67  E-value: 7.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   48 ETARVLSKRGAHVVIGARNMGAAEnAKTEILRQNANARVtllqLDLSSIKSIKAFVREFHALHLPLNLLINNAGV-MFCP 126
Cdd:PRK06180  19 ALAQAALAAGHRVVGTVRSEAARA-DFEALHPDRALARL----LDVTDFDAIDAVVADAEATFGPIDVLVNNAGYgHEGA 93
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18413950  127 YQLSEDgIEL--QFATNHIGHFLLTNLLLDTMKntAKTSgveGRILNVSSV 175
Cdd:PRK06180  94 IEESPL-AEMrrQFEVNVFGAVAMTKAVLPGMR--ARRR---GHIVNITSM 138
PRK06125 PRK06125
short chain dehydrogenase; Provisional
42-172 7.56e-04

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 40.41  E-value: 7.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEiLRQNANARVTLLQLDLSSIKSIKafvrEFHALHLPLNLLINNAG 121
Cdd:PRK06125  16 SKGIGAAAAEAFAAEGCHLHLVARDADALEALAAD-LRAAHGVDVAVHALDLSSPEARE----QLAAEAGDIDILVNNAG 90
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18413950  122 VMfcPyQLSEDGIELQ-----FATNHIGHFLLTNLLLDTMKntAKTSGVegrILNV 172
Cdd:PRK06125  91 AI--P-GGGLDDVDDAawragWELKVFGYIDLTRLAYPRMK--ARGSGV---IVNV 138
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
42-235 8.09e-04

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: 40.53  E-value: 8.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVigarnmgAAENAKTEILRQNANARvtLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:cd05331   7 AQGIGRAVARHLLQAGATVI-------ALDLPFVLLLEYGDPLR--LTPLDVADAAAVREVCSRLLAEHGPIDALVNCAG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 122 V--MFCPYQLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAktsgvEGRILNVSS-VAHIytyqegiqfdsindicSYSD 198
Cdd:cd05331  78 VlrPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRR-----TGAIVTVASnAAHV----------------PRIS 136
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 18413950 199 KRAYGQSKLAniLHANELSRQLQEEGVNITANSVHPG 235
Cdd:cd05331 137 MAAYGASKAA--LASLSKCLGLELAPYGVRCNVVSPG 171
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
42-245 8.99e-04

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: 40.03  E-value: 8.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEIlrQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:cd05347  14 SRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLI--EKEGVEATAFTCDVSDEEAIKAAVEAIEEDFGKIDILVNNAG 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 122 VmfcpyQLSEDGIELQ-------FATNHIGHFLLTNLLLDTMKNTAKtsgveGRILNVSSvahIYTYQEGIqfdsinDIC 194
Cdd:cd05347  92 I-----IRRHPAEEFPeaewrdvIDVNLNGVFFVSQAVARHMIKQGH-----GKIINICS---LLSELGGP------PVP 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 18413950 195 SYSDKRAyGQSKLANILhANELSRQlqeegvNITANSVHPGLILTNLFQHT 245
Cdd:cd05347 153 AYAASKG-GVAGLTKAL-ATEWARH------GIQVNAIAPGYFATEMTEAV 195
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
42-248 9.76e-04

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: 40.13  E-value: 9.76e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGarnmGAAENAKTEILRQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:cd05326  13 ASGIGEATARLFAKHGARVVIA----DIDDDAGQAVAAELGDPDISFVHCDVTVEADVRAAVDTAVARFGRLDIMFNNAG 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 122 VM--FCPYQL--SEDGIELQFATNHIGHFLltnllldTMKNTAKTSGVEGR--ILNVSSVAHIYTyqeGIqfdsindics 195
Cdd:cd05326  89 VLgaPCYSILetSLEEFERVLDVNVYGAFL-------GTKHAARVMIPAKKgsIVSVASVAGVVG---GL---------- 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 18413950 196 ysDKRAYGQSKLANILHANELSRQLQEEGVNItaNSVHPGLILTNLFQHTALL 248
Cdd:cd05326 149 --GPHAYTASKHAVLGLTRSAATELGEHGIRV--NCVSPYGVATPLLTAGFGV 197
PRK12828 PRK12828
short chain dehydrogenase; Provisional
42-239 1.06e-03

