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Conserved domains on  [gi|1918264442|ref|WP_193006717|]
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MULTISPECIES: 3-oxoacyl-ACP reductase [Psychrobacter]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
fabG super family cl32315
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
12-264 3.98e-111

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


The actual alignment was detected with superfamily member PRK08642:

Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 320.50  E-value: 3.98e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIvaaGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK08642    3 ISEQTVLVTGGSRGLGAAIARAFAREGARVVVNYHQSEDAAEALADEL---GDRAIALQADVTDREQVQAMFATATEHFG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 R-IDILVNNALPGYQFNPSADyTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYD 170
Cdd:PRK08642   80 KpITTVVNNALADFSFDGDAR-KKADDITWEDFQQQLEGSVKGALNTIQAALPGMREQGFGRIINIGTNLFQNPVVPYHD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 171 YTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSAA 250
Cdd:PRK08642  159 YTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRTTDASAATPDEVFDLIAATTPLRKVTTPQEFADAVLFFASPWARA 238
                         250
                  ....*....|....
gi 1918264442 251 ITGQSIAVDGGLTM 264
Cdd:PRK08642  239 VTGQNLVVDGGLVM 252
 
Name Accession Description Interval E-value
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
12-264 3.98e-111

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 320.50  E-value: 3.98e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIvaaGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK08642    3 ISEQTVLVTGGSRGLGAAIARAFAREGARVVVNYHQSEDAAEALADEL---GDRAIALQADVTDREQVQAMFATATEHFG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 R-IDILVNNALPGYQFNPSADyTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYD 170
Cdd:PRK08642   80 KpITTVVNNALADFSFDGDAR-KKADDITWEDFQQQLEGSVKGALNTIQAALPGMREQGFGRIINIGTNLFQNPVVPYHD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 171 YTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSAA 250
Cdd:PRK08642  159 YTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRTTDASAATPDEVFDLIAATTPLRKVTTPQEFADAVLFFASPWARA 238
                         250
                  ....*....|....
gi 1918264442 251 ITGQSIAVDGGLTM 264
Cdd:PRK08642  239 VTGQNLVVDGGLVM 252
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
15-264 4.34e-107

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: 310.16  E-value: 4.34e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADivaAGGQAFAYQADVTELEQMQGMANEVTARYGRID 94
Cdd:cd05349     1 QVVLVTGASRGLGAAIARSFAREGARVVVNYYRSTESAEAVAAE---AGERAIAIQADVRDRDQVQAMIEEAKNHFGPVD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  95 ILVNNALPGYQFNPSADYTsIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDYTTA 174
Cdd:cd05349    78 TIVNNALIDFPFDPDQRKT-FDTIDWEDYQQQLEGAVKGALNLLQAVLPDFKERGSGRVINIGTNLFQNPVVPYHDYTTA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 175 KSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSAAITGQ 254
Cdd:cd05349   157 KAALLGFTRNMAKELGPYGITVNMVSGGLLKVTDASAATPKEVFDAIAQTTPLGKVTTPQDIADAVLFFASPWARAVTGQ 236
                         250
                  ....*....|
gi 1918264442 255 SIAVDGGLTM 264
Cdd:cd05349   237 NLVVDGGLVM 246
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
12-264 7.06e-75

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: 228.13  E-value: 7.06e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNsQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:COG1028     4 LKGKVALVTGGSSGIGRAIARALAAEGARVVITDRD-AEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAFG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpGYQfnpsaDYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDY 171
Cdd:COG1028    83 RLDILVNNA--GIT-----PPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 172 TTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTT-EAVFDYIATTTPLRQATSVDDFANSVLLMASDLSAA 250
Cdd:COG1028   156 AASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGaEEVREALAARIPLGRLGTPEEVAAAVLFLASDAASY 235
                         250
                  ....*....|....
gi 1918264442 251 ITGQSIAVDGGLTM 264
Cdd:COG1028   236 ITGQVLAVDGGLTA 249
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
24-263 5.27e-55

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: 176.85  E-value: 5.27e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  24 RGLGAQIAQKMAGAGASVCVNYLNsqEAADTVVADIVAAGGQAfAYQADVTELEQMQGMANEVTARYGRIDILVNNAlpG 103
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLN--EALAKRVEELAEELGAA-VLPCDVTDEEQVEALVAAAVEKFGRLDILVNNA--G 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 104 YQFNPSADYTSIEtvqWSHFTQQIDGIVKGAVNAVQAVLPQMKAQktGKILNISTNLVYNPVVTYYDYTTAKSALIGLTR 183
Cdd:pfam13561  81 FAPKLKGPFLDTS---REDFDRALDVNLYSLFLLAKAALPLMKEG--GSIVNLSSIGAERVVPNYNAYGAAKAALEALTR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 184 NLAAELGQYGIRVNLLAGGLLKTTDASRLT-TEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSAAITGQSIAVDGGL 262
Cdd:pfam13561 156 YLAVELGPRGIRVNAISPGPIKTLAASGIPgFDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGGY 235

                  .
gi 1918264442 263 T 263
Cdd:pfam13561 236 T 236
23BDH TIGR02415
acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is ...
15-262 5.32e-31

acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is described as able to interconvert acetoin + NADH with meso-2,3-butanediol + NAD(+). It is also called capable of irreversible reduction of diacetyl with NADH to acetoin. Blomqvist, et al. decline to specify either EC 1.1.1.4 which is (R,R)-butanediol dehydrogenase, or EC 1.1.1.5, which is acetoin dehydrogenase without a specified stereochemistry, for this enzyme. This enzyme is a homotetramer in the family of short chain dehydrogenases (pfam00106). Another member of this family, from Corynebacterium glutamicum, is called L-2,3-butanediol dehydrogenase (). [Energy metabolism, Fermentation]


Pssm-ID: 131468 [Multi-domain]  Cd Length: 254  Bit Score: 115.63  E-value: 5.32e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVvADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRID 94
Cdd:TIGR02415   1 KVALVTGGAQGIGKGIAERLAKDGFAVAVADLNEETAKETA-KEINQAGGKAVAYKLDVSDKDQVFSAIDQAAEKFGGFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  95 ILVNNAlpgyqfnPSADYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKT-GKILNIST--NLVYNPVVTYYdy 171
Cdd:TIGR02415  80 VMVNNA-------GVAPITPILEITEEELKKVYNVNVKGVLFGIQAAARQFKKQGHgGKIINAASiaGHEGNPILSAY-- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 172 TTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAV----------FDYIATTTPLRQATSVDDFANSVL 241
Cdd:TIGR02415 151 SSTKFAVRGLTQTAAQELAPKGITVNAYCPGIVKTPMWEEIDEETSeiagkpigegFEEFSSEIALGRPSEPEDVAGLVS 230
                         250       260
                  ....*....|....*....|.
gi 1918264442 242 LMASDLSAAITGQSIAVDGGL 262
Cdd:TIGR02415 231 FLASEDSDYITGQSILVDGGM 251
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
15-144 4.85e-07

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: 48.63  E-value: 4.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442   15 KVVIVTGASRGLGAQIAQKMAGAGASVCVnyLNS-----QEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTAR 89
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGARRLV--LLSrsgpdAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAV 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1918264442   90 YGRIDILVNNALpgyqfnpSADYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQ 144
Cdd:smart00822  79 EGPLTGVIHAAG-------VLDDGVLASLTPERFAAVLAPKAAGAWNLHELTADL 126
 
Name Accession Description Interval E-value
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
12-264 3.98e-111

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 320.50  E-value: 3.98e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIvaaGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK08642    3 ISEQTVLVTGGSRGLGAAIARAFAREGARVVVNYHQSEDAAEALADEL---GDRAIALQADVTDREQVQAMFATATEHFG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 R-IDILVNNALPGYQFNPSADyTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYD 170
Cdd:PRK08642   80 KpITTVVNNALADFSFDGDAR-KKADDITWEDFQQQLEGSVKGALNTIQAALPGMREQGFGRIINIGTNLFQNPVVPYHD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 171 YTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSAA 250
Cdd:PRK08642  159 YTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRTTDASAATPDEVFDLIAATTPLRKVTTPQEFADAVLFFASPWARA 238
                         250
                  ....*....|....
gi 1918264442 251 ITGQSIAVDGGLTM 264
Cdd:PRK08642  239 VTGQNLVVDGGLVM 252
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
15-264 4.34e-107

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: 310.16  E-value: 4.34e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADivaAGGQAFAYQADVTELEQMQGMANEVTARYGRID 94
Cdd:cd05349     1 QVVLVTGASRGLGAAIARSFAREGARVVVNYYRSTESAEAVAAE---AGERAIAIQADVRDRDQVQAMIEEAKNHFGPVD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  95 ILVNNALPGYQFNPSADYTsIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDYTTA 174
Cdd:cd05349    78 TIVNNALIDFPFDPDQRKT-FDTIDWEDYQQQLEGAVKGALNLLQAVLPDFKERGSGRVINIGTNLFQNPVVPYHDYTTA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 175 KSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSAAITGQ 254
Cdd:cd05349   157 KAALLGFTRNMAKELGPYGITVNMVSGGLLKVTDASAATPKEVFDAIAQTTPLGKVTTPQDIADAVLFFASPWARAVTGQ 236
                         250
                  ....*....|
gi 1918264442 255 SIAVDGGLTM 264
Cdd:cd05349   237 NLVVDGGLVM 246
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
12-264 7.06e-75

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: 228.13  E-value: 7.06e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNsQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:COG1028     4 LKGKVALVTGGSSGIGRAIARALAAEGARVVITDRD-AEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAFG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpGYQfnpsaDYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDY 171
Cdd:COG1028    83 RLDILVNNA--GIT-----PPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 172 TTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTT-EAVFDYIATTTPLRQATSVDDFANSVLLMASDLSAA 250
Cdd:COG1028   156 AASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGaEEVREALAARIPLGRLGTPEEVAAAVLFLASDAASY 235
                         250
                  ....*....|....
gi 1918264442 251 ITGQSIAVDGGLTM 264
Cdd:COG1028   236 ITGQVLAVDGGLTA 249
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
17-259 2.06e-63

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: 198.66  E-value: 2.06e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  17 VIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADtvVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRIDIL 96
Cdd:cd05233     1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAE--LAAIEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDIL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  97 VNNAlpGYQFNPSADYTSIEtvqwsHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDYTTAKS 176
Cdd:cd05233    79 VNNA--GIARPGPLEELTDE-----DWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 177 ALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSAAITGQSI 256
Cdd:cd05233   152 ALEGLTRSLALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKELAAAIPLGRLGTPEEVAEAVVFLASDEASYITGQVI 231

                  ...
gi 1918264442 257 AVD 259
Cdd:cd05233   232 PVD 234
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
17-263 1.73e-61

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: 193.72  E-value: 1.73e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  17 VIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRIDIL 96
Cdd:cd05359     1 ALVTGGSRGIGKAIALRLAERGADVVINYRKSKDAAAEVAAEIEELGGKAVVVRADVSQPQDVEEMFAAVKERFGRLDVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  97 VNNALPGYqFNPSADYTsietvqWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDYTTAKS 176
Cdd:cd05359    81 VSNAAAGA-FRPLSELT------PAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALPNYLAVGTAKA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 177 ALIGLTRNLAAELGQYGIRVNLLAGGLLKtTDASR--LTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSAAITGQ 254
Cdd:cd05359   154 ALEALVRYLAVELGPRGIRVNAVSPGVID-TDALAhfPNREDLLEAAAANTPAGRVGTPQDVADAVGFLCSDAARMITGQ 232

                  ....*....
gi 1918264442 255 SIAVDGGLT 263
Cdd:cd05359   233 TLVVDGGLS 241
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
12-265 2.69e-60

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 190.79  E-value: 2.69e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK05557    3 LEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGAEALVAEIGALGGKALAVQGDVSDAESVERAVDEAKAEFG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpGY-QFNPSADYTSIEtvqwshFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYD 170
Cdd:PRK05557   83 GVDILVNNA--GItRDNLLMRMKEED------WDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGQAN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 171 YTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKtTDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSAA 250
Cdd:PRK05557  155 YAASKAGVIGFTKSLARELASRGITVNAVAPGFIE-TDMTDALPEDVKEAILAQIPLGRLGQPEEIASAVAFLASDEAAY 233
                         250
                  ....*....|....*
gi 1918264442 251 ITGQSIAVDGGLTMP 265
Cdd:PRK05557  234 ITGQTLHVNGGMVMG 248
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
12-264 1.55e-57

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 183.92  E-value: 1.55e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK12825    4 LMGRVALVTGAARGLGRAIALRLARAGADVVVHYRSDEEAAEELVEAVEALGRRAQAVQADVTDKAALEAAVAAAVERFG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpG-YQFNPSADYtSIEtvQWShftQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTnLVYNPVVTYY- 169
Cdd:PRK12825   84 RIDILVNNA--GiFEDKPLADM-SDD--EWD---EVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISS-VAGLPGWPGRs 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 170 DYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVFDYIAtTTPLRQATSVDDFANSVLLMASDLSA 249
Cdd:PRK12825  155 NYAAAKAGLVGLTKALARELAEYGITVNMVAPGDIDTDMKEATIEEAREAKDA-ETPLGRSGTPEDIARAVAFLCSDASD 233
                         250
                  ....*....|....*
gi 1918264442 250 AITGQSIAVDGGLTM 264
Cdd:PRK12825  234 YITGQVIEVTGGVDV 248
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
12-264 1.76e-57

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 183.82  E-value: 1.76e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVcVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK05653    3 LQGKTALVTGASRGIGRAIALRLAADGAKV-VIYDSNEEAAEALAAELRAAGGEARVLVFDVSDEAAVRALIEAAVEAFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlPGYQFNPSADYTSIEtvqwshFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNIS--TNLVYNPVVTyy 169
Cdd:PRK05653   82 ALDILVNNA-GITRDALLPRMSEED------WDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISsvSGVTGNPGQT-- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 170 DYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKtTDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSA 249
Cdd:PRK05653  153 NYSAAKAGVIGFTKALALELASRGITVNAVAPGFID-TDMTEGLPEEVKAEILKEIPLGRLGQPEEVANAVAFLASDAAS 231
                         250
                  ....*....|....*
gi 1918264442 250 AITGQSIAVDGGLTM 264
Cdd:PRK05653  232 YITGQVIPVNGGMYM 246
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
24-263 5.27e-55

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: 176.85  E-value: 5.27e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  24 RGLGAQIAQKMAGAGASVCVNYLNsqEAADTVVADIVAAGGQAfAYQADVTELEQMQGMANEVTARYGRIDILVNNAlpG 103
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLN--EALAKRVEELAEELGAA-VLPCDVTDEEQVEALVAAAVEKFGRLDILVNNA--G 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 104 YQFNPSADYTSIEtvqWSHFTQQIDGIVKGAVNAVQAVLPQMKAQktGKILNISTNLVYNPVVTYYDYTTAKSALIGLTR 183
Cdd:pfam13561  81 FAPKLKGPFLDTS---REDFDRALDVNLYSLFLLAKAALPLMKEG--GSIVNLSSIGAERVVPNYNAYGAAKAALEALTR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 184 NLAAELGQYGIRVNLLAGGLLKTTDASRLT-TEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSAAITGQSIAVDGGL 262
Cdd:pfam13561 156 YLAVELGPRGIRVNAISPGPIKTLAASGIPgFDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGGY 235

                  .
gi 1918264442 263 T 263
Cdd:pfam13561 236 T 236
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
12-263 1.50e-53

