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Conserved domains on  [gi|55727312|emb|CAH90412|]
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hypothetical protein [Pongo abelii]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10143144)

SDR family NAD(P)-dependent oxidoreductase with similarity to mammalian carbonyl reductase, which catalyzes the NADPH-dependent reduction of a wide range of substrates including quinones, prostaglandins, and other carbonyl-containing compounds

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 6-277 6.30e-127

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: 360.01  E-value: 6.30e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   6 HVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:cd05324   1 KVALVTGANRGIGFEIVRQLAKSGPGTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  86 VLVNNAGIAFKVADP-TPFHIQAEVTMKTNFFGTRDVCTELLPLIKP--QGRVVNVSSIMSVRalkscspelqqkfrset 162
Cdd:cd05324  81 ILVNNAGIAFKGFDDsTPTREQARETMKTNFFGTVDVTQALLPLLKKspAGRIVNVSSGLGSL----------------- 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 163 iteeelvglmnkfvedtkkgvhqkegwpSSAYGVTKIGVTVLSRIHARKLSEqrkgDRILLNACCPGWVRTDMAGPKATK 242
Cdd:cd05324 144 ----------------------------TSAYGVSKAALNALTRILAKELKE----TGIKVNACCPGWVKTDMGGGKAPK 191

                       250       260       270
                ....*....|....*....|....*....|....*
gi 55727312 243 SPEEGAETPVYLALLPPDAEgPHGQFVSEKRVEQW 277
Cdd:cd05324 192 TPEEGAETPVYLALLPPDGE-PTGKFFSDKKVVPW 225
 
Name Accession Description Interval E-value
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 6-277 6.30e-127

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: 360.01  E-value: 6.30e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   6 HVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:cd05324   1 KVALVTGANRGIGFEIVRQLAKSGPGTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  86 VLVNNAGIAFKVADP-TPFHIQAEVTMKTNFFGTRDVCTELLPLIKP--QGRVVNVSSIMSVRalkscspelqqkfrset 162
Cdd:cd05324  81 ILVNNAGIAFKGFDDsTPTREQARETMKTNFFGTVDVTQALLPLLKKspAGRIVNVSSGLGSL----------------- 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 163 iteeelvglmnkfvedtkkgvhqkegwpSSAYGVTKIGVTVLSRIHARKLSEqrkgDRILLNACCPGWVRTDMAGPKATK 242
Cdd:cd05324 144 ----------------------------TSAYGVSKAALNALTRILAKELKE----TGIKVNACCPGWVKTDMGGGKAPK 191

                       250       260       270
                ....*....|....*....|....*....|....*
gi 55727312 243 SPEEGAETPVYLALLPPDAEgPHGQFVSEKRVEQW 277
Cdd:cd05324 192 TPEEGAETPVYLALLPPDGE-PTGKFFSDKKVVPW 225
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 7-269 2.23e-42

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: 145.31  E-value: 2.23e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:COG1028   8 VALVTGGSSGIGRAIARALAA--EGaRVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAFGRLD 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  86 VLVNNAGIafkvADPTPFH-IQAEV---TMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSIMSVRALKscspelqqkfr 159
Cdd:COG1028  86 ILVNNAGI----TPPGPLEeLTEEDwdrVLDVNLKGPFLLTRAALPHMRERggGRIVNISSIAGLRGSP----------- 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 160 setiteeelvglmnkfvedtkkgvhqkeGWpsSAYGVTKIGVTVLSRIHARKLseqrKGDRILLNACCPGWVRTDMAGPK 239
Cdd:COG1028 151 ----------------------------GQ--AAYAASKAAVVGLTRSLALEL----APRGIRVNAVAPGPIDTPMTRAL 196

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 55727312 240 ATK-----------------SPEEGAEtpVYLALLPPDAEGPHGQFV 269
Cdd:COG1028 197 LGAeevrealaariplgrlgTPEEVAA--AVLFLASDAASYITGQVL 241
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 7-239 1.69e-36

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 128.50  E-value: 1.69e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312     7 VALVTGGNKGIGLAIVRdlcRLFS--GDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:pfam00106   2 VALVTGASSGIGRAIAK---RLAKegAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    85 DVLVNNAGIafkvADPTPFHIQAEV----TMKTNFFGTRDVCTELLPLIK--PQGRVVNVSSImsvralkscspelqqkf 158
Cdd:pfam00106  79 DILVNNAGI----TGLGPFSELSDEdwerVIDVNLTGVFNLTRAVLPAMIkgSGGRIVNISSV----------------- 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   159 rsetiteeelVGLMnkfvedtkkgvhqkeGWPS-SAYGVTKIGVTVLSRIHARKLSEqrkgDRILLNACCPGWVRTDMAG 237
Cdd:pfam00106 138 ----------AGLV---------------PYPGgSAYSASKAAVIGFTRSLALELAP----HGIRVNAVAPGGVDTDMTK 188


                  ..
gi 55727312   238 PK 239
Cdd:pfam00106 189 EL 190
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
5-255 4.67e-28

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 107.94  E-value: 4.67e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    5 MHVALVTGGNKGIGLAIVRDLCRLfsG-DVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGG 83
Cdd:PRK05653   5 GKTALVTGASRGIGRAIALRLAAD--GaKVVIYDSNEEAAEALAAELRAAGGEARVLVFDVSDEAAVRALIEAAVEAFGA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   84 LDVLVNNAGIafkvADPTPFH-IQAE---VTMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSImsvralkscspelqqk 157
Cdd:PRK05653  83 LDILVNNAGI----TRDALLPrMSEEdwdRVIDVNLTGTFNVVRAALPPMIKAryGRIVNISSV---------------- 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  158 frsetiteeelVGLMnkfvedtkkgvhqkeGWP-SSAYGVTKIGVTVLSRIHARKLseqrKGDRILLNACCPGWVRTDM- 235
Cdd:PRK05653 143 -----------SGVT---------------GNPgQTNYSAAKAGVIGFTKALALEL----ASRGITVNAVAPGFIDTDMt 192

                        250       260       270
                 ....*....|....*....|....*....|....
gi 55727312  236 ----AGPKATK----------SPEEGAETPVYLA 255
Cdd:PRK05653 193 eglpEEVKAEIlkeiplgrlgQPEEVANAVAFLA 226
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 8-235 1.15e-18

3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, also called 3-ketoacyl-acyl carrier protein reductase, an enzyme of fatty acid biosynthesis. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273824 [Multi-domain]  Cd Length: 239  Bit Score: 82.64  E-value: 1.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312     8 ALVTGGNKGIGLAIVRDLCRLFSgDVVLT-ARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGA-KVIITyRSSEEGAEEVVEELKALGVKALGVVLDVSDREDVKAVVEEIEEELGTIDI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    87 LVNNAGI-----AFKVADPtpfhiQAEVTMKTNFFGTRDVCTELL-PLIKP-QGRVVNVSSImsvralkscspelqqkfr 159
Cdd:TIGR01830  80 LVNNAGItrdnlLMRMKEE-----DWDAVIDTNLTGVFNLTQAVLrIMIKQrSGRIINISSV------------------ 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55727312   160 setiteeelVGLMnkfvedtkkgvhqkeGWPSSA-YGVTKIGVTVLSRIHARKLSeqRKGdrILLNACCPGWVRTDM 235
Cdd:TIGR01830 137 ---------VGLM---------------GNAGQAnYAASKAGVIGFTKSLAKELA--SRN--ITVNAVAPGFIDTDM 185
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 9-103 2.30e-08

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 52.48  E-value: 2.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312      9 LVTGGNKGIGLAIVRDLCRLFSGDVVLTAR--DVARGQAA-VQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGARRLVLLSRsgPDAPGAAAlLAELEAAGARVTVVACDVADRDALAAVLAAIPAVEGPLT 83

                           90
                   ....*....|....*...
gi 55727312     86 VLVNNAGiafkVADPTPF 103
Cdd:smart00822  84 GVIHAAG----VLDDGVL 97
 
Name Accession Description Interval E-value
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 6-277 6.30e-127

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: 360.01  E-value: 6.30e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   6 HVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:cd05324   1 KVALVTGANRGIGFEIVRQLAKSGPGTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  86 VLVNNAGIAFKVADP-TPFHIQAEVTMKTNFFGTRDVCTELLPLIKP--QGRVVNVSSIMSVRalkscspelqqkfrset 162
Cdd:cd05324  81 ILVNNAGIAFKGFDDsTPTREQARETMKTNFFGTVDVTQALLPLLKKspAGRIVNVSSGLGSL----------------- 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 163 iteeelvglmnkfvedtkkgvhqkegwpSSAYGVTKIGVTVLSRIHARKLSEqrkgDRILLNACCPGWVRTDMAGPKATK 242
Cdd:cd05324 144 ----------------------------TSAYGVSKAALNALTRILAKELKE----TGIKVNACCPGWVKTDMGGGKAPK 191

                       250       260       270
                ....*....|....*....|....*....|....*
gi 55727312 243 SPEEGAETPVYLALLPPDAEgPHGQFVSEKRVEQW 277
Cdd:cd05324 192 TPEEGAETPVYLALLPPDGE-PTGKFFSDKKVVPW 225
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 8-269 6.68e-43

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: 146.27  E-value: 6.68e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   8 ALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVARGQAAVQqLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAR--EGaKVVLADRNEEALAELAA-IEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDI 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  87 LVNNAGIAFkvaDPTPFHIQAEV---TMKTNFFGTRDVCTELLPLIK--PQGRVVNVSSIMSVRALKScspelqqkfrse 161
Cdd:cd05233  78 LVNNAGIAR---PGPLEELTDEDwdrVLDVNLTGVFLLTRAALPHMKkqGGGRIVNISSVAGLRPLPG------------ 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 162 titeeelvglmnkfvedtkkgvhqkegwpSSAYGVTKIGVTVLSRIHARKLseqrKGDRILLNACCPGWVRTDMAGPKAT 241
Cdd:cd05233 143 -----------------------------QAAYAASKAALEGLTRSLALEL----APYGIRVNAVAPGLVDTPMLAKLGP 189

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 55727312 242 K----------------SPEEGAETPVYLALlpPDAEGPHGQFV 269
Cdd:cd05233 190 EeaekelaaaiplgrlgTPEEVAEAVVFLAS--DEASYITGQVI 231
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 7-269 2.23e-42

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: 145.31  E-value: 2.23e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:COG1028   8 VALVTGGSSGIGRAIARALAA--EGaRVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAFGRLD 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  86 VLVNNAGIafkvADPTPFH-IQAEV---TMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSIMSVRALKscspelqqkfr 159
Cdd:COG1028  86 ILVNNAGI----TPPGPLEeLTEEDwdrVLDVNLKGPFLLTRAALPHMRERggGRIVNISSIAGLRGSP----------- 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 160 setiteeelvglmnkfvedtkkgvhqkeGWpsSAYGVTKIGVTVLSRIHARKLseqrKGDRILLNACCPGWVRTDMAGPK 239
Cdd:COG1028 151 ----------------------------GQ--AAYAASKAAVVGLTRSLALEL----APRGIRVNAVAPGPIDTPMTRAL 196

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 55727312 240 ATK-----------------SPEEGAEtpVYLALLPPDAEGPHGQFV 269
Cdd:COG1028 197 LGAeevrealaariplgrlgTPEEVAA--AVLFLASDAASYITGQVL 241
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-250 1.60e-41

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 143.09  E-value: 1.60e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   1 MSSGMHVALVTGGNKGIGLAIVRDLCRLfsG-DVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRK 79
Cdd:COG0300   1 MSLTGKTVLITGASSGIGRALARALAAR--GaRVVLVARDAERLEALAAELRAAGARVEVVALDVTDPDAVAALAEAVLA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  80 EYGGLDVLVNNAGIAF--KVADPTPFHIQAevTMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSIMSVRALKScspelq 155
Cdd:COG0300  79 RFGPIDVLVNNAGVGGggPFEELDLEDLRR--VFEVNVFGPVRLTRALLPLMRARgrGRIVNVSSVAGLRGLPG------ 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 156 qkfrsetiteeelvglmnkfvedtkkgvhqkegwpSSAYGVTKIGVTVLSRIHARKLseqrKGDRILLNACCPGWVRTDM 235
Cdd:COG0300 151 -----------------------------------MAAYAASKAALEGFSESLRAEL----APTGVRVTAVCPGPVDTPF 191

                       250       260
                ....*....|....*....|.
gi 55727312 236 AGP------KATKSPEEGAET 250
Cdd:COG0300 192 TARagapagRPLLSPEEVARA 212
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 7-277 1.74e-38

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: 135.81  E-value: 1.74e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQAEGLSPR--FHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:cd05327   3 VVVITGANSGIGKETARELAKR-GAHVIIACRNEEKGEEAAAEIKKETGNAKveVIQLDLSSLASVRQFAEEFLARFPRL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  85 DVLVNNAGIAFKVADPTPFHIqaEVTMKTNFFGTRDVCTELLPLIK--PQGRVVNVSSIMSVRALKScspelqqkfrset 162
Cdd:cd05327  82 DILINNAGIMAPPRRLTKDGF--ELQFAVNYLGHFLLTNLLLPVLKasAPSRIVNVSSIAHRAGPID------------- 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 163 iteeelvglmnkFVEDTKKGVHQKEGWPssAYGVTKigvtvLSRI-HARKLSEQRKGDRILLNACCPGWVRTDM------ 235
Cdd:cd05327 147 ------------FNDLDLENNKEYSPYK--AYGQSK-----LANIlFTRELARRLEGTGVTVNALHPGVVRTELlrrngs 207

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 55727312 236 -------AGPKATKSPEEGAETPVYLALLpPDAEGPHGQFVSEKRVEQW 277
Cdd:cd05327 208 ffllyklLRPFLKKSPEQGAQTALYAATS-PELEGVSGKYFSDCKIKMS 255
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 7-239 1.69e-36

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 128.50  E-value: 1.69e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312     7 VALVTGGNKGIGLAIVRdlcRLFS--GDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:pfam00106   2 VALVTGASSGIGRAIAK---RLAKegAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    85 DVLVNNAGIafkvADPTPFHIQAEV----TMKTNFFGTRDVCTELLPLIK--PQGRVVNVSSImsvralkscspelqqkf 158
Cdd:pfam00106  79 DILVNNAGI----TGLGPFSELSDEdwerVIDVNLTGVFNLTRAVLPAMIkgSGGRIVNISSV----------------- 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   159 rsetiteeelVGLMnkfvedtkkgvhqkeGWPS-SAYGVTKIGVTVLSRIHARKLSEqrkgDRILLNACCPGWVRTDMAG 237
Cdd:pfam00106 138 ----------AGLV---------------PYPGgSAYSASKAAVIGFTRSLALELAP----HGIRVNAVAPGGVDTDMTK 188


                  ..
gi 55727312   238 PK 239
Cdd:pfam00106 189 EL 190
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 1-261 5.49e-31

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: 115.28  E-value: 5.49e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   1 MSSGMHVALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVARGQAAVQQLqaeGLSPRFHQLDIDDLQSIRALRDFLRK 79
Cdd:COG4221   1 MSDKGKVALITGASSGIGAATARALAA--AGaRVVLAARRAERLEALAAEL---GGRALAVPLDVTDEAAVEAAVAAAVA 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  80 EYGGLDVLVNNAGIAF--KVADPTPFHIQAevTMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSIMSVRALkscspelq 155
Cdd:COG4221  76 EFGRLDVLVNNAGVALlgPLEELDPEDWDR--MIDVNVKGVLYVTRAALPAMRARgsGHIVNISSIAGLRPY-------- 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 156 qkfrsetiteeelvglmnkfvedtkkgvhqkEGWpsSAYGVTKIGVTVLSRIharkLSEQRKGDRILLNACCPGWVRTDM 235
Cdd:COG4221 146 -------------------------------PGG--AVYAATKAAVRGLSES----LRAELRPTGIRVTVIEPGAVDTEF 188

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 55727312 236 AG-------PKATK--------SPEEGAETPVYLALLPPDA 261
Cdd:COG4221 189 LDsvfdgdaEAAAAvyegleplTPEDVAEAVLFALTQPAHV 229
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
5-255 4.67e-28

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 107.94  E-value: 4.67e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    5 MHVALVTGGNKGIGLAIVRDLCRLfsG-DVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGG 83
Cdd:PRK05653   5 GKTALVTGASRGIGRAIALRLAAD--GaKVVIYDSNEEAAEALAAELRAAGGEARVLVFDVSDEAAVRALIEAAVEAFGA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   84 LDVLVNNAGIafkvADPTPFH-IQAE---VTMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSImsvralkscspelqqk 157
Cdd:PRK05653  83 LDILVNNAGI----TRDALLPrMSEEdwdRVIDVNLTGTFNVVRAALPPMIKAryGRIVNISSV---------------- 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  158 frsetiteeelVGLMnkfvedtkkgvhqkeGWP-SSAYGVTKIGVTVLSRIHARKLseqrKGDRILLNACCPGWVRTDM- 235
Cdd:PRK05653 143 -----------SGVT---------------GNPgQTNYSAAKAGVIGFTKALALEL----ASRGITVNAVAPGFIDTDMt 192

                        250       260       270
                 ....*....|....*....|....*....|....
gi 55727312  236 ----AGPKATK----------SPEEGAETPVYLA 255
Cdd:PRK05653 193 eglpEEVKAEIlkeiplgrlgQPEEVANAVAFLA 226
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 7-235 1.92e-26

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 103.90  E-value: 1.92e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK12939   9 RALVTGAARGLGAAFAEALAE--AGaTVAFNDGLAAEARELAAALEAAGGRAHAIAADLADPASVQRFFDAAAAALGGLD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   86 VLVNNAGIAfKVADPTPFHIQA-EVTMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSimsvralkscspelqqkfrset 162
Cdd:PRK12939  87 GLVNNAGIT-NSKSATELDIDTwDAVMNVNVRGTFLMLRAALPHLRDSgrGRIVNLAS---------------------- 143

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55727312  163 iteeelvglmnkfveDTkkgvhqkEGWPSSAYGV---TKIGVTVLSRIHARKLseqrKGDRILLNACCPGWVRTDM 235
Cdd:PRK12939 144 ---------------DT-------ALWGAPKLGAyvaSKGAVIGMTRSLAREL----GGRGITVNAIAPGLTATEA 193
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 9-141 1.93e-26

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: 103.70  E-value: 1.93e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   9 LVTGGNKGIGLAIVRDLCRLfsG-DVVLTARDVARGQAAVQQLqaeglsPRFH--QLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:COG3967   9 LITGGTSGIGLALAKRLHAR--GnTVIITGRREEKLEEAAAAN------PGLHtiVLDVADPASIAALAEQVTAEFPDLN 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  86 VLVNNAGI--AFKVADPTPFHIQAEVTMKTNFFGTRDVCTELLPLIK--PQGRVVNVSSI 141
Cdd:COG3967  81 VLINNAGImrAEDLLDEAEDLADAEREITTNLLGPIRLTAAFLPHLKaqPEAAIVNVSSG 140
FabG-like PRK07231
SDR family oxidoreductase;
6-236 2.88e-25

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 100.67  E-value: 2.88e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    6 HVALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVARGQAAVQQLQAEGLSpRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK07231   6 KVAIVTGASSGIGEGIARRFAA--EGaRVVVTDRNEEAAERVAAEILAGGRA-IAVAADVSDEADVEAAVAAALERFGSV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   85 DVLVNNAGI--AFKV---ADPTPFHIQAEVTMKTNFFGTRdvctELLPLIKPQ--GRVVNVSSIMSVRAlkscSPELqqk 157
Cdd:PRK07231  83 DILVNNAGTthRNGPlldVDEAEFDRIFAVNVKSPYLWTQ----AAVPAMRGEggGAIVNVASTAGLRP----RPGL--- 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55727312  158 frsetiteeelvglmnkfvedtkkgvhqkeGWpssaYGVTKIGVTVLSRIHARKLSEqrkgDRILLNACCPGWVRTDMA 236
Cdd:PRK07231 152 ------------------------------GW----YNASKGAVITLTKALAAELGP----DKIRVNAVAPVVVETGLL 192
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 14-255 5.26e-25

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: 99.43  E-value: 5.26e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    14 NKGIGLAIVRDLCRlfSG-DVVLTARDvARGQAAVQQLqAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVLVNNAG 92
Cdd:pfam13561   5 ESGIGWAIARALAE--EGaEVVLTDLN-EALAKRVEEL-AEELGAAVLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    93 IAFKVAdpTPFH-IQAE---VTMKTNFFGTRDVCTELLPLIKPQGRVVNVSSIMSVRAlkscspelqqkfrsetiteeel 168
Cdd:pfam13561  81 FAPKLK--GPFLdTSREdfdRALDVNLYSLFLLAKAALPLMKEGGSIVNLSSIGAERV---------------------- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   169 vglmnkfvedtkkgvhqkegWP-SSAYGVTKIGVTVLSRIHARKLSeqRKGDRIllNACCPGWVRTDMA-----GPKATK 242
Cdd:pfam13561 137 --------------------VPnYNAYGAAKAALEALTRYLAVELG--PRGIRV--NAISPGPIKTLAAsgipgFDELLA 192

                         250       260
                  ....*....|....*....|....*
gi 55727312   243 ------------SPEEGAETPVYLA 255
Cdd:pfam13561 193 aaearaplgrlgTPEEVANAAAFLA 217
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 8-249 7.82e-25

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: 98.91  E-value: 7.82e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   8 ALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDvARGQAAVQQLQAEGLSPRFHQLDIDDL--QSIRALRDFLRKeyGGLD 85
Cdd:cd05325   1 VLITGASRGIGLELVRQLLARGNNTVIATCRD-PSAATELAALGASHSRLHILELDVTDEiaESAEAVAERLGD--AGLD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  86 VLVNNAGIA--FKVADPTPfHIQAEVTMKTNFFGTRDVCTELLPLIKP--QGRVVNVSSIMSvralkscspelqqkfrse 161
Cdd:cd05325  78 VLINNAGILhsYGPASEVD-SEDLLEVFQVNVLGPLLLTQAFLPLLLKgaRAKIINISSRVG------------------ 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 162 TITeeelvglmnkfveDTKKGvhqkegwPSSAYGVTKIGVTVLSrihaRKLSEQRKGDRILLNACCPGWVRTDMAGPKA- 240
Cdd:cd05325 139 SIG-------------DNTSG-------GWYSYRASKAALNMLT----KSLAVELKRDGITVVSLHPGWVRTDMGGPFAk 194

                       250
                ....*....|..
gi 55727312 241 ---TKSPEEGAE 249
Cdd:cd05325 195 nkgPITPEESVA 206
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 6-141 1.04e-23

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: 96.53  E-value: 1.04e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   6 HVALVTGGNKGIGLAIVRDLCRlfSGDVVL-TARDvargQAAVQQLQAEgLSPRFH--QLDIDDLQSIRALRDFLRKEYG 82
Cdd:cd05374   1 KVVLITGCSSGIGLALALALAA--QGYRVIaTARN----PDKLESLGEL-LNDNLEvlELDVTDEESIKAAVKEVIERFG 73

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55727312  83 GLDVLVNNAGIA-FKVADPTPFHiQAEVTMKTNFFGTRDVCTELLPLIK--PQGRVVNVSSI 141
Cdd:cd05374  74 RIDVLVNNAGYGlFGPLEETSIE-EVRELFEVNVFGPLRVTRAFLPLMRkqGSGRIVNVSSV 134
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 7-274 1.15e-23

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


Pssm-ID: 187644 [Multi-domain]  Cd Length: 258  Bit Score: 96.36  E-value: 1.15e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTA-RDVARGQAAVQQLQAE-GLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:cd08940   4 VALVTGSTSGIGLGIARALAAA-GANIVLNGfGDAAEIEAVRAGLAAKhGVKVLYHGADLSKPAAIEDMVAYAQRQFGGV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  85 DVLVNNAGIAFkVADPTPFHIQA-----EVTMKTNFFGTRDVctelLPLIKPQ--GRVVNVSSIMSvralkscspelqqk 157
Cdd:cd08940  83 DILVNNAGIQH-VAPIEDFPTEKwdaiiALNLSAVFHTTRLA----LPHMKKQgwGRIINIASVHG-------------- 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 158 frsetiteeeLVGLMNKfvedtkkgvhqkegwpsSAYGVTKIGVTVLSRIHArkLSEQRKGdrILLNACCPGWVRTDM-- 235
Cdd:cd08940 144 ----------LVASANK-----------------SAYVAAKHGVVGLTKVVA--LETAGTG--VTCNAICPGWVLTPLve 192

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 55727312 236 ----AGPKATKSPEEGAETPVYLALLppdaegPHGQFVSEKRV 274
Cdd:cd08940 193 kqisALAQKNGVPQEQAARELLLEKQ------PSKQFVTPEQL 229
PRK12826 PRK12826
SDR family oxidoreductase;
7-238 2.24e-23

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 95.37  E-value: 2.24e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK12826   8 VALVTGAARGIGRAIAVRLAA--DGaEVIVVDICGDDAAATAELVEAAGGKARARQVDVRDRAALKAAVAAGVEDFGRLD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   86 VLVNNAGIafkvADPTPFHI----QAEVTMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSIMSVRAlkscspelqqkfr 159
Cdd:PRK12826  86 ILVANAGI----FPLTPFAEmddeQWERVIDVNLTGTFLLTQAALPALIRAggGRIVLTSSVAGPRV------------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  160 setiteeelvglmnkfvedtkkgvhqkeGWP-SSAYGVTKIGVTVLSRIHARKLSEqrkgDRILLNACCPGWVRTDMAGP 238
Cdd:PRK12826 149 ----------------------------GYPgLAHYAASKAGLVGFTRALALELAA----RNITVNSVHPGGVDTPMAGN 196
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 7-270 1.30e-22

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 93.27  E-value: 1.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLT-ARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK12937   7 VAIVTGASRGIGAAIARRLAA--DGfAVAVNyAGSAAAADELVAEIEAAGGRAIAVQADVADAAAVTRLFDAAETAFGRI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   85 DVLVNNAGIAF--KVADptpFHIQA-EVTMKTNFFGTRDVCTELLPLIKPQGRVVNVSSimSVRALKscspelqqkfrse 161
Cdd:PRK12937  85 DVLVNNAGVMPlgTIAD---FDLEDfDRTIATNLRGAFVVLREAARHLGQGGRIINLST--SVIALP------------- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  162 titeeelvglmnkfvedtkkgvhqkegWPS-SAYGVTKIGVTVLSRIHARKLseqrKGDRILLNACCPGWVRTDM----- 235
Cdd:PRK12937 147 ---------------------------LPGyGPYAASKAAVEGLVHVLANEL----RGRGITVNAVAPGPVATELffngk 195

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 55727312  236 AGPKATK-----------SPEEGAETPVYLAllppdaeGPHGQFVS 270
Cdd:PRK12937 196 SAEQIDQlaglaplerlgTPEEIAAAVAFLA-------GPDGAWVN 234
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 7-238 1.53e-22

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: 93.30  E-value: 1.53e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRlfSGDVVLTA--RDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:cd05337   3 VAIVTGASRGIGRAIATELAA--RGFDIAINdlPDDDQATEVVAEVLAAGRRAIYFQADIGELSDHEALLDQAWEDFGRL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  85 DVLVNNAGIAFKV------ADPTPFHIQAEVTMKTNFFGTRDVCTELL----PLIKPQGRVVNVSSIMSVRAlkscSPEl 154
Cdd:cd05337  81 DCLVNNAGIAVRPrgdlldLTEDSFDRLIAINLRGPFFLTQAVARRMVeqpdRFDGPHRSIIFVTSINAYLV----SPN- 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 155 qqkfRSEtiteeelvglmnkfvedtkkgvhqkegwpssaYGVTKIGVTVLSRIHARKLSEqrkgDRILLNACCPGWVRTD 234
Cdd:cd05337 156 ----RGE--------------------------------YCISKAGLSMATRLLAYRLAD----EGIAVHEIRPGLIHTD 195