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 39.78  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEIlrqnANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:PRK12828  16 FGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGV----PADALRIGGIDLVDPQAARRAVDEVNRQFGRLDALVNIAG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  122 VMfcPYQLSEDG----IELQFATNHIGHFLLTNLLLDTMKNTAKtsgveGRILNVSSVAHIYTyQEGIQfdsindicsys 197
Cdd:PRK12828  92 AF--VWGTIADGdadtWDRMYGVNVKTTLNASKAALPALTASGG-----GRIVNIGAGAALKA-GPGMG----------- 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 18413950  198 dkrAYGQSKLANILHANELSRQLQEEGvnITANSVHPGLILT 239
Cdd:PRK12828 153 ---AYAAAKAGVARLTEALAAELLDRG--ITVNAVLPSIIDT 189
PRK07062 PRK07062
SDR family oxidoreductase;
45-121 1.07e-03

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 40.02  E-value: 1.07e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18413950   45 IGMETARVLSKRGAHVVIGARNMGAAENAKTEILRQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:PRK07062  20 IGLATVELLLEAGASVAICGRDEERLASAEARLREKFPGARLLAARCDVLDEADVAAFAAAVEARFGGVDMLVNNAG 96
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
42-239 1.11e-03

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: 40.06  E-value: 1.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEILRQNAnARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:cd05358  12 SSGIGKAIAIRLATAGANVVVNYRSKEDAAEEVVEEIKAVG-GKAIAVQADVSKEEDVVALFQSAIKEFGTLDILVNNAG 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 122 VM--FCPYQLSEDGIELQFATNHIGHFLLTNLLLDTMkntaKTSGVEGRILNVSSVahiytyqegiqfdsiNDICSYSDK 199
Cdd:cd05358  91 LQgdASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRF----RKSKIKGKIINMSSV---------------HEKIPWPGH 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 18413950 200 RAYGQSKLANILHANELSRQLQEEGvnITANSVHPGLILT 239
Cdd:cd05358 152 VNYAASKGGVKMMTKTLAQEYAPKG--IRVNAIAPGAINT 189
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
42-245 1.15e-03

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: 39.80  E-value: 1.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEILrqnanARVTLLQLDLSSIKSIKAFV----REFHAlhlpLNLLI 117
Cdd:cd08929   9 SRGIGEATARLLHAEGYRVGICARDEARLAAAAAQEL-----EGVLGLAGDVRDEADVRRAVdameEAFGG----LDALV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 118 NNAGV-MFCP-YQLSEDGIELQFATNHIGHFLLTNLLLDTMKntaKTSGveGRILNVSSVAHIYTYQEGIqfdsindics 195
Cdd:cd08929  80 NNAGVgVMKPvEELTPEEWRLVLDTNLTGAFYCIHKAAPALL---RRGG--GTIVNVGSLAGKNAFKGGA---------- 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 18413950 196 ysdkrAYGQSKLANILHANELSRQLQEEGVNITanSVHPGLILTNLFQHT 245
Cdd:cd08929 145 -----AYNASKFGLLGLSEAAMLDLREANIRVV--NVMPGSVDTGFAGSP 187
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
42-243 1.39e-03

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 39.88  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEIlrQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:PRK13394  16 ASGIGKEIALELARAGAAVAIADLNQDGANAVADEI--NKAGGKAIGVAMDVTNEDAVNAGIDKVAERFGSVDILVSNAG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  122 VMFC-PYQ--LSEDGIELQfATNHIGHFLLTNLLLDTMKNTAKTsgveGRILNVSSVaHIYTYQEGiqfdsindicsysd 198
Cdd:PRK13394  94 IQIVnPIEnySFADWKKMQ-AIHVDGAFLTTKAALKHMYKDDRG----GVVIYMGSV-HSHEASPL-------------- 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 18413950  199 KRAYGQSKLANIlhanELSRQLQEEGV--NITANSVHPGLILTNLFQ 243
Cdd:PRK13394 154 KSAYVTAKHGLL----GLARVLAKEGAkhNVRSHVVCPGFVRTPLVD 196
PRK06841 PRK06841
short chain dehydrogenase; Provisional
42-241 1.52e-03