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: 173.62  E-value: 1.50e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:cd05362     1 LAGKVALVTGASRGIGRAIAKRLARDGASVVVNYASSKAAAEEVVAEIEAAGGKAIAVQADVSDPSQVARLFDAAEKAFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpG-YQFNPsadytsIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAqkTGKILNISTNLVYNPVVTYYD 170
Cdd:cd05362    81 GVDILVNNA--GvMLKKP------IAETSEEEFDRMFTVNTKGAFFVLQEAAKRLRD--GGRIINISSSLTAAYTPNYGA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 171 YTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSAA 250
Cdd:cd05362   151 YAGSKAAVEAFTRVLAKELGGRGITVNAVAPGPVDTDMFYAGKTEEAVEGYAKMSPLGRLGEPEDIAPVVAFLASPDGRW 230
                         250
                  ....*....|...
gi 1918264442 251 ITGQSIAVDGGLT 263
Cdd:cd05362   231 VNGQVIRANGGYV 243
FabG-like PRK07231
SDR family oxidoreductase;
12-263 5.32e-53

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 172.32  E-value: 5.32e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNsQEAADTVVADIvAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK07231    3 LEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRN-EEAAERVAAEI-LAGGRAIAVAADVSDEADVEAAVAAALERFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpgyQFNPSadYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNIST--NLVYNPVVTYY 169
Cdd:PRK07231   81 SVDILVNNA----GTTHR--NGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVAStaGLRPRPGLGWY 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 170 DytTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRL---TTEAVFDYIATTTPLRQATSVDDFANSVLLMASD 246
Cdd:PRK07231  155 N--ASKGAVITLTKALAAELGPDKIRVNAVAPVVVETGLLEAFmgePTPENRAKFLATIPLGRLGTPEDIANAALFLASD 232
                         250
                  ....*....|....*..
gi 1918264442 247 LSAAITGQSIAVDGGLT 263
Cdd:PRK07231  233 EASWITGVTLVVDGGRC 249
PRK12826 PRK12826
SDR family oxidoreductase;
12-265 5.82e-53

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 172.41  E-value: 5.82e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVvADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK12826    4 LEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATA-ELVEAAGGKARARQVDVRDRAALKAAVAAGVEDFG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpGYqfNPSADYTSIETVQWshfTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTnlVYNPVVTY--- 168
Cdd:PRK12826   83 RLDILVANA--GI--FPLTPFAEMDDEQW---ERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSS--VAGPRVGYpgl 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 169 YDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLS 248
Cdd:PRK12826  154 AHYAASKAGLVGFTRALALELAARNITVNSVHPGGVDTPMAGNLGDAQWAEAIAAAIPLGRLGEPEDIAAAVLFLASDEA 233
                         250
                  ....*....|....*..
gi 1918264442 249 AAITGQSIAVDGGLTMP 265
Cdd:PRK12826  234 RYITGQTLPVDGGATLP 250
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
12-264 2.64e-52

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: 170.64  E-value: 2.64e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:cd05358     1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVNYRSKEDAAEEVVEEIKAVGGKAIAVQADVSKEEDVVALFQSAIKEFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpGYQfnpsADYTSIEtVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQK-TGKILNISTNLVYNPVVTYYD 170
Cdd:cd05358    81 TLDILVNNA--GLQ----GDASSHE-MTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKiKGKIINMSSVHEKIPWPGHVN 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 171 YTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT-TDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSA 249
Cdd:cd05358   154 YAASKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTpINAEAWDDPEQRADLLSLIPMGRIGEPEEIAAAAAWLASDEAS 233
                         250
                  ....*....|....*
gi 1918264442 250 AITGQSIAVDGGLTM 264
Cdd:cd05358   234 YVTGTTLFVDGGMTL 248
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
15-263 3.66e-52

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: 170.04  E-value: 3.66e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSqEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRID 94
Cdd:cd05333     1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSE-EAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFGPVD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  95 ILVNNA-------LPgyqfnpsadYTSIEtvQWShftQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNIST--NLVYNPV 165
Cdd:cd05333    80 ILVNNAgitrdnlLM---------RMSEE--DWD---AVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSvvGLIGNPG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 166 VTyyDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT--TDASRlttEAVFDYIATTTPLRQATSVDDFANSVLLM 243
Cdd:cd05333   146 QA--NYAASKAGVIGFTKSLAKELASRGITVNAVAPGFIDTdmTDALP---EKVKEKILKQIPLGRLGTPEEVANAVAFL 220
                         250       260
                  ....*....|....*....|
gi 1918264442 244 ASDLSAAITGQSIAVDGGLT 263
Cdd:cd05333   221 ASDDASYITGQVLHVNGGMY 240
PRK12939 PRK12939
short chain dehydrogenase; Provisional
9-265 2.49e-51

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 168.23  E-value: 2.49e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442   9 PAFLLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADtVVADIVAAGGQAFAYQADVTELEQMQGMANEVTA 88
Cdd:PRK12939    2 ASNLAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARE-LAAALEAAGGRAHAIAADLADPASVQRFFDAAAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  89 RYGRIDILVNNAlpGYQFNPSADYTSIETvqwshFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTY 168
Cdd:PRK12939   81 ALGGLDGLVNNA--GITNSKSATELDIDT-----WDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPKL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 169 YDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLS 248
Cdd:PRK12939  154 GAYVASKGAVIGMTRSLARELGGRGITVNAIAPGLTATEATAYVPADERHAYYLKGRALERLQVPDDVAGAVLFLLSDAA 233
                         250
                  ....*....|....*..
gi 1918264442 249 AAITGQSIAVDGGLTMP 265
Cdd:PRK12939  234 RFVTGQLLPVNGGFVMN 250
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
12-263 1.72e-50

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 165.79  E-value: 1.72e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK05565    3 LMGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYDINEEAAQELLEEIKEEGGDAIAVKADVSSEEDVENLVEQIVEKFG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNALPGYqFNPSADyTSIETVQwshftQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNIST--NLVYNP--VVt 167
Cdd:PRK05565   83 KIDILVNNAGISN-FGLVTD-MTDEEWD-----RVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSiwGLIGASceVL- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 168 yydYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVFDyIATTTPLRQATSVDDFANSVLLMASDL 247
Cdd:PRK05565  155 ---YSASKGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEMWSSFSEEDKEG-LAEEIPLGRLGKPEEIAKVVLFLASDD 230
                         250
                  ....*....|....*.
gi 1918264442 248 SAAITGQSIAVDGGLT 263
Cdd:PRK05565  231 ASYITGQIITVDGGWT 246
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
15-263 7.69e-50

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 164.73  E-value: 7.69e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNYlNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRID 94
Cdd:PRK08213   13 KTALVTGGSRGLGLQIAEALGEAGARVVLSA-RKAEELEEAAAHLEALGIDALWIAADVADEADIERLAEETLERFGHVD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  95 ILVNNAlpGYQFNPSADYTSIETVQwshftQQIDGIVKGAVNAVQAVLPQ-MKAQKTGKILNIST--NLVYNP--VVTYY 169
Cdd:PRK08213   92 ILVNNA--GATWGAPAEDHPVEAWD-----KVMNLNVRGLFLLSQAVAKRsMIPRGYGRIINVASvaGLGGNPpeVMDTI 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 170 DYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTdASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSA 249
Cdd:PRK08213  165 AYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTK-MTRGTLERLGEDLLAHTPLGRLGDDEDLKGAALLLASDASK 243
                         250
                  ....*....|....
gi 1918264442 250 AITGQSIAVDGGLT 263
Cdd:PRK08213  244 HITGQILAVDGGVS 257
PRK12937 PRK12937
short chain dehydrogenase; Provisional
12-262 8.62e-50

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 164.14  E-value: 8.62e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK12937    3 LSNKVAIVTGASRGIGAAIARRLAADGFAVAVNYAGSAAAADELVAEIEAAGGRAIAVQADVADAAAVTRLFDAAETAFG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpGYQFNPSADYTSIETvqwshFTQQIDGIVKGAVNAVQAVLPQMKaqKTGKILNISTNLVYNPVVTYYDY 171
Cdd:PRK12937   83 RIDVLVNNA--GVMPLGTIADFDLED-----FDRTIATNLRGAFVVLREAARHLG--QGGRIINLSTSVIALPLPGYGPY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 172 TTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSAAI 251
Cdd:PRK12937  154 AASKAAVEGLVHVLANELRGRGITVNAVAPGPVATELFFNGKSAEQIDQLAGLAPLERLGTPEEIAAAVAFLAGPDGAWV 233
                         250
                  ....*....|.
gi 1918264442 252 TGQSIAVDGGL 262
Cdd:PRK12937  234 NGQVLRVNGGF 244
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
14-263 3.91e-49

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: 162.44  E-value: 3.91e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNsQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRI 93
Cdd:cd05344     1 GKVALVTAASSGIGLAIARALAREGARVAICARN-RENLERAASELRAGGAGVLAVVADLTDPEDIDRLVEKAGDAFGRV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  94 DILVNNALPGyqfnPSADYTSIETVQWshfTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDYTT 173
Cdd:cd05344    80 DILVNNAGGP----PPGPFAELTDEDW---LEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEPEPNLVLSNV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 174 AKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRL----------TTEAVFDYIATTTPLRQATSVDDFANSVLLM 243
Cdd:cd05344   153 ARAGLIGLVKTLSRELAPDGVTVNSVLPGYIDTERVRRLlearaekegiSVEEAEKEVASQIPLGRVGKPEELAALIAFL 232
                         250       260
                  ....*....|....*....|
gi 1918264442 244 ASDLSAAITGQSIAVDGGLT 263
Cdd:cd05344   233 ASEKASYITGQAILVDGGLT 252
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
12-263 6.96e-49

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: 161.76  E-value: 6.96e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNsQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:cd05347     3 LKGKVALVTGASRGIGFGIASGLAEAGANIVINSRN-EEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpGYQFNPSADYTSIEtvqwsHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDY 171
Cdd:cd05347    82 KIDILVNNA--GIIRRHPAEEFPEA-----EWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPAY 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 172 TTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT--TDASRlTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSA 249
Cdd:cd05347   155 AASKGGVAGLTKALATEWARHGIQVNAIAPGYFATemTEAVV-ADPEFNDDILKRIPAGRWGQPEDLVGAAVFLASDASD 233
                         250
                  ....*....|....
gi 1918264442 250 AITGQSIAVDGGLT 263
Cdd:cd05347   234 YVNGQIIFVDGGWL 247
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
15-206 8.51e-47

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 154.69  E-value: 8.51e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNyLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRID 94
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLV-DRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  95 ILVNNAlPGYQFNPSADYTSietvqwSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDYTTA 174
Cdd:pfam00106  80 ILVNNA-GITGLGPFSELSD------EDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSAS 152
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1918264442 175 KSALIGLTRNLAAELGQYGIRVNLLAGGLLKT 206
Cdd:pfam00106 153 KAAVIGFTRSLALELAPHGIRVNAVAPGGVDT 184
PRK07890 PRK07890
short chain dehydrogenase; Provisional
12-265 1.48e-46

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 155.89  E-value: 1.48e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVcVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK07890    3 LKGKVVVVSGVGPGLGRTLAVRAARAGADV-VLAARTAERLDEVAAEIDDLGRRALAVPTDITDEDQCANLVALALERFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNALPGYQFNPSADyTSIETVQWShftqqIDGIVKGAVNAVQAVLPQMKAQKtGKILNISTNLVYNPVVTYYDY 171
Cdd:PRK07890   82 RVDALVNNAFRVPSMKPLAD-ADFAHWRAV-----IELNVLGTLRLTQAFTPALAESG-GSIVMINSMVLRHSQPKYGAY 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 172 TTAKSALIGLTRNLAAELGQYGIRVNLLAGGLL----------KTTDASRLTTEAVFDYIATTTPLRQATSVDDFANSVL 241
Cdd:PRK07890  155 KMAKGALLAASQSLATELGPQGIRVNSVAPGYIwgdplkgyfrHQAGKYGVTVEQIYAETAANSDLKRLPTDDEVASAVL 234
                         250       260
                  ....*....|....*....|....
gi 1918264442 242 LMASDLSAAITGQSIAVDGGLTMP 265
Cdd:PRK07890  235 FLASDLARAITGQTLDVNCGEYHH 258
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
12-264 3.02e-46

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 155.43  E-value: 3.02e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNsQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK12429    2 LKGKVALVTGAASGIGLEIALALAKEGAKVVIADLN-DEAAAAAAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVETFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpGYQF-NPsadytsIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTnlvYNPVVTYYD 170
Cdd:PRK12429   81 GVDILVNNA--GIQHvAP------IEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMAS---VHGLVGSAG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 171 ---YTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT------TDASRLT-----TEAVFDYIATTTPLRQATSVDDF 236
Cdd:PRK12429  150 kaaYVSAKHGLIGLTKVVALEGATHGVTVNAICPGYVDTplvrkqIPDLAKErgiseEEVLEDVLLPLVPQKRFTTVEEI 229
                         250       260
                  ....*....|....*....|....*...
gi 1918264442 237 ANSVLLMASDLSAAITGQSIAVDGGLTM 264
Cdd:PRK12429  230 ADYALFLASFAAKGVTGQAWVVDGGWTA 257
PRK07774 PRK07774
SDR family oxidoreductase;
14-264 2.48e-45

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 152.59  E-value: 2.48e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSqEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRI 93
Cdd:PRK07774    6 DKVAIVTGAAGGIGQAYAEALAREGASVVVADINA-EGAERVAKQIVADGGTAIAVQVDVSDPDSAKAMADATVSAFGGI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  94 DILVNNAlpgyqfnpsADYTSIE-----TVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTN---LVYNPv 165
Cdd:PRK07774   85 DYLVNNA---------AIYGGMKldlliTVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTaawLYSNF- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 166 vtyydYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMAS 245
Cdd:PRK07774  155 -----YGLAKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTEATRTVTPKEFVADMVKGIPLSRMGTPEDLVGMCLFLLS 229
                         250
                  ....*....|....*....
gi 1918264442 246 DLSAAITGQSIAVDGGLTM 264
Cdd:PRK07774  230 DEASWITGQIFNVDGGQII 248
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
14-206 3.69e-45

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 152.33  E-value: 3.69e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNsQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRI 93
Cdd:COG0300     5 GKTVLITGASSGIGRALARALAARGARVVLVARD-AERLEALAAELRAAGARVEVVALDVTDPDAVAALAEAVLARFGPI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  94 DILVNNAlpGYqfnpsADYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDYTT 173
Cdd:COG0300    84 DVLVNNA--GV-----GGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAA 156
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1918264442 174 AKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT 206
Cdd:COG0300   157 SKAALEGFSESLRAELAPTGVRVTAVCPGPVDT 189
PRK07035 PRK07035
SDR family oxidoreductase;
12-263 4.65e-45

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 152.09  E-value: 4.65e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYlNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK07035    6 LTGKIALVTGASRGIGEAIAKLLAQQGAHVIVSS-RKLDGCQAVADAIVAAGGKAEALACHIGEMEQIDALFAHIRERHG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNALPGYQFNPSADytsieTVQWShFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNI-STNLVyNPVVTYYD 170
Cdd:PRK07035   85 RLDILVNNAAANPYFGHILD-----TDLGA-FQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVaSVNGV-SPGDFQGI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 171 YTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTT-EAVFDYIATTTPLRQATSVDDFANSVLLMASDLSA 249
Cdd:PRK07035  158 YSITKAAVISMTKAFAKECAPFGIRVNALLPGLTDTKFASALFKnDAILKQALAHIPLRRHAEPSEMAGAVLYLASDASS 237
                         250
                  ....*....|....
gi 1918264442 250 AITGQSIAVDGGLT 263
Cdd:PRK07035  238 YTTGECLNVDGGYL 251
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
14-264 2.92e-44