                ....
gi 55727312 235 MAGP 238
Cdd:cd05337 196 MTAP 199
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 7-255 1.87e-22

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 92.95  E-value: 1.87e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK05557   7 VALVTGASRGIGRAIAERLAAQGANVVINYASSEAGAEALVAEIGALGGKALAVQGDVSDAESVERAVDEAKAEFGGVDI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   87 LVNNAGIA-------FKVADptpFhiqaEVTMKTNFFGTRDVCTELLPLI--KPQGRVVNVSSImsvralkscspelqqk 157
Cdd:PRK05557  87 LVNNAGITrdnllmrMKEED---W----DRVIDTNLTGVFNLTKAVARPMmkQRSGRIINISSV---------------- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  158 frsetiteeelVGLMnkfvedtkkgvhqkeGWPS-SAYGVTKIGVTVLSRIHARKLSEqrKGdrILLNACCPGWVRTDM- 235
Cdd:PRK05557 144 -----------VGLM---------------GNPGqANYAASKAGVIGFTKSLARELAS--RG--ITVNAVAPGFIETDMt 193

                        250       260       270
                 ....*....|....*....|....*....|....
gi 55727312  236 -AGPKATK-------------SPEEGAETPVYLA 255
Cdd:PRK05557 194 dALPEDVKeailaqiplgrlgQPEEIASAVAFLA 227
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 8-142 2.26e-22

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: 92.37  E-value: 2.26e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   8 ALVTGGNKGIGLAIVRDLCRLfsGDVVLTArdvARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVL 87
Cdd:cd05370   8 VLITGGTSGIGLALARKFLEA--GNTVIIT---GRREERLAEAKKELPNIHTIVLDVGDAESVEALAEALLSEYPNLDIL 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 55727312  88 VNNAGIA--FKVADPTPFHIQAEVTMKTNFFGTRDVCTELLPLIK--PQGRVVNVSSIM 142
Cdd:cd05370  83 INNAGIQrpIDLRDPASDLDKADTEIDTNLIGPIRLIKAFLPHLKkqPEATIVNVSSGL 141
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 7-251 2.42e-22

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: 92.83  E-value: 2.42e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLqaeGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd05341   7 VAIVTGGARGLGLAHARLLVAE-GAKVVLSDILDEEGQAAAAEL---GDAARFFHLDVTDEDGWTAVVDTAREAFGRLDV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  87 LVNNAGIAfkvadpTPFHIQAEV------TMKTN----FFGTRDVctelLPLIKPQGR--VVNVSSImsvralkscspel 154
Cdd:cd05341  83 LVNNAGIL------TGGTVETTTleewrrLLDINltgvFLGTRAV----IPPMKEAGGgsIINMSSI------------- 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 155 qqkfrsetiteEELVGLMNkfvedtkkgvhqkegwpSSAYGVTKIGVTVLSRIHARKLSEQrkGDRILLNACCPGWVRTD 234
Cdd:cd05341 140 -----------EGLVGDPA-----------------LAAYNASKGAVRGLTKSAALECATQ--GYGIRVNSVHPGYIYTP 189

                       250
                ....*....|....*....
gi 55727312 235 M--AGPKATKSPEEGAETP 251
Cdd:cd05341 190 MtdELLIAQGEMGNYPNTP 208
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 7-249 2.96e-22

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: 92.42  E-value: 2.96e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRlFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd05347   7 VALVTGASRGIGFGIASGLAE-AGANIVINSRNEEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDFGKIDI 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  87 LVNNAGIAfKVADPTPFHIQA-EVTMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSIMSvralkscspelqqkfrseti 163
Cdd:cd05347  86 LVNNAGII-RRHPAEEFPEAEwRDVIDVNLNGVFFVSQAVARHMIKQghGKIINICSLLS-------------------- 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 164 teeELVGLmnkfvedtkkgvhqkegwPSSAYGVTKIGVTVLSRIHARKLSEqrkgDRILLNACCPGWVRTDMAgpKATKS 243
Cdd:cd05347 145 ---ELGGP------------------PVPAYAASKGGVAGLTKALATEWAR----HGIQVNAIAPGYFATEMT--EAVVA 197


                ....*.
gi 55727312 244 PEEGAE 249
Cdd:cd05347 198 DPEFND 203
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 7-170 1.24e-21

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: 90.54  E-value: 1.24e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDvargQAAVQQLQAEGLSpRFH--QLDIDDLQSIRALRDFLRKeyggL 84
Cdd:cd05354   5 TVLVTGANRGIGKAFVESLLAHGAKKVYAAVRD----PGSAAHLVAKYGD-KVVplRLDVTDPESIKAAAAQAKD----V 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  85 DVLVNNAGIaFKVADPTP--FHIQAEVTMKTNFFGTRDVCTELLPLIK--PQGRVVNVSSIMSVRALKSCSPELQQKFRS 160
Cdd:cd05354  76 DVVINNAGV-LKPATLLEegALEALKQEMDVNVFGLLRLAQAFAPVLKanGGGAIVNLNSVASLKNFPAMGTYSASKSAA 154

                       170
                ....*....|...
gi 55727312 161 ETITE---EELVG 170
Cdd:cd05354 155 YSLTQglrAELAA 167
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-238 1.41e-21

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 90.70  E-value: 1.41e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    1 MSSGMHVALVTGGNKGIGLAIVRDLCRlfSG-DVVLTAR-DVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLR 78
Cdd:PRK12825   2 GSLMGRVALVTGAARGLGRAIALRLAR--AGaDVVVHYRsDEEAAEELVEAVEALGRRAQAVQADVTDKAALEAAVAAAV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   79 KEYGGLDVLVNNAGIAF--KVADPTP--FHIQAEVTMKTNFFGTRDVcteLLPLIKPQ-GRVVNVSsimSVRALKscspe 153
Cdd:PRK12825  80 ERFGRIDILVNNAGIFEdkPLADMSDdeWDEVIDVNLSGVFHLLRAV---VPPMRKQRgGRIVNIS---SVAGLP----- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  154 lqqkfrsetiteeelvglmnkfvedtkkgvhqkeGWP-SSAYGVTKIGVTVLSRIHARKLSEQrkgdRILLNACCPGWVR 232
Cdd:PRK12825 149 ----------------------------------GWPgRSNYAAAKAGLVGLTKALARELAEY----GITVNMVAPGDID 190


                 ....*.
gi 55727312  233 TDMAGP 238
Cdd:PRK12825 191 TDMKEA 196
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 7-236 4.39e-21

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: 88.57  E-value: 4.39e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDvargQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd08932   2 VALVTGASRGIGIEIARALARD-GYRVSLGLRN----PEDLAALSASGGDVEAVPYDARDPEDARALVDALRDRFGRIDV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  87 LVNNAGIAFK--VADPTPFHIQAevTMKTNFFGTRDVCTELLPLI--KPQGRVVNVSSIMSVRALKScspelqqkfrset 162
Cdd:cd08932  77 LVHNAGIGRPttLREGSDAELEA--HFSINVIAPAELTRALLPALreAGSGRVVFLNSLSGKRVLAG------------- 141

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55727312 163 iteeelvglmnkfvedtkkgvhqkegwpSSAYGVTKIGVTVLSRIHARKLSEQrkGDRIllNACCPGWVRTDMA 236
Cdd:cd08932 142 ----------------------------NAGYSASKFALRALAHALRQEGWDH--GVRV--SAVCPGFVDTPMA 183
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 7-235 7.79e-21

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: 88.37  E-value: 7.79e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:cd05333   2 VALVTGASRGIGRAIALRLAA--EGaKVAVTDRSEEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFGPVD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  86 VLVNNAGI-------AFKVADptpfhiqAEVTMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSImsvralkscspelqq 156
Cdd:cd05333  80 ILVNNAGItrdnllmRMSEED-------WDAVINVNLTGVFNVTQAVIRAMIKRrsGRIINISSV--------------- 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 157 kfrsetiteeelVGLMnkfvedtkkgvhqkeGWPSSA-YGVTKIGVTVLSRIHARKLSeqRKGdrILLNACCPGWVRTDM 235
Cdd:cd05333 138 ------------VGLI---------------GNPGQAnYAASKAGVIGFTKSLAKELA--SRG--ITVNAVAPGFIDTDM 186
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-242 8.14e-21

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 88.87  E-value: 8.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTA-RDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK12745   4 VALVTGGRRGIGLGIARALAA--AGfDLAINDrPDDEELAATQQELRALGVEVIFFPADVADLSAHEAMLDAAQAAWGRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   85 DVLVNNAGIAFKV------ADPTPFHIQAEVTMKTNFFGTRDVCTELL----PLIKPQGRVVNVSSIMSVRAlkscSPEl 154
Cdd:PRK12745  82 DCLVNNAGVGVKVrgdlldLTPESFDRVLAINLRGPFFLTQAVAKRMLaqpePEELPHRSIVFVSSVNAIMV----SPN- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  155 qqkfRSEtiteeelvglmnkfvedtkkgvhqkegwpssaYGVTKIGVTVLSRIHARKLSEqrkgDRILLNACCPGWVRTD 234
Cdd:PRK12745 157 ----RGE--------------------------------YCISKAGLSMAAQLFAARLAE----EGIGVYEVRPGLIKTD 196


                 ....*...
gi 55727312  235 MAGPKATK 242
Cdd:PRK12745 197 MTAPVTAK 204
PRK06484 PRK06484
short chain dehydrogenase; Validated
 7-255 1.32e-20

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 91.06  E-value: 1.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRlfSGDVVLTA-RDVARGQAAVQQLqaeGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK06484   7 VVLVTGAAGGIGRAACQRFAR--AGDQVVVAdRNVERARERADSL---GPDHHALAMDVSDEAQIREGFEQLHREFGRID 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   86 VLVNNAGI----AFKVADPTPFHIQAevTMKTNFFGTRDVCTELLPLIKPQGR---VVNVSSIMSVRALKScspelqqkf 158
Cdd:PRK06484  82 VLVNNAGVtdptMTATLDTTLEEFAR--LQAINLTGAYLVAREALRLMIEQGHgaaIVNVASGAGLVALPK--------- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  159 rsetiteeelvglmnkfvedtkkgvhqkegwpSSAYGVTKIGVTVLSRIHARKLSEQrkgdRILLNACCPGWVRTDM--- 235
Cdd:PRK06484 151 --------------------------------RTAYSASKAAVISLTRSLACEWAAK----GIRVNAVLPGYVRTQMvae 194

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 55727312  236 ---AG---PKATKS---------PEEGAETPVYLA 255
Cdd:PRK06484 195 lerAGkldPSAVRSriplgrlgrPEEIAEAVFFLA 229
PRK09242 PRK09242
SDR family oxidoreductase;
8-238 1.88e-20

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 87.88  E-value: 1.88e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    8 ALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQL--DIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK09242  12 ALITGASKGIGLAIAREFLGL-GADVLIVARDADALAQARDELAEEFPEREVHGLaaDVSDDEDRRAILDWVEDHWDGLH 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   86 VLVNNAG--IAFKVADPTPFHIQAevTMKTNFFGTRDVCTELLPLIKPQG--RVVNVSSIMSVRALKSCSPelqqkfrse 161
Cdd:PRK09242  91 ILVNNAGgnIRKAAIDYTEDEWRG--IFETNLFSAFELSRYAHPLLKQHAssAIVNIGSVSGLTHVRSGAP--------- 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55727312  162 titeeelvglmnkfvedtkkgvhqkegwpssaYGVTKIGVTVLSrihaRKLSEQRKGDRILLNACCPGWVRTDMAGP 238
Cdd:PRK09242 160 --------------------------------YGMTKAALLQMT----RNLAVEWAEDGIRVNAVAPWYIRTPLTSG 200
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 7-151 1.99e-20

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: 87.34  E-value: 1.99e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTardVARGQAAVQQLQAE---GLSPRFHQLDIDDLQSIRALRDFLRKEYGG 83
Cdd:cd05367   1 VIILTGASRGIGRALAEELLKRGSPSVVVL---LARSEEPLQELKEElrpGLRVTTVKADLSDAAGVEQLLEAIRKLDGE 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55727312  84 LDVLVNNAGIAFKVADPTPFHIQAEVT-MKTNFFGTrdVCT-----ELLPLIKPQGRVVNVSSIMSVRALKSCS 151
Cdd:cd05367  78 RDLLINNAGSLGPVSKIEFIDLDELQKyFDLNLTSP--VCLtstllRAFKKRGLKKTVVNVSSGAAVNPFKGWG 149
PRK06914 PRK06914
SDR family oxidoreductase;
7-165 2.86e-20

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 87.77  E-value: 2.86e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQAEGLSPRFH--QLDIDDLQSIRALRDFLrKEYGGL 84
Cdd:PRK06914   5 IAIVTGASSGFGLLTTLELAKK-GYLVIATMRNPEKQENLLSQATQLNLQQNIKvqQLDVTDQNSIHNFQLVL-KEIGRI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   85 DVLVNNAGIAFK-VADPTP---FHIQAEvtmkTNFFGTRDVCTELLPLIKPQ--GRVVNVSSIMSVRALKSCSPELQQKF 158
Cdd:PRK06914  83 DLLVNNAGYANGgFVEEIPveeYRKQFE----TNVFGAISVTQAVLPYMRKQksGKIINISSISGRVGFPGLSPYVSSKY 158


                 ....*..
gi 55727312  159 RSETITE 165
Cdd:PRK06914 159 ALEGFSE 165
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 7-234 5.63e-20

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: 86.56  E-value: 5.63e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRLFSgDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd05344   3 VALVTAASSGIGLAIARALAREGA-RVAICARNRENLERAASELRAGGAGVLAVVADLTDPEDIDRLVEKAGDAFGRVDI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  87 LVNNAGiafkVADPTPFhiqAEVT-------MKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSiMSVRAlkscsPElqqk 157
Cdd:cd05344  82 LVNNAG----GPPPGPF---AELTdedwleaFDLKLLSVIRIVRAVLPGMKERgwGRIVNISS-LTVKE-----PE---- 144

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55727312 158 frsetiteeelvglmnkfvedtkkgvhqkEGWPSSayGVTKIGVTVLSRIHARKLSEqrkgDRILLNACCPGWVRTD 234
Cdd:cd05344 145 -----------------------------PNLVLS--NVARAGLIGLVKTLSRELAP----DGVTVNSVLPGYIDTE 186
PRK08264 PRK08264
SDR family oxidoreductase;
7-143 1.14e-19

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 85.33  E-value: 1.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVARgqaavqqlqAEGLSPRFH--QLDIDDLQSIRALRDFLrkeyGGL 84
Cdd:PRK08264   8 VVLVTGANRGIGRAFVEQLLARGAAKVYAAARDPES---------VTDLGPRVVplQLDVTDPASVAAAAEAA----SDV 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55727312   85 DVLVNNAGIAFK---VADPTPFHIQAEvtMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSIMS 143
Cdd:PRK08264  75 TILVNNAGIFRTgslLLEGDEDALRAE--METNYFGPLAMARAFAPVLAANggGAIVNVLSVLS 136
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 7-235 1.39e-19

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: 85.02  E-value: 1.39e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd05362   5 VALVTGASRGIGRAIAKRLARDGASVVVNYASSKAAAEEVVAEIEAAGGKAIAVQADVSDPSQVARLFDAAEKAFGGVDI 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  87 LVNNAGIAFK--VADPTP--FHIQAEVTMKTNFFGTRdvctELLPLIKPQGRVVNVSSImsvrALKSCSPElqqkfrset 162
Cdd:cd05362  85 LVNNAGVMLKkpIAETSEeeFDRMFTVNTKGAFFVLQ----EAAKRLRDGGRIINISSS----LTAAYTPN--------- 147

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55727312 163 iteeelvglmnkfvedtkkgvhqkegwpSSAYGVTKIGVTVLSRIHARKLseqrKGDRILLNACCPGWVRTDM 235
Cdd:cd05362 148 ----------------------------YGAYAGSKAAVEAFTRVLAKEL----GGRGITVNAVAPGPVDTDM 188
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 8-160 1.72e-19

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: 85.19  E-value: 1.72e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   8 ALVTGGNKGIGLAIVRDLCRlFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGG-LDV 86
Cdd:cd05329   9 ALVTGGTKGIGYAIVEELAG-LGAEVYTCARNQKELDECLTEWREKGFKVEGSVCDVSSRSERQELMDTVASHFGGkLNI 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  87 LVNNAG--IAFKVADPTPFHIQAevTMKTNFFGTRDVCTELLPLIKPQGR--VVNVSSIMSVRALKSCSP------ELQQ 156
Cdd:cd05329  88 LVNNAGtnIRKEAKDYTEEDYSL--IMSTNFEAAYHLSRLAHPLLKASGNgnIVFISSVAGVIAVPSGAPygatkgALNQ 165


                ....
gi 55727312 157 KFRS 160
Cdd:cd05329 166 LTRS 169
PRK07201 PRK07201
SDR family oxidoreductase;
4-141 5.72e-19

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 86.54  E-value: 5.72e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    4 GMHVaLVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGG 83
Cdd:PRK07201 371 GKVV-LITGASSGIGRATAIKVAEA-GATVFLVARNGEALDELVAEIRAKGGTAHAYTCDLTDSAAVDHTVKDILAEHGH 448

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55727312   84 LDVLVNNAG--IAFKVADPTP-FHiQAEVTMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSI 141
Cdd:PRK07201 449 VDYLVNNAGrsIRRSVENSTDrFH-DYERTMAVNYFGAVRLILGLLPHMRERrfGHVVNVSSI 510
PRK07326 PRK07326
SDR family oxidoreductase;
1-141 7.97e-19

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 82.75  E-value: 7.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    1 MSSGM-HVALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVARGQAAVQQLQAEGlspRFHQL--DIDDLQSIRALRDF 76
Cdd:PRK07326   1 MMSLKgKVALITGGSKGIGFAIAEALLA--EGyKVAITARDQKELEEAAAELNNKG---NVLGLaaDVRDEADVQRAVDA 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55727312   77 LRKEYGGLDVLVNNAGIA-FK-VADPTPFHIQAevTMKTNFFGTRDVCTELLP-LIKPQGRVVNVSSI 141
Cdd:PRK07326  76 IVAAFGGLDVLIANAGVGhFApVEELTPEEWRL--VIDTNLTGAFYTIKAAVPaLKRGGGYIINISSL 141
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 7-233 8.60e-19

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 83.40  E-value: 8.60e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK12429   6 VALVTGAASGIGLEIALALAKE-GAKVVIADLNDEAAAAAAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVETFGGVDI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   87 LVNNAGI-------AFKVADptpFHIQAEVTMKTNFFGTRDVctelLPLIKPQ--GRVVNVSSIMSVRALKSCSPELQQK 157
Cdd:PRK12429  85 LVNNAGIqhvapieDFPTEK---WKKMIAIMLDGAFLTTKAA----LPIMKAQggGRIINMASVHGLVGSAGKAAYVSAK 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55727312  158 frsetiteEELVGLmnkfvedTKkgVHQKEGWPSsaygvtkiGVTVlsriharklseqrkgdrillNACCPGWVRT 233
Cdd:PRK12429 158 --------HGLIGL-------TK--VVALEGATH--------GVTV--------------------NAICPGYVDT 188
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 8-235 1.15e-18

3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, also called 3-ketoacyl-acyl carrier protein reductase, an enzyme of fatty acid biosynthesis. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273824 [Multi-domain]  Cd Length: 239  Bit Score: 82.64  E-value: 1.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312     8 ALVTGGNKGIGLAIVRDLCRLFSgDVVLT-ARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGA-KVIITyRSSEEGAEEVVEELKALGVKALGVVLDVSDREDVKAVVEEIEEELGTIDI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    87 LVNNAGI-----AFKVADPtpfhiQAEVTMKTNFFGTRDVCTELL-PLIKP-QGRVVNVSSImsvralkscspelqqkfr 159
Cdd:TIGR01830  80 LVNNAGItrdnlLMRMKEE-----DWDAVIDTNLTGVFNLTQAVLrIMIKQrSGRIINISSV------------------ 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55727312   160 setiteeelVGLMnkfvedtkkgvhqkeGWPSSA-YGVTKIGVTVLSRIHARKLSeqRKGdrILLNACCPGWVRTDM 235
Cdd:TIGR01830 137 ---------VGLM---------------GNAGQAnYAASKAGVIGFTKSLAKELA--SRN--ITVNAVAPGFIDTDM 185
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 8-148 1.57e-18

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: 81.78  E-value: 1.57e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   8 ALVTGGNKGIGLAIVRDLCRLFSGdVVLTARDVARGQAAVQQLQaeglsPRFHQL--DIDDLQSIRALRDFLRKEYGGLD 85
Cdd:cd08929   3 ALVTGASRGIGEATARLLHAEGYR-VGICARDEARLAAAAAQEL-----EGVLGLagDVRDEADVRRAVDAMEEAFGGLD 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55727312  86 VLVNNAGIAF--KVADPTPFHIQAEV--TMKTNFFGTRDVCTELLPliKPQGRVVNVSSIMSVRALK 148
Cdd:cd08929  77 ALVNNAGVGVmkPVEELTPEEWRLVLdtNLTGAFYCIHKAAPALLR--RGGGTIVNVGSLAGKNAFK 141
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 8-260 2.16e-18

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


Pssm-ID: 187617 [Multi-domain]  Cd Length: 242  Bit Score: 82.01  E-value: 2.16e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   8 ALVTGGNKGIGLAIVRDLCRLfSGDVVLT-ARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd05359   1 ALVTGGSRGIGKAIALRLAER-GADVVINyRKSKDAAAEVAAEIEELGGKAVVVRADVSQPQDVEEMFAAVKERFGRLDV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  87 LVNNAGI-AFK-VADPTPFHIQAEVTM--KTNFFGTRDVcTELLPLIKpQGRVVNVSSIMSVRALkscspelqqkfrset 162
Cdd:cd05359  80 LVSNAAAgAFRpLSELTPAHWDAKMNTnlKALVHCAQQA-AKLMRERG-GGRIVAISSLGSIRAL--------------- 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 163 iteeelvglmnkfvedtkkgvhqkEGWpsSAYGVTKIGVTVLSRIHARKLSeqRKGdrILLNACCPGWVRTDMAG--PKA 240
Cdd:cd05359 143 ------------------------PNY--LAVGTAKAALEALVRYLAVELG--PRG--IRVNAVSPGVIDTDALAhfPNR 192

                       250       260
                ....*....|....*....|.
gi 55727312 241 TKSPEEGAE-TPVYLALLPPD 260
Cdd:cd05359 193 EDLLEAAAAnTPAGRVGTPQD 213
PRK06181 PRK06181
SDR family oxidoreductase;
5-141 5.74e-18

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 81.18  E-value: 5.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    5 MHVALVTGGNKGIGLAIVRDL----CRLfsgdvVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKE 80
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLaragAQL-----VLAARNETRLASLAQELADHGGEALVVPTDVSDAEACERLIEAAVAR 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55727312   81 YGGLDVLVNNAGI----AF-KVADPTPFhiqaEVTMKTNFFGTRdVCTEL-LP-LIKPQGRVVNVSSI 141
Cdd:PRK06181  76 FGGIDILVNNAGItmwsRFdELTDLSVF----ERVMRVNYLGAV-YCTHAaLPhLKASRGQIVVVSSL 138
PRK06138 PRK06138
SDR family oxidoreductase;
7-255 6.69e-18

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 80.58  E-value: 6.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRdlcrLFSGD---VVLTARDvARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGG 83
Cdd:PRK06138   7 VAIVTGAGSGIGRATAK----LFAREgarVVVADRD-AEAAERVAAAIAAGGRAFARQGDVGSAEAVEALVDFVAARWGR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   84 LDVLVNNAG--IAFKVADPTPFHIQAevTMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSIMSVRALKScspelqqkfr 159
Cdd:PRK06138  82 LDVLVNNAGfgCGGTVVTTDEADWDA--VMRVNVGGVFLWAKYAIPIMQRQggGSIVNTASQLALAGGRG---------- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  160 setiteeelvglmnkfvedtkkgvhqkegwpSSAYGVTKIGVTVLSRIHARKLSEqrkgDRILLNACCPGWVRTDM---- 235
Cdd:PRK06138 150 -------------------------------RAAYVASKGAIASLTRAMALDHAT----DGIRVNAVAPGTIDTPYfrri 194

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 55727312  236 ----AGPKATKS-------------PEEGAETPVYLA 255
Cdd:PRK06138 195 farhADPEALREalrarhpmnrfgtAEEVAQAALFLA 231
PRK06124 PRK06124
SDR family oxidoreductase;
7-141 7.25e-18

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 80.53  E-value: 7.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK06124  13 VALVTGSARGLGFEIARALAG--AGaHVLVNGRNAATLEAAVAALRAAGGAAEALAFDIADEEAVAAAFARIDAEHGRLD 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   86 VLVNNAGIAFK--VADPTPFHIQAevTMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSI 141
Cdd:PRK06124  91 ILVNNVGARDRrpLAELDDAAIRA--LLETDLVAPILLSRLAAQRMKRQgyGRIIAITSI 148
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 7-142 1.49e-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: 79.94  E-value: 1.49e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRLfsG-DVVLTARDVARGQAAVQQLQAEG-LSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:cd05332   5 VVIITGASSGIGEELAYHLARL--GaRLVLSARREERLEEVKSECLELGaPSPHVVPLDMSDLEDAEQVVEEALKLFGGL 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55727312  85 DVLVNNAGIA-FKVADPTPFHIQAEVtMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSIM 142
Cdd:cd05332  83 DILINNAGISmRSLFHDTSIDVDRKI-MEVNYFGPVALTKAALPHLIERsqGSIVVVSSIA 142
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 5-140 1.92e-17

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: 79.22  E-value: 1.92e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   5 MHVALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQAEGLSP----RFHQLDIDDLQSIRALRDFLRKE 80
Cdd:cd08939   1 GKHVLITGGSSGIGKALAKELVKE-GANVIIVARSESKLEEAVEEIEAEANASgqkvSYISADLSDYEEVEQAFAQAVEK 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55727312  81 YGGLDVLVNNAGIA----FKVADPTPFHIQaevtMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSS 140
Cdd:cd08939  80 GGPPDLVVNCAGISipglFEDLTAEEFERG----MDVNYFGSLNVAHAVLPLMKEQrpGHIVFVSS 141
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 7-235 2.98e-17

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: 78.69  E-value: 2.98e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQAEGLSPRfhqLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd08944   5 VAIVTGAGAGIGAACAARLARE-GARVVVADIDGGAAQAVVAQIAGGALALR---VDVTDEQQVAALFERAVEEFGGLDL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  87 LVNNAGIAfkVADPTPFHIQAEV---TMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSIMSVRAlkscspelqqkfrse 161
Cdd:cd08944  81 LVNNAGAM--HLTPAIIDTDLAVwdqTMAINLRGTFLCCRHAAPRMIARggGSIVNLSSIAGQSG--------------- 143

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55727312 162 titeeelVGLmnkfvedtkkgvhqkegwpSSAYGVTKIGVTVLSRIHARKLSEQrkgdRILLNACCPGWVRTDM 235
Cdd:cd08944 144 -------DPG-------------------YGAYGASKAAIRNLTRTLAAELRHA----GIRCNALAPGLIDTPL 187
PRK07454 PRK07454
SDR family oxidoreductase;
5-261 4.62e-17