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 39.64  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIGARNmGAAENAKTEILRQNANArvtlLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:PRK06841  24 ASGIGHAIAELFAAKGARVALLDRS-EDVAEVAAQLLGGNAKG----LVCDVSDSQSVEAAVAAVISAFGRIDILVNSAG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  122 V-MFCPYQ-LSEDGIELQFATNHIGHFLLTNLLLDTMKNTAKtsgveGRILNVSSVAHIYTYQEGIqfdsindicsysdk 199
Cdd:PRK06841  99 VaLLAPAEdVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGG-----GKIVNLASQAGVVALERHV-------------- 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 18413950  200 rAYGQSKLANIlhanELSRQLQEE--GVNITANSVHPGLILTNL 241
Cdd:PRK06841 160 -AYCASKAGVV----GMTKVLALEwgPYGITVNAISPTVVLTEL 198
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
42-176 1.65e-03

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 39.63  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEIlRQNANArvtlLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:PRK07067  15 ASGIGEAVAERYLAEGARVVIADIKPARARLAALEI-GPAAIA----VSLDVTRQDSIDRIVAAAVERFGGIDILFNNAA 89
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18413950  122 V--MFCPYQLSEDGIELQFATNHIGHFLLTNLLLDTMKNtaktSGVEGRILNVSSVA 176
Cdd:PRK07067  90 LfdMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVE----QGRGGKIINMASQA 142
PRK05693 PRK05693
SDR family oxidoreductase;
74-244 1.69e-03

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 39.39  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   74 KTEILRQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG--VMFCPYQLSEDGIELQFATNHIGHFLLTNL 151
Cdd:PRK05693  34 KAEDVEALAAAGFTAVQLDVNDGAALARLAEELEAEHGGLDVLINNAGygAMGPLLDGGVEAMRRQFETNVFAVVGVTRA 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  152 LLDTMKNTaktsgvEGRILNVSSVAHIY-TYQEGiqfdsindicsysdkrAYGQSKLAniLHAneLSRQLQEE--GVNIT 228
Cdd:PRK05693 114 LFPLLRRS------RGLVVNIGSVSGVLvTPFAG----------------AYCASKAA--VHA--LSDALRLElaPFGVQ 167
                        170
                 ....*....|....*.
gi 18413950  229 ANSVHPGLILTNLFQH 244
Cdd:PRK05693 168 VMEVQPGAIASQFASN 183
PRK12746 PRK12746
SDR family oxidoreductase;
42-241 2.04e-03

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 39.25  E-value: 2.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIG-ARNMGAAENAKTEIlrQNANARVTLLQLDLSSIKSIKAFVREF-HALHL-----PLN 114
Cdd:PRK12746  15 SRGIGRAIAMRLANDGALVAIHyGRNKQAADETIREI--ESNGGKAFLIEADLNSIDGVKKLVEQLkNELQIrvgtsEID 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  115 LLINNAGV--MFCPYQLSEDGIELQFATNHIGHFLLTNLLLDTMKntaktsgVEGRILNVSSVAHIYTYQEGIqfdsind 192
Cdd:PRK12746  93 ILVNNAGIgtQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLR-------AEGRVINISSAEVRLGFTGSI------- 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 18413950  193 icsysdkrAYGQSKLANILHANELSRQLQEEGvnITANSVHPGLILTNL 241
Cdd:PRK12746 159 --------AYGLSKGALNTMTLPLAKHLGERG--ITVNTIMPGYTKTDI 197
PRK05866 PRK05866
SDR family oxidoreductase;
42-121 2.47e-03

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 38.95  E-value: 2.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEILRQNANARVtlLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:PRK05866  49 SSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITRAGGDAMA--VPCDLSDLDAVDALVADVEKRIGGVDILINNAG 126
KR_fFAS_like_SDR_c_like cd08928
ketoacyl reductase (KR) domain of fungal-type fatty acid synthase (fFAS)-like, classical (c) ...
47-241 2.50e-03