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 149.87  E-value: 2.92e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRI 93
Cdd:PRK08063    4 GKVALVTGSSRGIGKAIALRLAEEGYDIAVNYARSRKAAEETAEEIEALGRKALAVKANVGDVEKIKEMFAQIDEEFGRL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  94 DILVNNALPGYQfnpsadyTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNIST--NLVYNPvvtyyDY 171
Cdd:PRK08063   84 DVFVNNAASGVL-------RPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLSSlgSIRYLE-----NY 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 172 TT---AKSALIGLTRNLAAELGQYGIRVNLLAGGLLKtTDA-----SRlttEAVFDYIATTTPLRQATSVDDFANSVLLM 243
Cdd:PRK08063  152 TTvgvSKAALEALTRYLAVELAPKGIAVNAVSGGAVD-TDAlkhfpNR---EELLEDARAKTPAGRMVEPEDVANAVLFL 227
                         250       260
                  ....*....|....*....|.
gi 1918264442 244 ASDLSAAITGQSIAVDGGLTM 264
Cdd:PRK08063  228 CSPEADMIRGQTIIVDGGRSL 248
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
14-246 9.51e-43

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: 145.71  E-value: 9.51e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNsQEAADTVVADIvaaGGQAFAYQADVTELEQMQGMANEVTARYGRI 93
Cdd:COG4221     5 GKVALITGASSGIGAATARALAAAGARVVLAARR-AERLEALAAEL---GGRALAVPLDVTDEAAVEAAVAAAVAEFGRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  94 DILVNNAlpGYqfnpsADYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDYTT 173
Cdd:COG4221    81 DVLVNNA--GV-----ALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAA 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1918264442 174 AKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVFDYIATTTPLrQATSVDDFANSVLLMASD 246
Cdd:COG4221   154 TKAAVRGLSESLRAELRPTGIRVTVIEPGAVDTEFLDSVFDGDAEAAAAVYEGL-EPLTPEDVAEAVLFALTQ 225
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
14-264 1.71e-40

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: 140.20  E-value: 1.71e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRI 93
Cdd:cd05366     2 SKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEAAKSTIQEISEAGYNAVAVGADVTDKDDVEALIDQAVEKFGSF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  94 DILVNNAlpgyqfnPSADYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQK-TGKILNIST--NLVYNPVVTYyd 170
Cdd:cd05366    82 DVMVNNA-------GIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGhGGKIINASSiaGVQGFPNLGA-- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 171 YTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAV----------FDYIATTTPLRQATSVDDFANSV 240
Cdd:cd05366   153 YSASKFAVRGLTQTAAQELAPKGITVNAYAPGIVKTEMWDYIDEEVGeiagkpegegFAEFSSSIPLGRLSEPEDVAGLV 232
                         250       260
                  ....*....|....*....|....
gi 1918264442 241 LLMASDLSAAITGQSIAVDGGLTM 264
Cdd:cd05366   233 SFLASEDSDYITGQTILVDGGMVY 256
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
14-261 2.97e-40

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: 139.64  E-value: 2.97e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNsQEAADTVVADIVAA-GGQAFAYQADVTELEQMQGMANEVTARYGR 92
Cdd:cd05369     3 GKVAFITGGGTGIGKAIAKAFAELGASVAIAGRK-PEVLEAAAEEISSAtGGRAHPIQCDVRDPEAVEAAVDETLKEFGK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  93 IDILVNNAlpGYQF-NPSADYTS--IETVqwshftqqIDGIVKGAVNAVQAVLPQ-MKAQKTGKILNISTNLVYNPVVTY 168
Cdd:cd05369    82 IDILINNA--AGNFlAPAESLSPngFKTV--------IDIDLNGTFNTTKAVGKRlIEAKHGGSILNISATYAYTGSPFQ 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 169 YDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDA-SRLTTEAVFDYIAT-TTPLRQATSVDDFANSVLLMASD 246
Cdd:cd05369   152 VHSAAAKAGVDALTRSLAVEWGPYGIRVNAIAPGPIPTTEGmERLAPSGKSEKKMIeRVPLGRLGTPEEIANLALFLLSD 231
                         250
                  ....*....|....*
gi 1918264442 247 LSAAITGQSIAVDGG 261
Cdd:cd05369   232 AASYINGTTLVVDGG 246
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
16-261 8.04e-40

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: 138.09  E-value: 8.04e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  16 VVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSqEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRIDI 95
Cdd:cd05365     1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKS-EGAEAVAAAIQQAGGQAIGLECNVTSEQDLEAVVKATVSQFGGITI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  96 LVNNALPGyqfNPSADYTSIETVQwshFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDYTTAK 175
Cdd:cd05365    80 LVNNAGGG---GPKPFDMPMTEED---FEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRIAAYGSSK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 176 SALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSAAITGQS 255
Cdd:cd05365   154 AAVNHMTRNLAFDLGPKGIRVNAVAPGAVKTDALASVLTPEIERAMLKHTPLGRLGEPEDIANAALFLCSPASAWVSGQV 233

                  ....*.
gi 1918264442 256 IAVDGG 261
Cdd:cd05365   234 LTVSGG 239
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
12-265 9.32e-40

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 138.78  E-value: 9.32e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVnyLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK08226    4 LTGKTALITGALQGIGEGIARVFARHGANLIL--LDISPEIEKLADELCGRGHRCTAVVADVRDPASVAAAIKRAKEKEG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNA----LPGYQFNPSADYTSietvqwshftqQIDGIVKGAVNAVQAVLPQMKAQKTGKILNIST---NLVYNP 164
Cdd:PRK08226   82 RIDILVNNAgvcrLGSFLDMSDEDRDF-----------HIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSvtgDMVADP 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 165 VVTyyDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEA-------VFDYIATTTPLRQATSVDDFA 237
Cdd:PRK08226  151 GET--AYALTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRTPMAESIARQSnpedpesVLTEMAKAIPLRRLADPLEVG 228
                         250       260
                  ....*....|....*....|....*...
gi 1918264442 238 NSVLLMASDLSAAITGQSIAVDGGLTMP 265
Cdd:PRK08226  229 ELAAFLASDESSYLTGTQNVIDGGSTLP 256
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
12-261 1.54e-39

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 138.06  E-value: 1.54e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNsQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK06113    9 LDGKCAIITGAGAGIGKEIAITFATAGASVVVSDIN-ADAANHVVDEIQQLGGQAFACRCDITSEQELSALADFALSKLG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNALPGyqfNPSADYTSIETVQWSHFTQqidgiVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDY 171
Cdd:PRK06113   88 KVDILVNNAGGG---GPKPFDMPMADFRRAYELN-----VFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 172 TTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSAAI 251
Cdd:PRK06113  160 ASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTDALKSVITPEIEQKMLQHTPIRRLGQPQDIANAALFLCSPAASWV 239
                         250
                  ....*....|
gi 1918264442 252 TGQSIAVDGG 261
Cdd:PRK06113  240 SGQILTVSGG 249
PRK06124 PRK06124
SDR family oxidoreductase;
12-263 7.01e-39

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 136.00  E-value: 7.01e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSqEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK06124    9 LAGQVALVTGSARGLGFEIARALAGAGAHVLVNGRNA-ATLEAAVAALRAAGGAAEALAFDIADEEAVAAAFARIDAEHG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNA-----LPGYQFNPSADYTSIETVQWSHFTQqidgivkgAVNAVQAvlpqMKAQKTGKILNISTnlVYNPVV 166
Cdd:PRK06124   88 RLDILVNNVgardrRPLAELDDAAIRALLETDLVAPILL--------SRLAAQR----MKRQGYGRIIAITS--IAGQVA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 167 TYYD--YTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT-TDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLM 243
Cdd:PRK06124  154 RAGDavYPAAKQGLTGLMRALAAEFGPHGITSNAIAPGYFATeTNAAMAADPAVGPWLAQRTPLGRWGRPEEIAGAAVFL 233
                         250       260
                  ....*....|....*....|
gi 1918264442 244 ASDLSAAITGQSIAVDGGLT 263
Cdd:PRK06124  234 ASPAASYVNGHVLAVDGGYS 253
PRK09135 PRK09135
pteridine reductase; Provisional
15-261 1.90e-38

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 134.67  E-value: 1.90e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAA-GGQAFAYQADVTELEQMQGMANEVTARYGRI 93
Cdd:PRK09135    7 KVALITGGARRIGAAIARTLHAAGYRVAIHYHRSAAEADALAAELNALrPGSAAALQADLLDPDALPELVAACVAAFGRL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  94 DILVNNAlpgYQFNPSaDYTSIETVQWshfTQQIDGIVKGAVNAVQAVLPQMKAQKtGKILNISTNLVYNPVVTYYDYTT 173
Cdd:PRK09135   87 DALVNNA---SSFYPT-PLGSITEAQW---DDLFASNLKAPFFLSQAAAPQLRKQR-GAIVNITDIHAERPLKGYPVYCA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 174 AKSALIGLTRNLAAELGQyGIRVNLLAGGLLKTTDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSaAITG 253
Cdd:PRK09135  159 AKAALEMLTRSLALELAP-EVRVNAVAPGAILWPEDGNSFDEEARQAILARTPLKRIGTPEDIAEAVRFLLADAS-FITG 236

                  ....*...
gi 1918264442 254 QSIAVDGG 261
Cdd:PRK09135  237 QILAVDGG 244
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
9-262 1.93e-38

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 142.29  E-value: 1.93e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442   9 PAFLLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNsQEAADTVVADIvAAGGQAFAYQADVTELEQMQGMANEVTA 88
Cdd:PRK08324  417 PKPLAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLD-EEAAEAAAAEL-GGPDRALGVACDVTDEAAVQAAFEEAAL 494
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  89 RYGRIDILVNNAlpGYQFNPSADYTSIETvqwshFTQQIDGIVKGAVNAVQAVLPQMKAQKTGK--ILNISTNLVyNPVV 166
Cdd:PRK08324  495 AFGGVDIVVSNA--GIAISGPIEETSDED-----WRRSFDVNATGHFLVAREAVRIMKAQGLGGsiVFIASKNAV-NPGP 566
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 167 TYYDYTTAKSALIGLTRNLAAELGQYGIRVN------------LLAGGLLKTTDASR-LTTEAVFDYIATTTPLRQATSV 233
Cdd:PRK08324  567 NFGAYGAAKAAELHLVRQLALELGPDGIRVNgvnpdavvrgsgIWTGEWIEARAAAYgLSEEELEEFYRARNLLKREVTP 646
                         250       260
                  ....*....|....*....|....*....
gi 1918264442 234 DDFANSVLLMASDLSAAITGQSIAVDGGL 262
Cdd:PRK08324  647 EDVAEAVVFLASGLLSKTTGAIITVDGGN 675
PRK06172 PRK06172
SDR family oxidoreductase;
14-263 2.30e-38

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 134.88  E-value: 2.30e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVvADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRI 93
Cdd:PRK06172    7 GKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETV-ALIREAGGEALFVACDVTRDAEVKALVEQTIAAYGRL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  94 DILVNNALPGYQFNPSADYTSIEtvqwshFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNIST--NLVYNPVVTYydY 171
Cdd:PRK06172   86 DYAFNNAGIEIEQGRLAEGSEAE------FDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASvaGLGAAPKMSI--Y 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 172 TTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKtTDASRLTTEA---VFDYIATTTPLRQATSVDDFANSVLLMASDLS 248
Cdd:PRK06172  158 AASKHAVIGLTKSAAIEYAKKGIRVNAVCPAVID-TDMFRRAYEAdprKAEFAAAMHPVGRIGKVEEVASAVLYLCSDGA 236
                         250
                  ....*....|....*
gi 1918264442 249 AAITGQSIAVDGGLT 263
Cdd:PRK06172  237 SFTTGHALMVDGGAT 251
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
12-261 2.32e-38

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 135.41  E-value: 2.32e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNsQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK08277    8 LKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRN-QEKAEAVVAEIKAAGGEALAVKADVLDKESLEQARQQILEDFG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNA---LPGYQFNPSADYtSIETVQwSHFTQQIDGIVK-------GAVNAVQAVLPQMKAQKTGKILNISTNLV 161
Cdd:PRK08277   87 PCDILINGAggnHPKATTDNEFHE-LIEPTK-TFFDLDEEGFEFvfdlnllGTLLPTQVFAKDMVGRKGGNIINISSMNA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 162 YNPVVTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGG---------LLKTTDASrLTTEAvfDYIATTTPLRQATS 232
Cdd:PRK08277  165 FTPLTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGfflteqnraLLFNEDGS-LTERA--NKILAHTPMGRFGK 241
                         250       260       270
                  ....*....|....*....|....*....|
gi 1918264442 233 VDDFANSVLLMASDLSAA-ITGQSIAVDGG 261
Cdd:PRK08277  242 PEELLGTLLWLADEKASSfVTGVVLPVDGG 271
PRK12829 PRK12829
short chain dehydrogenase; Provisional
15-262 5.88e-38

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 134.03  E-value: 5.88e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNYLnSQEAADTVVADivAAGGQAFAYQADVTELEQMQGMANEVTARYGRID 94
Cdd:PRK12829   12 LRVLVTGGASGIGRAIAEAFAEAGARVHVCDV-SEAALAATAAR--LPGAKVTATVADVADPAQVERVFDTAVERFGGLD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  95 ILVNNAlpGYqFNPSADYTSIETVQWShftQQIDGIVKGAVNAVQAVLPQMKAQKTGK-ILNISTNlvyNPVVTY---YD 170
Cdd:PRK12829   89 VLVNNA--GI-AGPTGGIDEITPEQWE---QTLAVNLNGQFYFARAAVPLLKASGHGGvIIALSSV---AGRLGYpgrTP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 171 YTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASR-------LTTEAVF----DYIATTtPLRQATSVDDFANS 239
Cdd:PRK12829  160 YAASKWAVVGLVKSLAIELGPLGIRVNAILPGIVRGPRMRRviearaqQLGIGLDemeqEYLEKI-SLGRMVEPEDIAAT 238
                         250       260
                  ....*....|....*....|...
gi 1918264442 240 VLLMASDLSAAITGQSIAVDGGL 262
Cdd:PRK12829  239 ALFLASPAARYITGQAISVDGNV 261
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
15-261 7.02e-38

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 133.37  E-value: 7.02e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVaaggqaFAYQADVTELEQMQGMANEVTARYGRID 94
Cdd:PRK06463    8 KVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAENEAKELREKGV------FTIKCDVGNRDQVKKSKEVVEKEFGRVD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  95 ILVNNA-----LPGYQFNPSadytsietvqwsHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPV---V 166
Cdd:PRK06463   82 VLVNNAgimylMPFEEFDEE------------KYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIGTAaegT 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 167 TYYDYTtaKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT----TDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLL 242
Cdd:PRK06463  150 TFYAIT--KAGIIILTRRLAFELGKYGIRVNAVAPGWVETdmtlSGKSQEEAEKLRELFRNKTVLKTTGKPEDIANIVLF 227
                         250
                  ....*....|....*....
gi 1918264442 243 MASDLSAAITGQSIAVDGG 261
Cdd:PRK06463  228 LASDDARYITGQVIVADGG 246
PRK12827 PRK12827
short chain dehydrogenase; Provisional
12-262 1.10e-37

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 132.92  E-value: 1.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNS---QEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTA 88
Cdd:PRK12827    4 LDSRRVLITGGSGGLGRAIAVRLAADGADVIVLDIHPmrgRAEADAVAAGIEAAGGKALGLAFDVRDFAATRAALDAGVE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  89 RYGRIDILVNNAlpgyqfnPSADYTSIETVQWSHFTQQIDGIVKGAVNAVQAVL-PQMKAQKTGKILNISTNLVYNPVVT 167
Cdd:PRK12827   84 EFGRLDILVNNA-------GIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALpPMIRARRGGRIVNIASVAGVRGNRG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 168 YYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLtteAVFDYIATTTPLRQATSVDDFANSVLLMASDL 247
Cdd:PRK12827  157 QVNYAASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPMADNA---APTEHLLNPVPVQRLGEPDEVAALVAFLVSDA 233
                         250
                  ....*....|....*
gi 1918264442 248 SAAITGQSIAVDGGL 262
Cdd:PRK12827  234 ASYVTGQVIPVDGGF 248
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
12-264 2.32e-37