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 78.08  E-value: 4.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    5 MHVALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGG 83
Cdd:PRK07454   6 MPRALITGASSGIGKATALAFAK--AGwDLALVARSQDALEALAAELRSTGVKAAAYSIDLSNPEAIAPGIAELLEQFGC 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   84 LDVLVNNAGIAFK--VADpTPFHiQAEVTMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSIMSVRALkscsPelqqkfr 159
Cdd:PRK07454  84 PDVLINNAGMAYTgpLLE-MPLS-DWQWVIQLNLTSVFQCCSAVLPGMRARggGLIINVSSIAARNAF----P------- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  160 setiteeelvglmnkfvedtkkgvhqkeGWpsSAYGVTKIGVTVLSRIharkLSEQRKGDRILLNACCPGWVRT-----D 234
Cdd:PRK07454 151 ----------------------------QW--GAYCVSKAALAAFTKC----LAEEERSHGIRVCTITLGAVNTplwdtE 196

                        250       260       270
                 ....*....|....*....|....*....|.
gi 55727312  235 MAGP----KATKSPEEGAETPVYLALLPPDA 261
Cdd:PRK07454 197 TVQAdfdrSAMLSPEQVAQTILHLAQLPPSA 227
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 7-276 4.80e-17

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: 78.66  E-value: 4.80e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQAEGLSPRF--HQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:cd09807   3 TVIITGANTGIGKETARELARR-GARVIMACRDMAKCEEAAAEIRRDTLNHEVivRHLDLASLKSIRAFAAEFLAEEDRL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  85 DVLVNNAGIA----FKVADptPFHIQAEVTMKTNFFGTrdvcTELLPLIKPQG--RVVNVSSIMSVRA------LKScsp 152
Cdd:cd09807  82 DVLINNAGVMrcpySKTED--GFEMQFGVNHLGHFLLT----NLLLDLLKKSApsRIVNVSSLAHKAGkinfddLNS--- 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 153 elQQKFrsetiteeelvglmnkfveDTKKgvhqkegwpssAYGVTKIGVTVLSRIHARKLseqrKGDRILLNACCPGWVR 232
Cdd:cd09807 153 --EKSY-------------------NTGF-----------AYCQSKLANVLFTRELARRL----QGTGVTVNALHPGVVR 196

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55727312 233 TD------MAGPKAT-----------KSPEEGAETPVYLAlLPPDAEGPHGQFVSEKRVEQ 276
Cdd:cd09807 197 TElgrhtgIHHLFLStllnplfwpfvKTPREGAQTSIYLA-LAEELEGVSGKYFSDCKLKE 256
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 6-146 9.86e-17

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: 77.19  E-value: 9.86e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   6 HVALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:cd08934   4 KVALVTGASSGIGEATARALAAE-GAAVAIAARRVDRLEALADELEAEGGKALVLELDVTDEQQVDAAVERTVEALGRLD 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55727312  86 VLVNNAGI----AFKVADPTPFhiqaEVTMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSIMSVRA 146
Cdd:cd08934  83 ILVNNAGImllgPVEDADTTDW----TRMIDTNLLGLMYTTHAALPHHLLRnkGTIVNISSVAGRVA 145
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 7-269 1.04e-16

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: 77.43  E-value: 1.04e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARG------------QAAVQQLQAEGLSPRFHQLDIDDLQSIRALR 74
Cdd:cd05338   5 VAFVTGASRGIGRAIALRLAKA-GATVVVAAKTASEGdngsakslpgtiEETAEEIEAAGGQALPIVVDVRDEDQVRALV 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  75 DFLRKEYGGLDVLVNNAGIAF--KVADpTPFHiQAEVTMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSIMSVRAlksc 150
Cdd:cd05338  84 EATVDQFGRLDILVNNAGAIWlsLVED-TPAK-RFDLMQRVNLRGTYLLSQAALPHMVKAgqGHILNISPPLSLRP---- 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 151 spelqqkfrsetiteeelvglmnkfvedtkkgvhqkeGWPSSAYGVTKIGVTVLsrihARKLSEQRKGDRILLNACCPG- 229
Cdd:cd05338 158 -------------------------------------ARGDVAYAAGKAGMSRL----TLGLAAELRRHGIAVNSLWPSt 196

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 55727312 230 ----WVRTDMAGPK---ATKSPEEGAETpvYLALLPPDAEGPHGQFV 269
Cdd:cd05338 197 aietPAATELSGGSdpaRARSPEILSDA--VLAILSRPAAERTGLVV 241
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 7-252 1.47e-16

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: 76.96  E-value: 1.47e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd05323   2 VAIITGGASGIGLATAKLLLKK-GAKVAILDRNENPGAAAELQAINPKVKATFVQCDVTSWEQLAAAFKKAIEKFGRVDI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  87 LVNNAGIA-----FKVADPTPfhiQAEVTMKTNFFGTRDVCTELLPLIK-----PQGRVVNVSSIMSVRALKSCspelqq 156
Cdd:cd05323  81 LINNAGILdeksyLFAGKLPP---PWEKTIDVNLTGVINTTYLALHYMDknkggKGGVIVNIGSVAGLYPAPQF------ 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 157 kfrsetiteeelvglmnkfvedtkkgvhqkegwpsSAYGVTKIGVTVLSRiHARKLSEQRKGdrILLNACCPGWVRTDMA 236
Cdd:cd05323 152 -----------------------------------PVYSASKHGVVGFTR-SLADLLEYKTG--VRVNAICPGFTNTPLL 193

                       250
                ....*....|....*.
gi 55727312 237 GPKATKSPEEGAETPV 252
Cdd:cd05323 194 PDLVAKEAEMLPSAPT 209
PRK07774 PRK07774
SDR family oxidoreductase;
7-246 1.61e-16

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 76.71  E-value: 1.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK07774   8 VAIVTGAAGGIGQAYAEALARE-GASVVVADINAEGAERVAKQIVADGGTAIAVQVDVSDPDSAKAMADATVSAFGGIDY 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   87 LVNNAGIaFKVADPTPFhIQAEVT-----MKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSIMSvralkscspelqqkfr 159
Cdd:PRK07774  87 LVNNAAI-YGGMKLDLL-ITVPWDyykkfMSVNLDGALVCTRAVYKHMAKRggGAIVNQSSTAA---------------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  160 setiteeelvglmnkfvedtkkgvhqkegWPSSA-YGVTKIGVTVLSRIHARKLSeqrkGDRILLNACCPGWVRTDMAgp 238
Cdd:PRK07774 149 -----------------------------WLYSNfYGLAKVGLNGLTQQLARELG----GMNIRVNAIAPGPIDTEAT-- 193


                 ....*...
gi 55727312  239 kATKSPEE 246
Cdd:PRK07774 194 -RTVTPKE 200
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-246 2.83e-16

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 76.36  E-value: 2.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDvargQAAVQQLQAEGLSprFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK06463   9 VALITGGTRGIGRAIAEAFLREGAKVAVLYNSA----ENEAKELREKGVF--TIKCDVGNRDQVKKSKEVVEKEFGRVDV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   87 LVNNAGIAFKVadptPF----HIQAEVTMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSimsvralkscspelqqkfrs 160
Cdd:PRK06463  83 LVNNAGIMYLM----PFeefdEEKYNKMIKINLNGAIYTTYEFLPLLKLSknGAIVNIAS-------------------- 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  161 etiteeelvglmNKFVEDTKKGvhqkegwpSSAYGVTKIGVTVLSRIHARKLSEQrkgdRILLNACCPGWVRTDMAgpKA 240
Cdd:PRK06463 139 ------------NAGIGTAAEG--------TTFYAITKAGIIILTRRLAFELGKY----GIRVNAVAPGWVETDMT--LS 192


                 ....*.
gi 55727312  241 TKSPEE 246
Cdd:PRK06463 193 GKSQEE 198
PRK05650 PRK05650
SDR family oxidoreductase;
9-262 3.05e-16

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 76.62  E-value: 3.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    9 LVTGGNKGIGLAI----VRDLCRLFSGDVvltarDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK05650   4 MITGAASGLGRAIalrwAREGWRLALADV-----NEEGGEETLKLLREAGGDGFYQRCDVRDYSQLTALAQACEEKWGGI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   85 DVLVNNAGIAF--KVADPTPfhIQAEVTMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSimsvralkscspelqqkfrs 160
Cdd:PRK05650  79 DVIVNNAGVASggFFEELSL--EDWDWQIAINLMGVVKGCKAFLPLFKRQksGRIVNIAS-------------------- 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  161 etiteeeLVGLMNkfvedtkkgvhqkeGWPSSAYGVTKIGVTVLSrihaRKLSEQRKGDRILLNACCPGWVRTDMAGPKA 240
Cdd:PRK05650 137 -------MAGLMQ--------------GPAMSSYNVAKAGVVALS----ETLLVELADDEIGVHVVCPSFFQTNLLDSFR 191

                        250       260
                 ....*....|....*....|..
gi 55727312  241 TKSPEEGAETPVYLALLPPDAE 262
Cdd:PRK05650 192 GPNPAMKAQVGKLLEKSPITAA 213
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 7-236 3.06e-16

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: 76.42  E-value: 3.06e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd08945   5 VALVTGATSGIGLAIARRLGKE-GLRVFVCARGEEGLATTVKELREAGVEADGRTCDVRSVPEIEALVAAAVARYGPIDV 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  87 LVNNAG------IAfKVADPTPFHIqAEVTMKTNFFGTRDVCTELLPLIKPQGRVVNVSSIMSvralkscspelqqkfrs 160
Cdd:cd08945  84 LVNNAGrsgggaTA-ELADELWLDV-VETNLTGVFRVTKEVLKAGGMLERGTGRIINIASTGG----------------- 144

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55727312 161 etiteeelvglmnkfvedtKKGVHQKEGWPSSAYGVtkIGVTvlsriHARKLSEQRKGdrILLNACCPGWVRTDMA 236
Cdd:cd08945 145 -------------------KQGVVHAAPYSASKHGV--VGFT-----KALGLELARTG--ITVNAVCPGFVETPMA 192
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 7-258 5.95e-16

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: 75.50  E-value: 5.95e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd05358   5 VALVTGASSGIGKAIAIRLATAGANVVVNYRSKEDAAEEVVEEIKAVGGKAIAVQADVSKEEDVVALFQSAIKEFGTLDI 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  87 LVNNAGIAFKVA----DPTPFHIQAEVTMKTNFFGTRDVCTEllpLIKPQ--GRVVNVSSimsvralkscspelqqkfrs 160
Cdd:cd05358  85 LVNNAGLQGDASshemTLEDWNKVIDVNLTGQFLCAREAIKR---FRKSKikGKIINMSS-------------------- 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 161 etiteeelvglmnkfvedtkkgVHQKEGWPS-SAYGVTKIGVTVLSRIHARKLSEQrkgdRILLNACCPGWVRTDMAGPk 239
Cdd:cd05358 142 ----------------------VHEKIPWPGhVNYAASKGGVKMMTKTLAQEYAPK----GIRVNAIAPGAINTPINAE- 194

                       250
                ....*....|....*....
gi 55727312 240 ATKSPEEGAETpvyLALLP 258
Cdd:cd05358 195 AWDDPEQRADL---LSLIP 210
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 7-143 6.07e-16

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: 74.97  E-value: 6.07e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLtarDVARGQAAVQQLQAEGLSPRFH--QLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:cd05339   1 IVLITGGGSGIGRLLALEFAKRGAKVVIL---DINEKGAEETANNVRKAGGKVHyyKCDVSKREEVYEAAKKIKKEVGDV 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55727312  85 DVLVNNAGIafkVADPTPFHIQ---AEVTMKTNFFGTRDVCTELLPLI--KPQGRVVNVSSIMS 143
Cdd:cd05339  78 TILINNAGV---VSGKKLLELPdeeIEKTFEVNTLAHFWTTKAFLPDMleRNHGHIVTIASVAG 138
PRK06128 PRK06128
SDR family oxidoreductase;
8-251 7.56e-16

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 75.67  E-value: 7.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    8 ALVTGGNKGIGLAIVRDLCRLfSGDVVLT--------ARDVargqaaVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRK 79
Cdd:PRK06128  58 ALITGADSGIGRATAIAFARE-GADIALNylpeeeqdAAEV------VQLIQAEGRKAVALPGDLKDEAFCRQLVERAVK 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   80 EYGGLDVLVNNAG--IAFK-VADPTpfHIQAEVTMKTNFFGTRDVCTELLPLIKPQGRVVNVSSIMSVRAlkscSPELQQ 156
Cdd:PRK06128 131 ELGGLDILVNIAGkqTAVKdIADIT--TEQFDATFKTNVYAMFWLCKAAIPHLPPGASIINTGSIQSYQP----SPTLLD 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  157 kfrsetiteeelvglmnkfvedtkkgvhqkegwpssaYGVTKIGVTVLSRIHARKLSEqrKGDRIllNACCPGWVRTDM- 235
Cdd:PRK06128 205 -------------------------------------YASTKAAIVAFTKALAKQVAE--KGIRV--NAVAPGPVWTPLq 243

                        250
                 ....*....|....*...
gi 55727312  236 --AGPKATKSPEEGAETP 251
Cdd:PRK06128 244 psGGQPPEKIPDFGSETP 261
PRK07063 PRK07063
SDR family oxidoreductase;
7-259 1.22e-15

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 74.70  E-value: 1.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRdlcrLFSGD---VVLTARDVARGQAAVQQLQAEGLSPR--FHQLDIDDLQSIRALRDFLRKEY 81
Cdd:PRK07063   9 VALVTGAAQGIGAAIAR----AFAREgaaVALADLDAALAERAAAAIARDVAGARvlAVPADVTDAASVAAAVAAAEEAF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   82 GGLDVLVNNAGI-AFkvADPTpfhiqaEVT-------MKTNFFGTRDVCTELLPLIKPQGR--VVNVSSIMSVRALKSCS 151
Cdd:PRK07063  85 GPLDVLVNNAGInVF--ADPL------AMTdedwrrcFAVDLDGAWNGCRAVLPGMVERGRgsIVNIASTHAFKIIPGCF 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  152 PelqqkfrsetiteeelvglmnkfvedtkkgvhqkegwpssaYGVTKIGVTVLSRihARKLSEQRKGDRIllNACCPGWV 231
Cdd:PRK07063 157 P-----------------------------------------YPVAKHGLLGLTR--ALGIEYAARNVRV--NAIAPGYI 191

                        250       260
                 ....*....|....*....|....*...
gi 55727312  232 RTDMAGPKATKSPEEGAETPVYLALLPP 259
Cdd:PRK07063 192 ETQLTEDWWNAQPDPAAARAETLALQPM 219
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 8-152 1.28e-15

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 74.42  E-value: 1.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    8 ALVTGGNKGIGLAIVRDLCRlFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVL 87
Cdd:PRK07523  13 ALVTGSSQGIGYALAEGLAQ-AGAEVILNGRDPAKLAAAAESLKGQGLSAHALAFDVTDHDAVRAAIDAFEAEIGPIDIL 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55727312   88 VNNAGIAFKvadpTP---FHIQA-EVTMKTN----FFGTRDVCTELLPliKPQGRVVNVSSIMSVRALKSCSP 152
Cdd:PRK07523  92 VNNAGMQFR----TPledFPADAfERLLRTNissvFYVGQAVARHMIA--RGAGKIINIASVQSALARPGIAP 158
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 7-263 1.32e-15

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: 74.29  E-value: 1.32e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRdLCRLFSGDVVLTARDVARGQAAVQQLQAE-GLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:cd05352  10 VAIVTGGSRGIGLAIAR-ALAEAGADVAIIYNSAPRAEEKAEELAKKyGVKTKAYKCDVSSQESVEKTFKQIQKDFGKID 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  86 VLVNNAGIAF-KVADPTPFHIQAEVtMKTNFFGTRDVCTELLPLIKPQGR--VVNVSSIMSVRALKscsPELQqkfrset 162
Cdd:cd05352  89 ILIANAGITVhKPALDYTYEQWNKV-IDVNLNGVFNCAQAAAKIFKKQGKgsLIITASMSGTIVNR---PQPQ------- 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 163 iteeelvglmnkfvedtkkgvhqkegwpsSAYGVTKIGVTVLsrihARKLSEQRKGDRILLNACCPGWVRTDMAGPKATK 242
Cdd:cd05352 158 -----------------------------AAYNASKAAVIHL----AKSLAVEWAKYFIRVNSISPGYIDTDLTDFVDKE 204

                       250       260
                ....*....|....*....|..
gi 55727312 243 -SPEEGAETPVYLALLPPDAEG 263
Cdd:cd05352 205 lRKKWESYIPLKRIALPEELVG 226
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 7-141 1.73e-15

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 74.68  E-value: 1.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQAE--GLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK06197  18 VAVVTGANTGLGYETAAALAAK-GAHVVLAVRNLDKGKAAAARITAAtpGADVTLQELDLTSLASVRAAADALRAAYPRI 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55727312   85 DVLVNNAGIAFkvadpTPFHIQA---EVTMKTNFFG----TRDVCTELLPLikPQGRVVNVSSI 141
Cdd:PRK06197  97 DLLINNAGVMY-----TPKQTTAdgfELQFGTNHLGhfalTGLLLDRLLPV--PGSRVVTVSSG 153
PRK07856 PRK07856
SDR family oxidoreductase;
7-237 2.07e-15

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 73.81  E-value: 2.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLcrLFSGDVVLTArdvARGQAAVqqlqAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK07856   8 VVLVTGGTRGIGAGIARAF--LAAGATVVVC---GRRAPET----VDGRPAEFHAADVRDPDQVAALVDAIVERHGRLDV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   87 LVNNAGIAFKV--ADPTP-FHiqaEVTMKTNFFGTRDVCTELLPLIKPQ---GRVVNVSSIMSVRAlkscSPElqqkfrs 160
Cdd:PRK07856  79 LVNNAGGSPYAlaAEASPrFH---EKIVELNLLAPLLVAQAANAVMQQQpggGSIVNIGSVSGRRP----SPG------- 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55727312  161 etiteeelvglmnkfvedtkkgvhqkegwpSSAYGVTKIGVTVLSRIHArklseQRKGDRILLNACCPGWVRTDMAG 237
Cdd:PRK07856 145 ------------------------------TAAYGAAKAGLLNLTRSLA-----VEWAPKVRVNAVVVGLVRTEQSE 186
PRK06484 PRK06484
short chain dehydrogenase; Validated
 7-233 2.15e-15

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 75.66  E-value: 2.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLfsGD-VVLTARDVARGQAAVQQLQAEGLSprfHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK06484 271 VVAITGGARGIGRAVADRFAAA--GDrLLIIDRDAEGAKKLAEALGDEHLS---VQADITDEAAVESAFAQIQARWGRLD 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   86 VLVNNAGIA---FKVADPTPFHIqaEVTMKTNFFGTRDVCTELLPLIKPQGRVVNVSSIMSVRALKscspelqqkfrset 162
Cdd:PRK06484 346 VLVNNAGIAevfKPSLEQSAEDF--TRVYDVNLSGAFACARAAARLMSQGGVIVNLGSIASLLALP-------------- 409

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55727312  163 iteeelvglmnkfvedtkkgvhqkegwPSSAYGVTKIGVTVLSRIHARKLSEQrkGDRIllNACCPGWVRT 233
Cdd:PRK06484 410 ---------------------------PRNAYCASKAAVTMLSRSLACEWAPA--GIRV--NTVAPGYIET 449
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 7-236 2.65e-15

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 73.44  E-value: 2.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLcRLFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK08213  14 TALVTGGSRGLGLQIAEAL-GEAGARVVLSARKAEELEEAAAHLEALGIDALWIAADVADEADIERLAEETLERFGHVDI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   87 LVNNAGIAFKV-ADPTPFHIQAEVtMKTN----FFGTRDVCTEllpLIKPQ--GRVVNVSSIMsvrALKSCSPELQQkfr 159
Cdd:PRK08213  93 LVNNAGATWGApAEDHPVEAWDKV-MNLNvrglFLLSQAVAKR---SMIPRgyGRIINVASVA---GLGGNPPEVMD--- 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55727312  160 seTIteeelvglmnkfvedtkkgvhqkegwpssAYGVTKIGVTVLSRIHARKLSeqRKGdrILLNACCPGWVRTDMA 236
Cdd:PRK08213 163 --TI-----------------------------AYNTSKGAVINFTRALAAEWG--PHG--IRVNAIAPGFFPTKMT 204
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
5-237 2.76e-15

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 73.26  E-value: 2.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    5 MHVALVTGGNKGIGLAIVRDLCRlfSGDVVLTArDVARGQAAVQQLQAEGLSP---RFHQLDIDDLQSIRALRDFLRKEY 81
Cdd:PRK12824   2 KKIALVTGAKRGIGSAIARELLN--DGYRVIAT-YFSGNDCAKDWFEEYGFTEdqvRLKELDVTDTEECAEALAEIEEEE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   82 GGLDVLVNNAGI----AFKVADPTPFhiqAEVtMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSImsvRALKScspelq 155
Cdd:PRK12824  79 GPVDILVNNAGItrdsVFKRMSHQEW---NDV-INTNLNSVFNVTQPLFAAMCEQgyGRIINISSV---NGLKG------ 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  156 qkfrsetiteeeLVGLMNkfvedtkkgvhqkegwpssaYGVTKIGVTVLSRIHARKLSeqRKGdrILLNACCPGWVRTDM 235
Cdd:PRK12824 146 ------------QFGQTN--------------------YSAAKAGMIGFTKALASEGA--RYG--ITVNCIAPGYIATPM 189


                 ..
gi 55727312  236 AG 237
Cdd:PRK12824 190 VE 191
PRK05854 PRK05854
SDR family oxidoreductase;
8-141 4.18e-15

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 73.95  E-value: 4.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    8 ALVTGGNKGIGLAIVRdlcRLFSG--DVVLTARDVARGQAAVQQLQAEglSPR----FHQLDIDDLQSIRALRDFLRKEY 81
Cdd:PRK05854  17 AVVTGASDGLGLGLAR---RLAAAgaEVILPVRNRAKGEAAVAAIRTA--VPDaklsLRALDLSSLASVAALGEQLRAEG 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55727312   82 GGLDVLVNNAGIAfkvadpTPFHIQA-----EVTMKTNFFGTRDVCTELLPLIKP-QGRVVNVSSI 141
Cdd:PRK05854  92 RPIHLLINNAGVM------TPPERQTtadgfELQFGTNHLGHFALTAHLLPLLRAgRARVTSQSSI 151
PRK06949 PRK06949
SDR family oxidoreductase;
7-235 4.63e-15

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 72.87  E-value: 4.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLFSGdVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK06949  11 VALVTGASSGLGARFAQVLAQAGAK-VVLASRRVERLKELRAEIEAEGGAAHVVSLDVTDYQSIKAAVAHAETEAGTIDI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   87 LVNNAGIAF--KVADPTP--FHIQAEVTMKTNFFGTRDVCTELL------PLIKPQGRVVNVSSIMSVRALkscsPELqq 156
Cdd:PRK06949  90 LVNNSGVSTtqKLVDVTPadFDFVFDTNTRGAFFVAQEVAKRMIarakgaGNTKPGGRIINIASVAGLRVL----PQI-- 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55727312  157 kfrsetiteeelvglmnkfvedtkkgvhqkegwpsSAYGVTKIGVTVLSRihARKLSEQRKGdrILLNACCPGWVRTDM 235
Cdd:PRK06949 164 -----------------------------------GLYCMSKAAVVHMTR--AMALEWGRHG--INVNAICPGYIDTEI 203
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 7-141 6.09e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 72.73  E-value: 6.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK06198   8 VALVTGGTQGLGAAIARAFAERGAAGLVICGRNAEKGEAQAAELEALGAKAVFVQADLSDVEDCRRVVAAADEAFGRLDA 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 55727312   87 LVNNAGI----AFKVADPTPFHIQAEVTMKTNFFGTRDVcTELLPLIKPQGRVVNVSSI 141
Cdd:PRK06198  88 LVNAAGLtdrgTILDTSPELFDRHFAVNVRAPFFLMQEA-IKLMRRRKAEGTIVNIGSM 145
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
6-152 7.08e-15

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 74.11  E-value: 7.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    6 HVALVTGGNKGIGLAIVRDLCRLfsG-DVVLTARDVARGQAAVQQLQAEGlSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK08324 423 KVALVTGAAGGIGKATAKRLAAE--GaCVVLADLDEEAAEAAAAELGGPD-RALGVACDVTDEAAVQAAFEEAALAFGGV 499

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55727312   85 DVLVNNAGIAFkvadPTPFhiqAEVTMKT-------NFFGTRDVCTELLPLIKPQ---GRVVNVSSIMSVRALKSCSP 152
Cdd:PRK08324 500 DIVVSNAGIAI----SGPI---EETSDEDwrrsfdvNATGHFLVAREAVRIMKAQglgGSIVFIASKNAVNPGPNFGA 570
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 7-145 8.59e-15

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: 72.06  E-value: 8.59e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRK---EYGG 83
Cdd:cd05364   5 VAIITGSSSGIGAGTAILFARL-GARLALTGRDAERLEETRQSCLQAGVSEKKILLVVADLTEEEGQDRIISTtlaKFGR 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55727312  84 LDVLVNNAGIAFKVADPTPFHIQAEVTMKTNFFGTRDVCTELLP-LIKPQGRVVNVSSIMSVR 145
Cdd:cd05364  84 LDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPhLIKTKGEIVNVSSVAGGR 146
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 8-141 1.32e-14

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: 71.54  E-value: 1.32e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   8 ALVTGGNKGIGLAIvrdlCRLFSG---DVVLTARDVARGQAAVQQLQAEgLSPRFH--QLDIDDLQSIRALRDFLRKEYG 82
Cdd:cd05346   3 VLITGASSGIGEAT----ARRFAKagaKLILTGRRAERLQELADELGAK-FPVKVLplQLDVSDRESIEAALENLPEEFR 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55727312  83 GLDVLVNNAGIAFKVADPTPFHIQAEVTM-KTNFFGTRDVCTELLP--LIKPQGRVVNVSSI 141
Cdd:cd05346  78 DIDILVNNAGLALGLDPAQEADLEDWETMiDTNVKGLLNVTRLILPimIARNQGHIINLGSI 139
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-140 1.39e-14

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 71.26  E-value: 1.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK07666   9 NALITGAGRGIGRAVAIALAK--EGvNVGLLARTEENLKAVAEEVEAYGVKVVIATADVSDYEEVTAAIEQLKNELGSID 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 55727312   86 VLVNNAGIA-F-KVADPTPfhIQAEVTMKTNFFGTRDVCTELLP-LI-KPQGRVVNVSS 140
Cdd:PRK07666  87 ILINNAGISkFgKFLELDP--AEWEKIIQVNLMGVYYATRAVLPsMIeRQSGDIINISS 143
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 8-141 1.55e-14

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: 72.16  E-value: 1.55e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   8 ALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVL 87
Cdd:cd09810   4 VVITGASSGLGLAAAKALARRGEWHVVMACRDFLKAEQAAQEVGMPKDSYSVLHCDLASLDSVRQFVDNFRRTGRPLDAL 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 55727312  88 VNNAGIAFKVADPTPFHIQA-EVTMKTNFFGTRDVCTELLPLIK----PQGRVVNVSSI 141
Cdd:cd09810  84 VCNAAVYLPTAKEPRFTADGfELTVGVNHLGHFLLTNLLLEDLQrsenASPRIVIVGSI 142
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 7-236 2.84e-14