ketoacyl reductase (KR) domain of fungal-type fatty acid synthase (fFAS)-like, classical (c)-like SDRs; KR domain of FAS, including the fungal-type multidomain FAS alpha chain, and the single domain daunorubicin C-13 ketoreductase. Fungal-type FAS is a heterododecameric FAS composed of alpha and beta multifunctional polypeptide chains. The KR, an SDR family member is located centrally in the alpha chain. KR catalyzes the NADP-dependent reduction of ketoacyl-ACP to hydroxyacyl-ACP. KR shares the critical active site Tyr of the classical SDR and has partial identity of the active site tetrad, but the upstream Asn is replaced in KR by Met. As in other SDRs, there is a glycine rich NAD(P)-binding motif, but the pattern found in KR does not match the classical SDRs, and is not strictly conserved within this group. Daunorubicin is a clinically important therapeutic compound used in some cancer treatments. Single domain 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: 187633 [Multi-domain]  Cd Length: 248  Bit Score: 38.81  E-value: 2.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  47 METARVLSKRGAHVVIGARNMGAAENAKTEILRQNANARVTLLQLDLSSIKSikafVREFHAL---HLPLNLLINNAGVM 123
Cdd:cd08928  13 AEVLQGLLNGGAKVYVTTSRFSRQVTKYYQDIYAACGAAGSVLIVVPFNQGS----KQDVEALaigIYDTVNGLGWDLDL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 124 FCPY-QLSEDGIELQF--ATNHIGHFLLTNLLLdTMKNTAKTSGVEGRIlNVSSVAHIYTYQEGIQfdsindicSYSDKR 200
Cdd:cd08928  89 YGPFaAIPETGIEIPAidSKSEVAHRIMLTNLL-RPKGLVKIQKQLRGQ-ETRPAQVILPFSPNHG--------TFGDDG 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 18413950 201 AYGQSKLANILHANELSRqlQEEGVNITANSVHPGLILTNL 241
Cdd:cd08928 159 AYSESKLHLETLFNRWAS--ESWGNDLTVCGAHIGWTRGTL 197
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
42-237 2.56e-03

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 38.74  E-value: 2.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVvigarNMGAAENAKTEILRQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:PRK12936  15 SGGIGEEIARLLHAQGAIV-----GLHGTRVEKLEALAAELGERVKIFPANLSDRDEVKALGQKAEADLEGVDILVNNAG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  122 V----MFCpyQLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAktsgvEGRILNVSSVAHIyTYQEGiqfdsindicsys 197
Cdd:PRK12936  90 ItkdgLFV--RMSDEDWDSVLEVNLTATFRLTRELTHPMMRRR-----YGRIINITSVVGV-TGNPG------------- 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 18413950  198 dKRAYGQSKLANILHANELSRQLQEEgvNITANSVHPGLI 237
Cdd:PRK12936 149 -QANYCASKAGMIGFSKSLAQEIATR--NVTVNCVAPGFI 185
PRK12743 PRK12743
SDR family oxidoreductase;
42-239 2.62e-03

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 38.86  E-value: 2.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIG-ARNMGAAENAKTEIlrQNANARVTLLQLDLSSI----KSIKAFVREFHAlhlpLNLL 116
Cdd:PRK12743  11 DSGIGKACALLLAQQGFDIGITwHSDEEGAKETAEEV--RSHGVRAEIRQLDLSDLpegaQALDKLIQRLGR----IDVL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  117 INNAGVMFcpyqlSEDGIELQFAT-------NHIGHFLLTNLLLDTMkntaKTSGVEGRILNVSSVaHIYTYQEGiqfds 189
Cdd:PRK12743  85 VNNAGAMT-----KAPFLDMDFDEwrkiftvDVDGAFLCSQIAARHM----VKQGQGGRIINITSV-HEHTPLPG----- 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 18413950  190 indicsysdKRAYGQSKLANILHANELSRQLQEEgvNITANSVHPGLILT 239
Cdd:PRK12743 150 ---------ASAYTAAKHALGGLTKAMALELVEH--GILVNAVAPGAIAT 188
PRK06181 PRK06181
SDR family oxidoreductase;
42-244 2.85e-03

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 38.81  E-value: 2.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEIlrQNANARVTLLQLDLSS----IKSIKAFVREFHAlhlpLNLLI 117
Cdd:PRK06181  10 SEGIGRALAVRLARAGAQLVLAARNETRLASLAQEL--ADHGGEALVVPTDVSDaeacERLIEAAVARFGG----IDILV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  118 NNAGVMFCPY--QLSEDGI-ELQFATNHIGHFLLTNLLLDTMKNTaktsgvEGRILNVSSVAHiYTYQEGiqfdsindic 194
Cdd:PRK06181  84 NNAGITMWSRfdELTDLSVfERVMRVNYLGAVYCTHAALPHLKAS------RGQIVVVSSLAG-LTGVPT---------- 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 18413950  195 sysdKRAYGQSKLANILHANELSRQLQEEGVNITAnsVHPGLILTNLFQH 244
Cdd:PRK06181 147 ----RSGYAASKHALHGFFDSLRIELADDGVAVTV--VCPGFVATDIRKR 190
PRK09291 PRK09291
SDR family oxidoreductase;
44-239 3.60e-03