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 132.33  E-value: 2.32e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNsQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK13394    5 LNGKTAVVTGAASGIGKEIALELARAGAAVAIADLN-QDGANAVADEINKAGGKAIGVAMDVTNEDAVNAGIDKVAERFG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpGYQF-NPSADYTSietVQWSHFtQQIDgiVKGAVNAVQAVLPQM-KAQKTGKILNIST--NLVYNPVVT 167
Cdd:PRK13394   84 SVDILVSNA--GIQIvNPIENYSF---ADWKKM-QAIH--VDGAFLTTKAALKHMyKDDRGGVVIYMGSvhSHEASPLKS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 168 yyDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT--------TDASRL---TTEAVFDYIATTTPLRQATSVDDF 236
Cdd:PRK13394  156 --AYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTplvdkqipEQAKELgisEEEVVKKVMLGKTVDGVFTTVEDV 233
                         250       260
                  ....*....|....*....|....*...
gi 1918264442 237 ANSVLLMASDLSAAITGQSIAVDGGLTM 264
Cdd:PRK13394  234 AQTVLFLSSFPSAALTGQSFVVSHGWFM 261
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
12-264 3.61e-37

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 131.67  E-value: 3.61e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK12935    4 LNGKVAIVTGGAKGIGKAITVALAQEGAKVVINYNSSKEAAENLVNELGKEGHDVYAVQADVSKVEDANRLVEEAVNHFG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpgyQFNPSADYTSIETVQWShftQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDY 171
Cdd:PRK12935   84 KVDILVNNA----GITRDRTFKKLNREDWE---RVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFGQTNY 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 172 TTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLtTEAVFDYIATTTPLRQATSVDDFANSVLLMASDlSAAI 251
Cdd:PRK12935  157 SAAKAGMLGFTKSLALELAKTNVTVNAICPGFIDTEMVAEV-PEEVRQKIVAKIPKKRFGQADEIAKGVVYLCRD-GAYI 234
                         250
                  ....*....|...
gi 1918264442 252 TGQSIAVDGGLTM 264
Cdd:PRK12935  235 TGQQLNINGGLYM 247
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
15-261 5.65e-37

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: 130.47  E-value: 5.65e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRID 94
Cdd:cd05357     1 AVALVTGAAKRIGRAIAEALAAEGYRVVVHYNRSEAEAQRLKDELNALRNSAVLVQADLSDFAACADLVAAAFRAFGRCD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  95 ILVNNAlpgyqfnpSADYTSiETVQWSHftQQIDGIVKGAVNA----VQAVLPQMKAQKTGKILNISTNLVYNPVVTYYD 170
Cdd:cd05357    81 VLVNNA--------SAFYPT-PLGQGSE--DAWAELFGINLKApyllIQAFARRLAGSRNGSIINIIDAMTDRPLTGYFA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 171 YTTAKSALIGLTRNLAAELGQYgIRVNLLAGGLLKTTDASrltTEAVFDYIATTTPLRQATSVDDFANSVLLMASdlSAA 250
Cdd:cd05357   150 YCMSKAALEGLTRSAALELAPN-IRVNGIAPGLILLPEDM---DAEYRENALRKVPLKRRPSAEEIADAVIFLLD--SNY 223
                         250
                  ....*....|.
gi 1918264442 251 ITGQSIAVDGG 261
Cdd:cd05357   224 ITGQIIKVDGG 234
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
12-263 6.11e-37

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: 130.97  E-value: 6.11e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSqEAADTVVADIvaaGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:cd05341     3 LKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILD-EEGQAAAAEL---GDAARFFHLDVTDEDGWTAVVDTAREAFG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNA---LPGYqfnpsadytsIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTY 168
Cdd:cd05341    79 RLDVLVNNAgilTGGT----------VETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPAL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 169 YDYTTAKSALIGLTRNLAAELGQ--YGIRVNLLAGGLLKT--TDASRLTTEAVFDYiaTTTPLRQATSVDDFANSVLLMA 244
Cdd:cd05341   149 AAYNASKGAVRGLTKSAALECATqgYGIRVNSVHPGYIYTpmTDELLIAQGEMGNY--PNTPMGRAGEPDEIAYAVVYLA 226
                         250
                  ....*....|....*....
gi 1918264442 245 SDLSAAITGQSIAVDGGLT 263
Cdd:cd05341   227 SDESSFVTGSELVVDGGYT 245
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
12-261 1.10e-36

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: 130.20  E-value: 1.10e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSqEAADTVVADIvaaGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:cd05345     3 LEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINA-DGAERVAADI---GEAAIAIQADVTKRADVEAMVEAALSKFG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNALPGYQFNPSADYTSIEtvqwshFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDY 171
Cdd:cd05345    79 RLDILVNNAGITHRNKPMLEVDEEE------FDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGLRPRPGLTWY 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 172 TTAKSALIGLTRNLAAELGQYGIRVNLLA-----GGLLKTTDASRlTTEAVFDYIAtTTPLRQATSVDDFANSVLLMASD 246
Cdd:cd05345   153 NASKGWVVTATKAMAVELAPRNIRVNCLCpvageTPLLSMFMGED-TPENRAKFRA-TIPLGRLSTPDDIANAALYLASD 230
                         250
                  ....*....|....*
gi 1918264442 247 LSAAITGQSIAVDGG 261
Cdd:cd05345   231 EASFITGVALEVDGG 245
PRK09134 PRK09134
SDR family oxidoreductase;
15-261 2.76e-36

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 129.28  E-value: 2.76e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRID 94
Cdd:PRK09134   10 RAALVTGAARRIGRAIALDLAAHGFDVAVHYNRSRDEAEALAAEIRALGRRAVALQADLADEAEVRALVARASAALGPIT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  95 ILVNNAlpgyqfnpSA-DYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDYTT 173
Cdd:PRK09134   90 LLVNNA--------SLfEYDSAASFTRASWDRHMATNLRAPFVLAQAFARALPADARGLVVNMIDQRVWNLNPDFLSYTL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 174 AKSALIGLTRNLAAELGQYgIRVNLLAGGLlktTDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASdlSAAITG 253
Cdd:PRK09134  162 SKAALWTATRTLAQALAPR-IRVNAIGPGP---TLPSGRQSPEDFARQHAATPLGRGSTPEEIAAAVRYLLD--APSVTG 235

                  ....*...
gi 1918264442 254 QSIAVDGG 261
Cdd:PRK09134  236 QMIAVDGG 243
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
12-262 9.89e-36

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 128.26  E-value: 9.89e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNsQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK07097    8 LKGKIALITGASYGIGFAIAKAYAKAGATIVFNDIN-QELVDKGLAAYRELGIEAHGYVCDVTDEDGVQAMVSQIEKEVG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpGYqfnpsADYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNIS---TNLVYNPVVTy 168
Cdd:PRK07097   87 VIDILVNNA--GI-----IKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICsmmSELGRETVSA- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 169 ydYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT--TDASRLTTEAV----FD-YIATTTPLRQATSVDDFANSVL 241
Cdd:PRK07097  159 --YAAAKGGLKMLTKNIASEYGEANIQCNGIGPGYIATpqTAPLRELQADGsrhpFDqFIIAKTPAARWGDPEDLAGPAV 236
                         250       260
                  ....*....|....*....|.
gi 1918264442 242 LMASDLSAAITGQSIAVDGGL 262
Cdd:PRK07097  237 FLASDASNFVNGHILYVDGGI 257
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
14-261 1.37e-35

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: 127.45  E-value: 1.37e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRI 93
Cdd:cd08930     2 DKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKNRVIALELDITSKESIKELIESYLEKFGRI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  94 DILVNNALPgyqfNPSADYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNL------------- 160
Cdd:cd08930    82 DILINNAYP----SPKVWGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYgviapdfriyent 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 161 -VYNPVVtyydYTTAKSALIGLTRNLAAELGQYGIRVNLLA-GGLLKTTDasrlttEAVFDYIATTTPLRQATSVDDFAN 238
Cdd:cd08930   158 qMYSPVE----YSVIKAGIIHLTKYLAKYYADTGIRVNAISpGGILNNQP------SEFLEKYTKKCPLKRMLNPEDLRG 227
                         250       260
                  ....*....|....*....|...
gi 1918264442 239 SVLLMASDLSAAITGQSIAVDGG 261
Cdd:cd08930   228 AIIFLLSDASSYVTGQNLVIDGG 250
PRK07063 PRK07063
SDR family oxidoreductase;
12-264 2.37e-35

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 127.09  E-value: 2.37e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNS---QEAADTVVADIvaAGGQAFAYQADVTELEQMQGMANEVTA 88
Cdd:PRK07063    5 LAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAalaERAAAAIARDV--AGARVLAVPADVTDAASVAAAVAAAEE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  89 RYGRIDILVNNAlpgyQFNPSADYTSIETVQWSH-FTqqIDgiVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVT 167
Cdd:PRK07063   83 AFGPLDVLVNNA----GINVFADPLAMTDEDWRRcFA--VD--LDGAWNGCRAVLPGMVERGRGSIVNIASTHAFKIIPG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 168 YYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTdasrlTTEAVFDYIATTTPLRQAT----------SVDDFA 237
Cdd:PRK07063  155 CFPYPVAKHGLLGLTRALGIEYAARNVRVNAIAPGYIETQ-----LTEDWWNAQPDPAAARAETlalqpmkrigRPEEVA 229
                         250       260
                  ....*....|....*....|....*..
gi 1918264442 238 NSVLLMASDLSAAITGQSIAVDGGLTM 264
Cdd:PRK07063  230 MTAVFLASDEAPFINATCITIDGGRSV 256
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
12-263 3.20e-35

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: 126.42  E-value: 3.20e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVnyLNSQEAADTVVADIVAAGGQAFAYqADVTELEQMQGMANEVTARYG 91
Cdd:cd05326     2 LDGKVAIITGGASGIGEATARLFAKHGARVVI--ADIDDDAGQAVAAELGDPDISFVH-CDVTVEADVRAAVDTAVARFG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpGYQfnpSADYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDY 171
Cdd:cd05326    79 RLDIMFNNA--GVL---GAPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPHAY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 172 TTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT---TDASRLTTEAVFDYI-ATTTPLRQATSVDDFANSVLLMASDL 247
Cdd:cd05326   154 TASKHAVLGLTRSAATELGEHGIRVNCVSPYGVATpllTAGFGVEDEAIEEAVrGAANLKGTALRPEDIAAAVLYLASDD 233
                         250
                  ....*....|....*.
gi 1918264442 248 SAAITGQSIAVDGGLT 263
Cdd:cd05326   234 SRYVSGQNLVVDGGLT 249
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
13-265 4.48e-35

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 126.03  E-value: 4.48e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  13 LNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGR 92
Cdd:PRK12824    1 MKKIALVTGAKRGIGSAIARELLNDGYRVIATYFSGNDCAKDWFEEYGFTEDQVRLKELDVTDTEECAEALAEIEEEEGP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  93 IDILVNNAlpgyqfNPSADyTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDYT 172
Cdd:PRK12824   81 VDILVNNA------GITRD-SVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQFGQTNYS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 173 TAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEaVFDYIATTTPLRQATSVDDFANSVLLMASDLSAAIT 252
Cdd:PRK12824  154 AAKAGMIGFTKALASEGARYGITVNCIAPGYIATPMVEQMGPE-VLQSIVNQIPMKRLGTPEEIAAAVAFLVSEAAGFIT 232
                         250
                  ....*....|...
gi 1918264442 253 GQSIAVDGGLTMP 265
Cdd:PRK12824  233 GETISINGGLYMH 245
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
15-264 4.52e-35

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: 126.10  E-value: 4.52e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGAsvCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRID 94
Cdd:cd08937     5 KVVVVTGAAQGIGRGVAERLAGEGA--RVLLVDRSELVHEVLAEILAAGDAAHVHTADLETYAGAQGVVRAAVERFGRVD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  95 ILVNNAlPGYQFNPSADYTSIETVQwshftQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNpvVTYYDYTTA 174
Cdd:cd08937    83 VLINNV-GGTIWAKPYEHYEEEQIE-----AEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSIATRG--IYRIPYSAA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 175 KSALIGLTRNLAAELGQYGIRVNLLAGGLLKT------------TDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLL 242
Cdd:cd08937   155 KGGVNALTASLAFEHARDGIRVNAVAPGGTEApprkiprnaapmSEQEKVWYQRIVDQTLDSSLMGRYGTIDEQVRAILF 234
                         250       260
                  ....*....|....*....|..
gi 1918264442 243 MASDLSAAITGQSIAVDGGLTM 264
Cdd:cd08937   235 LASDEASYITGTVLPVGGGDLG 256
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
12-261 6.79e-35

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: 126.03  E-value: 6.79e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNsQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:cd08935     3 LKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRN-QEKGDKVAKEITALGGRAIALAADVLDRASLERAREEIVAQFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNA---LPG-------YQFNPSADYTSIETVQWSHFTqqiDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLV 161
Cdd:cd08935    82 TVDILINGAggnHPDattdpehYEPETEQNFFDLDEEGWEFVF---DLNLNGSFLPSQVFGKDMLEQKGGSIINISSMNA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 162 YNPVVTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGG---------LLKTTDASrLTTEAvfDYIATTTPLRQATS 232
Cdd:cd08935   159 FSPLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGffvtpqnrkLLINPDGS-YTDRS--NKILGRTPMGRFGK 235
                         250       260       270
                  ....*....|....*....|....*....|
gi 1918264442 233 VDDFANSVLLMASDL-SAAITGQSIAVDGG 261
Cdd:cd08935   236 PEELLGALLFLASEKaSSFVTGVVIPVDGG 265
PRK06138 PRK06138
SDR family oxidoreductase;
12-263 7.48e-35

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 125.65  E-value: 7.48e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVnyLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK06138    3 LAGRVAIVTGAGSGIGRATAKLFAREGARVVV--ADRDAEAAERVAAAIAAGGRAFARQGDVGSAEAVEALVDFVAARWG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpgyQFNPSADYTSIETVQWSHFtqqIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDY 171
Cdd:PRK06138   81 RLDVLVNNA----GFGCGGTVVTTDEADWDAV---MRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGRAAY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 172 TTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTT-----EAVFDYIATTTPLRQATSVDDFANSVLLMASD 246
Cdd:PRK06138  154 VASKGAIASLTRAMALDHATDGIRVNAVAPGTIDTPYFRRIFArhadpEALREALRARHPMNRFGTAEEVAQAALFLASD 233
                         250
                  ....*....|....*..
gi 1918264442 247 LSAAITGQSIAVDGGLT 263
Cdd:PRK06138  234 ESSFATGTTLVVDGGWL 250
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
15-254 9.69e-35

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: 125.20  E-value: 9.69e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEA-----------ADTVVADIVAAGGQAFAYQADVTELEQMQGMA 83
Cdd:cd05338     4 KVAFVTGASRGIGRAIALRLAKAGATVVVAAKTASEGdngsakslpgtIEETAEEIEAAGGQALPIVVDVRDEDQVRALV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  84 NEVTARYGRIDILVNNAlpgyqfnPSADYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYN 163
Cdd:cd05338    84 EATVDQFGRLDILVNNA-------GAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLSLR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 164 PVVTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLA-GGLLKTTDASRLTTEAVFDyiatttplrQATSVDDFANSVLL 242
Cdd:cd05338   157 PARGDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWpSTAIETPAATELSGGSDPA---------RARSPEILSDAVLA 227
                         250
                  ....*....|..
gi 1918264442 243 MASDLSAAITGQ 254
Cdd:cd05338   228 ILSRPAAERTGL 239
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
11-261 9.97e-35