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 70.86  E-value: 2.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDvargQAAVQQLQAE--GLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK12829  13 RVLVTGGASGIGRAIAEAFAEA-GARVHVCDVS----EAALAATAARlpGAKVTATVADVADPAQVERVFDTAVERFGGL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   85 DVLVNNAGIA---FKVADPTPFHIQAevTMKTNFFGTRDVCTELLPLIK--PQGRVVNVSSIMSVRAlkscspelqqkfr 159
Cdd:PRK12829  88 DVLVNNAGIAgptGGIDEITPEQWEQ--TLAVNLNGQFYFARAAVPLLKasGHGGVIIALSSVAGRL------------- 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55727312  160 setiteeelvglmnkfvedtkkgvhqkeGWP-SSAYGVTKIGVTVLSRIHARKLSEQrkgdRILLNACCPGWVRTDMA 236
Cdd:PRK12829 153 ----------------------------GYPgRTPYAASKWAVVGLVKSLAIELGPL----GIRVNAILPGIVRGPRM 198
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 7-235 3.94e-14

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: 70.48  E-value: 3.94e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVARG-QAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:cd05366   4 VAIITGAAQGIGRAIAERLAA--DGfNIVLADLNLEEAaKSTIQEISEAGYNAVAVGADVTDKDDVEALIDQAVEKFGSF 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  85 DVLVNNAGIafkvADPTPF-HIQAEVTMKT---NFFGTRDVCTELLPLIKPQ---GRVVNVSSIMSVRALkscsPELqqk 157
Cdd:cd05366  82 DVMVNNAGI----APITPLlTITEEDLKKVyavNVFGVLFGIQAAARQFKKLghgGKIINASSIAGVQGF----PNL--- 150

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55727312 158 frsetiteeelvglmnkfvedtkkgvhqkegwpsSAYGVTKIGVTVLSRIHARKLSeqRKGdrILLNACCPGWVRTDM 235
Cdd:cd05366 151 ----------------------------------GAYSASKFAVRGLTQTAAQELA--PKG--ITVNAYAPGIVKTEM 190
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 9-267 4.65e-14

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


Pssm-ID: 187589 [Multi-domain]  Cd Length: 250  Bit Score: 69.83  E-value: 4.65e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   9 LVTGGNKGIGLAiVRDLCRlFSGDVVLTardVARGQAAVQQlqaeglsprfhqlDIDDLQSIR-ALRDFLRKEYGGLDVL 87
Cdd:cd05328   3 VITGAASGIGAA-TAELLE-DAGHTVIG---IDLREADVIA-------------DLSTPEGRAaAIADVLARCSGVLDGL 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  88 VNNAGiafkVADPTPfhiqAEVTMKTNFFGTRDVCTELLPLIKP--QGRVVNVSSIMSVralkscspELQQKfrsetitE 165
Cdd:cd05328  65 VNCAG----VGGTTV----AGLVLKVNYFGLRALMEALLPRLRKghGPAAVVVSSIAGA--------GWAQD-------K 121

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 166 EELVGLMNKFVEDTKKGVHQKEGWPSS-AYGVTKIGVTVLSRIHARKlSEQRKGDRIllNACCPGWVRT--------DMA 236
Cdd:cd05328 122 LELAKALAAGTEARAVALAEHAGQPGYlAYAGSKEALTVWTRRRAAT-WLYGAGVRV--NTVAPGPVETpilqaflqDPR 198

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 55727312 237 GPKATKS----------PEEGAetPVYLALLPPDAEGPHGQ 267
Cdd:cd05328 199 GGESVDAfvtpmgrraePDEIA--PVIAFLASDAASWINGA 237
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 7-146 5.56e-14

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: 69.92  E-value: 5.56e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQAEGLSPRF-HQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:cd05369   5 VAFITGGGTGIGKAIAKAFAEL-GASVAIAGRKPEVLEAAAEEISSATGGRAHpIQCDVRDPEAVEAAVDETLKEFGKID 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55727312  86 VLVNNAGIAFkvadPTPF-HIQA---EVTMKTNFFGTRDVCTELLP-LI--KPQGRVVNVSSIMSVRA 146
Cdd:cd05369  84 ILINNAAGNF----LAPAeSLSPngfKTVIDIDLNGTFNTTKAVGKrLIeaKHGGSILNISATYAYTG 147
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 7-141 6.45e-14

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 69.93  E-value: 6.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDL----CRLFSgdvvlTARDVARgqaavqqlqAEGLSP-RFHQLDIDDLQSIRALRDFLRKEY 81
Cdd:PRK06179   6 VALVTGASSGIGRATAEKLaragYRVFG-----TSRNPAR---------AAPIPGvELLELDVTDDASVQAAVDEVIARA 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55727312   82 GGLDVLVNNAGIAFkVADPTPFHI-QAEVTMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSI 141
Cdd:PRK06179  72 GRIDVLVNNAGVGL-AGAAEESSIaQAQALFDTNVFGILRMTRAVLPHMRAQgsGRIINISSV 133
PRK07035 PRK07035
SDR family oxidoreductase;
7-237 6.53e-14

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 69.66  E-value: 6.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRlFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK07035  10 IALVTGASRGIGEAIAKLLAQ-QGAHVIVSSRKLDGCQAVADAIVAAGGKAEALACHIGEMEQIDALFAHIRERHGRLDI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   87 LVNNAGiafkvADPTPFHIQA----------EVTMKTNFFgtrdVCTELLPLIKPQGR--VVNVSSIMSVralkscSPEL 154
Cdd:PRK07035  89 LVNNAA-----ANPYFGHILDtdlgafqktvDVNIRGYFF----MSVEAGKLMKEQGGgsIVNVASVNGV------SPGD 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  155 QQkfrsetiteeelvglmnkfvedtkkGVhqkegwpssaYGVTKIGVTVLSRIHARKLSEqrkgDRILLNACCPGWVRTD 234
Cdd:PRK07035 154 FQ-------------------------GI----------YSITKAAVISMTKAFAKECAP----FGIRVNALLPGLTDTK 194


                 ...
gi 55727312  235 MAG 237
Cdd:PRK07035 195 FAS 197
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-246 6.65e-14

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 69.49  E-value: 6.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK05565   7 VAIVTGASGGIGRAIAELLAKEGAKVVIAYDINEEAAQELLEEIKEEGGDAIAVKADVSSEEDVENLVEQIVEKFGKIDI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   87 LVNNAGIAFKVadptPFhiqAEVT-------MKTNFFGTRDVCTELLPLI--KPQGRVVNVSSImsvRALKSCSPElqqk 157
Cdd:PRK05565  87 LVNNAGISNFG----LV---TDMTdeewdrvIDVNLTGVMLLTRYALPYMikRKSGVIVNISSI---WGLIGASCE---- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  158 frsetiteeelvglmnkfvedtkkgvhqkegwpsSAYGVTKIGVTVLSRIHARKLSEQrkgdRILLNACCPGWVRTDMAg 237
Cdd:PRK05565 153 ----------------------------------VLYSASKGAVNAFTKALAKELAPS----GIRVNAVAPGAIDTEMW- 193


                 ....*....
gi 55727312  238 pkATKSPEE 246
Cdd:PRK05565 194 --SSFSEED 200
PRK06182 PRK06182
short chain dehydrogenase; Validated
 3-141 7.21e-14

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 69.60  E-value: 7.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    3 SGMHVALVTGGNKGIGLAIVRDLCRLfsGDVVLTArdvARGQAAVQQLQAEGLSPRfhQLDIDDLQSIRALRDFLRKEYG 82
Cdd:PRK06182   1 MQKKVALVTGASSGIGKATARRLAAQ--GYTVYGA---ARRVDKMEDLASLGVHPL--SLDVTDEASIKAAVDTIIAEEG 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55727312   83 GLDVLVNNAGI-AFKVADPTPFHiQAEVTMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSI 141
Cdd:PRK06182  74 RIDVLVNNAGYgSYGAIEDVPID-EARRQFEVNLFGAARLTQLVLPHMRAQrsGRIINISSM 134
PRK07806 PRK07806
SDR family oxidoreductase;
7-184 1.08e-13

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 68.98  E-value: 1.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK07806   8 TALVTGSSRGIGADTAKILAGAGAHVVVNYRQKAPRANKVVAEIEAAGGRASAVGADLTDEESVAALMDTAREEFGGLDA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   87 LVNNA-GIAFKVADPtpfhiqaEVTMKTNFFGTRDVCTELLPLIKPQGRVVNVSS-----IMSVRALkscsPELQQKFRS 160
Cdd:PRK07806  88 LVLNAsGGMESGMDE-------DYAMRLNRDAQRNLARAALPLMPAGSRVVFVTShqahfIPTVKTM----PEYEPVARS 156

                        170       180
                 ....*....|....*....|....
gi 55727312  161 ETITEEELVGLMNKFvedTKKGVH 184
Cdd:PRK07806 157 KRAGEDALRALRPEL---AEKGIG 177
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 1-147 1.69e-13

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 69.18  E-value: 1.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    1 MSSGMHVALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRK 79
Cdd:PRK07109   4 KPIGRQVVVITGASAGVGRATARAFAR--RGaKVVLLARGEEGLEALAAEIRAAGGEALAVVADVADAEAVQAAADRAEE 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55727312   80 EYGGLDVLVNNAGIA-FKVADPTPFHIQAEVTmKTNFFGTrdVCTEL--LPLIKPQGR--VVNVSSIMSVRAL 147
Cdd:PRK07109  82 ELGPIDTWVNNAMVTvFGPFEDVTPEEFRRVT-EVTYLGV--VHGTLaaLRHMRPRDRgaIIQVGSALAYRSI 151
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 7-248 2.22e-13

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: 68.33  E-value: 2.22e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVARGQAAVQQLQAEGL-SPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:cd08933  11 VVIVTGGSRGIGRGIVRAFVE--NGaKVVFCARGEAAGQALESELNRAGPgSCKFVPCDVTKEEDIKTLISVTVERFGRI 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  85 DVLVNNAGIAfkvadptPFHIQAEVT--------MKTNFFGTRDVCTELLP-LIKPQGRVVNVSSimsvralkscspelq 155
Cdd:cd08933  89 DCLVNNAGWH-------PPHQTTDETsaqefrdlLNLNLISYFLASKYALPhLRKSQGNIINLSS--------------- 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 156 qkfrsetiteeeLVGLMNkfvedtkkgvhQKEGWPssaYGVTKIGVTVLSRihARKLSEQRKGDRIllNACCPGWVRTDM 235
Cdd:cd08933 147 ------------LVGSIG-----------QKQAAP---YVATKGAITAMTK--ALAVDESRYGVRV--NCISPGNIWTPL 196

                       250
                ....*....|...
gi 55727312 236 AGPKATKSPEEGA 248
Cdd:cd08933 197 WEELAAQTPDTLA 209
PRK08017 PRK08017
SDR family oxidoreductase;
9-142 2.81e-13

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 67.80  E-value: 2.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    9 LVTGGNKGIGLAIVRDLCRlfSGDVVLTArdvARGQAAVQQLQAEGLSPRfhQLDIDDLQSI-RALRDFLRKEYGGLDVL 87
Cdd:PRK08017   6 LITGCSSGIGLEAALELKR--RGYRVLAA---CRKPDDVARMNSLGFTGI--LLDLDDPESVeRAADEVIALTDNRLYGL 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 55727312   88 VNNAGiaFKVADP--TPFHIQAEVTMKTNFFGTRDVCTELLPLIKP--QGRVVNVSSIM 142
Cdd:PRK08017  79 FNNAG--FGVYGPlsTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPhgEGRIVMTSSVM 135
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 7-276 4.24e-13

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 67.61  E-value: 4.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK13394   9 TAVVTGAASGIGKEIALELARA-GAAVAIADLNQDGANAVADEINKAGGKAIGVAMDVTNEDAVNAGIDKVAERFGSVDI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   87 LVNNAGIafKVADPT---PFH----IQAeVTMKTNFFGTRDVcteLLPLIKPQ--GRVVNVSSimsvralkscspelqqk 157
Cdd:PRK13394  88 LVSNAGI--QIVNPIenySFAdwkkMQA-IHVDGAFLTTKAA---LKHMYKDDrgGVVIYMGS----------------- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  158 frsetiteeelvglmnkfvedtkkgVHQKEGWP-SSAYGVTKIGVTVLSRIharkLSEQRKGDRILLNACCPGWVRT--- 233
Cdd:PRK13394 145 -------------------------VHSHEASPlKSAYVTAKHGLLGLARV----LAKEGAKHNVRSHVVCPGFVRTplv 195

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 55727312  234 DMAGPKATKspEEG-AETPVYLALLPPDAegPHGQFVSEKRVEQ 276
Cdd:PRK13394 196 DKQIPEQAK--ELGiSEEEVVKKVMLGKT--VDGVFTTVEDVAQ 235
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 16-145 4.47e-13

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 67.29  E-value: 4.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   16 GIGLAIVRDLCRLFS---GDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVLVNNAG 92
Cdd:PRK07890  12 GVGPGLGRTLAVRAAragADVVLAARTAERLDEVAAEIDDLGRRALAVPTDITDEDQCANLVALALERFGRVDALVNNAF 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 55727312   93 I--AFK-VADPTPFHIQAevTMKTNFFGTRDVCTELLPLIKPQ-GRVVNVSSiMSVR 145
Cdd:PRK07890  92 RvpSMKpLADADFAHWRA--VIELNVLGTLRLTQAFTPALAESgGSIVMINS-MVLR 145
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 7-250 4.55e-13

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: 67.15  E-value: 4.55e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRlFSGDVVLTARDVARGQAAVQQLQAEGLSPRF-HQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:cd05343   8 VALVTGASVGIGAAVARALVQ-HGMKVVGCARRVDKIEALAAECQSAGYPTLFpYQCDLSNEEQILSMFSAIRTQHQGVD 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  86 VLVNNAGIAFkvadPTPFhiqaevtmktnFFGTRDVCTELLPLikpqgrvvnvssimSVRALKSCSPELQQKFRSETITE 165
Cdd:cd05343  87 VCINNAGLAR----PEPL-----------LSGKTEGWKEMFDV--------------NVLALSICTREAYQSMKERNVDD 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 166 EELVgLMNKFVedtkkGVHQKEGWPSSAYGVTKIGVTVLSRIHARKLSEQRKgdRILLNACCPGWVRTDMAGPKATKSPE 245
Cdd:cd05343 138 GHII-NINSMS-----GHRVPPVSVFHFYAATKHAVTALTEGLRQELREAKT--HIRATSISPGLVETEFAFKLHDNDPE 209


                ....*
gi 55727312 246 EGAET 250
Cdd:cd05343 210 KAAAT 214
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
7-250 5.73e-13

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 67.13  E-value: 5.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAvQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK08226   8 TALITGALQGIGEGIARVFARH-GANLILLDISPEIEKLA-DELCGRGHRCTAVVADVRDPASVAAAIKRAKEKEGRIDI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   87 LVNNAGI---AFKVADPTP---FHIQaevtmkTNFFGTRDVCTELLP--LIKPQGRVVNVSSImsvralkscspelqqkf 158
Cdd:PRK08226  86 LVNNAGVcrlGSFLDMSDEdrdFHID------INIKGVWNVTKAVLPemIARKDGRIVMMSSV----------------- 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  159 rsetiteeelVGLMnkfVEDtkkgvhqkEGwpSSAYGVTKIGVTVLSRIHARKLSEQrkgdRILLNACCPGWVRTDMAGP 238
Cdd:PRK08226 143 ----------TGDM---VAD--------PG--ETAYALTKAAIVGLTKSLAVEYAQS----GIRVNAICPGYVRTPMAES 195

                        250
                 ....*....|..
gi 55727312  239 KATKSPEEGAET 250
Cdd:PRK08226 196 IARQSNPEDPES 207
PRK05866 PRK05866
SDR family oxidoreductase;
9-140 6.41e-13

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 67.46  E-value: 6.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    9 LVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVLV 88
Cdd:PRK05866  44 LLTGASSGIGEAAAEQFARR-GATVVAVARREDLLDAVADRITRAGGDAMAVPCDLSDLDAVDALVADVEKRIGGVDILI 122

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 55727312   89 NNAG--IAFKVADPTP-FHiQAEVTMKTNFFGTRDVCTELLP--LIKPQGRVVNVSS 140
Cdd:PRK05866 123 NNAGrsIRRPLAESLDrWH-DVERTMVLNYYAPLRLIRGLAPgmLERGDGHIINVAT 178
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 7-147 7.42e-13

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: 66.71  E-value: 7.42e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIV----RDLCRLFSgdVVLTARDVARGQAAVQQLQAE-GLSPRFHQLDIDDLQSIRALRDFLRKey 81
Cdd:cd09806   2 VVLITGCSSGIGLHLAvrlaSDPSKRFK--VYATMRDLKKKGRLWEAAGALaGGTLETLQLDVCDSKSVAAAVERVTE-- 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55727312  82 GGLDVLVNNAGIAFKvadpTPFHIQAEVTMK----TNFFGTRDVCTELLPLIKP--QGRVVNVSSIMSVRAL 147
Cdd:cd09806  78 RHVDVLVCNAGVGLL----GPLEALSEDAMAsvfdVNVFGTVRMLQAFLPDMKRrgSGRILVTSSVGGLQGL 145
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
7-148 7.65e-13

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 66.67  E-value: 7.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK08063   6 VALVTGSSRGIGKAIALRLAEEGYDIAVNYARSRKAAEETAEEIEALGRKALAVKANVGDVEKIKEMFAQIDEEFGRLDV 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55727312   87 LVNNAgiAFKVADPTpfhIQAEV-----TMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSIMSVRALK 148
Cdd:PRK08063  86 FVNNA--ASGVLRPA---MELEEshwdwTMNINAKALLFCAQEAAKLMEKVggGKIISLSSLGSIRYLE 149
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 7-147 7.67e-13

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 66.61  E-value: 7.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRdlcrLFS---GDVVLTARDVARGQAAVQQLQAEGLSprfHQLDIDDLQSIRALRDFLRKEYGG 83
Cdd:PRK06841  17 VAVVTGGASGIGHAIAE----LFAakgARVALLDRSEDVAEVAAQLLGGNAKG---LVCDVSDSQSVEAAVAAVISAFGR 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55727312   84 LDVLVNNAGIAF--KVADPTPFHIQA--EVTMKTNFFGTRDVCTELLPliKPQGRVVNVSSIMSVRAL 147
Cdd:PRK06841  90 IDILVNSAGVALlaPAEDVSEEDWDKtiDINLKGSFLMAQAVGRHMIA--AGGGKIVNLASQAGVVAL 155
PRK07074 PRK07074
SDR family oxidoreductase;
7-245 8.16e-13

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 66.72  E-value: 8.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLcrLFSGDVVLTA-RDVARGQAAVQQLQAEGLSPRfhQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK07074   4 TALVTGAAGGIGQALARRF--LAAGDRVLALdIDAAALAAFADALGDARFVPV--ACDLTDAASLAAALANAAAERGPVD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   86 VLVNNAGIAFKV--ADPTPFHIQAEVTMKTN--FFGTRDVCTELLPliKPQGRVVNVSSIMSVRALkscspelqqkfrse 161
Cdd:PRK07074  80 VLVANAGAARAAslHDTTPASWRADNALNLEaaYLCVEAVLEGMLK--RSRGAVVNIGSVNGMAAL-------------- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  162 titeeelvglmnkfvedtkkgvhqkeGWPssAYGVTKIGVTVLSRIHARKLSEqrkgDRILLNACCPGWVRTDMAGPKAT 241
Cdd:PRK07074 144 --------------------------GHP--AYSAAKAGLIHYTKLLAVEYGR----FGIRANAVAPGTVKTQAWEARVA 191


                 ....
gi 55727312  242 KSPE 245
Cdd:PRK07074 192 ANPQ 195
PRK05693 PRK05693
SDR family oxidoreductase;
5-144 8.97e-13

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 66.74  E-value: 8.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    5 MHVALVTGGNKGIGLAIVrDLCRLFSGDVVLTARDVARgqaaVQQLQAEGLSPRfhQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK05693   1 MPVVLITGCSSGIGRALA-DAFKAAGYEVWATARKAED----VEALAAAGFTAV--QLDVNDGAALARLAEELEAEHGGL 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55727312   85 DVLVNNAGiaFKVADP--TPFHIQAEVTMKTNFFGTRDVCTELLPLI-KPQGRVVNVSSIMSV 144
Cdd:PRK05693  74 DVLINNAG--YGAMGPllDGGVEAMRRQFETNVFAVVGVTRALFPLLrRSRGLVVNIGSVSGV 134
PRK08628 PRK08628
SDR family oxidoreductase;
6-93 9.92e-13

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 66.52  E-value: 9.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    6 HVALVTGGNKGIGLAIVRDLCRlfSGDV-VLTARDvARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK08628   8 KVVIVTGGASGIGAAISLRLAE--EGAIpVIFGRS-APDDEFAEELRALQPRAEFVQVDLTDDAQCRDAVEQTVAKFGRI 84


                 ....*....
gi 55727312   85 DVLVNNAGI 93
Cdd:PRK08628  85 DGLVNNAGV 93
PRK06953 PRK06953
SDR family oxidoreductase;
5-246 1.20e-12

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 65.48  E-value: 1.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    5 MHVALVTGGNKGIGLAIVRDLCRlfSGD-VVLTARDvargQAAVQQLQAegLSPRFHQLDIDDLQSIRALRDFLRKEygG 83
Cdd:PRK06953   1 MKTVLIVGASRGIGREFVRQYRA--DGWrVIATARD----AAALAALQA--LGAEALALDVADPASVAGLAWKLDGE--A 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   84 LDVLVNNAGI--AFKVADPTPFHIQAEVTMKTNFFGTRDVCTELLPLIK-PQGRVVNVSSIMSvralkscspelqqkfrs 160
Cdd:PRK06953  71 LDAAVYVAGVygPRTEGVEPITREDFDAVMHTNVLGPMQLLPILLPLVEaAGGVLAVLSSRMG----------------- 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  161 etiteeeLVGlmnkfvedtkkGVHQKEGWpssAYGVTKIGVTVLSRIharkLSEQRKgdrillNACC----PGWVRTDMA 236
Cdd:PRK06953 134 -------SIG-----------DATGTTGW---LYRASKAALNDALRA----ASLQAR------HATCialhPGWVRTDMG 182

                        250
                 ....*....|
gi 55727312  237 GPKATKSPEE 246
Cdd:PRK06953 183 GAQAALDPAQ 192
PRK06196 PRK06196
oxidoreductase; Provisional
 7-141 1.67e-12

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 66.24  E-value: 1.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCrLFSGDVVLTARDVARGQAAVQQLqaEGLSprFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK06196  28 TAIVTGGYSGLGLETTRALA-QAGAHVIVPARRPDVAREALAGI--DGVE--VVMLDLADLESVRAFAERFLDSGRRIDI 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 55727312   87 LVNNAGIafkVADP-TPFHIQAEVTMKTNFFGTRDVCTELLPLIKPQG--RVVNVSSI 141
Cdd:PRK06196 103 LINNAGV---MACPeTRVGDGWEAQFATNHLGHFALVNLLWPALAAGAgaRVVALSSA 157
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 7-256 2.01e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 65.52  E-value: 2.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRdlcRLFS--GDVVLTARDVARGQAAVQQLqaEGLsprFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK06057   9 VAVITGGGSGIGLATAR---RLAAegATVVVGDIDPEAGKAAADEV--GGL---FVPTDVTDEDAVNALFDTAAETYGSV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   85 DVLVNNAGIA------FKVADPTPFHIQAEVTMKTNFFgtrdVCTELLPLIKPQGR--VVNVSSIMSVraLKSCSPELqq 156
Cdd:PRK06057  81 DIAFNNAGISppeddsILNTGLDAWQRVQDVNLTSVYL----CCKAALPHMVRQGKgsIINTASFVAV--MGSATSQI-- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  157 kfrsetiteeelvglmnkfvedtkkgvhqkegwpssAYGVTKIGVTVLSrihaRKLSEQRKGDRILLNACCPGWVRTDMA 236
Cdd:PRK06057 153 ------------------------------------SYTASKGGVLAMS----RELGVQFARQGIRVNALCPGPVNTPLL 192

                        250       260
                 ....*....|....*....|
gi 55727312  237 GPKATKSPEEGAETPVYLAL 256
Cdd:PRK06057 193 QELFAKDPERAARRLVHVPM 212
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 7-145 2.01e-12

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


Pssm-ID: 187613 [Multi-domain]  Cd Length: 270  Bit Score: 65.78  E-value: 2.01e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLT--------ARDVAR--GQAAVQQLQAEGlsprfhqlDIDDLQSIRALRD 75
Cdd:cd05355  28 KALITGGDSGIGRAVAIAFAR--EGaDVAINylpeeeddAEETKKliEEEGRKCLLIPG--------DLGDESFCRDLVK 97

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55727312  76 FLRKEYGGLDVLVNNAG---IAFKVADPTPfhIQAEVTMKTNFFGTRDVCTELLPLIKPQGRVVNVSSIMSVR 145
Cdd:cd05355  98 EVVKEFGKLDILVNNAAyqhPQESIEDITT--EQLEKTFRTNIFSMFYLTKAALPHLKKGSSIINTTSVTAYK 168
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 7-234 2.18e-12

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: 65.56  E-value: 2.18e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd08935   7 VAVITGGTGVLGGAMARALAQA-GAKVAALGRNQEKGDKVAKEITALGGRAIALAADVLDRASLERAREEIVAQFGTVDI 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  87 LVNNAGIAFKVADPTPFHIQAEVTmkTNFFGTRDVCTEllplikpqgRVVNVSSIMSVRALKSCSPELQQKFRSETITee 166
Cdd:cd08935  86 LINGAGGNHPDATTDPEHYEPETE--QNFFDLDEEGWE---------FVFDLNLNGSFLPSQVFGKDMLEQKGGSIIN-- 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55727312 167 elVGLMNKFVEDTKkgvhqkegwpSSAYGVTKIGVTVLSRIHARKLSEQrkGDRIllNACCPGWVRTD 234
Cdd:cd08935 153 --ISSMNAFSPLTK----------VPAYSAAKAAVSNFTQWLAVEFATT--GVRV--NAIAPGFFVTP 204
PRK09072 PRK09072
SDR family oxidoreductase;
9-141 2.23e-12

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 65.35  E-value: 2.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    9 LVTGGNKGIGLAIVRDLCRlfSGDVVLTardVARGQAAVQQLQAEGLSPRFHQL---DIDDLQSIRALRDFLRkEYGGLD 85
Cdd:PRK09072   9 LLTGASGGIGQALAEALAA--AGARLLL---VGRNAEKLEALAARLPYPGRHRWvvaDLTSEAGREAVLARAR-EMGGIN 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   86 VLVNNAGIA-FK-VADPTPFHIQAEVTmkTNFFGTRDVCTELLPLIK--PQGRVVNVSSI 141
Cdd:PRK09072  83 VLINNAGVNhFAlLEDQDPEAIERLLA--LNLTAPMQLTRALLPLLRaqPSAMVVNVGST 140
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 7-146 2.55e-12

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 65.13  E-value: 2.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLcRLFSGDVVLTARDVARG----QAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYG 82
Cdd:PRK12827   8 RVLITGGSGGLGRAIAVRL-AADGADVIVLDIHPMRGraeaDAVAAGIEAAGGKALGLAFDVRDFAATRAALDAGVEEFG 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55727312   83 GLDVLVNNAGIAFKVADPTPFHIQAEVTMKTNFFGTRDVCTELL-PLIKPQ--GRVVNVSSIMSVRA 146
Cdd:PRK12827  87 RLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALpPMIRARrgGRIVNIASVAGVRG 153
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 9-142 2.78e-12

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: 65.38  E-value: 2.78e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   9 LVTGGNKGIGLAIVRDLCRLfsGDVVLtardvargqAAVQQLQ---AEGL----SPRFH--QLDIDDLQSIRALRDFLRK 79
Cdd:cd09805   4 LITGCDSGFGNLLAKKLDSL--GFTVL---------AGCLTKNgpgAKELrrvcSDRLRtlQLDVTKPEQIKRAAQWVKE 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55727312  80 EYG--GLDVLVNNAGIA--FKVADPTPFHIQAEVtMKTNFFGTRDVCTELLPLI-KPQGRVVNVSSIM 142
Cdd:cd09805  73 HVGekGLWGLVNNAGILgfGGDEELLPMDDYRKC-MEVNLFGTVEVTKAFLPLLrRAKGRVVNVSSMG 139
PRK08219 PRK08219
SDR family oxidoreductase;
3-140 3.08e-12