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 38.44  E-value: 3.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   44 GIGMETARVLSKRGAHVVIGARNMGAAenakTEiLRQNANAR---VTLLQLDLSSIKSIKafvrefHALHLPLNLLINNA 120
Cdd:PRK09291  13 GFGREVALRLARKGHNVIAGVQIAPQV----TA-LRAEAARRglaLRVEKLDLTDAIDRA------QAAEWDVDVLLNNA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  121 GVMfcpyqlsEDG------IEL---QFATNHIGHFLLTNLLLDTMKNTAKtsgveGRILNVSSVAHIYTyqegIQFDSin 191
Cdd:PRK09291  82 GIG-------EAGavvdipVELvreLFETNVFGPLELTQGFVRKMVARGK-----GKVVFTSSMAGLIT----GPFTG-- 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 18413950  192 dicsysdkrAYGQSKlanilHANE-----LSRQLQEEGVNITanSVHPGLILT 239
Cdd:PRK09291 144 ---------AYCASK-----HALEaiaeaMHAELKPFGIQVA--TVNPGPYLT 180
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
42-124 4.90e-03

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 37.82  E-value: 4.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEILRQNANARVtlLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:PRK07523  19 SQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQGLSAHA--LAFDVTDHDAVRAAIDAFEAEIGPIDILVNNAG 96

                 ...
gi 18413950  122 VMF 124
Cdd:PRK07523  97 MQF 99
PRK07677 PRK07677
short chain dehydrogenase; Provisional
42-133 5.02e-03

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 38.12  E-value: 5.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEIlrQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINN-A 120
Cdd:PRK07677  10 SSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEI--EQFPGQVLTVQMDVRNPEDVQKMVEQIDEKFGRIDALINNaA 87
                         90
                 ....*....|....
gi 18413950  121 GVMFCPYQ-LSEDG 133
Cdd:PRK07677  88 GNFICPAEdLSVNG 101
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
42-244 6.36e-03

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: 37.65  E-value: 6.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVI-GARNMGAAENAKTEIlrqnanaRVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNA 120
Cdd:cd05371  11 ASGLGLATVERLLAQGAKVVIlDLPNSPGETVAKLGD-------NCRFVPVDVTSEKDVKAALALAKAKFGRLDIVVNCA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 121 GVMFCPYQLSEDGI------ELQFA--TNHIGHFLLTNLLLDTM-KNTAKTSGVEGRILNVSSVAhIYTYQEGIQfdsin 191
Cdd:cd05371  84 GIAVAAKTYNKKGQqphsleLFQRVinVNLIGTFNVIRLAAGAMgKNEPDQGGERGVIINTASVA-AFEGQIGQA----- 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 18413950 192 dicsysdkrAYGQSKLANILHANELSRQLQEEGvnITANSVHPGLILTNLFQH 244
Cdd:cd05371 158 ---------AYSASKGGIVGMTLPIARDLAPQG--IRVVTIAPGLFDTPLLAG 199
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
43-249 6.52e-03

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: 37.51  E-value: 6.52e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  43 GGIGMETARVLSKRGAHVVIGARNMGAAENAKTEILRQNANARVTLLqLDLSSIKSIKAFVREFHALHLPLNLLINNAGv 122
Cdd:cd08933  19 RGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAGPGSCKFVP-CDVTKEEDIKTLISVTVERFGRIDCLVNNAG- 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 123 MFCPYQLSEDGIELQFAT----NHIGHFLLTNLLLDTMKNTaktsgvEGRILNVSS-VAHIytyqegiqfdsindicSYS 197
Cdd:cd08933  97 WHPPHQTTDETSAQEFRDllnlNLISYFLASKYALPHLRKS------QGNIINLSSlVGSI----------------GQK 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 18413950 198 DKRAYGQSKLANILHANELSrqLQEEGVNITANSVHPGLILTNLFQHTALLM 249
Cdd:cd08933 155 QAAPYVATKGAITAMTKALA--VDESRYGVRVNCISPGNIWTPLWEELAAQT 204
PRK07069 PRK07069
short chain dehydrogenase; Validated
42-244 6.83e-03