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


Pssm-ID: 440388 [Multi-domain]  Cd Length: 254  Bit Score: 125.14  E-value: 9.97e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  11 FLLNKVVIVTGA--SRGLGAQIAQKMAGAGASVCVNYLNsqEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTA 88
Cdd:COG0623     2 LLKGKRGLITGVanDRSIAWGIAKALHEEGAELAFTYQG--EALKKRVEPLAEELGSALVLPCDVTDDEQIDALFDEIKE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  89 RYGRIDILV-------NNALPGyqfnpsaDYTsieTVQWSHFTQQIDgivkgaVNA------VQAVLPQMKAQktGKILN 155
Cdd:COG0623    80 KWGKLDFLVhsiafapKEELGG-------RFL---DTSREGFLLAMD------ISAyslvalAKAAEPLMNEG--GSIVT 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 156 IStnlvY---NPVVTYYDY-TTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTT-EAVFDYIATTTPLRQA 230
Cdd:COG0623   142 LT----YlgaERVVPNYNVmGVAKAALEASVRYLAADLGPKGIRVNAISAGPIKTLAASGIPGfDKLLDYAEERAPLGRN 217
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1918264442 231 TSVDDFANSVLLMASDLSAAITGQSIAVDGG 261
Cdd:COG0623   218 VTIEEVGNAAAFLLSDLASGITGEIIYVDGG 248
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
12-263 6.47e-34

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: 123.21  E-value: 6.47e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYlNSQEAADTVVADIVAAGG-QAFAYQADVTELEQMQGMANEVTARY 90
Cdd:cd05352     6 LKGKVAIVTGGSRGIGLAIARALAEAGADVAIIY-NSAPRAEEKAEELAKKYGvKTKAYKCDVSSQESVEKTFKQIQKDF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  91 GRIDILVNNAlpGYQFNPSADYTSIEtvQWsHFTQQIDgiVKGAVNAVQAVLPQMKAQKTGKILNIS--TNLVYNPVVTY 168
Cdd:cd05352    85 GKIDILIANA--GITVHKPALDYTYE--QW-NKVIDVN--LNGVFNCAQAAAKIFKKQGKGSLIITAsmSGTIVNRPQPQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 169 YDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKtTDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLS 248
Cdd:cd05352   158 AAYNASKAAVIHLAKSLAVEWAKYFIRVNSISPGYID-TDLTDFVDKELRKKWESYIPLKRIALPEELVGAYLYLASDAS 236
                         250
                  ....*....|....*
gi 1918264442 249 AAITGQSIAVDGGLT 263
Cdd:cd05352   237 SYTTGSDLIIDGGYT 251
PRK06484 PRK06484
short chain dehydrogenase; Validated
15-263 9.56e-34

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 127.66  E-value: 9.56e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAadtvVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRID 94
Cdd:PRK06484  270 RVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGA----KKLAEALGDEHLSVQADITDEAAVESAFAQIQARWGRLD 345
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  95 ILVNNALPGYQFNPSADytsiETVQwsHFTQQIDGIVKGAVNAVQAVLPQMKaqKTGKILNISTNLVYNPVVTYYDYTTA 174
Cdd:PRK06484  346 VLVNNAGIAEVFKPSLE----QSAE--DFTRVYDVNLSGAFACARAAARLMS--QGGVIVNLGSIASLLALPPRNAYCAS 417
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 175 KSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRL--TTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSAAIT 252
Cdd:PRK06484  418 KAAVTMLSRSLACEWAPAGIRVNTVAPGYIETPAVLALkaSGRADFDSIRRRIPLGRLGDPEEVAEAIAFLASPAASYVN 497
                         250
                  ....*....|.
gi 1918264442 253 GQSIAVDGGLT 263
Cdd:PRK06484  498 GATLTVDGGWT 508
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
14-262 1.58e-33

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 122.14  E-value: 1.58e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNsQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRI 93
Cdd:PRK08643    2 SKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYN-EETAQAAADKLSKDGGKAIAVKADVSDRDQVFAAVRQVVDTFGDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  94 DILVNNALPGyqfnPSadyTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQK-TGKILNISTN--LVYNPVVTYYD 170
Cdd:PRK08643   81 NVVVNNAGVA----PT---TPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGhGGKIINATSQagVVGNPELAVYS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 171 YTtaKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT---TDASRLTTEAV-------FDYIATTTPLRQATSVDDFANSV 240
Cdd:PRK08643  154 ST--KFAVRGLTQTAARDLASEGITVNAYAPGIVKTpmmFDIAHQVGENAgkpdewgMEQFAKDITLGRLSEPEDVANCV 231
                         250       260
                  ....*....|....*....|..
gi 1918264442 241 LLMASDLSAAITGQSIAVDGGL 262
Cdd:PRK08643  232 SFLAGPDSDYITGQTIIVDGGM 253
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
12-261 2.10e-33

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: 121.75  E-value: 2.10e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVAdIVAAGG---QAFAYQADVTELEQMQGMANEVTA 88
Cdd:cd05364     1 LSGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQS-CLQAGVsekKILLVVADLTEEEGQDRIISTTLA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  89 RYGRIDILVNNA---LPGyqfnpsadytSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKtGKILNISTNLVYNPV 165
Cdd:cd05364    80 KFGRLDILVNNAgilAKG----------GGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTK-GEIVNVSSVAGGRSF 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 166 VTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRL-----TTEAVFDYIATTTPLRQATSVDDFANSV 240
Cdd:cd05364   149 PGVLYYCISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHRRMgmpeeQYIKFLSRAKETHPLGRPGTVDEVAEAI 228
                         250       260
                  ....*....|....*....|.
gi 1918264442 241 LLMASDLSAAITGQSIAVDGG 261
Cdd:cd05364   229 AFLASDASSFITGQLLPVDGG 249
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
14-263 2.16e-33

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: 121.79  E-value: 2.16e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAA-GGQAFAYQADVTELEQMQGMANEVTARYGR 92
Cdd:cd08940     2 GKVALVTGSTSGIGLGIARALAAAGANIVLNGFGDAAEIEAVRAGLAAKhGVKVLYHGADLSKPAAIEDMVAYAQRQFGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  93 IDILVNNAlpGYQFnpsadYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTnlVYNPV--VTYYD 170
Cdd:cd08940    82 VDILVNNA--GIQH-----VAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIAS--VHGLVasANKSA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 171 YTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT----------TDASRLTTEAVF-DYIATTTPLRQATSVDDFANS 239
Cdd:cd08940   153 YVAAKHGVVGLTKVVALETAGTGVTCNAICPGWVLTplvekqisalAQKNGVPQEQAArELLLEKQPSKQFVTPEQLGDT 232
                         250       260
                  ....*....|....*....|....
gi 1918264442 240 VLLMASDLSAAITGQSIAVDGGLT 263
Cdd:cd08940   233 AVFLASDAASQITGTAVSVDGGWT 256
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
12-261 2.46e-33

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 121.77  E-value: 2.46e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQeaADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK06935   13 LDGKVAIVTGGNTGLGQGYAVALAKAGADIIITTHGTN--WDETRRLIEKEGRKVTFVQVDLTKPESAEKVVKEALEEFG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpG-YQFNPSADYTSIEtvqWSHftqqidgIVKGAVNAV----QAVLPQMKAQKTGKILNISTNLVYNPVV 166
Cdd:PRK06935   91 KIDILVNNA--GtIRRAPLLEYKDED---WNA-------VMDINLNSVyhlsQAVAKVMAKQGSGKIINIASMLSFQGGK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 167 TYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT--TDASRlTTEAVFDYIATTTPLRQATSVDDFANSVLLMA 244
Cdd:PRK06935  159 FVPAYTASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKTanTAPIR-ADKNRNDEILKRIPAGRWGEPDDLMGAAVFLA 237
                         250
                  ....*....|....*..
gi 1918264442 245 SDLSAAITGQSIAVDGG 261
Cdd:PRK06935  238 SRASDYVNGHILAVDGG 254
PRK06123 PRK06123
SDR family oxidoreductase;
14-261 2.48e-33

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 121.42  E-value: 2.48e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRI 93
Cdd:PRK06123    2 RKVMIITGASRGIGAATALLAAERGYAVCLNYLRNRDAAEAVVQAIRRQGGEALAVAADVADEADVLRLFEAVDRELGRL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  94 DILVNNAlpgYQFNPSADYTSIETVQWSH-FTQQIDGIVKGAVNAVQAVLPQmKAQKTGKILNISTNLVY-NPVVTYYDY 171
Cdd:PRK06123   82 DALVNNA---GILEAQMRLEQMDAARLTRiFATNVVGSFLCAREAVKRMSTR-HGGRGGAIVNVSSMAARlGSPGEYIDY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 172 TTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSAAI 251
Cdd:PRK06123  158 AASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEIHASGGEPGRVDRVKAGIPMGRGGTAEEVARAILWLLSDEASYT 237
                         250
                  ....*....|
gi 1918264442 252 TGQSIAVDGG 261
Cdd:PRK06123  238 TGTFIDVSGG 247
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
16-265 3.28e-33

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: 121.42  E-value: 3.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  16 VVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRIDI 95
Cdd:cd05337     3 VAIVTGASRGIGRAIATELAARGFDIAINDLPDDDQATEVVAEVLAAGRRAIYFQADIGELSDHEALLDQAWEDFGRLDC 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  96 LVNNAlpGYQFNPSADYTSIETvqwSHFTQQIDGIVKGAVNAVQAVLPQMKAQKT------GKILNISTNLVYNPVVTYY 169
Cdd:cd05337    83 LVNNA--GIAVRPRGDLLDLTE---DSFDRLIAINLRGPFFLTQAVARRMVEQPDrfdgphRSIIFVTSINAYLVSPNRG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 170 DYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKtTDASRLTTEAVFDYIAT-TTPLRQATSVDDFANSVLLMASDLS 248
Cdd:cd05337   158 EYCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIH-TDMTAPVKEKYDELIAAgLVPIRRWGQPEDIAKAVRTLASGLL 236
                         250
                  ....*....|....*..
gi 1918264442 249 AAITGQSIAVDGGLTMP 265
Cdd:cd05337   237 PYSTGQPINIDGGLSMR 253
PRK06180 PRK06180
short chain dehydrogenase; Provisional
14-231 4.59e-33

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 121.56  E-value: 4.59e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVcVNYLNSQEAadtvVADIVA-AGGQAFAYQADVTELEQMQGMANEVTARYGR 92
Cdd:PRK06180    4 MKTWLITGVSSGFGRALAQAALAAGHRV-VGTVRSEAA----RADFEAlHPDRALARLLDVTDFDAIDAVVADAEATFGP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  93 IDILVNNALPGYQfnpsadyTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNIST--NLVYNPVVTYYD 170
Cdd:PRK06180   79 IDVLVNNAGYGHE-------GAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSmgGLITMPGIGYYC 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1918264442 171 YTtaKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEA---VFDYIATTTPLRQAT 231
Cdd:PRK06180  152 GS--KFALEGISESLAKEVAPFGIHVTAVEPGSFRTDWAGRSMVRTprsIADYDALFGPIRQAR 213
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
12-261 6.53e-33

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: 120.72  E-value: 6.53e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYlNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:cd08936     8 LANKVALVTASTDGIGLAIARRLAQDGAHVVVSS-RKQQNVDRAVATLQGEGLSVTGTVCHVGKAEDRERLVATAVNLHG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNALPGYQFNPSADYTsiETVqWShftQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDY 171
Cdd:cd08936    87 GVDILVSNAAVNPFFGNILDST--EEV-WD---KILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAAFHPFPGLGPY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 172 TTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRL-TTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSAA 250
Cdd:cd08936   161 NVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSSALwMDKAVEESMKETLRIRRLGQPEDCAGIVSFLCSEDASY 240
                         250
                  ....*....|.
gi 1918264442 251 ITGQSIAVDGG 261
Cdd:cd08936   241 ITGETVVVGGG 251
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
12-261 9.45e-33

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: 120.47  E-value: 9.45e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLN-SQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARY 90
Cdd:cd05355    24 LKGKKALITGGDSGIGRAVAIAFAREGADVAINYLPeEEDDAEETKKLIEEEGRKCLLIPGDLGDESFCRDLVKEVVKEF 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  91 GRIDILVNNAlpGYQFnPSADYTSIETVQWSHfTQQIDgiVKGAVNAVQAVLPQMKaqKTGKILNISTNLVYNPVVTYYD 170
Cdd:cd05355   104 GKLDILVNNA--AYQH-PQESIEDITTEQLEK-TFRTN--IFSMFYLTKAALPHLK--KGSSIINTTSVTAYKGSPHLLD 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 171 YTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTT-DASRLTTEAVFDYiATTTPLRQATSVDDFANSVLLMASDLSA 249
Cdd:cd05355   176 YAATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPlIPSSFPEEKVSEF-GSQVPMGRAGQPAEVAPAYVFLASQDSS 254
                         250
                  ....*....|..
gi 1918264442 250 AITGQSIAVDGG 261
Cdd:cd05355   255 YVTGQVLHVNGG 266
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
14-264 9.87e-33

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 119.99  E-value: 9.87e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVCvnylnsqeAADTVVADivAAGGQAFAYQADVTELEQMQGMANEVTARYGRI 93
Cdd:PRK08220    8 GKTVWVTGAAQGIGYAVALAFVEAGAKVI--------GFDQAFLT--QEDYPFATFVLDVSDAAAVAQVCQRLLAETGPL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  94 DILVNNAlpGYQFNPSADYTSIEtvQWShftQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDYTT 173
Cdd:PRK08220   78 DVLVNAA--GILRMGATDSLSDE--DWQ---QTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAAHVPRIGMAAYGA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 174 AKSALIGLTRNLAAELGQYGIRVNLLAGG---------LLKTTDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMA 244
Cdd:PRK08220  151 SKAALTSLAKCVGLELAPYGVRCNVVSPGstdtdmqrtLWVDEDGEQQVIAGFPEQFKLGIPLGKIARPQEIANAVLFLA 230
                         250       260
                  ....*....|....*....|
gi 1918264442 245 SDLSAAITGQSIAVDGGLTM 264
Cdd:PRK08220  231 SDLASHITLQDIVVDGGATL 250
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
12-263 1.70e-32

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 119.73  E-value: 1.70e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVcvnylnsqeaadtVVADIVAAGGQA---FAYQADVTELEQMQGMANEVTA 88
Cdd:PRK06171    7 LQGKIIIVTGGSSGIGLAIVKELLANGANV-------------VNADIHGGDGQHenyQFVPTDVSSAEEVNHTVAEIIE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  89 RYGRIDILVNNA---LPGY---QFNPSADYTSIETVqwshFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVY 162
Cdd:PRK06171   74 KFGRIDGLVNNAginIPRLlvdEKDPAGKYELNEAA----FDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 163 NPVVTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVFDYI--------------ATTTPLR 228
Cdd:PRK06171  150 EGSEGQSCYAATKAALNSFTRSWAKELGKHNIRVVGVAPGILEATGLRTPEYEEALAYTrgitveqlragytkTSTIPLG 229
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1918264442 229 QATSVDDFANSVLLMASDLSAAITGQSIAVDGGLT 263
Cdd:PRK06171  230 RSGKLSEVADLVCYLLSDRASYITGVTTNIAGGKT 264
PRK07074 PRK07074
SDR family oxidoreductase;
14-263 3.68e-32

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 118.72  E-value: 3.68e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSqEAADTVVADIVAAGgqAFAYQADVTELEQMQGMANEVTARYGRI 93
Cdd:PRK07074    2 KRTALVTGAAGGIGQALARRFLAAGDRVLALDIDA-AALAAFADALGDAR--FVPVACDLTDAASLAAALANAAAERGPV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  94 DILVNNAlpgyqfnPSADYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNI-STNLVYnpVVTYYDYT 172
Cdd:PRK07074   79 DVLVANA-------GAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIgSVNGMA--ALGHPAYS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 173 TAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTT--DASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSAA 250
Cdd:PRK07074  150 AAKAGLIHYTKLLAVEYGRFGIRANAVAPGTVKTQawEARVAANPQVFEELKKWYPLQDFATPDDVANAVLFLASPAARA 229
                         250
                  ....*....|...
gi 1918264442 251 ITGQSIAVDGGLT 263
Cdd:PRK07074  230 ITGVCLPVDGGLT 242
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
15-206 7.89e-32