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 64.57  E-value: 3.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    3 SGMHVALVTGGNKGIGLAIVRDLCRlfSGDVVLTARDVARGQAAVQQL-QAEGLsprfhQLDIDDLQSIRALRDFLrkey 81
Cdd:PRK08219   1 MERPTALITGASRGIGAAIARELAP--THTLLLGGRPAERLDELAAELpGATPF-----PVDLTDPEAIAAAVEQL---- 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55727312   82 GGLDVLVNNAGIAF--KVADPTPfhIQAEVTMKTNFFGTRDVCTELLPLIK-PQGRVVNVSS 140
Cdd:PRK08219  70 GRLDVLVHNAGVADlgPVAESTV--DEWRATLEVNVVAPAELTRLLLPALRaAHGHVVFINS 129
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 8-236 3.09e-12

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: 64.66  E-value: 3.09e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   8 ALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd05350   1 VLITGASSGIGRALAREFAK--AGyNVALAARRTDRLDELKAELLNPNPSVEVEILDVTDEERNQLVIAELEAELGGLDL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  87 LVNNAGIAFkvadPTPFHI-QAEV---TMKTNFFGTRDVCTELLPLIKPQGR--VVNVSSIMSVRalkscspelqqkfrs 160
Cdd:cd05350  79 VIINAGVGK----GTSLGDlSFKAfreTIDTNLLGAAAILEAALPQFRAKGRghLVLISSVAALR--------------- 139

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55727312 161 etiteeelvglmnkfvedtkkgvhqkeGWP-SSAYGVTKIGVTVLsrihARKLSEQRKGDRILLNACCPGWVRTDMA 236
Cdd:cd05350 140 ---------------------------GLPgAAAYSASKAALSSL----AESLRYDVKKRGIRVTVINPGFIDTPLT 185
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 9-273 3.25e-12

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


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 64.92  E-value: 3.25e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   9 LVTGGNKGIG----LAIVRDlcrlfSGDVVLTARDVARGQAAVQQLQAEGLSPR--FHQLDIDDLQSIRALRDFLRKEYG 82
Cdd:cd09808   5 LITGANSGIGkaaaLAIAKR-----GGTVHMVCRNQTRAEEARKEIETESGNQNifLHIVDMSDPKQVWEFVEEFKEEGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  83 GLDVLVNNAGIAFKVADPTPFHIqaEVTMKTNFFGTRDVCTELLPLIK--PQGRVVNVSSimsvralkscSPELQQKFRS 160
Cdd:cd09808  80 KLHVLINNAGCMVNKRELTEDGL--EKNFATNTLGTYILTTHLIPVLEkeEDPRVITVSS----------GGMLVQKLNT 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 161 ETITEEE--LVGLMnKFVEDTKKGVHQKEGWpSSAYGVTKigvtvLSRIHarklseqrkgdrillnaccPGW-----VRT 233
Cdd:cd09808 148 NNLQSERtaFDGTM-VYAQNKRQQVIMTEQW-AKKHPEIH-----FSVMH-------------------PGWadtpaVRN 201

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 55727312 234 DMAGPKAT-----KSPEEGAETPVYLALLPPDAEGPHGQFVSEKR 273
Cdd:cd09808 202 SMPDFHARfkdrlRSEEQGADTVVWLALSSAAAKAPSGRFYQDRK 246
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 7-91 3.63e-12

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 64.64  E-value: 3.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRlFSGDVVLTARDVARGQAAVQQLqaeGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK08265   8 VAIVTGGATLIGAAVARALVA-AGARVAIVDIDADNGAAVAASL---GERARFIATDITDDAAIERAVATVVARFGRVDI 83


                 ....*
gi 55727312   87 LVNNA 91
Cdd:PRK08265  84 LVNLA 88
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-235 3.78e-12

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 64.74  E-value: 3.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    1 MSSGMHVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKE 80
Cdd:PRK06077   2 YSLKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKKRAEEMNETLKMVKENGGEGIGVLADVSTREGCETLAKATIDR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   81 YGGLDVLVNNAGIA----FKVADPTPFHIQAEVTMKTNFFgtrdvCT-ELLPLIKPQGRVVNVSSIMSVRAlkscspelq 155
Cdd:PRK06077  82 YGVADILVNNAGLGlfspFLNVDDKLIDKHISTDFKSVIY-----CSqELAKEMREGGAIVNIASVAGIRP--------- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  156 qkfrsetiteeeLVGLmnkfvedtkkgvhqkegwpsSAYGVTKIGVTVLSRIHARKLSEqrkgdRILLNACCPGWVRTDM 235
Cdd:PRK06077 148 ------------AYGL--------------------SIYGAMKAAVINLTKYLALELAP-----KIRVNAIAPGFVKTKL 190
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 6-236 3.86e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 64.35  E-value: 3.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    6 HVALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVARGQAAVQQLQAEGLSprfhqLDIDDLQSIRALRDflrkEYGGL 84
Cdd:PRK07060  10 KSVLVTGASSGIGRACAVALAQ--RGaRVVAAARNAAALDRLAGETGCEPLR-----LDVGDDAAIRAALA----AAGAF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   85 DVLVNNAGIAFKVADPTPFHIQAEVTMKTNFFGTRDVCTELLPLIKPQGR---VVNVSSIMSVRALKScspelqqkfrse 161
Cdd:PRK07060  79 DGLVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAAGRggsIVNVSSQAALVGLPD------------ 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55727312  162 titeeelvglmnkfvedtkkgvHqkegwpsSAYGVTKIGVTVLSRIHARKLSEQrkGDRIllNACCPGWVRTDMA 236
Cdd:PRK07060 147 ----------------------H-------LAYCASKAALDAITRVLCVELGPH--GIRV--NSVNPTVTLTPMA 188
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 6-139 4.87e-12

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


Pssm-ID: 187647 [Multi-domain]  Cd Length: 250  Bit Score: 64.34  E-value: 4.87e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   6 HVALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQqlqAEGLSPRFH--QLDIDDLQSIRALRDFLRKEYGG 83
Cdd:cd08943   2 KVALVTGGASGIGLAIAKRLAAE-GAAVVVADIDPEIAEKVAE---AAQGGPRALgvQCDVTSEAQVQSAFEQAVLEFGG 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55727312  84 LDVLVNNAGIAFkvadPTPFhiqAEVTMKT-------NFFGTRDVCTELLPLIKPQGR----VVNVS 139
Cdd:cd08943  78 LDIVVSNAGIAT----SSPI---AETSLEDwnrsmdiNLTGHFLVSREAFRIMKSQGIggniVFNAS 137
PRK06172 PRK06172
SDR family oxidoreductase;
7-248 5.20e-12

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 64.39  E-value: 5.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK06172   9 VALVTGGAAGIGRATALAFARE-GAKVVVADRDAAGGEETVALIREAGGEALFVACDVTRDAEVKALVEQTIAAYGRLDY 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   87 LVNNAGI---AFKVADPTPFHIQAevTMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSIMSvralkscspelqqkfrse 161
Cdd:PRK06172  88 AFNNAGIeieQGRLAEGSEAEFDA--IMGVNVKGVWLCMKYQIPLMLAQggGAIVNTASVAG------------------ 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  162 titeeeLVGLMNkfvedtkkgvhqkegwpSSAYGVTKIGVTVLSRIHArkLSEQRKGDRIllNACCPGWVRTDMAGPKAT 241
Cdd:PRK06172 148 ------LGAAPK-----------------MSIYAASKHAVIGLTKSAA--IEYAKKGIRV--NAVCPAVIDTDMFRRAYE 200


                 ....*..
gi 55727312  242 KSPEEGA 248
Cdd:PRK06172 201 ADPRKAE 207
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 7-235 5.53e-12

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 64.05  E-value: 5.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQAEGLspRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK12828   9 VVAITGGFGGLGRATAAWLAAR-GARVALIGRGAAPLSQTLPGVPADAL--RIGGIDLVDPQAARRAVDEVNRQFGRLDA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   87 LVNNAGiAF---KVADPTPfhIQAEVTMKTNFFGTRDVCTELLP-LIK-PQGRVVNVSSIMSVRAlkscspelqqkfrse 161
Cdd:PRK12828  86 LVNIAG-AFvwgTIADGDA--DTWDRMYGVNVKTTLNASKAALPaLTAsGGGRIVNIGAGAALKA--------------- 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55727312  162 titeeelvglmnkfvedtkkgvhqKEGWpsSAYGVTKIGVTVLSRIHARKLSEQrkgdRILLNACCPGWVRTDM 235
Cdd:PRK12828 148 ------------------------GPGM--GAYAAAKAGVARLTEALAAELLDR----GITVNAVLPSIIDTPP 191
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 7-235 6.38e-12

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 63.87  E-value: 6.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK12935   8 VAIVTGGAKGIGKAITVALAQEGAKVVINYNSSKEAAENLVNELGKEGHDVYAVQADVSKVEDANRLVEEAVNHFGKVDI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   87 LVNNAGI----AFKVADPTPFHIQAEVTMKTNFFGTRDVCTELLPliKPQGRVVNVSSIMSvralkscspelqqkfrset 162
Cdd:PRK12935  88 LVNNAGItrdrTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITE--AEEGRIISISSIIG------------------- 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55727312  163 iteeelvglmnkfvedtkkgvhQKEGWPSSAYGVTKIGVTVLSRIHARKLSEQrkgdRILLNACCPGWVRTDM 235
Cdd:PRK12935 147 ----------------------QAGGFGQTNYSAAKAGMLGFTKSLALELAKT----NVTVNAICPGFIDTEM 193
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
7-235 6.50e-12

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 63.98  E-value: 6.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVrdlCRLFSG--DVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK08643   4 VALVTGAGQGIGFAIA---KRLVEDgfKVAIVDYNEETAQAAADKLSKDGGKAIAVKADVSDRDQVFAAVRQVVDTFGDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   85 DVLVNNAGIA--FKVADPTP--FHIQAEVTMKTNFFGTRdVCTELLPLIKPQGRVVNVSSimsvRALKSCSPELqqkfrs 160
Cdd:PRK08643  81 NVVVNNAGVAptTPIETITEeqFDKVYNINVGGVIWGIQ-AAQEAFKKLGHGGKIINATS----QAGVVGNPEL------ 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55727312  161 etiteeelvglmnkfvedtkkgvhqkegwpsSAYGVTKIGVTVLSRIHARKLSEqrKGdrILLNACCPGWVRTDM 235
Cdd:PRK08643 150 -------------------------------AVYSSTKFAVRGLTQTAARDLAS--EG--ITVNAYAPGIVKTPM 189
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 7-145 6.83e-12

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: 63.95  E-value: 6.83e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRdlcrLFSGD---VVLTARDVARGQAAVQQLqaeGLSPRFHQLDIDDLQSIRALRDFLRKEYGG 83
Cdd:cd05345   7 VAIVTGAGSGFGEGIAR----RFAQEgarVVIADINADGAERVAADI---GEAAIAIQADVTKRADVEAMVEAALSKFGR 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55727312  84 LDVLVNNAGIAFKVA-----DPTPFHIQAEVTMKTNFFGTRdvctELLPLIKPQGRVV--NVSSIMSVR 145
Cdd:cd05345  80 LDILVNNAGITHRNKpmlevDEEEFDRVFAVNVKSIYLSAQ----ALVPHMEEQGGGViiNIASTAGLR 144
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 7-251 7.12e-12

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 64.28  E-value: 7.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVrdlcrlfsgdvVLTAR---DVA------RGQAAV--QQLQAEGLSPRFHQLDIDDLQSIRALRD 75
Cdd:PRK06701  48 VALITGGDSGIGRAVA-----------VLFAKegaDIAivyldeHEDANEtkQRVEKEGVKCLLIPGDVSDEAFCKDAVE 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   76 FLRKEYGGLDVLVNNAgiAFK-----VADPTPFHIqaEVTMKTNFFGTRDVCTELLPLIKPQGRVVNVSSIMSVRAlksc 150
Cdd:PRK06701 117 ETVRELGRLDILVNNA--AFQypqqsLEDITAEQL--DKTFKTNIYSYFHMTKAALPHLKQGSAIINTGSITGYEG---- 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  151 SPELQQkfrsetiteeelvglmnkfvedtkkgvhqkegwpssaYGVTKIGvtvlsrIHA--RKLSEQRKGDRILLNACCP 228
Cdd:PRK06701 189 NETLID-------------------------------------YSATKGA------IHAftRSLAQSLVQKGIRVNAVAP 225

                        250       260
                 ....*....|....*....|....*..
gi 55727312  229 GWVRTDMaGPkATKSPEE----GAETP 251
Cdd:PRK06701 226 GPIWTPL-IP-SDFDEEKvsqfGSNTP 250
PRK07062 PRK07062
SDR family oxidoreductase;
7-143 8.70e-12

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 63.91  E-value: 8.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLcrLFSG-DVVLTARDVARGQAAVQQL-----QAEGLSPRFHQLDIDDlqsIRALRDFLRKE 80
Cdd:PRK07062  10 VAVVTGGSSGIGLATVELL--LEAGaSVAICGRDEERLASAEARLrekfpGARLLAARCDVLDEAD---VAAFAAAVEAR 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55727312   81 YGGLDVLVNNAGIAFKV--ADPTPFHIQAEVTMKtnFFGTRDVCTELLPLIK--PQGRVVNVSSIMS 143
Cdd:PRK07062  85 FGGVDMLVNNAGQGRVStfADTTDDAWRDELELK--YFSVINPTRAFLPLLRasAAASIVCVNSLLA 149
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 7-143 1.42e-11

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: 63.56  E-value: 1.42e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVrdlCRLFSGD-------VVLTARDVARGQAAVQQLQAeglsprFH----------QLDIDDLQS 69
Cdd:cd08941   3 VVLVTGANSGLGLAIC---ERLLAEDdenpeltLILACRNLQRAEAACRALLA------SHpdarvvfdyvLVDLSNMVS 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  70 IRALRDFLRKEYGGLDVLVNNAGI----------AFKVADPTPFHIQAEVTMK-----------------------TNFF 116
Cdd:cd08941  74 VFAAAKELKKRYPRLDYLYLNAGImpnpgidwigAIKEVLTNPLFAVTNPTYKiqaegllsqgdkatedglgevfqTNVF 153

                       170       180       190
                ....*....|....*....|....*....|
gi 55727312 117 GTRDVCTELLPLIKPQ---GRVVNVSSIMS 143
Cdd:cd08941 154 GHYYLIRELEPLLCRSdggSQIIWTSSLNA 183
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 3-147 1.55e-11

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 63.04  E-value: 1.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    3 SGMHVAlVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLqaeGLsPRFHQLDIDDLQSIRALRDFLRKEYG 82
Cdd:PRK07825   4 RGKVVA-ITGGARGIGLATARALAAL-GARVAIGDLDEALAKETAAEL---GL-VVGGPLDVTDPASFAAFLDAVEADLG 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55727312   83 GLDVLVNNAGI----AFKVADPTPFHIQAEVTMKTNFFGTRDVctelLPLIKPQGR--VVNVSSIMSVRAL 147
Cdd:PRK07825  78 PIDVLVNNAGVmpvgPFLDEPDAVTRRILDVNVYGVILGSKLA----APRMVPRGRghVVNVASLAGKIPV 144
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 7-252 2.07e-11

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


Pssm-ID: 187662 [Multi-domain]  Cd Length: 242  Bit Score: 62.21  E-value: 2.07e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLcrLFSGD-VVLTARDVARGqaaVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:cd09761   3 VAIVTGGGHGIGKQICLDF--LEAGDkVVFADIDEERG---ADFAEAEGPNLFFVHGDVADETLVKFVVYAMLEKLGRID 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  86 VLVNNAGIAFKVADPTPFHIQAEVTMKTNFFGTRDV---CTEllPLIKPQGRVVNvssIMSVRAlkscspelqqkFRSET 162
Cdd:cd09761  78 VLVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELsryCRD--ELIKNKGRIIN---IASTRA-----------FQSEP 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 163 ITEeelvglmnkfvedtkkgvhqkegwpssAYGVTKIGVTVLSRIHARKLseqrkGDRILLNACCPGWVRTDMAGPK--A 240
Cdd:cd09761 142 DSE---------------------------AYAASKGGLVALTHALAMSL-----GPDIRVNCISPGWINTTEQQEFtaA 189

                       250
                ....*....|..
gi 55727312 241 TKSPEEGAETPV 252
Cdd:cd09761 190 PLTQEDHAQHPA 201
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 7-267 2.88e-11

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


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 61.82  E-value: 2.88e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRlFSGDVVLTARDVARGQAAVQQLQAEG-LSPRFHQLDIDDL--QSIRALRDFLRKEYGG 83
Cdd:cd05340   6 IILVTGASDGIGREAALTYAR-YGATVILLGRNEEKLRQVADHINEEGgRQPQWFILDLLTCtsENCQQLAQRIAVNYPR 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  84 LDVLVNNAGIAFKV---ADPTPFHIQ--AEVTMKTNFFGTRdvctELLPLIKPqgrvvnvssimsvralkscSPELQQKF 158
Cdd:cd05340  85 LDGVLHNAGLLGDVcplSEQNPQVWQdv*QVNVNATFMLTQ----ALLPLLLK-------------------SDAGSLVF 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 159 RSETIteeelvglmnkfvedtkkGVHQKEGWpsSAYGVTKIGVTVLSRIharkLSEQRKGDRILLNACCPGWVRTDM--- 235
Cdd:cd05340 142 TSSSV------------------GRQGRANW--GAYAVSKFATEGL*QV----LADEYQQRNLRVNCINPGGTRTAMras 197

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 55727312 236 ----AGPKATKSPEEgaETPVYLALLPPDAEGPHGQ 267
Cdd:cd05340 198 afptEDPQKLKTPAD--IMPLYLWLMGDDSRRKTGM 231
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 6-93 3.21e-11

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


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 63.16  E-value: 3.21e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   6 HVALVTGGNKGIGLAIVRDLCRLFSGDVVLTAR----DVARGQA-AVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKE 80
Cdd:cd08953 206 GVYLVTGGAGGIGRALARALARRYGARLVLLGRsplpPEEEWKAqTLAALEALGARVLYISADVTDAAAVRRLLEKVRER 285

                        90
                ....*....|...
gi 55727312  81 YGGLDVLVNNAGI 93
Cdd:cd08953 286 YGAIDGVIHAAGV 298
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
7-238 3.39e-11

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 62.06  E-value: 3.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDvaRGQAAVQQL-QAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK06935  17 VAIVTGGNTGLGQGYAVALAK--AGaDIIITTHG--TNWDETRRLiEKEGRKVTFVQVDLTKPESAEKVVKEALEEFGKI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   85 DVLVNNAGI-------AFKVADptpFHIQAEVTMKTNFFGTRDVCTELLPliKPQGRVVNVSSIMSVRAlkscspelqqk 157
Cdd:PRK06935  93 DILVNNAGTirrapllEYKDED---WNAVMDINLNSVYHLSQAVAKVMAK--QGSGKIINIASMLSFQG----------- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  158 frsetiteeelvglmNKFVedtkkgvhqkegwpsSAYGVTKIGVTVLSRIHARKLSEQrkgdRILLNACCPGWVRTDMAG 237
Cdd:PRK06935 157 ---------------GKFV---------------PAYTASKHGVAGLTKAFANELAAY----NIQVNAIAPGYIKTANTA 202


                 .
gi 55727312  238 P 238
Cdd:PRK06935 203 P 203
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 7-229 5.66e-11

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: 61.20  E-value: 5.66e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLcRLFSGDVVLTARDVARGQAAVQQLQAEGlSPRFH--QLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:cd08930   4 IILITGAAGLIGKAFCKAL-LSAGARLILADINAPALEQLKEELTNLY-KNRVIalELDITSKESIKELIESYLEKFGRI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  85 DVLVNNAGIAFKVaDPTPFH------IQAEVTMktNFFGTRDVCTELLPLIKPQGR--VVNVSSIMSVRAlkscsPelqq 156
Cdd:cd08930  82 DILINNAYPSPKV-WGSRFEefpyeqWNEVLNV--NLGGAFLCSQAFIKLFKKQGKgsIINIASIYGVIA-----P---- 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55727312 157 KFRSETITEeelvglMNKFVEdtkkgvhqkegwpssaYGVTKIGVTVLSRIHARKLSeqrkGDRILLNACCPG 229
Cdd:cd08930 150 DFRIYENTQ------MYSPVE----------------YSVIKAGIIHLTKYLAKYYA----DTGIRVNAISPG 196
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 8-92 5.93e-11

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 61.21  E-value: 5.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    8 ALVTGGNKGIGLAivrdLCRLFSGD---VVLTARDVARGQAAVQQLQAE-GLSPRFHQLDIDDLQSiralRDFLRKEYGG 83
Cdd:PRK06125  10 VLITGASKGIGAA----AAEAFAAEgchLHLVARDADALEALAADLRAAhGVDVAVHALDLSSPEA----REQLAAEAGD 81


                 ....*....
gi 55727312   84 LDVLVNNAG 92
Cdd:PRK06125  82 IDILVNNAG 90
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 7-255 6.32e-11

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: 60.96  E-value: 6.32e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQAEGlSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd08942   8 IVLVTGGSRGIGRMIAQGFLEA-GARVIISARKAEACADAAEELSAYG-ECIAIPADLSSEEGIEALVARVAERSDRLDV 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  87 LVNNAGIAFKVA-DPTP---FHIQAEVTMKTNFFGTrdvcTELLPLIKPQG------RVVNVSSIMSVRAlkscspelqq 156
Cdd:cd08942  86 LVNNAGATWGAPlEAFPesgWDKVMDINVKSVFFLT----QALLPLLRAAAtaenpaRVINIGSIAGIVV---------- 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 157 kfrsetiteeelvglmnkfvedtkkgvhqkEGWPSSAYGVTKIGVTVLSRIHARKLSeqrkGDRILLNACCPG------- 229
Cdd:cd08942 152 ------------------------------SGLENYSYGASKAAVHQLTRKLAKELA----GEHITVNAIAPGrfpskmt 197

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 55727312 230 -WVRTDMAGPKATK---------SPEEGAETPVYLA 255
Cdd:cd08942 198 aFLLNDPAALEAEEksiplgrwgRPEDMAGLAIMLA 233
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 7-141 8.75e-11

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 60.82  E-value: 8.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLcrLFSGD-VVLTARDVARGQAAVQQLQaEGLSPRfhQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK08263   5 VWFITGASRGFGRAWTEAA--LERGDrVVATARDTATLADLAEKYG-DRLLPL--ALDVTDRAAVFAAVETAVEHFGRLD 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 55727312   86 VLVNNAGIAFKVADPTPFHIQAEVTMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSI 141
Cdd:PRK08263  80 IVVNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQrsGHIIQISSI 137
PRK05993 PRK05993
SDR family oxidoreductase;
9-148 9.40e-11

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 60.81  E-value: 9.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    9 LVTGGNKGIGLAIVRDLCRlfSG-DVVLTAR---DVARgqaavqqLQAEGLSPrfHQLDIDDLQSIRALRD-FLRKEYGG 83
Cdd:PRK05993   8 LITGCSSGIGAYCARALQS--DGwRVFATCRkeeDVAA-------LEAEGLEA--FQLDYAEPESIAALVAqVLELSGGR 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55727312   84 LDVLVNNA--GIAFKVAD-PT-PFHIQAEvtmkTNFFGTRDVCTELLPLIKPQ--GRVVNVSSIMSVRALK 148
Cdd:PRK05993  77 LDALFNNGayGQPGAVEDlPTeALRAQFE----ANFFGWHDLTRRVIPVMRKQgqGRIVQCSSILGLVPMK 143
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 7-145 1.09e-10

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


Pssm-ID: 187642 [Multi-domain]  Cd Length: 256  Bit Score: 60.62  E-value: 1.09e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDvARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd08937   6 VVVVTGAAQGIGRGVAERLAGE-GARVLLVDRS-ELVHEVLAEILAAGDAAHVHTADLETYAGAQGVVRAAVERFGRVDV 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55727312  87 LVNNAG--IAFKVADPTPF-HIQAEVtmKTNFFGTRDVCTELLP--LIKPQGRVVNVSSImSVR 145
Cdd:cd08937  84 LINNVGgtIWAKPYEHYEEeQIEAEI--RRSLFPTLWCCRAVLPhmLERQQGVIVNVSSI-ATR 144
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 7-255 1.21e-10

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: 60.16  E-value: 1.21e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRlFSGDVVLTARDVARGQAAVQQLQAEGLSprFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd05326   6 VAIITGGASGIGEATARLFAK-HGARVVIADIDDDAGQAVAAELGDPDIS--FVHCDVTVEADVRAAVDTAVARFGRLDI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  87 LVNNAGIafkVADPTP---------FHIQAEVTMKTNFFGTRDVCTELLPliKPQGRVVNVSSIMSVRAlkscspelqqk 157
Cdd:cd05326  83 MFNNAGV---LGAPCYsiletsleeFERVLDVNVYGAFLGTKHAARVMIP--AKKGSIVSVASVAGVVG----------- 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 158 frsetiteeelvglmnkfvedtkkgvhqkeGWPSSAYGVTKIGVTVLSRIHARKLSEQrkgdRILLNACCPGWVRTDMAG 237
Cdd:cd05326 147 ------------------------------GLGPHAYTASKHAVLGLTRSAATELGEH----GIRVNCVSPYGVATPLLT 192

                       250       260       270
                ....*....|....*....|....*....|....*...
gi 55727312 238 -------------------PKATK-SPEEGAETPVYLA 255
Cdd:cd05326 193 agfgvedeaieeavrgaanLKGTAlRPEDIAAAVLYLA 230
PRK09730 PRK09730
SDR family oxidoreductase;
5-143 1.37e-10

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 60.25  E-value: 1.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    5 MHVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK09730   1 MAIALVTGGSRGIGRATALLLAQEGYTVAVNYQQNLHAAQEVVNLITQAGGKAFVLQADISDENQVVAMFTAIDQHDEPL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55727312   85 DVLVNNAGIAFKVAdpTPFHIQAE---VTMKTNFFGTRDVCTELLPLIKPQ-----GRVVNVSSIMS 143
Cdd:PRK09730  81 AALVNNAGILFTQC--TVENLTAErinRVLSTNVTGYFLCCREAVKRMALKhggsgGAIVNVSSAAS 145
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-93 1.47e-10

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 61.01  E-value: 1.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRlfSGDVVLtARDVARGQAAVQQLqAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK08261 212 VALVTGAARGIGAAIAEVLAR--DGAHVV-CLDVPAAGEALAAV-ANRVGGTALALDITAPDAPARIAEHLAERHGGLDI 287


                 ....*..
gi 55727312   87 LVNNAGI 93
Cdd:PRK08261 288 VVHNAGI 294
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 7-260 1.84e-10

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: 59.51  E-value: 1.84e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRlFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd05365   1 VAIVTGGAAGIGKAIAGTLAK-AGASVVIADLKSEGAEAVAAAIQQAGGQAIGLECNVTSEQDLEAVVKATVSQFGGITI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  87 LVNNAGIAFKVADPTPFHI-QAEVTMKTNFFGtrdvctellplikpqgrvvnvssimSVRALKSCSPELQQKFRSETITE 165
Cdd:cd05365  80 LVNNAGGGGPKPFDMPMTEeDFEWAFKLNLFS-------------------------AFRLSQLCAPHMQKAGGGAILNI 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 166 EELVGlMNKFVEdtkkgvhqkegwpSSAYGVTKIGVTVLSRIHARKLSEqrkgDRILLNACCPGWVRTDMAGPKATKSPE 245
Cdd:cd05365 135 SSMSS-ENKNVR-------------IAAYGSSKAAVNHMTRNLAFDLGP----KGIRVNAVAPGAVKTDALASVLTPEIE 196