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 37.38  E-value: 6.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEILRQNANARVTL-LQLDLSSIKSIKAFVREFHALHLPLNLLINNA 120
Cdd:PRK07069   8 AGGLGRAIARRMAEQGAKVFLTDINDAAGLDAFAAEINAAHGEGVAFaAVQDVTDEAQWQALLAQAADAMGGLSVLVNNA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  121 GV--MFCPYQLSEDGIELQFATNHIGHFLLTNLLLDTMKNTAKTSgvegrILNVSSVAhiytyqeGIQFDsindicsySD 198
Cdd:PRK07069  88 GVgsFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPAS-----IVNISSVA-------AFKAE--------PD 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 18413950  199 KRAYGQSKLANILHANELSRQLQEEGVNITANSVHPGL----ILTNLFQH 244
Cdd:PRK07069 148 YTAYNASKAAVASLTKSIALDCARRGLDVRCNSIHPTFirtgIVDPIFQR 197
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
42-240 7.09e-03

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 37.52  E-value: 7.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   42 TGGIGMETARVLSKRGAHVVIGARNMGAAENAKTEIlrQNANARVTLLQLDLSSIKSIKAFVREFHALHLPLNLLINNAG 121
Cdd:PRK06113  20 GAGIGKEIAITFATAGASVVVSDINADAANHVVDEI--QQLGGQAFACRCDITSEQELSALADFALSKLGKVDILVNNAG 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  122 VMFC-PYQLSEDGIELQFATNHIGHFLLTNLLLDTMkntAKTSGveGRILNVSSVAHiytyqegiqfDSINdicsySDKR 200
Cdd:PRK06113  98 GGGPkPFDMPMADFRRAYELNVFSFFHLSQLVAPEM---EKNGG--GVILTITSMAA----------ENKN-----INMT 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 18413950  201 AYGQSKLAnilhANELSRQLQEE--GVNITANSVHPGLILTN 240
Cdd:PRK06113 158 SYASSKAA----ASHLVRNMAFDlgEKNIRVNGIAPGAILTD 195
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
42-238 9.43e-03

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: 36.87  E-value: 9.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950  42 TGGIGMETARVLSKRGAHVVIGARN-MGAAENAKTEIlrQNANARVTLLQLDLSSIKSIKAFV-REFHALHlPLNLLINN 119
Cdd:cd05357   9 AKRIGRAIAEALAAEGYRVVVHYNRsEAEAQRLKDEL--NALRNSAVLVQADLSDFAACADLVaAAFRAFG-RCDVLVNN 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950 120 AGVMFC--PYQLSEDGIELQFATNHIGHFLLTnllldtmKNTAK--TSGVEGRILNVsSVAHIYTYqegiqfdsindics 195
Cdd:cd05357  86 ASAFYPtpLGQGSEDAWAELFGINLKAPYLLI-------QAFARrlAGSRNGSIINI-IDAMTDRP-------------- 143
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 18413950 196 YSDKRAYGQSK--LANilhaneLSRQL-QEEGVNITANSVHPGLIL 238
Cdd:cd05357 144 LTGYFAYCMSKaaLEG------LTRSAaLELAPNIRVNGIAPGLIL 183
PRK07102 PRK07102
SDR family oxidoreductase;
49-176 9.59e-03

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 37.21  E-value: 9.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413950   49 TARVLSKRGAHVVIGARNMGAAENAKTEILRQNAnARVTLLQLDLSSIKSIKAFVREFHAlhLPLNLLInnaGVMFCPYQ 128
Cdd:PRK07102  17 CARRYAAAGARLYLAARDVERLERLADDLRARGA-VAVSTHELDILDTASHAAFLDSLPA--LPDIVLI---AVGTLGDQ 90
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 18413950  129 -LSEDGIEL---QFATNHIGHFLLTNLLLDTMknTAKTSGVegrILNVSSVA 176
Cdd:PRK07102  91 aACEADPALalrEFRTNFEGPIALLTLLANRF--EARGSGT---IVGISSVA 137
 
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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