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: 117.33  E-value: 7.89e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGasvcvnylnsqeaaDTVVA----------DIVAAGGQAFAYQADVTELEQMQGMAN 84
Cdd:cd05374     1 KVVLITGCSSGIGLALALALAAQG--------------YRVIAtarnpdklesLGELLNDNLEVLELDVTDEESIKAAVK 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  85 EVTARYGRIDILVNNAlpGY-QFNPSADyTSIETVQwshftQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYN 163
Cdd:cd05374    67 EVIERFGRIDVLVNNA--GYgLFGPLEE-TSIEEVR-----ELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLV 138
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1918264442 164 PVVTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT 206
Cdd:cd05374   139 PTPFLGPYCASKAALEALSESLRLELAPFGIKVTIIEPGPVRT 181
PRK12828 PRK12828
short chain dehydrogenase; Provisional
15-265 8.67e-32

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 117.20  E-value: 8.67e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVvADIVAAGGQAFAyqADVTELEQMQGMANEVTARYGRID 94
Cdd:PRK12828    8 KVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTL-PGVPADALRIGG--IDLVDPQAARRAVDEVNRQFGRLD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  95 ILVNNAlpgyqfnPSADYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDYTTA 174
Cdd:PRK12828   85 ALVNIA-------GAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAGPGMGAYAAA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 175 KSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVFDYIATttplrqatsVDDFANSVLLMASDLSAAITGQ 254
Cdd:PRK12828  158 KAGVARLTEALAAELLDRGITVNAVLPSIIDTPPNRADMPDADFSRWVT---------PEQIAAVIAFLLSDEAQAITGA 228
                         250
                  ....*....|.
gi 1918264442 255 SIAVDGGLTMP 265
Cdd:PRK12828  229 SIPVDGGVALP 239
PRK07478 PRK07478
short chain dehydrogenase; Provisional
12-261 1.13e-31

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 117.34  E-value: 1.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNyLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK07478    4 LNGKVAIITGASSGIGRAAAKLFAREGAKVVVG-ARRQAELDQLVAEIRAEGGEAVALAGDVRDEAYAKALVALAVERFG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNALPGYQFNPSADytsIETVQWSHftqQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYN---PVVTy 168
Cdd:PRK07478   83 GLDIAFNNAGTLGEMGPVAE---MSLEGWRE---TLATNLTSAFLGAKHQIPAMLARGGGSLIFTSTFVGHTagfPGMA- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 169 yDYTTAKSALIGLTRNLAAELGQYGIRVN-LLAGGLLktTDASRL--TTEAVFDYIATTTPLRQATSVDDFANSVLLMAS 245
Cdd:PRK07478  156 -AYAASKAGLIGLTQVLAAEYGAQGIRVNaLLPGGTD--TPMGRAmgDTPEALAFVAGLHALKRMAQPEEIAQAALFLAS 232
                         250
                  ....*....|....*.
gi 1918264442 246 DLSAAITGQSIAVDGG 261
Cdd:PRK07478  233 DAASFVTGTALLVDGG 248
PRK08628 PRK08628
SDR family oxidoreductase;
12-263 2.85e-31

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 116.21  E-value: 2.85e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVnyLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK08628    5 LKDKVVIVTGGASGIGAAISLRLAEEGAIPVI--FGRSAPDDEFAEELRALQPRAEFVQVDLTDDAQCRDAVEQTVAKFG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpGYQFNPSADYT------SIETVQWSHFTQqidgivkgavnaVQAVLPQMKAQKtGKILNISTNLVYNPV 165
Cdd:PRK08628   83 RIDGLVNNA--GVNDGVGLEAGreafvaSLERNLIHYYVM------------AHYCLPHLKASR-GAIVNISSKTALTGQ 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 166 VTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGG-----LLKTTDASRLTTEAVFDYIATTTPL-RQATSVDDFANS 239
Cdd:PRK08628  148 GGTSGYAAAKGAQLALTREWAVALAKDGVRVNAVIPAevmtpLYENWIATFDDPEAKLAAITAKIPLgHRMTTAEEIADT 227
                         250       260
                  ....*....|....*....|....
gi 1918264442 240 VLLMASDLSAAITGQSIAVDGGLT 263
Cdd:PRK08628  228 AVFLLSERSSHTTGQWLFVDGGYV 251
PRK06841 PRK06841
short chain dehydrogenase; Provisional
1-263 3.41e-31

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 115.91  E-value: 3.41e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442   1 MTQTNAVIPAFLLN-KVVIVTGASRGLGAQIAQKMAGAGASVCVnyLNSQEAADTVVADIvaAGGQAFAYQADVTELEQM 79
Cdd:PRK06841    1 MTDTKQFDLAFDLSgKVAVVTGGASGIGHAIAELFAAKGARVAL--LDRSEDVAEVAAQL--LGGNAKGLVCDVSDSQSV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  80 QGMANEVTARYGRIDILVNNALPGYqFNPSADYTsieTVQWSHfTQQIDgiVKGAVNAVQAVLPQMKAQKTGKILNISTN 159
Cdd:PRK06841   77 EAAVAAVISAFGRIDILVNSAGVAL-LAPAEDVS---EEDWDK-TIDIN--LKGSFLMAQAVGRHMIAAGGGKIVNLASQ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 160 LVYNPVVTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVFDYIATTTPLRQATSVDDFANS 239
Cdd:PRK06841  150 AGVVALERHVAYCASKAGVVGMTKVLALEWGPYGITVNAISPTVVLTELGKKAWAGEKGERAKKLIPAGRFAYPEEIAAA 229
                         250       260
                  ....*....|....*....|....
gi 1918264442 240 VLLMASDLSAAITGQSIAVDGGLT 263
Cdd:PRK06841  230 ALFLASDAAAMITGENLVIDGGYT 253
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
17-264 3.60e-31

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: 115.64  E-value: 3.60e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  17 VIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAAdtvvadivAAGGQAFAYQADVTELEQMQGMANEVTARYGRIDIL 96
Cdd:cd05331     1 VIVTGAAQGIGRAVARHLLQAGATVIALDLPFVLLL--------EYGDPLRLTPLDVADAAAVREVCSRLLAEHGPIDAL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  97 VNNAlpGYQFNPSADYTSIEtvQWShftQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDYTTAKS 176
Cdd:cd05331    73 VNCA--GVLRPGATDPLSTE--DWE---QTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRISMAAYGASKA 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 177 ALIGLTRNLAAELGQYGIRVNLLAGGllkTTDASRLTTEAVFDYIATTT------------PLRQATSVDDFANSVLLMA 244
Cdd:cd05331   146 ALASLSKCLGLELAPYGVRCNVVSPG---STDTAMQRTLWHDEDGAAQViagvpeqfrlgiPLGKIAQPADIANAVLFLA 222
                         250       260
                  ....*....|....*....|
gi 1918264442 245 SDLSAAITGQSIAVDGGLTM 264
Cdd:cd05331   223 SDQAGHITMHDLVVDGGATL 242
23BDH TIGR02415
acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is ...
15-262 5.32e-31

acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is described as able to interconvert acetoin + NADH with meso-2,3-butanediol + NAD(+). It is also called capable of irreversible reduction of diacetyl with NADH to acetoin. Blomqvist, et al. decline to specify either EC 1.1.1.4 which is (R,R)-butanediol dehydrogenase, or EC 1.1.1.5, which is acetoin dehydrogenase without a specified stereochemistry, for this enzyme. This enzyme is a homotetramer in the family of short chain dehydrogenases (pfam00106). Another member of this family, from Corynebacterium glutamicum, is called L-2,3-butanediol dehydrogenase (). [Energy metabolism, Fermentation]


Pssm-ID: 131468 [Multi-domain]  Cd Length: 254  Bit Score: 115.63  E-value: 5.32e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVvADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRID 94
Cdd:TIGR02415   1 KVALVTGGAQGIGKGIAERLAKDGFAVAVADLNEETAKETA-KEINQAGGKAVAYKLDVSDKDQVFSAIDQAAEKFGGFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  95 ILVNNAlpgyqfnPSADYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKT-GKILNIST--NLVYNPVVTYYdy 171
Cdd:TIGR02415  80 VMVNNA-------GVAPITPILEITEEELKKVYNVNVKGVLFGIQAAARQFKKQGHgGKIINAASiaGHEGNPILSAY-- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 172 TTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAV----------FDYIATTTPLRQATSVDDFANSVL 241
Cdd:TIGR02415 151 SSTKFAVRGLTQTAAQELAPKGITVNAYCPGIVKTPMWEEIDEETSeiagkpigegFEEFSSEIALGRPSEPEDVAGLVS 230
                         250       260
                  ....*....|....*....|.
gi 1918264442 242 LMASDLSAAITGQSIAVDGGL 262
Cdd:TIGR02415 231 FLASEDSDYITGQSILVDGGM 251
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
15-261 5.51e-31

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: 115.27  E-value: 5.51e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVcvnYLNSQEA-ADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRI 93
Cdd:cd08942     7 KIVLVTGGSRGIGRMIAQGFLEAGARV---IISARKAeACADAAEELSAYGECIAIPADLSSEEGIEALVARVAERSDRL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  94 DILVNNALPGYQfnpsadyTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMK----AQKTGKILNI-STNLVYNPVVTY 168
Cdd:cd08942    84 DVLVNNAGATWG-------APLEAFPESGWDKVMDINVKSVFFLTQALLPLLRaaatAENPARVINIgSIAGIVVSGLEN 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 169 YDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLL--KTTdASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASD 246
Cdd:cd08942   157 YSYGASKAAVHQLTRKLAKELAGEHITVNAIAPGRFpsKMT-AFLLNDPAALEAEEKSIPLGRWGRPEDMAGLAIMLASR 235
                         250
                  ....*....|....*
gi 1918264442 247 LSAAITGQSIAVDGG 261
Cdd:cd08942   236 AGAYLTGAVIPVDGG 250
PRK07856 PRK07856
SDR family oxidoreductase;
12-265 6.20e-31

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 115.42  E-value: 6.20e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAaggqafayqADVTELEQMQGMANEVTARYG 91
Cdd:PRK07856    4 LTGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRAPETVDGRPAEFHA---------ADVRDPDQVAALVDAIVERHG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlPGYQFNPSADYTsietvqwSHFTQQIDGI-VKGAVNAVQAVLPQMKAQKT-GKILNISTNLVYNPVVTYY 169
Cdd:PRK07856   75 RLDVLVNNA-GGSPYALAAEAS-------PRFHEKIVELnLLAPLLVAQAANAVMQQQPGgGSIVNIGSVSGRRPSPGTA 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 170 DYTTAKSALIGLTRNLAAELGQyGIRVNLLAGGLLKtTDASRLT--TEAVFDYIATTTPLRQATSVDDFANSVLLMASDL 247
Cdd:PRK07856  147 AYGAAKAGLLNLTRSLAVEWAP-KVRVNAVVVGLVR-TEQSELHygDAEGIAAVAATVPLGRLATPADIAWACLFLASDL 224
                         250
                  ....*....|....*...
gi 1918264442 248 SAAITGQSIAVDGGLTMP 265
Cdd:PRK07856  225 ASYVSGANLEVHGGGERP 242
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
14-261 1.43e-30

(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: 114.34  E-value: 1.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVCVNYL--------NSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMAne 85
Cdd:cd05353     5 GRVVLVTGAGGGLGRAYALAFAERGAKVVVNDLggdrkgsgKSSSAADKVVDEIKAAGGKAVANYDSVEDGEKIVKTA-- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  86 vTARYGRIDILVNNA--LPGYQFNPS--ADYTSIETVQwshftqqidgiVKGAVNAVQAVLPQMKAQKTGKILNISTNLV 161
Cdd:cd05353    83 -IDAFGRVDILVNNAgiLRDRSFAKMseEDWDLVMRVH-----------LKGSFKVTRAAWPYMRKQKFGRIINTSSAAG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 162 YNPVVTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAggllkTTDASRLtTEAVFDYiatttPLRQATSVDDFANSVL 241
Cdd:cd05353   151 LYGNFGQANYSAAKLGLLGLSNTLAIEGAKYNITCNTIA-----PAAGSRM-TETVMPE-----DLFDALKPEYVAPLVL 219
                         250       260
                  ....*....|....*....|
gi 1918264442 242 LMASDLSaAITGQSIAVDGG 261
Cdd:cd05353   220 YLCHESC-EVTGGLFEVGAG 238
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
12-242 1.63e-30

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: 114.22  E-value: 1.63e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNsQEAADTVVADIVAAGG-QAFAYQADVTELEQMQGMANEVTARY 90
Cdd:cd05332     1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARR-EERLEEVKSECLELGApSPHVVPLDMSDLEDAEQVVEEALKLF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  91 GRIDILVNNALpGYQFNPsADYTSIETVQWShftqqIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYD 170
Cdd:cd05332    80 GGLDILINNAG-ISMRSL-FHDTSIDVDRKI-----MEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTA 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1918264442 171 YTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLL 242
Cdd:cd05332   153 YAASKHALQGFFDSLRAELSEPNISVTVVCPGLIDTNIAMNALSGDGSMSAKMDDTTANGMSPEECALEILK 224
PRK07069 PRK07069
short chain dehydrogenase; Validated
19-262 1.69e-30

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 114.04  E-value: 1.69e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  19 VTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQ--AFAYQADVTELEQMQGMANEVTARYGRIDIL 96
Cdd:PRK07069    4 ITGAAGGLGRAIARRMAEQGAKVFLTDINDAAGLDAFAAEINAAHGEgvAFAAVQDVTDEAQWQALLAQAADAMGGLSVL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  97 VNNALPGYQFNPsadyTSIETVQWSH-FTQQIDGIVKGAvnavQAVLPQMKAQKTGKILNIST--NLVYNPvvTYYDYTT 173
Cdd:PRK07069   84 VNNAGVGSFGAI----EQIELDEWRRvMAINVESIFLGC----KHALPYLRASQPASIVNISSvaAFKAEP--DYTAYNA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 174 AKSALIGLTRNLAAELG--QYGIRVNLLAGGLLKT----TDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDL 247
Cdd:PRK07069  154 SKAAVASLTKSIALDCArrGLDVRCNSIHPTFIRTgivdPIFQRLGEEEATRKLARGVPLGRLGEPDDVAHAVLYLASDE 233
                         250
                  ....*....|....*
gi 1918264442 248 SAAITGQSIAVDGGL 262
Cdd:PRK07069  234 SRFVTGAELVIDGGI 248
PRK05650 PRK05650
SDR family oxidoreductase;
17-214 2.89e-30

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 113.98  E-value: 2.89e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  17 VIVTGASRGLGAQIAQKMAGAGASVCVNYLNsQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRIDIL 96
Cdd:PRK05650    3 VMITGAASGLGRAIALRWAREGWRLALADVN-EEGGEETLKLLREAGGDGFYQRCDVRDYSQLTALAQACEEKWGGIDVI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  97 VNNAlpGYQFNPSADYTSIETVQWshftqQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDYTTAKS 176
Cdd:PRK05650   82 VNNA--GVASGGFFEELSLEDWDW-----QIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAMSSYNVAKA 154
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1918264442 177 ALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTT 214
Cdd:PRK05650  155 GVVALSETLLVELADDEIGVHVVCPSFFQTNLLDSFRG 192
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
14-261 4.07e-30