                       250
                ....*....|....*..
gi 55727312 246 EG--AETPVYLALLPPD 260
Cdd:cd05365 197 RAmlKHTPLGRLGEPED 213
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-269 2.62e-10

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 59.80  E-value: 2.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    6 HVALVTGGNKGIGLAIVRDLCRLFSGDVVltaRDVARGQAA---VQQLQAEGLSPRFHQLDIDDLQSIRALRDfLRKEYG 82
Cdd:PRK07792  13 KVAVVTGAAAGLGRAEALGLARLGATVVV---NDVASALDAsdvLDEIRAAGAKAVAVAGDISQRATADELVA-TAVGLG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   83 GLDVLVNNAGIafkVADPTPFHIQAE-------VTMKTNFFGTRDVCTELLPLIKPQ-----GRVVNVSSimsvralksc 150
Cdd:PRK07792  89 GLDIVVNNAGI---TRDRMLFNMSDEewdaviaVHLRGHFLLTRNAAAYWRAKAKAAggpvyGRIVNTSS---------- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  151 spelqqkfrsetitEEELVGlmnkfvedtkkgvhqKEGWPSsaYGVTKIGVTVLSRIHARKLSeqRKGDRIllNACCPGw 230
Cdd:PRK07792 156 --------------EAGLVG---------------PVGQAN--YGAAKAGITALTLSAARALG--RYGVRA--NAICPR- 199

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 55727312  231 VRTDM--------AGPKATK----SPEEGAETPVYLAllPPDAEGPHGQ-FV 269
Cdd:PRK07792 200 ARTAMtadvfgdaPDVEAGGidplSPEHVVPLVQFLA--SPAAAEVNGQvFI 249
PRK07832 PRK07832
SDR family oxidoreductase;
8-147 2.79e-10

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 59.29  E-value: 2.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    8 ALVTGGNKGIGLAIVRDLCRlFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQ-LDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK07832   3 CFVTGAASGIGRATALRLAA-QGAELFLTDRDADGLAQTVADARALGGTVPEHRaLDISDYDAVAAFAADIHAAHGSMDV 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55727312   87 LVNNAGIAF--KVADPTpfHIQAEVTMKTNFFGTRDVCTELLPLIKPQGR---VVNVSSIMSVRAL 147
Cdd:PRK07832  82 VMNIAGISAwgTVDRLT--HEQWRRMVDVNLMGPIHVIETFVPPMVAAGRgghLVNVSSAAGLVAL 145
PRK05855 PRK05855
SDR family oxidoreductase;
8-140 2.82e-10

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 60.38  E-value: 2.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    8 ALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVL 87
Cdd:PRK05855 318 VVVTGAGSGIGRETALAFARE-GAEVVASDIDEAAAERTAELIRAAGAVAHAYRVDVSDADAMEAFAEWVRAEHGVPDIV 396

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55727312   88 VNNAGI--AFKVADPTPFHIQAevTMKTNFFGTRDVCTellpLIKPQ-------GRVVNVSS 140
Cdd:PRK05855 397 VNNAGIgmAGGFLDTSAEDWDR--VLDVNLWGVIHGCR----LFGRQmvergtgGHIVNVAS 452
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 1-244 3.32e-10

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 59.16  E-value: 3.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    1 MSSgMHVALVTGGNKGIGLAIVRDLcrLFSGD-VVLTARDvargQAAVQQLqAEGLSPRFH--QLDIDDLQSIRALRDFL 77
Cdd:PRK06180   1 MSS-MKTWLITGVSSGFGRALAQAA--LAAGHrVVGTVRS----EAARADF-EALHPDRALarLLDVTDFDAIDAVVADA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   78 RKEYGGLDVLVNNAGI----AFKVADPTPFHIQAEVtmktNFFGTRDVCTELLPLIKPQ--GRVVNVSSIMSVRALKSCS 151
Cdd:PRK06180  73 EATFGPIDVLVNNAGYghegAIEESPLAEMRRQFEV----NVFGAVAMTKAVLPGMRARrrGHIVNITSMGGLITMPGIG 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  152 PELQQKFRSETITE---EELVGLmnkfvedtkkGVHqkegwpssaygVTkigvtvlsriharklseqrkgdrillnACCP 228
Cdd:PRK06180 149 YYCGSKFALEGISEslaKEVAPF----------GIH-----------VT---------------------------AVEP 180

                        250
                 ....*....|....*.
gi 55727312  229 GWVRTDMAGPKATKSP 244
Cdd:PRK06180 181 GSFRTDWAGRSMVRTP 196
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 8-140 4.67e-10

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: 58.63  E-value: 4.67e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   8 ALVTGGNKGIGLAIVRdlcRLFSGDVVLTARDVArgqaaVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVL 87
Cdd:cd05331   1 VIVTGAAQGIGRAVAR---HLLQAGATVIALDLP-----FVLLLEYGDPLRLTPLDVADAAAVREVCSRLLAEHGPIDAL 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 55727312  88 VNNAGIaFKVADPTPFHIQA-EVTMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSS 140
Cdd:cd05331  73 VNCAGV-LRPGATDPLSTEDwEQTFAVNVTGVFNLLQAVAPHMKDRrtGAIVTVAS 127
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 8-144 4.71e-10

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 58.76  E-value: 4.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    8 ALVTGGNKGIGLAIVRDLCRLfsGDVVLTArdvARGQAAVQQLQAEglsprFHQLDIDDLQSIRALRDFLRKEYGGLDVL 87
Cdd:PRK06523  12 ALVTGGTKGIGAATVARLLEA--GARVVTT---ARSRPDDLPEGVE-----FVAADLTTAEGCAAVARAVLERLGGVDIL 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55727312   88 VNNAG--IAFK--VADPTPFHIQAEvtMKTNFFGTRDVCTELLPLIKPQGR--VVNVSSIMSV 144
Cdd:PRK06523  82 VHVLGgsSAPAggFAALTDEEWQDE--LNLNLLAAVRLDRALLPGMIARGSgvIIHVTSIQRR 142
PRK08267 PRK08267
SDR family oxidoreductase;
5-140 5.25e-10

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 58.41  E-value: 5.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    5 MHVALVTGGNKGIGLAIVRdlcrLFSGD---VVLTARDvargQAAVQQLQAE--GLSPRFHQLDIDDLQSI-RALRDFLR 78
Cdd:PRK08267   1 MKSIFITGAASGIGRATAL----LFAAEgwrVGAYDIN----EAGLAALAAElgAGNAWTGALDVTDRAAWdAALADFAA 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55727312   79 KEYGGLDVLVNNAGI----AFKVADPTPFHIQAEVtmktNFFGTRDVCTELLPLIK--PQGRVVNVSS 140
Cdd:PRK08267  73 ATGGRLDVLFNNAGIlrggPFEDIPLEAHDRVIDI----NVKGVLNGAHAALPYLKatPGARVINTSS 136
PRK06500 PRK06500
SDR family oxidoreductase;
8-255 6.03e-10

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 58.04  E-value: 6.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    8 ALVTGGNKGIGLAIVrdlcRLFSGD---VVLTARDVARGQAAVQQLQAEGLSPRfhqLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK06500   9 ALITGGTSGIGLETA----RQFLAEgarVAITGRDPASLEAARAELGESALVIR---ADAGDVAAQKALAQALAEAFGRL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   85 DVLVNNAGiafkVADPTPFHIQAEV----TMKTNFFGTRDVCTELLPLI-KPQGRVVNVSsiMSVRalkscspelqqkfr 159
Cdd:PRK06500  82 DAVFINAG----VAKFAPLEDWDEAmfdrSFNTNVKGPYFLIQALLPLLaNPASIVLNGS--INAH-------------- 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  160 setiteeelVGLMNkfvedtkkgvhqkegwpSSAYGVTKIGVTVLsrihARKLSEQRKGDRILLNACCPGWVRTDMAG-- 237
Cdd:PRK06500 142 ---------IGMPN-----------------SSVYAASKAALLSL----AKTLSGELLPRGIRVNAVSPGPVQTPLYGkl 191

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 55727312  238 --PKATK-----------------SPEEGAETPVYLA 255
Cdd:PRK06500 192 glPEATLdavaaqiqalvplgrfgTPEEIAKAVLYLA 228
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 7-148 6.09e-10

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: 58.25  E-value: 6.09e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRlfSGDVVLTardVARGQAAVQQLQAE--GLSPRfhQLDIDDLQSIRalrdFLRKEYGGL 84
Cdd:cd05351   9 RALVTGAGKGIGRATVKALAK--AGARVVA---VSRTQADLDSLVREcpGIEPV--CVDLSDWDATE----EALGSVGPV 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55727312  85 DVLVNNAGIA----FKVADPTPFHIQAEVTMKTNFFGTRDVCTELLPLIKPqGRVVNVSSIMSVRALK 148
Cdd:cd05351  78 DLLVNNAAVAilqpFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGVP-GSIVNVSSQASQRALT 144
PRK06940 PRK06940
short chain dehydrogenase; Provisional
 7-270 6.73e-10

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 58.49  E-value: 6.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNkGIGLAIVRdlcRLFSGDVVLTA-RDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRkEYGGLD 85
Cdd:PRK06940   4 VVVVIGAG-GIGQAIAR---RVGAGKKVLLAdYNEENLEAAAKTLREAGFDVSTQEVDVSSRESVKALAATAQ-TLGPVT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   86 VLVNNAGIafkvadpTPFHIQAEVTMKTNFFGTRDVCTELLPLIKPQGRVVNVSSiMSVRALKSCSPELQQKFrsETITE 165
Cdd:PRK06940  79 GLVHTAGV-------SPSQASPEAILKVDLYGTALVLEEFGKVIAPGGAGVVIAS-QSGHRLPALTAEQERAL--ATTPT 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  166 EELVGLMNKFVEDTKKGVHqkegwpssAYGVTKIGVTVlsRIHARKLSEQRKGDRIllNACCPGWVRTDMA-----GPKA 240
Cdd:PRK06940 149 EELLSLPFLQPDAIEDSLH--------AYQIAKRANAL--RVMAEAVKWGERGARI--NSISPGIISTPLAqdelnGPRG 216

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 55727312  241 T-------KSPEEGAETPVYLALLPPDAEGPHGQFVS 270
Cdd:PRK06940 217 DgyrnmfaKSPAGRPGTPDEIAALAEFLMGPRGSFIT 253
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 7-140 9.26e-10

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


Pssm-ID: 187607 [Multi-domain]  Cd Length: 246  Bit Score: 57.47  E-value: 9.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVARGQAAVQQLQAEGLSPRFhqlDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd05349   2 VVLVTGASRGLGAAIARSFAREGARVVVNYYRSTESAEAVAAEAGERAIAIQA---DVRDRDQVQAMIEEAKNHFGPVDT 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55727312  87 LVNNAGIAFKV---ADPTP-------FHIQAEVTMKtnffGTRDVCTELLPLIKPQ--GRVVNVSS 140
Cdd:cd05349  79 IVNNALIDFPFdpdQRKTFdtidwedYQQQLEGAVK----GALNLLQAVLPDFKERgsGRVINIGT 140
PRK07831 PRK07831
SDR family oxidoreductase;
7-149 1.33e-09

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 57.35  E-value: 1.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGG-NKGIGLAIVRDlCRLFSGDVVLTARDVARGQAAVQQLQAE-GLSPRFHQL-DIDDLQSIRALRDFLRKEYGG 83
Cdd:PRK07831  19 VVLVTAAaGTGIGSATARR-ALEEGARVVISDIHERRLGETADELAAElGLGRVEAVVcDVTSEAQVDALIDAAVERLGR 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55727312   84 LDVLVNNAGIA--FKVADPT--PFHIQAEVTMKTNFFGTRdvctELLPLIKPQGR---VVNVSSIMSVRALKS 149
Cdd:PRK07831  98 LDVLVNNAGLGgqTPVVDMTddEWSRVLDVTLTGTFRATR----AALRYMRARGHggvIVNNASVLGWRAQHG 166
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 9-267 1.38e-09

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 57.19  E-value: 1.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    9 LVTGGNKGIGLAIVRDLCRlFSGDVVLTARDVARGQAAVQQLQAEGLS-PRFHQLDID--DLQSIRALRDFLRKEYGGLD 85
Cdd:PRK08945  16 LVTGAGDGIGREAALTYAR-HGATVILLGRTEEKLEAVYDEIEAAGGPqPAIIPLDLLtaTPQNYQQLADTIEEQFGRLD 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   86 VLVNNAGIafkVADPTPF-HIQAEV---TMKTNFFGTRDVCTELLPLIK--PQGRVVNVSSimSVralkscspelqqkfr 159
Cdd:PRK08945  95 GVLHNAGL---LGELGPMeQQDPEVwqdVMQVNVNATFMLTQALLPLLLksPAASLVFTSS--SV--------------- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  160 setiteeelvglmnkfvedtkkGVHQKEGWpsSAYGVTKIGVTVLSRIharkLSEQRKGDRILLNACCPGWVRTDMagpK 239
Cdd:PRK08945 155 ----------------------GRQGRANW--GAYAVSKFATEGMMQV----LADEYQGTNLRVNCINPGGTRTAM---R 203

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 55727312  240 ATKSPEEGAET--------PVYLALLPPDAEGPHGQ 267
Cdd:PRK08945 204 ASAFPGEDPQKlktpedimPLYLYLMGDDSRRKNGQ 239
PRK12743 PRK12743
SDR family oxidoreductase;
7-98 1.47e-09

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 57.35  E-value: 1.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLT-ARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK12743   4 VAIVTASDSGIGKACALLLAQ--QGfDIGITwHSDEEGAKETAEEVRSHGVRAEIRQLDLSDLPEGAQALDKLIQRLGRI 81

                         90
                 ....*....|....
gi 55727312   85 DVLVNNAGIAFKVA 98
Cdd:PRK12743  82 DVLVNNAGAMTKAP 95
PRK06398 PRK06398
aldose dehydrogenase; Validated
 7-151 1.52e-09

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 57.15  E-value: 1.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDvaRGQAAVQqlqaeglsprFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK06398   8 VAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKE--PSYNDVD----------YFKVDVSNKEQVIKGIDYVISKYGRIDI 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55727312   87 LVNNAGI-AFKVADPTPFHIQAEVtMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSIMSVRALKSCS 151
Cdd:PRK06398  76 LVNNAGIeSYGAIHAVEEDEWDRI-INVNVNGIFLMSKYTIPYMLKQdkGVIINIASVQSFAVTRNAA 142
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
7-98 1.68e-09

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 56.96  E-value: 1.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQAEGLSPRfhqLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK07067   8 VALLTGAASGIGEAVAERYLAE-GARVVIADIKPARARLAALEIGPAAIAVS---LDVTRQDSIDRIVAAAVERFGGIDI 83

                         90
                 ....*....|..
gi 55727312   87 LVNNAGIaFKVA 98
Cdd:PRK07067  84 LFNNAAL-FDMA 94
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 10-140 2.20e-09

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


Pssm-ID: 187636 [Multi-domain]  Cd Length: 227  Bit Score: 56.31  E-value: 2.20e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  10 VTGGNKGIGLAIVRDLCR--LFSGdvvltARDV-ARGQAAVQ-QLQAEGLSPrfHQLDIDDLQSIR-ALRDFLRKEYGGL 84
Cdd:cd08931   5 ITGAASGIGRETALLFARngWFVG-----LYDIdEDGLAALAaELGAENVVA--GALDVTDRAAWAaALADFAAATGGRL 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55727312  85 DVLVNNAGIafkvADPTPFHIQ----AEVTMKTNFFGTRDVCTELLPLIK--PQGRVVNVSS 140
Cdd:cd08931  78 DALFNNAGV----GRGGPFEDVplaaHDRMVDINVKGVLNGAYAALPYLKatPGARVINTAS 135
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 7-140 2.61e-09

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 56.43  E-value: 2.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLcrlfsgdvvltardVARGqAAV-----QQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEY 81
Cdd:PRK08220  10 TVWVTGAAQGIGYAVALAF--------------VEAG-AKVigfdqAFLTQEDYPFATFVLDVSDAAAVAQVCQRLLAET 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55727312   82 GGLDVLVNNAGIaFKVADPTPFHIQA-EVTMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSS 140
Cdd:PRK08220  75 GPLDVLVNAAGI-LRMGATDSLSDEDwQQTFAVNAGGAFNLFRAVMPQFRRQrsGAIVTVGS 135
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 7-140 2.98e-09

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 56.17  E-value: 2.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLcrLFSGDVVLTArDVARGQAAVQQLQaeglsprFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK06171  11 IIIVTGGSSGIGLAIVKEL--LANGANVVNA-DIHGGDGQHENYQ-------FVPTDVSSAEEVNHTVAEIIEKFGRIDG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55727312   87 LVNNAGIAFK--VADPTPFHIQAE-----------VTMKTNFFGTRDVCTELLPliKPQGRVVNVSS 140
Cdd:PRK06171  81 LVNNAGINIPrlLVDEKDPAGKYElneaafdkmfnINQKGVFLMSQAVARQMVK--QHDGVIVNMSS 145
PRK08589 PRK08589
SDR family oxidoreductase;
7-146 3.47e-09

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 56.33  E-value: 3.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRlfSGDVVLTArDVARG-QAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK08589   8 VAVITGASTGIGQASAIALAQ--EGAYVLAV-DIAEAvSETVDKIKSNGGKAKAYHVDISDEQQVKDFASEIKEQFGRVD 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55727312   86 VLVNNAGI---AFKVADpTPFHIQAEVtMKTNFFGTRDVCTELLPLIKPQ-GRVVNVSSiMSVRA 146
Cdd:PRK08589  85 VLFNNAGVdnaAGRIHE-YPVDVFDKI-MAVDMRGTFLMTKMLLPLMMEQgGSIINTSS-FSGQA 146
PRK06114 PRK06114
SDR family oxidoreductase;
7-150 3.56e-09

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 55.94  E-value: 3.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAA-VQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK06114  10 VAFVTGAGSGIGQRIAIGLAQA-GADVALFDLRTDDGLAEtAEHIEAAGRRAIQIAADVTSKADLRAAVARTEAELGALT 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   86 VLVNNAGIAFKVADPTPFHIQAEVTMKTNFFGTRDVCTELLPLIKPQGR--VVNVSSIMSV---RALKSC 150
Cdd:PRK06114  89 LAVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGgsIVNIASMSGIivnRGLLQA 158
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-93 4.20e-09

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 55.74  E-value: 4.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK08217   7 VIVITGGAQGLGRAMAEYLAQ--KGaKLALIDLNQEKLEEAVAECGALGTEVRGYAANVTDEEDVEATFAQIAEDFGQLN 84


                 ....*...
gi 55727312   86 VLVNNAGI 93
Cdd:PRK08217  85 GLINNAGI 92
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 7-141 4.47e-09

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: 55.76  E-value: 4.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLtardVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd05371   4 VAVVTGGASGLGLATVERLLAQ-GAKVVI----LDLPNSPGETVAKLGDNCRFVPVDVTSEKDVKAALALAKAKFGRLDI 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  87 LVNNAGIA-------FKVADPTPFHIQAEVtMKTNFFGTRDVCTELLPLI--------KPQGRVVNVSSI 141
Cdd:cd05371  79 VVNCAGIAvaaktynKKGQQPHSLELFQRV-INVNLIGTFNVIRLAAGAMgknepdqgGERGVIINTASV 147
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 7-147 5.03e-09

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 55.68  E-value: 5.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK08277  12 VAVITGGGGVLGGAMAKELAR--AGaKVAILDRNQEKAEAVVAEIKAAGGEALAVKADVLDKESLEQARQQILEDFGPCD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   86 VLVNNAG--IAFKVADPTPFHIQAEVT-------------MKTNFFGTrdvcteLLP--------LIKPQGRVVNVSSIM 142
Cdd:PRK08277  90 ILINGAGgnHPKATTDNEFHELIEPTKtffdldeegfefvFDLNLLGT------LLPtqvfakdmVGRKGGNIINISSMN 163


                 ....*
gi 55727312  143 SVRAL 147
Cdd:PRK08277 164 AFTPL 168
PRK12746 PRK12746
SDR family oxidoreductase;
7-140 5.52e-09

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 55.43  E-value: 5.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEY----- 81
Cdd:PRK12746   8 VALVTGASRGIGRAIAMRLANDGALVAIHYGRNKQAADETIREIESNGGKAFLIEADLNSIDGVKKLVEQLKNELqirvg 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55727312   82 -GGLDVLVNNAGIAFK--VADPTP--FHIQAEVTMKTNFFgtrdVCTELLPLIKPQGRVVNVSS 140
Cdd:PRK12746  88 tSEIDILVNNAGIGTQgtIENTTEeiFDEIMAVNIKAPFF----LIQQTLPLLRAEGRVINISS 147
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 7-144 7.25e-09

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 55.07  E-value: 7.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLFSGDVV--LTARDVARGQAAvqqLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK07097  12 IALITGASYGIGFAIAKAYAKAGATIVFndINQELVDKGLAA---YRELGIEAHGYVCDVTDEDGVQAMVSQIEKEVGVI 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55727312   85 DVLVNNAGI-------AFKVADptpFHIQAEVTMKTNFFGTRDVCTELLPliKPQGRVVNVSSIMSV 144
Cdd:PRK07097  89 DILVNNAGIikripmlEMSAED---FRQVIDIDLNAPFIVSKAVIPSMIK--KGHGKIINICSMMSE 150
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 8-93 8.17e-09

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 55.15  E-value: 8.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    8 ALVTGGNKGIGLAIVRDLCRlFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVL 87
Cdd:PRK08085  12 ILITGSAQGIGFLLATGLAE-YGAEIIINDITAERAELAVAKLRQEGIKAHAAPFNVTHKQEVEAAIEHIEKDIGPIDVL 90


                 ....*.
gi 55727312   88 VNNAGI 93
Cdd:PRK08085  91 INNAGI 96
PRK08177 PRK08177
SDR family oxidoreductase;
5-240 8.97e-09

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 54.65  E-value: 8.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    5 MHVALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVARGQA--AVQQLQAEglsprfhQLDIDDLQSIRALRDFLRKEY 81
Cdd:PRK08177   1 KRTALIIGASRGLGLGLVDRLLE--RGwQVTATVRGPQQDTAlqALPGVHIE-------KLDMNDPASLDQLLQRLQGQR 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   82 ggLDVLVNNAGIAfKVADPTPFHIQAEVTMK---TNFFGTRDVCTELLPLIKP-QGRVVNVSSIM-SVRALKSCSPELQQ 156
Cdd:PRK08177  72 --FDLLFVNAGIS-GPAHQSAADATAAEIGQlflTNAIAPIRLARRLLGQVRPgQGVLAFMSSQLgSVELPDGGEMPLYK 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  157 KFRSetiteeELVGLMNKFVEDtkkgvhqkegwpssaygVTKIGVTVLSrIHarklseqrkgdrillnaccPGWVRTDMA 236
Cdd:PRK08177 149 ASKA------ALNSMTRSFVAE-----------------LGEPTLTVLS-MH-------------------PGWVKTDMG 185


                 ....
gi 55727312  237 GPKA 240
Cdd:PRK08177 186 GDNA 189
PRK06947 PRK06947
SDR family oxidoreductase;
5-143 9.35e-09

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 54.81  E-value: 9.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    5 MHVALVTGGNKGIGLAIVRdLCRLFSGDVVLT-ARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGG 83
Cdd:PRK06947   2 RKVVLITGASRGIGRATAV-LAAARGWSVGINyARDAAAAEETADAVRAAGGRACVVAGDVANEADVIAMFDAVQSAFGR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55727312   84 LDVLVNNAGI---AFKVADPTPFHIQAevTMKTNFFGTRDVCTELLPLIKPQ-----GRVVNVSSIMS 143
Cdd:PRK06947  81 LDALVNNAGIvapSMPLADMDAARLRR--MFDTNVLGAYLCAREAARRLSTDrggrgGAIVNVSSIAS 146
PLN02253 PLN02253
xanthoxin dehydrogenase
 7-144 9.63e-09

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 54.83  E-value: 9.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVArGQAAVQQLQAEGLSPRFHqLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PLN02253  20 VALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDL-GQNVCDSLGGEPNVCFFH-CDVTVEDDVSRAVDFTVDKFGTLDI 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55727312   87 LVNNAGIA------FKVADPTPFHIQAEVTMKTNFFGTRDVCTELLPLIKpqGRVVNVSSIMSV 144
Cdd:PLN02253  98 MVNNAGLTgppcpdIRNVELSEFEKVFDVNVKGVFLGMKHAARIMIPLKK--GSIVSLCSVASA 159
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 7-146 1.01e-08

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: 54.31  E-value: 1.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRdlcrLFSGD---VVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGG 83
Cdd:cd05360   2 VVVITGASSGIGRATAL----AFAERgakVVLAARSAEALHELAREVRELGGEAIAVVADVADAAQVERAADTAVERFGR 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55727312  84 LDVLVNNAGIA-FKVADPTPFHIQAEVtMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSIMSVRA 146
Cdd:cd05360  78 IDTWVNNAGVAvFGRFEDVTPEEFRRV-FDVNYLGHVYGTLAALPHLRRRggGALINVGSLLGYRS 142
PRK07814 PRK07814
SDR family oxidoreductase;
7-275 1.14e-08

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 54.78  E-value: 1.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK07814  12 VAVVTGAGRGLGAAIALAFAEA-GADVLIAARTESQLDEVAEQIRAAGRRAHVVAADLAHPEATAGLAGQAVEAFGRLDI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   87 LVNNAGIAFkvadPTPFHIQAEVTMKTNF-FGT---RDVCTELLPLI---KPQGRVVNVSSIMSVRAlkscspelQQKFr 159
Cdd:PRK07814  91 VVNNVGGTM----PNPLLSTSTKDLADAFtFNVataHALTVAAVPLMlehSGGGSVINISSTMGRLA--------GRGF- 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  160 setiteeelvglmnkfvedtkkgvhqkegwpsSAYGVTKIGVTVLSRIHARKLSEqrkgdRILLNACCPGWVRT------ 233
Cdd:PRK07814 158 --------------------------------AAYGTAKAALAHYTRLAALDLCP-----RIRVNAIAPGSILTsalevv 200

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 55727312  234 ----DMAGPKATKSP-------EEGAETPVYLAllppdaeGPHGQFVSEKRVE 275
Cdd:PRK07814 201 aandELRAPMEKATPlrrlgdpEDIAAAAVYLA-------SPAGSYLTGKTLE 246
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 7-96 1.72e-08

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: 53.82  E-value: 1.72e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVARG-QAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:cd05357   2 VALVTGAAKRIGRAIAEALAA--EGyRVVVHYNRSEAEaQRLKDELNALRNSAVLVQADLSDFAACADLVAAAFRAFGRC 79

                        90
                ....*....|..
gi 55727312  85 DVLVNNAGIAFK 96
Cdd:cd05357  80 DVLVNNASAFYP 91
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 9-103 2.30e-08

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 52.48  E-value: 2.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312      9 LVTGGNKGIGLAIVRDLCRLFSGDVVLTAR--DVARGQAA-VQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGARRLVLLSRsgPDAPGAAAlLAELEAAGARVTVVACDVADRDALAAVLAAIPAVEGPLT 83

                           90
                   ....*....|....*...
gi 55727312     86 VLVNNAGiafkVADPTPF 103
Cdd:smart00822  84 GVIHAAG----VLDDGVL 97
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
7-141 2.71e-08

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 53.48  E-value: 2.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK12938   5 IAYVTGGMGGIGTSICQRLHKDGFKVVAGCGPNSPRRVKWLEDQKALGFDFIASEGNVGDWDSTKAAFDKVKAEVGEIDV 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 55727312   87 LVNNAGIAFKVADPTPFHIQAEVTMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSI 141
Cdd:PRK12938  85 LVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERgwGRIINISSV 141
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-140 3.25e-08

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 53.17  E-value: 3.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLFSGDVVltarDVARGQAAVQQLQAEgLSPRF--HQLDIDDLQSIRALRDFLRKEYG-G 83
Cdd:PRK08642   7 TVLVTGGSRGLGAAIARAFAREGARVVV----NYHQSEDAAEALADE-LGDRAiaLQADVTDREQVQAMFATATEHFGkP 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55727312   84 LDVLVNNAGIAFK---VADPTP-------FHIQAEVTMKtnffGTRDVCTELLPLIKPQ--GRVVNVSS 140
Cdd:PRK08642  82 ITTVVNNALADFSfdgDARKKAdditwedFQQQLEGSVK----GALNTIQAALPGMREQgfGRIINIGT 146
PRK09135 PRK09135
pteridine reductase; Provisional
 7-148 4.14e-08

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 53.01  E-value: 4.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARdvaRGQAAVQQLQAEgL------SPRFHQLDIDDLQSIRALRDFLRK 79
Cdd:PRK09135   8 VALITGGARRIGAAIARTLHA--AGyRVAIHYH---RSAAEADALAAE-LnalrpgSAAALQADLLDPDALPELVAACVA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   80 EYGGLDVLVNNAGIAFkvadPTPFHiqaEVT-------MKTN----FFGTRDVCTELLpliKPQGRVVNVSSIMSVRALK 148
Cdd:PRK09135  82 AFGRLDALVNNASSFY----PTPLG---SITeaqwddlFASNlkapFFLSQAAAPQLR---KQRGAIVNITDIHAERPLK 151
PRK07069 PRK07069
short chain dehydrogenase; Validated
 8-146 4.69e-08

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 52.79  E-value: 4.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    8 ALVTGGNKGIGLAIVRDL----CRLFSGDVVLTArDVARGQAAVQQLQAEGLSPRFhQLDIDDLQSIRALRDFLRKEYGG 83
Cdd:PRK07069   2 AFITGAAGGLGRAIARRMaeqgAKVFLTDINDAA-GLDAFAAEINAAHGEGVAFAA-VQDVTDEAQWQALLAQAADAMGG 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55727312   84 LDVLVNNAGI----AFKVADPTPFHIQAEVTMKTNFFGtrdvCTELLPLIKPQ--GRVVNVSSIMSVRA 146
Cdd:PRK07069  80 LSVLVNNAGVgsfgAIEQIELDEWRRVMAINVESIFLG----CKHALPYLRASqpASIVNISSVAAFKA 144
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 7-141 5.30e-08

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 52.81  E-value: 5.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK08936   9 VVVITGGSTGLGRAMAVRFGKEKAKVVINYRSDEEEANDVAEEIKKAGGEAIAVKGDVTVESDVVNLIQTAVKEFGTLDV 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55727312   87 LVNNAGIafkvADPTPFHiqaEVTMK-------TN----FFGTRDVCTELLPLIKPqGRVVNVSSI 141
Cdd:PRK08936  89 MINNAGI----ENAVPSH---EMSLEdwnkvinTNltgaFLGSREAIKYFVEHDIK-GNIINMSSV 146
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 7-268 5.60e-08

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


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 52.60  E-value: 5.60e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCrLFSGDVVLTARDVARGQAAVQQLQAEGLSPR--FHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:cd09809   3 VIIITGANSGIGFETARSFA-LHGAHVILACRNMSRASAAVSRILEEWHKARveAMTLDLASLRSVQRFAEAFKAKNSPL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  85 DVLVNNAGIafkVADPTPFHIQA-EVTMKTNFFGTRDVCTELLPLIK--PQGRVVNVSSimsvralkscspelqqkfRSE 161
Cdd:cd09809  82 HVLVCNAAV---FALPWTLTEDGlETTFQVNHLGHFYLVQLLEDVLRrsAPARVIVVSS------------------ESH 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 162 TITeeelvglmNKFVEDTKKGVH-----QKEGWPSSAYGVTKIGVTVLSRIHARKLSEQrkgdRILLNACCPG------- 229
Cdd:cd09809 141 RFT--------DLPDSCGNLDFSllsppKKKYWSMLAYNRAKLCNILFSNELHRRLSPR----GITSNSLHPGnmmyssi 208

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 55727312 230 ----WVRT---DMAGPkATKSPEEGAETPVYLALLpPDAEGPHGQF 268
Cdd:cd09809 209 hrnwWVYTllfTLARP-FTKSMQQGAATTVYCATA-PELEGLGGMY 252
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 9-255 7.41e-08

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: 52.11  E-value: 7.41e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   9 LVTGGNKGIGLAIVRDLcrLFSG-DVVLTARDVARGqAAVQQLQAEGLSprfhqLDIDDLQSIRALRDFLRK--EYGGLD 85
Cdd:cd08951  11 FITGSSDGLGLAAARTL--LHQGhEVVLHARSQKRA-ADAKAACPGAAG-----VLIGDLSSLAETRKLADQvnAIGRFD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  86 VLVNNAGIafkvadptpfhIQAEVTMKTNFFGTRDVCTELLP------LIKPQGRVVNVSSIMSVRAlkscspelqqkfr 159
Cdd:cd08951  83 AVIHNAGI-----------LSGPNRKTPDTGIPAMVAVNVLApyvltaLIRRPKRLIYLSSGMHRGG------------- 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 160 setiteEELVGLMNKFvedtkkgvhqKEGWPSS-AYGVTKIGVTVLSRIHARKLSEqrkgdrILLNACCPGWVRTDMAGP 238
Cdd:cd08951 139 ------NASLDDIDWF----------NRGENDSpAYSDSKLHVLTLAAAVARRWKD------VSSNAVHPGWVPTKMGGA 196

                       250
                ....*....|....*..
gi 55727312 239 KATKSPEEGAETPVYLA 255
Cdd:cd08951 197 GAPDDLEQGHLTQVWLA 213
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 7-141 7.68e-08

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 52.25  E-value: 7.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARdvargQAAVQQLQAEGLSPRFHQL----DIDDLQSIRALRDFLRKEYG 82
Cdd:PRK12823  10 VVVVTGAAQGIGRGVALRAAAE-GARVVLVDR-----SELVHEVAAELRAAGGEALaltaDLETYAGAQAAMAAAVEAFG 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55727312   83 GLDVLVNNAG--IAFK-VADPTPFHIQAEVtmKTNFFGTRDVCTELLPLIKPQGR--VVNVSSI 141
Cdd:PRK12823  84 RIDVLINNVGgtIWAKpFEEYEEEQIEAEI--RRSLFPTLWCCRAVLPHMLAQGGgaIVNVSSI 145
PRK07985 PRK07985
SDR family oxidoreductase;
8-260 9.16e-08

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 52.30  E-value: 9.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    8 ALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAA-VQQLQAE-GLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:PRK07985  52 ALVTGGDSGIGRAAAIAYARE-GADVAISYLPVEEEDAQdVKKIIEEcGRKAVLLPGDLSDEKFARSLVHEAHKALGGLD 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   86 VLVNNAGIAFKV---ADPTPFHIQAevTMKTNFFGTRDVCTELLPLIKPQGRVVNVSSIMSVRAlkscSPELQQkfrset 162
Cdd:PRK07985 131 IMALVAGKQVAIpdiADLTSEQFQK--TFAINVFALFWLTQEAIPLLPKGASIITTSSIQAYQP----SPHLLD------ 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  163 iteeelvglmnkfvedtkkgvhqkegwpssaYGVTKIGVTVLSRIHARKLSEqrKGDRILLNACCPGWVRTDMAGPKAT- 241
Cdd:PRK07985 199 -------------------------------YAATKAAILNYSRGLAKQVAE--KGIRVNIVAPGPIWTALQISGGQTQd 245

                        250
                 ....*....|....*....
gi 55727312  242 KSPEEGAETPVYLALLPPD 260
Cdd:PRK07985 246 KIPQFGQQTPMKRAGQPAE 264
PLN00015 PLN00015
protochlorophyllide reductase
 9-141 9.50e-08

protochlorophyllide reductase


Pssm-ID: 177654  Cd Length: 308  Bit Score: 52.02  E-value: 9.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    9 LVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVLV 88
Cdd:PLN00015   1 IITGASSGLGLATAKALAETGKWHVVMACRDFLKAERAAKSAGMPKDSYTVMHLDLASLDSVRQFVDNFRRSGRPLDVLV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 55727312   89 NNAGIAFKVA-DPTPFHIQAEVTMKTNFFGTRDVCTELLPLIK----PQGRVVNVSSI 141
Cdd:PLN00015  81 CNAAVYLPTAkEPTFTADGFELSVGTNHLGHFLLSRLLLDDLKksdyPSKRLIIVGSI 138
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 7-93 9.69e-08

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 51.85  E-value: 9.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGlaivRDLCRLFSGD---VVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGG 83
Cdd:PRK07478   8 VAIITGASSGIG----RAAAKLFAREgakVVVGARRQAELDQLVAEIRAEGGEAVALAGDVRDEAYAKALVALAVERFGG 83

                         90
                 ....*....|
gi 55727312   84 LDVLVNNAGI 93
Cdd:PRK07478  84 LDIAFNNAGT 93
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 7-141 1.03e-07

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 51.89  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLqaeGLSPRFHQL--DIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK05872  11 VVVVTGAARGIGAELARRLHAR-GAKLALVDLEEAELAALAAEL---GGDDRVLTVvaDVTDLAAMQAAAEEAVERFGGI 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55727312   85 DVLVNNAGIA----FKVADPTPFhiqaEVTMKTNFFGTRDVCTELLP-LIKPQGRVVNVSSI 141
Cdd:PRK05872  87 DVVVANAGIAsggsVAQVDPDAF----RRVIDVNLLGVFHTVRATLPaLIERRGYVLQVSSL 144
PRK09186 PRK09186
flagellin modification protein A; Provisional
 7-148 1.46e-07

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 51.14  E-value: 1.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCrLFSGDVVLTARDVARGQAAVQQLQAEGLSPR--FHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK09186   6 TILITGAGGLIGSALVKAIL-EAGGIVIAADIDKEALNELLESLGKEFKSKKlsLVELDITDQESLEEFLSKSAEKYGKI 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55727312   85 DVLVNNA-------GIAFKVADPTPFHIQAEVTMKTNFFGTRDVCTELlpLIKPQGRVVNVSSIMSVRALK 148
Cdd:PRK09186  85 DGAVNCAyprnkdyGKKFFDVSLDDFNENLSLHLGSSFLFSQQFAKYF--KKQGGGNLVNISSIYGVVAPK 153
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 8-144 1.69e-07

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 51.07  E-value: 1.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    8 ALVTGGNKGIGLAIVRDLCRlfSGDVV-LTARDVARGQAAVQQLqaeGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK12936   9 ALVTGASGGIGEEIARLLHA--QGAIVgLHGTRVEKLEALAAEL---GERVKIFPANLSDRDEVKALGQKAEADLEGVDI 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55727312   87 LVNNAGIA-----FKVADPTpFHIQAEVTMKTNFFGTRDVCTellPLIKPQ-GRVVNVSSIMSV 144
Cdd:PRK12936  84 LVNNAGITkdglfVRMSDED-WDSVLEVNLTATFRLTRELTH---PMMRRRyGRIINITSVVGV 143
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
59-141 1.93e-07

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 50.77  E-value: 1.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   59 FHQLDIDDLQSIRALrdfLRKEYGGLDVLVNNAGIAfKVADPtpfhiqaEVTMKTNFFGTRDVCTELLPLIKPQGRVVNV 138
Cdd:PRK12428  27 FIQADLGDPASIDAA---VAALPGRIDALFNIAGVP-GTAPV-------ELVARVNFLGLRHLTEALLPRMAPGGAIVNV 95


                 ...
gi 55727312  139 SSI 141
Cdd:PRK12428  96 ASL 98
PRK06482 PRK06482
SDR family oxidoreductase;
9-140 2.65e-07

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 50.50  E-value: 2.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    9 LVTGGNKGIGLAIVRDLcrLFSGD-VVLTARDVArgqaAVQQLQAE-GLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK06482   6 FITGASSGFGRGMTERL--LARGDrVAATVRRPD----ALDDLKARyGDRLWVLQLDVTDSAAVRAVVDRAFAALGRIDV 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55727312   87 LVNNAGI-----AFKVADPtpfhiQAEVTMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSS 140
Cdd:PRK06482  80 VVSNAGYglfgaAEELSDA-----QIRRQIDTNLIGSIQVIRAALPHLRRQggGRIVQVSS 135
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 8-141 3.33e-07

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


Pssm-ID: 187614 [Multi-domain]  Cd Length: 239  Bit Score: 49.91  E-value: 3.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   8 ALVTGGNKGIGLAIVRDLCRlfSG-DVVLtardVARGQAAVQQLQAE-----GLSPRFHQLDIDDLQSIralRDFLRKEY 81
Cdd:cd05356   4 AVVTGATDGIGKAYAEELAK--RGfNVIL----ISRTQEKLDAVAKEieekyGVETKTIAADFSAGDDI---YERIEKEL 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55727312  82 GGLDV--LVNNAGIAFKVadPTPFHiqaEV-------TMKTNFFGTRDVCTELLPLIKPQGR--VVNVSSI 141
Cdd:cd05356  75 EGLDIgiLVNNVGISHSI--PEYFL---ETpedelqdIINVNVMATLKMTRLILPGMVKRKKgaIVNISSF 140
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 7-152 3.56e-07

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


Pssm-ID: 187641 [Multi-domain]  Cd Length: 256  Bit Score: 50.23  E-value: 3.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd08936  12 VALVTASTDGIGLAIARRLAQD-GAHVVVSSRKQQNVDRAVATLQGEGLSVTGTVCHVGKAEDRERLVATAVNLHGGVDI 90

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55727312  87 LVNNAGI---AFKVADPTP--FHIQAEVTMKTNFFGTRDVCTELLPliKPQGRVVNVSSIMSVRALKSCSP 152
Cdd:cd08936  91 LVSNAAVnpfFGNILDSTEevWDKILDVNVKATALMTKAVVPEMEK--RGGGSVVIVSSVAAFHPFPGLGP 159
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 7-91 4.65e-07

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


Pssm-ID: 187664 [Multi-domain]  Cd Length: 265  Bit Score: 49.75  E-value: 4.65e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRlfSGDVV-LTARDVARGQAAV-QQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGG- 83
Cdd:cd09763   5 IALVTGASRGIGRGIALQLGE--AGATVyITGRTILPQLPGTaEEIEARGGKCIPVRCDHSDDDEVEALFERVAREQQGr 82


                ....*...
gi 55727312  84 LDVLVNNA 91
Cdd:cd09763  83 LDILVNNA 90
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 7-140 5.00e-07

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 49.76  E-value: 5.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRlfSGDVVLTArdvARGQAAVQQLQAEgLSPRFH--QLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK10538   2 IVLVTGATAGFGECITRRFIQ--QGHKVIAT---GRRQERLQELKDE-LGDNLYiaQLDVRNRAAIEEMLASLPAEWRNI 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55727312   85 DVLVNNAGIAFKVadpTPFHiQAEV----TM-KTNFFGTRDVCTELLP--LIKPQGRVVNVSS 140
Cdd:PRK10538  76 DVLVNNAGLALGL---EPAH-KASVedweTMiDTNNKGLVYMTRAVLPgmVERNHGHIINIGS 134
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
9-141 6.37e-07

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 49.59  E-value: 6.37e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   9 LVTGGNKGIGLAIVRDLCRLfsG-DVVLTARDVARGQAAVQQLQAEglsprFHQLDIDDLQSI-RALRDFlrkeygglDV 86
Cdd:COG0451   3 LVTGGAGFIGSHLARRLLAR--GhEVVGLDRSPPGAANLAALPGVE-----FVRGDLRDPEALaAALAGV--------DA 67

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 55727312  87 LVNNAGIA-FKVADPtpfhiqaEVTMKTNFFGTRDVCTELLPliKPQGRVVNVSSI 141
Cdd:COG0451  68 VVHLAAPAgVGEEDP-------DETLEVNVEGTLNLLEAARA--AGVKRFVYASSS 114
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 3-139 8.27e-07

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 49.18  E-value: 8.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    3 SGMHVaLVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYG 82
Cdd:PRK07576   8 AGKNV-VVVGGTSGINLGIAQAFARA-GANVAVASRSQEKVDAAVAQLQQAGPEGLGVSADVRDYAAVEAAFAQIADEFG 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55727312   83 GLDVLVNNAGIAFkvadPTPfhiqaEVTMKTNFF---------GTRDVCTELLPLI-KPQGRVVNVS 139
Cdd:PRK07576  86 PIDVLVSGAAGNF----PAP-----AAGMSANGFktvvdidllGTFNVLKAAYPLLrRPGASIIQIS 143
PRK06123 PRK06123
SDR family oxidoreductase;
7-143 8.44e-07

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 49.01  E-value: 8.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK06123   4 VMIITGASRGIGAATALLAAERGYAVCLNYLRNRDAAEAVVQAIRRQGGEALAVAADVADEADVLRLFEAVDRELGRLDA 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55727312   87 LVNNAGI---AFKVADPTPFHIQAevTMKTNFFGTRDVCTELLPLIKPQ-----GRVVNVSSIMS 143
Cdd:PRK06123  84 LVNNAGIleaQMRLEQMDAARLTR--IFATNVVGSFLCAREAVKRMSTRhggrgGAIVNVSSMAA 146
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 6-141 8.97e-07

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 49.07  E-value: 8.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    6 HVALVTGGNKGIGLAIVRDLCRLFSGDVVL-----TARDVArgqAAVQQL--QAEGLSprfhqLDIDDLQSIRALRDFLR 78
Cdd:PRK06113  12 KCAIITGAGAGIGKEIAITFATAGASVVVSdinadAANHVV---DEIQQLggQAFACR-----CDITSEQELSALADFAL 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55727312   79 KEYGGLDVLVNNAGiafkVADPTPFHIQAEV---TMKTNFFGTRDVCTELLPLIKPQ--GRVVNVSSI 141
Cdd:PRK06113  84 SKLGKVDILVNNAG----GGGPKPFDMPMADfrrAYELNVFSFFHLSQLVAPEMEKNggGVILTITSM 147
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
7-264 8.98e-07

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 48.75  E-value: 8.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLfSGDVVltarDVARGQAAVQQLQAEGLSPRFHQL--DIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK12481  10 VAIITGCNTGLGQGMAIGLAKA-GADIV----GVGVAEAPETQAQVEALGRKFHFItaDLIQQKDIDSIVSQAVEVMGHI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   85 DVLVNNAGIaFKVADPTPFHIQ-----AEVTMKTNFFGTRDVCTEllpLIKPQ--GRVVNVSSIMSVRAlkscspelqqk 157
Cdd:PRK12481  85 DILINNAGI-IRRQDLLEFGNKdwddvININQKTVFFLSQAVAKQ---FVKQGngGKIINIASMLSFQG----------- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  158 frsetiteeelvglmnkfvedtkkgvhqkeGWPSSAYGVTKIGVTVLSRIHARKLSEQrkgdRILLNACCPGWVRTD-MA 236
Cdd:PRK12481 150 ------------------------------GIRVPSYTASKSAVMGLTRALATELSQY----NINVNAIAPGYMATDnTA 195

                        250       260       270
                 ....*....|....*....|....*....|
gi 55727312  237 GPKATKSPEEG--AETPVYLALLPPDAEGP 264
Cdd:PRK12481 196 ALRADTARNEAilERIPASRWGTPDDLAGP 225
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 7-93 1.00e-06

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 48.90  E-value: 1.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLA------------IVRDLCRLFSGdvvlTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALR 74
Cdd:PRK07791   8 VVIVTGAGGGIGRAhalafaaegarvVVNDIGVGLDG----SASGGSAAQAVVDEIVAAGGEAVANGDDIADWDGAANLV 83

                         90
                 ....*....|....*....
gi 55727312   75 DFLRKEYGGLDVLVNNAGI 93
Cdd:PRK07791  84 DAAVETFGGLDVLVNNAGI 102
PRK12742 PRK12742
SDR family oxidoreductase;
8-270 1.04e-06

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 48.60  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    8 ALVTGGNKGIGLAIVRdlcRLFS--GDVVLTardVARGQAAVQQLQAEGLSPRFhQLDIDDlqsIRALRDFLRkEYGGLD 85
Cdd:PRK12742   9 VLVLGGSRGIGAAIVR---RFVTdgANVRFT---YAGSKDAAERLAQETGATAV-QTDSAD---RDAVIDVVR-KSGALD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   86 VLVNNAGIA----------------FKVADPTPFHIQAEVTMKtnffgtrdvctellplIKPQGRVVNVSSIMSVRAlks 149
Cdd:PRK12742  78 ILVVNAGIAvfgdaleldaddidrlFKINIHAPYHASVEAARQ----------------MPEGGRIIIIGSVNGDRM--- 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  150 cspelqqkfrsetiteeELVGLmnkfvedtkkgvhqkegwpsSAYGVTKIGVTVLSRIHARKLseqrkGDR-ILLNACCP 228
Cdd:PRK12742 139 -----------------PVAGM--------------------AAYAASKSALQGMARGLARDF-----GPRgITINVVQP 176

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 55727312  229 GWVRTD-----------MAGPKATK---SPEEGAETPVYLAllppdaeGPHGQFVS 270
Cdd:PRK12742 177 GPIDTDanpangpmkdmMHSFMAIKrhgRPEEVAGMVAWLA-------GPEASFVT 225
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 7-91 1.56e-06

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 48.14  E-value: 1.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK07677   3 VVIITGGSSGMGKAMAKRFAEE-GANVVITGRTKEKLEEAKLEIEQFPGQVLTVQMDVRNPEDVQKMVEQIDEKFGRIDA 81


                 ....*
gi 55727312   87 LVNNA 91
Cdd:PRK07677  82 LINNA 86
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 7-255 1.85e-06

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


Pssm-ID: 187626 [Multi-domain]  Cd Length: 241  Bit Score: 47.85  E-value: 1.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRlfSGDVVLtARDVarGQAAVQQLQAEGLSPRfHQLDIDDLQSIRALRdflrKEYGGLDV 86
Cdd:cd05368   4 VALITAAAQGIGRAIALAFAR--EGANVI-ATDI--NEEKLKELERGPGITT-RVLDVTDKEQVAALA----KEEGRIDV 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  87 LVNNAGIAF--KVADPTP----FHIqaEVTMKTNFFGTRDVCTELLPliKPQGRVVNVSSIMSvralkscspelqqkfrs 160
Cdd:cd05368  74 LFNCAGFVHhgSILDCEDddwdFAM--NLNVRSMYLMIKAVLPKMLA--RKDGSIINMSSVAS----------------- 132

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 161 etiteeELVGLMNKFVedtkkgvhqkegwpssaYGVTKIGVTVLSRIHARKLSEQrkGDRIllNACCPGWVRT------- 233
Cdd:cd05368 133 ------SIKGVPNRFV-----------------YSTTKAAVIGLTKSVAADFAQQ--GIRC--NAICPGTVDTpsleeri 185

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 55727312 234 -----------DMAGPKATK---SPEEGAETPVYLA 255
Cdd:cd05368 186 qaqpdpeealkAFAARQPLGrlaTPEEVAALAVYLA 221
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
5-93 5.39e-06

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 46.60  E-value: 5.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    5 MHVALVTGGNKGIGLAIVRDLcrLFSGDVVLTardVARGQAAVQQLQAEGLSPR--FHQLDIDDLQSI-RALRDFLR--- 78
Cdd:PRK06924   1 MRYVIITGTSQGLGEAIANQL--LEKGTHVIS---ISRTENKELTKLAEQYNSNltFHSLDLQDVHELeTNFNEILSsiq 75

                         90
                 ....*....|....*.
gi 55727312   79 -KEYGGLdVLVNNAGI 93
Cdd:PRK06924  76 eDNVSSI-HLINNAGM 90
PRK05717 PRK05717
SDR family oxidoreductase;
7-231 5.69e-06

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 46.42  E-value: 5.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLcrLFSG-DVVLTARDVARGQAAVQQLqaeGLSPRFHQLDI-DDLQSIRALRDFLRkEYGGL 84
Cdd:PRK05717  12 VALVTGAARGIGLGIAAWL--IAEGwQVVLADLDRERGSKVAKAL---GENAWFIAMDVaDEAQVAAGVAEVLG-QFGRL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   85 DVLVNNAGIafkvADPtpfhiqaevtmktnffgtRDVCTELLPLiKPQGRVVNVSSIMSVRALKSCSPELQqkfrsetit 164
Cdd:PRK05717  86 DALVCNAAI----ADP------------------HNTTLESLSL-AHWNRVLAVNLTGPMLLAKHCAPYLR--------- 133

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55727312  165 eeelvGLMNKFVEDTKKGVHQKEGwPSSAYGVTKIGVTVLSriHARKLSeqrKGDRILLNACCPGWV 231
Cdd:PRK05717 134 -----AHNGAIVNLASTRARQSEP-DTEAYAASKGGLLALT--HALAIS---LGPEIRVNAVSPGWI 189
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 9-144 7.60e-06

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. 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: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 46.61  E-value: 7.60e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   9 LVTGGNKGIGLAIVRDLCRLFSGDVVLTARDV--ARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEyGGLDV 86
Cdd:cd05274 154 LITGGLGGLGLLVARWLAARGARHLVLLSRRGpaPRAAARAALLRAGGARVSVVRCDVTDPAALAALLAELAAG-GPLAG 232

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  87 LVNNAGIAFK--VADPTPFHIQAEVTMKTNffGTRDVCtELLPLiKPQGRVVNVSSIMSV 144
Cdd:cd05274 233 VIHAAGVLRDalLAELTPAAFAAVLAAKVA--GALNLH-ELTPD-LPLDFFVLFSSVAAL 288
PRK06194 PRK06194
hypothetical protein; Provisional
 7-94 8.06e-06

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 46.16  E-value: 8.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTarDVARG--QAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK06194   8 VAVITGAASGFGLAFARIGAAL-GMKLVLA--DVQQDalDRAVAELRAQGAEVLGVRTDVSDAAQVEALADAALERFGAV 84

                         90
                 ....*....|
gi 55727312   85 DVLVNNAGIA 94
Cdd:PRK06194  85 HLLFNNAGVG 94
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 6-99 9.09e-06

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 46.83  E-value: 9.09e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   6 HVALVTGGNKGIGLAIVRdlcRLFS--GDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDID--DLQSIRALRDFLRKEY 81
Cdd:COG3347 426 RVALVTGGAGGIGRATAA---RLAAegAAVVVADLDGEAAEAAAAELGGGYGADAVDATDVDvtAEAAVAAAFGFAGLDI 502

                        90
                ....*....|....*...
gi 55727312  82 GGLDVLVNNAGIAFKVAD 99
Cdd:COG3347 503 GGSDIGVANAGIASSSPE 520
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 8-235 9.44e-06