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 113.50  E-value: 4.07e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVCVnyLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRI 93
Cdd:PRK12823    8 GKVVVVTGAAQGIGRGVALRAAAEGARVVL--VDRSELVHEVAAELRAAGGEALALTADLETYAGAQAAMAAAVEAFGRI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  94 DILVNNALPGYQFNPSADYTsietvqwshfTQQIDGIVKGAVN----AVQAVLPQMKAQKTGKILNISTNLVYNpvVTYY 169
Cdd:PRK12823   86 DVLINNVGGTIWAKPFEEYE----------EEQIEAEIRRSLFptlwCCRAVLPHMLAQGGGAIVNVSSIATRG--INRV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 170 DYTTAKSALIGLTRNLAAELGQYGIRVNLLA-GGLL-----------KTTDASRLTTEAVFDYIATTTPLRQATSVDDFA 237
Cdd:PRK12823  154 PYSAAKGGVNALTASLAFEYAEHGIRVNAVApGGTEapprrvprnaaPQSEQEKAWYQQIVDQTLDSSLMKRYGTIDEQV 233
                         250       260
                  ....*....|....*....|....
gi 1918264442 238 NSVLLMASDLSAAITGQSIAVDGG 261
Cdd:PRK12823  234 AAILFLASDEASYITGTVLPVGGG 257
PRK06398 PRK06398
aldose dehydrogenase; Validated
12-263 5.01e-30

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 113.00  E-value: 5.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVcVNyLNSQEAADTVVADIvaaggqafayQADVTELEQMQGMANEVTARYG 91
Cdd:PRK06398    4 LKDKVAIVTGGSQGIGKAVVNRLKEEGSNV-IN-FDIKEPSYNDVDYF----------KVDVSNKEQVIKGIDYVISKYG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpGYQfnpsaDYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTnlVYNPVVT--YY 169
Cdd:PRK06398   72 RIDILVNNA--GIE-----SYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIAS--VQSFAVTrnAA 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 170 DYTTAKSALIGLTRNLAAELGQYgIRVNLLAGGLLKT---TDASRLTT----EAVFDYI---ATTTPLRQATSVDDFANS 239
Cdd:PRK06398  143 AYVTSKHAVLGLTRSIAVDYAPT-IRCVAVCPGSIRTpllEWAAELEVgkdpEHVERKIrewGEMHPMKRVGKPEEVAYV 221
                         250       260
                  ....*....|....*....|....
gi 1918264442 240 VLLMASDLSAAITGQSIAVDGGLT 263
Cdd:PRK06398  222 VAFLASDLASFITGECVTVDGGLR 245
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
14-264 5.02e-30

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 113.21  E-value: 5.02e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSqEAADTVVADIVAAGG--QAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK12384    2 NQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINS-EKAANVAQEINAEYGegMAYGFGADATSEQSVLALSRGVDEIFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNALPGYqfnpSADYTSIETVQWshftqqiDGIVKgaVN-------AVQAVLPQMKAQKTGKILNIstNLVYNP 164
Cdd:PRK12384   81 RVDLLVYNAGIAK----AAFITDFQLGDF-------DRSLQ--VNlvgyflcAREFSRLMIRDGIQGRIIQI--NSKSGK 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 165 VVTYYD--YTTAKSALIGLTRNLAAELGQYGIRVN-LLAGGLLKT--------TDASRL--TTEAVFDYIATTTPLRQAT 231
Cdd:PRK12384  146 VGSKHNsgYSAAKFGGVGLTQSLALDLAEYGITVHsLMLGNLLKSpmfqsllpQYAKKLgiKPDEVEQYYIDKVPLKRGC 225
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1918264442 232 SVDDFANSVLLMASDLSAAITGQSIAVDGGLTM 264
Cdd:PRK12384  226 DYQDVLNMLLFYASPKASYCTGQSINVTGGQVM 258
PRK08416 PRK08416
enoyl-ACP reductase;
11-263 1.07e-29

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 112.17  E-value: 1.07e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  11 FLLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGG-QAFAYQADVTELEQMQGMANEVTAR 89
Cdd:PRK08416    5 EMKGKTLVISGGTRGIGKAIVYEFAQSGVNIAFTYNSNVEEANKIAEDLEQKYGiKAKAYPLNILEPETYKELFKKIDED 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  90 YGRIDILVNNAL-----------PGYQFNPSAdytsIETVqwshFTQQIDGIVKGAVNAVQavlpQMKAQKTGKILNIST 158
Cdd:PRK08416   85 FDRVDFFISNAIisgravvggytKFMRLKPKG----LNNI----YTATVNAFVVGAQEAAK----RMEKVGGGSIISLSS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 159 --NLVYNPvvTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKtTDASRLTT--EAVFDYIATTTPLRQATSVD 234
Cdd:PRK08416  153 tgNLVYIE--NYAGHGTSKAAVETMVKYAATELGEKNIRVNAVSGGPID-TDALKAFTnyEEVKAKTEELSPLNRMGQPE 229
                         250       260
                  ....*....|....*....|....*....
gi 1918264442 235 DFANSVLLMASDLSAAITGQSIAVDGGLT 263
Cdd:PRK08416  230 DLAGACLFLCSEKASWLTGQTIVVDGGTT 258
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
14-261 1.21e-29

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: 112.23  E-value: 1.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQ--EAADTVVADIVAAGgQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:cd05330     3 DKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEglEAAKAALLEIAPDA-EVLLIKADVSDEAQVEAYVDATVEQFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNA-LPGYQfNPSADYTSIEtvqwshFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYD 170
Cdd:cd05330    82 RIDGFFNNAgIEGKQ-NLTEDFGADE------FDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQSG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 171 YTTAKSALIGLTRNLAAELGQYGIRVNLLA-GGLLKTTDASRLTT------EAVFDYIATTTPLRQATSVDDFANSVLLM 243
Cdd:cd05330   155 YAAAKHGVVGLTRNSAVEYGQYGIRINAIApGAILTPMVEGSLKQlgpenpEEAGEEFVSVNPMKRFGEPEEVAAVVAFL 234
                         250
                  ....*....|....*...
gi 1918264442 244 ASDLSAAITGQSIAVDGG 261
Cdd:cd05330   235 LSDDAGYVNAAVVPIDGG 252
PRK06484 PRK06484
short chain dehydrogenase; Validated
15-263 2.41e-29

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 115.72  E-value: 2.41e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVnyLNSQEAADTVVADivAAGGQAFAYQADVTELEQMQGMANEVTARYGRID 94
Cdd:PRK06484    6 RVVLVTGAAGGIGRAACQRFARAGDQVVV--ADRNVERARERAD--SLGPDHHALAMDVSDEAQIREGFEQLHREFGRID 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  95 ILVNNA-LPGYQFNPSADyTSIETVQwshftqQIDGI-VKGAVNAVQAVLPQMKAQKTGK-ILNIST--NLVYNPVVTyy 169
Cdd:PRK06484   82 VLVNNAgVTDPTMTATLD-TTLEEFA------RLQAInLTGAYLVAREALRLMIEQGHGAaIVNVASgaGLVALPKRT-- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 170 DYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVFD--YIATTTPLRQATSVDDFANSVLLMASDL 247
Cdd:PRK06484  153 AYSASKAAVISLTRSLACEWAAKGIRVNAVLPGYVRTQMVAELERAGKLDpsAVRSRIPLGRLGRPEEIAEAVFFLASDQ 232
                         250
                  ....*....|....*.
gi 1918264442 248 SAAITGQSIAVDGGLT 263
Cdd:PRK06484  233 ASYITGSTLVVDGGWT 248
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
15-262 2.55e-29

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: 111.13  E-value: 2.55e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGAS--RGLGAQIAQKMAGAGASVCVNYLNsqEAADTVVADIVA-AGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:cd05372     2 KRILITGIAndRSIAWGIAKALHEAGAELAFTYQP--EALRKRVEKLAErLGESALVLPCDVSNDEEIKELFAEVKKDWG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILV-------NNALPGyqfnpsaDYtsIETVQwSHFTQQIDGIVKGAVNAVQAVLPQMKAQktGKILNIStnlvYNP 164
Cdd:cd05372    80 KLDGLVhsiafapKVQLKG-------PF--LDTSR-KGFLKALDISAYSLVSLAKAALPIMNPG--GSIVTLS----YLG 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 165 ----VVTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTT-EAVFDYIATTTPLRQATSVDDFANS 239
Cdd:cd05372   144 servVPGYNVMGVAKAALESSVRYLAYELGRKGIRVNAISAGPIKTLAASGITGfDKMLEYSEQRAPLGRNVTAEEVGNT 223
                         250       260
                  ....*....|....*....|...
gi 1918264442 240 VLLMASDLSAAITGQSIAVDGGL 262
Cdd:cd05372   224 AAFLLSDLSSGITGEIIYVDGGY 246
PRK06114 PRK06114
SDR family oxidoreductase;
12-263 3.69e-29

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 110.64  E-value: 3.69e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK06114    6 LDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDGLAETAEHIEAAGRRAIQIAADVTSKADLRAAVARTEAELG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpgyqfnPSADYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNIS--TNLVYNPVVTYY 169
Cdd:PRK06114   86 ALTLAVNAA-------GIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIAsmSGIIVNRGLLQA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 170 DYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSA 249
Cdd:PRK06114  159 HYNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATPMNTRPEMVHQTKLFEEQTPMQRMAKVDEMVGPAVFLLSDAAS 238
                         250
                  ....*....|....
gi 1918264442 250 AITGQSIAVDGGLT 263
Cdd:PRK06114  239 FCTGVDLLVDGGFV 252
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
12-263 4.38e-29

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: 110.62  E-value: 4.38e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVcVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARY- 90
Cdd:cd05329     4 LEGKTALVTGGTKGIGYAIVEELAGLGAEV-YTCARNQKELDECLTEWREKGFKVEGSVCDVSSRSERQELMDTVASHFg 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  91 GRIDILVNNAlPGYQFNPSADYTSIEtvqwshFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYD 170
Cdd:cd05329    83 GKLNILVNNA-GTNIRKEAKDYTEED------YSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 171 YTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTtdasRLTTEAV-----FDYIATTTPLRQATSVDDFANSVLLMAS 245
Cdd:cd05329   156 YGATKGALNQLTRSLACEWAKDNIRVNAVAPWVIAT----PLVEPVIqqkenLDKVIERTPLKRFGEPEEVAALVAFLCM 231
                         250
                  ....*....|....*...
gi 1918264442 246 DLSAAITGQSIAVDGGLT 263
Cdd:cd05329   232 PAASYITGQIIAVDGGLT 249
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
14-263 5.42e-29

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: 109.98  E-value: 5.42e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADtvVADivAAGGQAFAYQADVTELEQMQGMANEVTARYGRI 93
Cdd:cd09761     1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGAD--FAE--AEGPNLFFVHGDVADETLVKFVVYAMLEKLGRI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  94 DILVNNALPGyqfNPSadytSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKtGKILNISTNLVYNPVVTYYDYTT 173
Cdd:cd09761    77 DVLVNNAARG---SKG----ILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNK-GRIINIASTRAFQSEPDSEAYAA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 174 AKSALIGLTRNLAAELGQYgIRVNLLAGGLLKTTDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSAAITG 253
Cdd:cd09761   149 SKGGLVALTHALAMSLGPD-IRVNCISPGWINTTEQQEFTAAPLTQEDHAQHPAGRVGTPKDIANLVLFLCQQDAGFITG 227
                         250
                  ....*....|
gi 1918264442 254 QSIAVDGGLT 263
Cdd:cd09761   228 ETFIVDGGMT 237
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
12-264 7.09e-29

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 110.20  E-value: 7.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK08936    5 LEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSDEEEANDVAEEIKKAGGEAIAVKGDVTVESDVVNLIQTAVKEFG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpGYQfNPSADytsiETVQWSHFTQQIDGIVKGAVNAVQAVLPQM-KAQKTGKILNISTNLVYNPVVTYYD 170
Cdd:PRK08936   85 TLDVMINNA--GIE-NAVPS----HEMSLEDWNKVINTNLTGAFLGSREAIKYFvEHDIKGNIINMSSVHEQIPWPLFVH 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 171 YTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT-TDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSA 249
Cdd:PRK08936  158 YAASKGGVKLMTETLAMEYAPKGIRVNNIGPGAINTpINAEKFADPKQRADVESMIPMGYIGKPEEIAAVAAWLASSEAS 237
                         250
                  ....*....|....*
gi 1918264442 250 AITGQSIAVDGGLTM 264
Cdd:PRK08936  238 YVTGITLFADGGMTL 252
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
15-264 8.34e-29

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: 109.48  E-value: 8.34e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADtvvadiVAAGGQAFAYQADVTELEQMQGMANEVtaryGRID 94
Cdd:cd05368     3 KVALITAAAQGIGRAIALAFAREGANVIATDINEEKLKE------LERGPGITTRVLDVTDKEQVAALAKEE----GRID 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  95 ILVNNAlpgyQFNPSADYTSIETVQWShFTQQIDgiVKGAVNAVQAVLPQMKAQKTGKILNIST-NLVYNPVVTYYDYTT 173
Cdd:cd05368    73 VLFNCA----GFVHHGSILDCEDDDWD-FAMNLN--VRSMYLMIKAVLPKMLARKDGSIINMSSvASSIKGVPNRFVYST 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 174 AKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDA-----SRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLS 248
Cdd:cd05368   146 TKAAVIGLTKSVAADFAQQGIRCNAICPGTVDTPSLeeriqAQPDPEEALKAFAARQPLGRLATPEEVAALAVYLASDES 225
                         250
                  ....*....|....*.
gi 1918264442 249 AAITGQSIAVDGGLTM 264
Cdd:cd05368   226 AYVTGTAVVIDGGWSL 241
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
15-261 8.83e-29

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: 109.40  E-value: 8.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADtvVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRID 94
Cdd:cd08943     2 KVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEK--VAEAAQGGPRALGVQCDVTSEAQVQSAFEQAVLEFGGLD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  95 ILVNNAlpGYQFNPSADYTSIETVQWSHftqqiDGIVKGAVNAVQAVLPQMKAQKTGKIL--NISTNLVyNPVVTYYDYT 172
Cdd:cd08943    80 IVVSNA--GIATSSPIAETSLEDWNRSM-----DINLTGHFLVSREAFRIMKSQGIGGNIvfNASKNAV-APGPNAAAYS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 173 TAKSALIGLTRNLAAELGQYGIRVNLL------------AGGLLKTTDASRLTTEAvfDYIATTTpLRQATSVDDFANSV 240
Cdd:cd08943   152 AAKAAEAHLARCLALEGGEDGIRVNTVnpdavfrgskiwEGVWRAARAKAYGLLEE--EYRTRNL-LKREVLPEDVAEAV 228
                         250       260
                  ....*....|....*....|.
gi 1918264442 241 LLMASDLSAAITGQSIAVDGG 261
Cdd:cd08943   229 VAMASEDFGKTTGAIVTVDGG 249
PRK05867 PRK05867
SDR family oxidoreductase;
12-265 1.46e-28

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 108.97  E-value: 1.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSqEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK05867    7 LHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHL-DALEKLADEIGTSGGKVVPVCCDVSQHQQVTSMLDQVTAELG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNA----LPGYQFNPSADYTSIETVqwshftqQIDGIVKGAVNAVQAVLPQ-------MKAQKTGKILNISTNL 160
Cdd:PRK05867   86 GIDIAVCNAgiitVTPMLDMPLEEFQRLQNT-------NVTGVFLTAQAAAKAMVKQgqggviiNTASMSGHIINVPQQV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 161 VYnpvvtyydYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTdasrlTTEAVFDYIAT---TTPLRQATSVDDFA 237
Cdd:PRK05867  159 SH--------YCASKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTE-----LVEPYTEYQPLwepKIPLGRLGRPEELA 225
                         250       260
                  ....*....|....*....|....*...
gi 1918264442 238 NSVLLMASDLSAAITGQSIAVDGGLTMP 265
Cdd:PRK05867  226 GLYLYLASEASSYMTGSDIVIDGGYTCP 253
PRK12743 PRK12743
SDR family oxidoreductase;
14-263 1.75e-28