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 46.10  E-value: 9.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    8 ALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVL 87
Cdd:PRK05876   9 AVITGGASGIGLATGTEFARR-GARVVLGDVDKPGLRQAVNHLRAEGFDVHGVMCDVRHREEVTHLADEAFRLLGHVDVV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   88 VNNAGI--AFKVADPTpfHIQAEVTMKTNFFGTRDVCTELLPLIKPQGRVVNVSSIMSVRALkscspelqqkfrsetite 165
Cdd:PRK05876  88 FSNAGIvvGGPIVEMT--HDDWRWVIDVDLWGSIHTVEAFLPRLLEQGTGGHVVFTASFAGL------------------ 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  166 eelvglmnkfVEDTKKGvhqkegwpssAYGVTKIGVTVLsrihARKLSEQRKGDRILLNACCPGWVRTDM 235
Cdd:PRK05876 148 ----------VPNAGLG----------AYGVAKYGVVGL----AETLAREVTADGIGVSVLCPMVVETNL 193
PRK08278 PRK08278
SDR family oxidoreductase;
8-92 1.21e-05

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 45.66  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    8 ALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARdVARGQA--------AVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLR 78
Cdd:PRK08278   9 LFITGASRGIGLAIALRAAR--DGaNIVIAAK-TAEPHPklpgtihtAAEEIEAAGGQALPLVGDVRDEDQVAAAVAKAV 85

                         90
                 ....*....|....
gi 55727312   79 KEYGGLDVLVNNAG 92
Cdd:PRK08278  86 ERFGGIDICVNNAS 99
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 7-235 1.22e-05

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 45.45  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGG--- 83
Cdd:PRK12747   6 VALVTGASRGIGRAIAKRLANDGALVAIHYGNRKEEAEETVYEIQSNGGSAFSIGANLESLHGVEALYSSLDNELQNrtg 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   84 ---LDVLVNNAGI---AFkVADPTP--FHIQAEVTMKTNFFgtrdVCTELLPLIKPQGRVVNVSSIMSVRALKScspelq 155
Cdd:PRK12747  86 stkFDILINNAGIgpgAF-IEETTEqfFDRMVSVNAKAPFF----IIQQALSRLRDNSRIINISSAATRISLPD------ 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  156 qkfrsetiteeelvglmnkFVedtkkgvhqkegwpssAYGVTKIGVTVLSRIHARKLSEQrkgdRILLNACCPGWVRTDM 235
Cdd:PRK12747 155 -------------------FI----------------AYSMTKGAINTMTFTLAKQLGAR----GITVNAILPGFIKTDM 195
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
 8-211 1.22e-05

NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 45.37  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312     8 ALVTGGNKGIGLAIVRdlcRLFSGDVVLTARDvaRGQAAVQQLQAEGLspRFHQLDIDDlqsIRALRDFLRKEygGLDVL 87
Cdd:pfam01370   1 ILVTGATGFIGSHLVR---RLLEKGYEVIGLD--RLTSASNTARLADL--RFVEGDLTD---RDALEKLLADV--RPDAV 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    88 VNNAGIAFKVADptpfHIQAEVTMKTNFFGTRDVCTELLplIKPQGRVVNVSSimsvralkSCS-PELQQKFRSETITEE 166
Cdd:pfam01370  69 IHLAAVGGVGAS----IEDPEDFIEANVLGTLNLLEAAR--KAGVKRFLFASS--------SEVyGDGAEIPQEETTLTG 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 55727312   167 ELVglmnkfvedtkkgvhqkegwPSSAYGVTKIGVTVLSRIHARK 211
Cdd:pfam01370 135 PLA--------------------PNSPYAAAKLAGEWLVLAYAAA 159
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 9-258 1.36e-05

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 45.56  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    9 LVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQAEGL--SPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK05875  11 LVTGGGSGIGKGVAAGLVAA-GAAVMIVGRNPDKLAAAAEEIEALKGagAVRYEPADVTDEDQVARAVDAATAWHGRLHG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   87 LVNNAGIAFKVADPTPFHIQA-EVTMKTNFFGTrdvctelLPLIKPQGR---------VVNVSSIMSvralkscspelqq 156
Cdd:PRK05875  90 VVHCAGGSETIGPITQIDSDAwRRTVDLNVNGT-------MYVLKHAARelvrggggsFVGISSIAA------------- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  157 kfrSETiteeelvglmnkfvedtkkgvHQKEGwpssAYGVTKIGVTVLSRIHARKLSEQrkgdRILLNACCPGWVRTDMA 236
Cdd:PRK05875 150 ---SNT---------------------HRWFG----AYGVTKSAVDHLMKLAADELGPS----WVRVNSIRPGLIRTDLV 197

                        250       260
                 ....*....|....*....|..
gi 55727312  237 GPkATKSPEEGAEtpvYLALLP 258
Cdd:PRK05875 198 AP-ITESPELSAD---YRACTP 215
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 9-93 1.38e-05

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


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 44.48  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312     9 LVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVA---RGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:pfam08659   4 LITGGLGGLGRELARWLAERGARHLVLLSRSAAprpDAQALIAELEARGVEVVVVACDVSDPDAVAALLAEIKAEGPPIR 83


                  ....*...
gi 55727312    86 VLVNNAGI 93
Cdd:pfam08659  84 GVIHAAGV 91
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 7-152 1.46e-05

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: 45.20  E-value: 1.46e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCR----LFSGDVVLTARDVARGQAAVQQLQAEGLSPRfhqLDIDDLQSIRALRDFLRKEYG 82
Cdd:cd05330   5 VVLITGGGSGLGLATAVRLAKegakLSLVDLNEEGLEAAKAALLEIAPDAEVLLIK---ADVSDEAQVEAYVDATVEQFG 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55727312  83 GLDVLVNNAGIAFKVA-----DPTPFHIQAEVTMKTNFFGTRDVctelLPLIKPQ--GRVVNVSSIMSVRALKSCSP 152
Cdd:cd05330  82 RIDGFFNNAGIEGKQNltedfGADEFDKVVSINLRGVFYGLEKV----LKVMREQgsGMIVNTASVGGIRGVGNQSG 154
PRK07775 PRK07775
SDR family oxidoreductase;
8-145 1.81e-05

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 45.13  E-value: 1.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    8 ALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVL 87
Cdd:PRK07775  13 ALVAGASSGIGAATAIELAAA-GFPVALGARRVEKCEELVDKIRADGGEAVAFPLDVTDPDSVKSFVAQAEEALGEIEVL 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55727312   88 VNNAG-IAFKVA---DPTPFHIQAEVtmktNFFGTRDVCTELLP--LIKPQGRVVNVSSIMSVR 145
Cdd:PRK07775  92 VSGAGdTYFGKLheiSTEQFESQVQI----HLVGANRLATAVLPgmIERRRGDLIFVGSDVALR 151
PRK09134 PRK09134
SDR family oxidoreductase;
1-93 2.64e-05

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 44.53  E-value: 2.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    1 MSSGMHVALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARD-VARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLR 78
Cdd:PRK09134   5 SMAAPRAALVTGAARRIGRAIALDLAA--HGfDVAVHYNRsRDEAEALAAEIRALGRRAVALQADLADEAEVRALVARAS 82

                         90
                 ....*....|....*
gi 55727312   79 KEYGGLDVLVNNAGI 93
Cdd:PRK09134  83 AALGPITLLVNNASL 97
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 7-146 2.70e-05

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


Pssm-ID: 187631 [Multi-domain]  Cd Length: 238  Bit Score: 44.30  E-value: 2.70e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVAR-GQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:cd05373   1 VAAVVGAGDGLGAAIARRFAA--EGfSVALAARREAKlEALLVDIIRDAGGSAKAVPTDARDEDEVIALFDLIEEEIGPL 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55727312  85 DVLVNNAG--IAFKVADPTP--FHIQAEVTMKTNFFGTRDVCTELLPliKPQGRVVNVSSIMSVRA 146
Cdd:cd05373  79 EVLVYNAGanVWFPILETTPrvFEKVWEMAAFGGFLAAREAAKRMLA--RGRGTIIFTGATASLRG 142
PRK07577 PRK07577
SDR family oxidoreductase;
8-140 3.72e-05

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 43.95  E-value: 3.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    8 ALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVargqaavqqlqAEGLSPRFHQLDIDDL-QSIRALRDFLrkEYGGLDV 86
Cdd:PRK07577   6 VLVTGATKGIGLALSLRLANL-GHQVIGIARSA-----------IDDFPGELFACDLADIeQTAATLAQIN--EIHPVDA 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55727312   87 LVNNAGIAFkvadPTPF------HIQAevTMKTNFFGTRDVCTELLP--LIKPQGRVVNVSS 140
Cdd:PRK07577  72 IVNNVGIAL----PQPLgkidlaALQD--VYDLNVRAAVQVTQAFLEgmKLREQGRIVNICS 127
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
7-143 4.90e-05

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 43.71  E-value: 4.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVltARDVARGQAAVQQLQAEG---LSPRFHQLDIDDLQSI--RALrdflrKE 80
Cdd:PRK08993  12 VAVVTGCDTGLGQGMALGLAE--AGcDIV--GINIVEPTETIEQVTALGrrfLSLTADLRKIDGIPALleRAV-----AE 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55727312   81 YGGLDVLVNNAGIaFKVADPTPFHIQ-----AEVTMKTNFFGTRDVCTELLPLIKpQGRVVNVSSIMS 143
Cdd:PRK08993  83 FGHIDILVNNAGL-IRREDAIEFSEKdwddvMNLNIKSVFFMSQAAAKHFIAQGN-GGKIINIASMLS 148
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 7-93 5.51e-05

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 43.41  E-value: 5.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRdlcrlfsgdvvltaRDVARG-QAAVQQLQAEGLSPRFHQL---------DIDDLQSIRALRDF 76
Cdd:PRK06200   8 VALITGGGSGIGRALVE--------------RFLAEGaRVAVLERSAEKLASLRQRFgdhvlvvegDVTSYADNQRAVDQ 73

                         90
                 ....*....|....*..
gi 55727312   77 LRKEYGGLDVLVNNAGI 93
Cdd:PRK06200  74 TVDAFGKLDCFVGNAGI 90
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 7-140 5.51e-05

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


Pssm-ID: 187611 [Multi-domain]  Cd Length: 250  Bit Score: 43.46  E-value: 5.51e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLA------------IVRDLcrlfSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSI--RA 72
Cdd:cd05353   7 VVLVTGAGGGLGRAyalafaergakvVVNDL----GGDRKGSGKSSSAADKVVDEIKAAGGKAVANYDSVEDGEKIvkTA 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55727312  73 LrdflrKEYGGLDVLVNNAGI----AFKVADPTPFHIQAEVTMKTNFFGTRDVctelLPLIKPQ--GRVVNVSS 140
Cdd:cd05353  83 I-----DAFGRVDILVNNAGIlrdrSFAKMSEEDWDLVMRVHLKGSFKVTRAA----WPYMRKQkfGRIINTSS 147
PRK07102 PRK07102
SDR family oxidoreductase;
9-141 5.82e-05

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 43.37  E-value: 5.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    9 LVTGGNKGIGLAIVRdlcrLFSG---DVVLTARDVARGQAAVQQLQAEG-LSPRFHQLDIDDLQSIRALrdflrkeYGGL 84
Cdd:PRK07102   5 LIIGATSDIARACAR----RYAAagaRLYLAARDVERLERLADDLRARGaVAVSTHELDILDTASHAAF-------LDSL 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55727312   85 DVLVNNAGIAF------KVADPTPFHIQAEvtMKTNFFGTRDVCTELLPLIKPQGR--VVNVSSI 141
Cdd:PRK07102  74 PALPDIVLIAVgtlgdqAACEADPALALRE--FRTNFEGPIALLTLLANRFEARGSgtIVGISSV 136
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 8-266 7.49e-05

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


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 42.89  E-value: 7.49e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   8 ALVTGGNKGIGLAIVRDLcRLFSGDVVLTARDvargQAAVQQLqAEGLSPRFHQLDIDDLQSIRALRdflrKEYGGLDVL 87
Cdd:cd11730   1 ALILGATGGIGRALARAL-AGRGWRLLLSGRD----AGALAGL-AAEVGALARPADVAAELEVWALA----QELGPLDLL 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  88 VNNAGIAFK--VADPTPfhIQAEVTMKTNFFGTRDVCTELLPLIKPQGRVVNVSSimsvralkscspelqqkfRSETITe 165
Cdd:cd11730  71 VYAAGAILGkpLARTKP--AAWRRILDANLTGAALVLKHALALLAAGARLVFLGA------------------YPELVM- 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312 166 eeLVGLmnkfvedtkkgvhqkegwpsSAYGVTKIGVTVLSRIhARKlsEQRkGDRILLnaCCPGWVRTDM-----AGPKA 240
Cdd:cd11730 130 --LPGL--------------------SAYAAAKAALEAYVEV-ARK--EVR-GLRLTL--VRPPAVDTGLwappgRLPKG 181

                       250       260
                ....*....|....*....|....*.
gi 55727312 241 TKSPEEGAEtpvylALLPPDAEGPHG 266
Cdd:cd11730 182 ALSPEDVAA-----AILEAHQGEPQG 202
PRK05867 PRK05867
SDR family oxidoreductase;
8-238 1.12e-04

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 42.71  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    8 ALVTGGNKGIGLAIVrdLCRLFSG-DVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK05867  12 ALITGASTGIGKRVA--LAYVEAGaQVAIAARHLDALEKLADEIGTSGGKVVPVCCDVSQHQQVTSMLDQVTAELGGIDI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   87 LVNNAGIafkvadptpFHIQAEVTMktnffgtrdvctellPLIKPQgRV--VNVSSIMsVRALKSCSPELQQKFRSETIT 164
Cdd:PRK05867  90 AVCNAGI---------ITVTPMLDM---------------PLEEFQ-RLqnTNVTGVF-LTAQAAAKAMVKQGQGGVIIN 143

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55727312  165 EEELVG-LMNkfvedtkkgVHQKEGwpssAYGVTKIGVTVLSRIHARKLSEQrkgdRILLNACCPGWVRTDMAGP 238
Cdd:PRK05867 144 TASMSGhIIN---------VPQQVS----HYCASKAAVIHLTKAMAVELAPH----KIRVNSVSPGYILTELVEP 201
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
47-145 1.78e-04

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


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 42.04  E-value: 1.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   47 VQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVLVNNAGIAFKVADPTPF-HIQAE---VTMKTNFFGTRDVC 122
Cdd:PRK08415  47 VEPIAQELGSDYVYELDVSKPEHFKSLAESLKKDLGKIDFIVHSVAFAPKEALEGSFlETSKEafnIAMEISVYSLIELT 126

                         90       100
                 ....*....|....*....|...
gi 55727312  123 TELLPLIKPQGRVVNVSSIMSVR 145
Cdd:PRK08415 127 RALLPLLNDGASVLTLSYLGGVK 149
PRK09009 PRK09009
SDR family oxidoreductase;
5-93 2.40e-04

SDR family oxidoreductase;


Pssm-ID: 181609 [Multi-domain]  Cd Length: 235  Bit Score: 41.59  E-value: 2.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    5 MHVaLVTGGNKGIGLAIVRDLCRLFSGdvvltARDVARGQAAVQQLQAEGLSprFHQLDIDDLQSIRAlrdfLRKEYGGL 84
Cdd:PRK09009   1 MNI-LIVGGSGGIGKAMVKQLLERYPD-----ATVHATYRHHKPDFQHDNVQ--WHALDVTDEAEIKQ----LSEQFTQL 68


                 ....*....
gi 55727312   85 DVLVNNAGI 93
Cdd:PRK09009  69 DWLINCVGM 77
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 8-151 2.55e-04

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


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 41.03  E-value: 2.55e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   8 ALVTGGNKGIGLAIVRDLCRlfSGDVVLTArdvargqaavqqlqaeGLSPRFHQLDIDDLQSIRALrdFlrKEYGGLDVL 87
Cdd:cd11731   1 IIVIGATGTIGLAVAQLLSA--HGHEVITA----------------GRSSGDYQVDITDEASIKAL--F--EKVGHFDAI 58

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55727312  88 VNNAGIAFKV--ADPTPfhIQAEVTMKTNFFGTRDVCTELLPLIKPQGRVVNVSSIMSVRALKSCS 151
Cdd:cd11731  59 VSTAGDAEFAplAELTD--ADFQRGLNSKLLGQINLVRHGLPYLNDGGSITLTSGILAQRPIPGGA 122
PRK12744 PRK12744
SDR family oxidoreductase;
7-137 2.89e-04

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 41.26  E-value: 2.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLFSGDVVL---TARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGG 83
Cdd:PRK12744  10 VVLIAGGAKNLGGLIARDLAAQGAKAVAIhynSAASKADAEETVAAVKAAGAKAVAFQADLTTAAAVEKLFDDAKAAFGR 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   84 LDVLVNNAGIAFKvaDPTPFHIQAE------VTMKTNFFgtrdvctellpLIKPQGRVVN 137
Cdd:PRK12744  90 PDIAINTVGKVLK--KPIVEISEAEydemfaVNSKSAFF-----------FIKEAGRHLN 136
PRK08251 PRK08251
SDR family oxidoreductase;
9-147 4.88e-04

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 40.69  E-value: 4.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    9 LVTGGNKGIGlaivRDLCRLFSG---DVVLTARDVARGQAAVQQLQAE--GLSPRFHQLDIDDLQSIRALRDFLRKEYGG 83
Cdd:PRK08251   6 LITGASSGLG----AGMAREFAAkgrDLALCARRTDRLEELKAELLARypGIKVAVAALDVNDHDQVFEVFAEFRDELGG 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55727312   84 LDVLVNNAGIAfKVADPTPFHIQA-EVTMKTNFFGTRDVCTELLPLIKPQGR--VVNVSSIMSVRAL 147
Cdd:PRK08251  82 LDRVIVNAGIG-KGARLGTGKFWAnKATAETNFVAALAQCEAAMEIFREQGSghLVLISSVSAVRGL 147
PRK07041 PRK07041
SDR family oxidoreductase;
9-151 8.22e-04

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 40.02  E-value: 8.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    9 LVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQaEGLSPRFHQLDIDDLQSIRALrdFlrKEYGGLDVLV 88
Cdd:PRK07041   1 LVVGGSSGIGLALARAFAAE-GARVTIASRSRDRLAAAARALG-GGAPVRTAALDITDEAAVDAF--F--AEAGPFDHVV 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   89 NNAGI-------AFKVADptpfhiqAEVTMKTNFFGTRDVCTEllPLIKPQGRVVNVSSIMSVRALKSCS 151
Cdd:PRK07041  75 ITAADtpggpvrALPLAA-------AQAAMDSKFWGAYRVARA--ARIAPGGSLTFVSGFAAVRPSASGV 135
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 7-151 8.36e-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: 39.90  E-value: 8.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312     7 VALVTGGNKGIGLAIVRDL--CRLFSG-DVVLTARDvargQAAVQQLQAEGLSPRfHQLDID----DLQSIRALRDFLR- 78
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELakCLKSPGsVLVLSARN----DEALRQLKAEIGAER-SGLRVVrvslDLGAEAGLEQLLKa 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    79 -------KEYGGLdVLVNNAGIAF---KVADPTPFHIQAEVTMKTNFFGTRDVCTELLPLIKP-QG---RVVNVSSIMSV 144
Cdd:TIGR01500  77 lrelprpKGLQRL-LLINNAGTLGdvsKGFVDLSDSTQVQNYWALNLTSMLCLTSSVLKAFKDsPGlnrTVVNISSLCAI 155


                  ....*..
gi 55727312   145 RALKSCS 151
Cdd:TIGR01500 156 QPFKGWA 162
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 7-117 1.17e-03

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


Pssm-ID: 187583 [Multi-domain]  Cd Length: 257  Bit Score: 39.37  E-value: 1.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVARGQAAVQQLQAE-GLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:cd05322   4 VAVVIGGGQTLGEFLCHGLAE--AGyDVAVADINSENAEKVADEINAEyGEKAYGFGADATNEQSVIALSKGVDEIFKRV 81

                        90       100       110
                ....*....|....*....|....*....|....
gi 55727312  85 DVLVNNAGIAfKVADPTPFHIQA-EVTMKTNFFG 117
Cdd:cd05322  82 DLLVYSAGIA-KSAKITDFELGDfDRSLQVNLVG 114
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-146 1.44e-03

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 39.18  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLcrLFSGDVVLtardvargqaAVQQLQAEGLSPRFH--QLDI-DDLQSiralrdfLRKEYGG 83
Cdd:PRK06550   7 TVLITGAASGIGLAQARAF--LAQGAQVY----------GVDKQDKPDLSGNFHflQLDLsDDLEP-------LFDWVPS 67

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55727312   84 LDVLVNNAGI--AFK----VADPTPFHIqaevtMKTNFFGTRDVCTELLPLIKPQGR--VVNVSSIMSVRA 146
Cdd:PRK06550  68 VDILCNTAGIldDYKplldTSLEEWQHI-----FDTNLTSTFLLTRAYLPQMLERKSgiIINMCSIASFVA 133
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
 6-93 1.81e-03

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs; This subgroup of extended SDR-like proteins are atypical SDRs. They have a glycine-rich NAD(P)-binding motif similar to the typical SDRs, GXXGXXG, and have the YXXXK active site motif (though not the other residues of the SDR tetrad). Members identified include NDUFA9 (mitochondrial) and putative nucleoside-diphosphate-sugar epimerase. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.


Pssm-ID: 187579 [Multi-domain]  Cd Length: 273  Bit Score: 39.15  E-value: 1.81e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   6 HVALVTGGNKGIGLAIVRDLCRlfSG-DVVLTARDVArgQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDflrkeygGL 84
Cdd:cd05271   1 MVVTVFGATGFIGRYVVNRLAK--RGsQVIVPYRCEA--YARRLLVMGDLGQVLFVEFDLRDDESIRKALE-------GS 69


                ....*....
gi 55727312  85 DVLVNNAGI 93
Cdd:cd05271  70 DVVINLVGR 78
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 7-98 1.90e-03

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


Pssm-ID: 187621 [Multi-domain]  Cd Length: 254  Bit Score: 38.75  E-value: 1.90e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQAEGLSPrfhQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:cd05363   5 TALITGSARGIGRAFAQAYVRE-GARVAIADINLEAARATAAEIGPAACAI---SLDVTDQASIDRCVAALVDRWGSIDI 80

                        90
                ....*....|..
gi 55727312  87 LVNNAGiAFKVA 98
Cdd:cd05363  81 LVNNAA-LFDLA 91
PRK06720 PRK06720
hypothetical protein; Provisional
 7-93 1.99e-03

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 38.03  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK06720  18 VAIVTGGGIGIGRNTALLLAKQ-GAKVIVTDIDQESGQATVEEITNLGGEALFVSYDMEKQGDWQRVISITLNAFSRIDM 96


                 ....*..
gi 55727312   87 LVNNAGI 93
Cdd:PRK06720  97 LFQNAGL 103
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 8-146 2.13e-03

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


Pssm-ID: 187630 [Multi-domain]  Cd Length: 250  Bit Score: 38.72  E-value: 2.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   8 ALVTG--GNKGIGLAIVRDLCRLfSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLD 85
Cdd:cd05372   4 ILITGiaNDRSIAWGIAKALHEA-GAELAFTYQPEALRKRVEKLAERLGESALVLPCDVSNDEEIKELFAEVKKDWGKLD 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55727312  86 VLVNNAGIAFKVADPTPFHiqaEVTMKtNFFGTRD--------VCTELLPLIKPQGRVVNVSSIMSVRA 146
Cdd:cd05372  83 GLVHSIAFAPKVQLKGPFL---DTSRK-GFLKALDisayslvsLAKAALPIMNPGGSIVTLSYLGSERV 147
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
 9-91 2.19e-03

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 38.76  E-value: 2.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    9 LVTGGNKGIGLAIVRDLcrLFSG-DVVLTARdvaRGQAAVQQLQAEGLSprFHQLDIDDLQSIRALRDFLRKEYGGLDVL 87
Cdd:PRK06483   6 LITGAGQRIGLALAWHL--LAQGqPVIVSYR---THYPAIDGLRQAGAQ--CIQADFSTNAGIMAFIDELKQHTDGLRAI 78


                 ....
gi 55727312   88 VNNA 91
Cdd:PRK06483  79 IHNA 82
PRK06139 PRK06139
SDR family oxidoreductase;
7-141 2.39e-03

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 38.93  E-value: 2.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    7 VALVTGGNKGIGLAIVRDLCRLFSgDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDV 86
Cdd:PRK06139   9 VVVITGASSGIGQATAEAFARRGA-RLVLAARDEEALQAVAEECRALGAEVLVVPTDVTDADQVKALATQAASFGGRIDV 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 55727312   87 LVNNAGI-AFKVADPTPFHIQAEVtMKTNFFGTRDVCTELLPLIKPQGRVVNVSSI 141
Cdd:PRK06139  88 WVNNVGVgAVGRFEETPIEAHEQV-IQTNLIGYMRDAHAALPIFKKQGHGIFINMI 142
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 7-93 2.58e-03

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


Pssm-ID: 187606 [Multi-domain]  Cd Length: 257  Bit Score: 38.49  E-value: 2.58e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312   7 VALVTGGNKGIGLAIVRdlcrlfsgdvvltaRDVARG-QAAVQQLQAEGLSPRFHQL---------DIDDLQSIRALRDF 76
Cdd:cd05348   6 VALITGGGSGLGRALVE--------------RFVAEGaKVAVLDRSAEKVAELRADFgdavvgvegDVRSLADNERAVAR 71

                        90
                ....*....|....*..
gi 55727312  77 LRKEYGGLDVLVNNAGI 93
Cdd:cd05348  72 CVERFGKLDCFIGNAGI 88
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 10-139 4.53e-03

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


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 37.81  E-value: 4.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312  10 VTGGNKGIGLAIVRDLCRlFSGDVVLTARD----------VARGQAAVQQLQAEGLSPRfhqLDIDDLQSIRALRDFLRK 79
Cdd:cd09762   8 ITGASRGIGKAIALKAAR-DGANVVIAAKTaephpklpgtIYTAAEEIEAAGGKALPCI---VDIRDEDQVRAAVEKAVE 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55727312  80 EYGGLDVLVNNA-GIAFKVADPTPFHiQAEVTMKTNFFGTRDVCTELLPLIK--PQGRVVNVS 139
Cdd:cd09762  84 KFGGIDILVNNAsAISLTGTLDTPMK-RYDLMMGVNTRGTYLCSKACLPYLKksKNPHILNLS 145
PRK07023 PRK07023
SDR family oxidoreductase;
5-93 4.99e-03

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 37.69  E-value: 4.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    5 MHVALVTGGNKGIGLAIVRDLcrLFSGDVVLTardVARGQAAVQQLQAeGLSPRFHQLDIDDLQSI------RALRDFLR 78
Cdd:PRK07023   1 AVRAIVTGHSRGLGAALAEQL--LQPGIAVLG---VARSRHPSLAAAA-GERLAEVELDLSDAAAAaawlagDLLAAFVD 74

                         90
                 ....*....|....*..
gi 55727312   79 --KEYggldVLVNNAGI 93
Cdd:PRK07023  75 gaSRV----LLINNAGT 87
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 8-140 5.69e-03

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 37.54  E-value: 5.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55727312    8 ALVTGGNKGIGLAIVRDLCRlfSG-DVVLTAR------DVARG-QAAVQQLQAEGLSPRFHQlDIDdlQSIRALRDFLRk 79
Cdd:PLN02780  56 ALVTGPTDGIGKGFAFQLAR--KGlNLVLVARnpdklkDVSDSiQSKYSKTQIKTVVVDFSG-DID--EGVKRIKETIE- 129

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55727312   80 eygGLDV--LVNNAGIAFKVAdpTPFH-IQAEVT---MKTNFFGTRDVCTELLP--LIKPQGRVVNVSS 140
Cdd:PLN02780 130 ---GLDVgvLINNVGVSYPYA--RFFHeVDEELLknlIKVNVEGTTKVTQAVLPgmLKRKKGAIINIGS 193
 
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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