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 108.97  E-value: 1.75e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRI 93
Cdd:PRK12743    2 AQVAIVTASDSGIGKACALLLAQQGFDIGITWHSDEEGAKETAEEVRSHGVRAEIRQLDLSDLPEGAQALDKLIQRLGRI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  94 DILVNNAlpGYQFNPSADYTSIETVQwSHFTQQIDgivkGAVNAVQAVLPQMKAQKT-GKILNISTNLVYNPVVTYYDYT 172
Cdd:PRK12743   82 DVLVNNA--GAMTKAPFLDMDFDEWR-KIFTVDVD----GAFLCSQIAARHMVKQGQgGRIINITSVHEHTPLPGASAYT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 173 TAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT-------TDASRLTTEAVfdyiatttPLRQATSVDDFANSVLLMAS 245
Cdd:PRK12743  155 AAKHALGGLTKAMALELVEHGILVNAVAPGAIATpmngmddSDVKPDSRPGI--------PLGRPGDTHEIASLVAWLCS 226
                         250
                  ....*....|....*...
gi 1918264442 246 DLSAAITGQSIAVDGGLT 263
Cdd:PRK12743  227 EGASYTTGQSLIVDGGFM 244
PRK09242 PRK09242
SDR family oxidoreductase;
12-262 2.21e-28

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 108.68  E-value: 2.21e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQ--EAADTVVADiVAAGGQAFAYQADVTELEQMQGMANEVTAR 89
Cdd:PRK09242    7 LDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADalAQARDELAE-EFPEREVHGLAADVSDDEDRRAILDWVEDH 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  90 YGRIDILVNNAlpGYQFNPSA-DYTSIEtvqWSHFTQqIDgiVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTY 168
Cdd:PRK09242   86 WDGLHILVNNA--GGNIRKAAiDYTEDE---WRGIFE-TN--LFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 169 YDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASR-LTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDL 247
Cdd:PRK09242  158 APYGMTKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSGpLSDPDYYEQVIERTPMRRVGEPEEVAAAVAFLCMPA 237
                         250
                  ....*....|....*
gi 1918264442 248 SAAITGQSIAVDGGL 262
Cdd:PRK09242  238 ASYITGQCIAVDGGF 252
PRK12746 PRK12746
SDR family oxidoreductase;
15-264 2.75e-28

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 108.58  E-value: 2.75e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMA----NEVTARY 90
Cdd:PRK12746    7 KVALVTGASRGIGRAIAMRLANDGALVAIHYGRNKQAADETIREIESNGGKAFLIEADLNSIDGVKKLVeqlkNELQIRV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  91 G--RIDILVNNALPGYQfnpsadyTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQktGKILNISTNLVYNPVVTY 168
Cdd:PRK12746   87 GtsEIDILVNNAGIGTQ-------GTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLRAE--GRVINISSAEVRLGFTGS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 169 YDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT-TDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDL 247
Cdd:PRK12746  158 IAYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTdINAKLLDDPEIRNFATNSSVFGRIGQVEDIADAVAFLASSD 237
                         250
                  ....*....|....*..
gi 1918264442 248 SAAITGQSIAVDGGLTM 264
Cdd:PRK12746  238 SRWVTGQIIDVSGGFCL 254
PRK08589 PRK08589
SDR family oxidoreductase;
12-262 3.19e-28

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 108.71  E-value: 3.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNsqEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK08589    4 LENKVAVITGASTGIGQASAIALAQEGAYVLAVDIA--EAVSETVDKIKSNGGKAKAYHVDISDEQQVKDFASEIKEQFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNALPGYQFNPSADYtSIETvqwshFTQQIDGIVKGAVNAVQAVLPQMkAQKTGKILNISTNLVYNPVVTYYDY 171
Cdd:PRK08589   82 RVDVLFNNAGVDNAAGRIHEY-PVDV-----FDKIMAVDMRGTFLMTKMLLPLM-MEQGGSIINTSSFSGQAADLYRSGY 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 172 TTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLT-------TEAVFDYIATTTPLRQATSVDDFANSVLLMA 244
Cdd:PRK08589  155 NAAKGAVINFTKSIAIEYGRDGIRANAIAPGTIETPLVDKLTgtsedeaGKTFRENQKWMTPLGRLGKPEEVAKLVVFLA 234
                         250
                  ....*....|....*...
gi 1918264442 245 SDLSAAITGQSIAVDGGL 262
Cdd:PRK08589  235 SDDSSFITGETIRIDGGV 252
PRK07677 PRK07677
short chain dehydrogenase; Provisional
14-261 3.55e-28

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 108.23  E-value: 3.55e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNsQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRI 93
Cdd:PRK07677    1 EKVVIITGGSSGMGKAMAKRFAEEGANVVITGRT-KEKLEEAKLEIEQFPGQVLTVQMDVRNPEDVQKMVEQIDEKFGRI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  94 DILVNNAlpGYQFNPSADYTSIETvqWSHFtqqIDGIVKGAVNAVQAVLPQMKAQKT-GKILNISTNLVYNPVVTYYDYT 172
Cdd:PRK07677   80 DALINNA--AGNFICPAEDLSVNG--WNSV---IDIVLNGTFYCSQAVGKYWIEKGIkGNIINMVATYAWDAGPGVIHSA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 173 TAKSALIGLTRNLAAELG-QYGIRVNLLAGGLL-KTTDASRL-TTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSA 249
Cdd:PRK07677  153 AAKAGVLAMTRTLAVEWGrKYGIRVNAIAPGPIeRTGGADKLwESEEAAKRTIQSVPLGRLGTPEEIAGLAYFLLSDEAA 232
                         250
                  ....*....|..
gi 1918264442 250 AITGQSIAVDGG 261
Cdd:PRK07677  233 YINGTCITMDGG 244
PRK07201 PRK07201
SDR family oxidoreductase;
12-194 3.67e-28

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 112.74  E-value: 3.67e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNsQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK07201  369 LVGKVVLITGASSGIGRATAIKVAEAGATVFLVARN-GEALDELVAEIRAKGGTAHAYTCDLTDSAAVDHTVKDILAEHG 447
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpGYQFNPSA--------DYTsiETVQWSHFtqqidgivkGAVNAVQAVLPQMKAQKTGKILNISTN--LV 161
Cdd:PRK07201  448 HVDYLVNNA--GRSIRRSVenstdrfhDYE--RTMAVNYF---------GAVRLILGLLPHMRERRFGHVVNVSSIgvQT 514
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1918264442 162 YNPvvTYYDYTTAKSALIGLTRNLAAELGQYGI 194
Cdd:PRK07201  515 NAP--RFSAYVASKAALDAFSDVAASETLSDGI 545
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
12-264 4.10e-28

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 107.81  E-value: 4.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSqEAADTVVADIvaaGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK07067    4 LQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKP-ARARLAALEI---GPAAIAVSLDVTRQDSIDRIVAAAVERFG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpgyqfnPSADYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQ-KTGKILNISTNLVY--NPVVTY 168
Cdd:PRK07067   80 GIDILFNNA-------ALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQgRGGKIINMASQAGRrgEALVSH 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 169 YDYTtaKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT-----TDA-------------SRLTTEAVfdyiatttPLRQA 230
Cdd:PRK07067  153 YCAT--KAAVISYTQSAALALIRHGINVNAIAPGVVDTpmwdqVDAlfaryenrppgekKRLVGEAV--------PLGRM 222
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1918264442 231 TSVDDFANSVLLMASDLSAAITGQSIAVDGGLTM 264
Cdd:PRK07067  223 GVPDDLTGMALFLASADADYIVAQTYNVDGGNWM 256
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
12-261 7.04e-28

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 107.11  E-value: 7.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK06077    4 LKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKKRAEEMNETLKMVKENGGEGIGVLADVSTREGCETLAKATIDRYG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNALPGYqFNP--SADYTSIEtvqwshftQQIDGIVKGAVNAVQAVLPQMKaqKTGKILNISTNLVYNPVVTYY 169
Cdd:PRK06077   84 VADILVNNAGLGL-FSPflNVDDKLID--------KHISTDFKSVIYCSQELAKEMR--EGGAIVNIASVAGIRPAYGLS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 170 DYTTAKSALIGLTRNLAAELGQYgIRVNLLAGGLLKTT------DASRLTTEavfDYIATTTPLRQATSVDDFANSVLLM 243
Cdd:PRK06077  153 IYGAMKAAVINLTKYLALELAPK-IRVNAIAPGFVKTKlgeslfKVLGMSEK---EFAEKFTLMGKILDPEEVAEFVAAI 228
                         250
                  ....*....|....*...
gi 1918264442 244 ASdlSAAITGQSIAVDGG 261
Cdd:PRK06077  229 LK--IESITGQVFVLDSG 244
PRK09730 PRK09730
SDR family oxidoreductase;
15-261 7.66e-28

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 107.24  E-value: 7.66e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRID 94
Cdd:PRK09730    2 AIALVTGGSRGIGRATALLLAQEGYTVAVNYQQNLHAAQEVVNLITQAGGKAFVLQADISDENQVVAMFTAIDQHDEPLA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  95 ILVNNAlpGYQFNPSadytSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGK---ILNISTNLV-YNPVVTYYD 170
Cdd:PRK09730   82 ALVNNA--GILFTQC----TVENLTAERINRVLSTNVTGYFLCCREAVKRMALKHGGSggaIVNVSSAASrLGAPGEYVD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 171 YTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSAA 250
Cdd:PRK09730  156 YAASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEMHASGGEPGRVDRVKSNIPMQRGGQPEEVAQAIVWLLSDKASY 235
                         250
                  ....*....|.
gi 1918264442 251 ITGQSIAVDGG 261
Cdd:PRK09730  236 VTGSFIDLAGG 246
PRK07814 PRK07814
SDR family oxidoreductase;
12-265 8.28e-28

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 107.17  E-value: 8.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYlNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK07814    8 LDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAA-RTESQLDEVAEQIRAAGRRAHVVAADLAHPEATAGLAGQAVEAFG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNaLPGYQFNPSADYTSIETVQWSHFTqqidgiVKGAVNAVQAVLPQM-KAQKTGKILNISTNLVYNPVVTYYD 170
Cdd:PRK07814   87 RLDIVVNN-VGGTMPNPLLSTSTKDLADAFTFN------VATAHALTVAAVPLMlEHSGGGSVINISSTMGRLAGRGFAA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 171 YTTAKSALIGLTRNLAAELGQYgIRVNLLA-GGLLKTTDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSA 249
Cdd:PRK07814  160 YGTAKAALAHYTRLAALDLCPR-IRVNAIApGSILTSALEVVAANDELRAPMEKATPLRRLGDPEDIAAAAVYLASPAGS 238
                         250
                  ....*....|....*.
gi 1918264442 250 AITGQSIAVDGGLTMP 265
Cdd:PRK07814  239 YLTGKTLEVDGGLTFP 254
PRK06947 PRK06947
SDR family oxidoreductase;
15-261 1.41e-27

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 106.43  E-value: 1.41e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRID 94
Cdd:PRK06947    3 KVVLITGASRGIGRATAVLAAARGWSVGINYARDAAAAEETADAVRAAGGRACVVAGDVANEADVIAMFDAVQSAFGRLD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  95 ILVNNAlpGYqFNPSADYTSIETvqwSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGK---ILNIST--NLVYNPvVTYY 169
Cdd:PRK06947   83 ALVNNA--GI-VAPSMPLADMDA---ARLRRMFDTNVLGAYLCAREAARRLSTDRGGRggaIVNVSSiaSRLGSP-NEYV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 170 DYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSA 249
Cdd:PRK06947  156 DYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEIHASGGQPGRAARLGAQTPLGRAGEADEVAETIVWLLSDAAS 235
                         250
                  ....*....|..
gi 1918264442 250 AITGQSIAVDGG 261
Cdd:PRK06947  236 YVTGALLDVGGG 247
PLN02253 PLN02253
xanthoxin dehydrogenase
12-263 1.49e-27

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 107.22  E-value: 1.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVnyLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PLN02253   16 LLGKVALVTGGATGIGESIVRLFHKHGAKVCI--VDLQDDLGQNVCDSLGGEPNVCFFHCDVTVEDDVSRAVDFTVDKFG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpGYQFNPSADytsIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDY 171
Cdd:PLN02253   94 TLDIMVNNA--GLTGPPCPD---IRNVELSEFEKVFDVNVKGVFLGMKHAARIMIPLKKGSIVSLCSVASAIGGLGPHAY 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 172 TTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDA------SRLTTEAVFDYIATTTplRQAT------SVDDFANS 239
Cdd:PLN02253  169 TGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALAlahlpeDERTEDALAGFRAFAG--KNANlkgvelTVDDVANA 246
                         250       260
                  ....*....|....*....|....
gi 1918264442 240 VLLMASDLSAAITGQSIAVDGGLT 263
Cdd:PLN02253  247 VLFLASDEARYISGLNLMIDGGFT 270
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
12-261 3.41e-27

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: 105.26  E-value: 3.41e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSqEAADTVVADIvaaGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:cd08944     1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDG-GAAQAVVAQI---AGGALALRVDVTDEQQVAALFERAVEEFG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpgyqfnpSADYTS--IETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYY 169
Cdd:cd08944    77 GLDLLVNNA--------GAMHLTpaIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGDPGYG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 170 DYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTdasrLTTEAVFDYIATTTPLRQATSVD----------DFANS 239
Cdd:cd08944   149 AYGASKAAIRNLTRTLAAELRHAGIRCNALAPGLIDTP----LLLAKLAGFEGALGPGGFHLLIHqlqgrlgrpeDVAAA 224
                         250       260
                  ....*....|....*....|..
gi 1918264442 240 VLLMASDLSAAITGQSIAVDGG 261
Cdd:cd08944   225 VVFLLSDDASFITGQVLCVDGG 246
PRK08265 PRK08265
short chain dehydrogenase; Provisional
12-264 5.57e-27

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 105.09  E-value: 5.57e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVcvnylnsqeaadtVVADIVAAGGQAFA---------YQADVTELEQMQGM 82
Cdd:PRK08265    4 LAGKVAIVTGGATLIGAAVARALVAAGARV-------------AIVDIDADNGAAVAaslgerarfIATDITDDAAIERA 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  83 ANEVTARYGRIDILVNNAL----PGYQFNPSadytsietvQWShftQQIDGIVKGAVNAVQAVLPQMKAQKtGKILNIST 158
Cdd:PRK08265   71 VATVVARFGRVDILVNLACtyldDGLASSRA---------DWL---AALDVNLVSAAMLAQAAHPHLARGG-GAIVNFTS 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 159 NLVYNPVVTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGG------LLKTTDASRLTTEAVfdyIATTTPLRQATS 232
Cdd:PRK08265  138 ISAKFAQTGRWLYPASKAAIRQLTRSMAMDLAPDGIRVNSVSPGwtwsrvMDELSGGDRAKADRV---AAPFHLLGRVGD 214
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1918264442 233 VDDFANSVLLMASDLSAAITGQSIAVDGGLTM 264
Cdd:PRK08265  215 PEEVAQVVAFLCSDAASFVTGADYAVDGGYSA 246
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
15-261 6.48e-27

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: 104.31  E-value: 6.48e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASV-CVNYLNSQEAADTVVAdiVAAGGQAFAYQADVTELEQMQGMANEVTARYGRI 93
Cdd:cd05323     1 KVAIITGGASGIGLATAKLLLKKGAKVaILDRNENPGAAAELQA--INPKVKATFVQCDVTSWEQLAAAFKKAIEKFGRV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  94 DILVNNAlpGYQFNPSADYTSIETVQWshfTQQIDGIVKGAVNAVQAVLPQMKAQKTGK---ILNISTNLVYNPVVTYYD 170
Cdd:cd05323    79 DILINNA--GILDEKSYLFAGKLPPPW---EKTIDVNLTGVINTTYLALHYMDKNKGGKggvIVNIGSVAGLYPAPQFPV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 171 YTTAKSALIGLTRNLAAEL-GQYGIRVNLLAGGLLKTTDASRLTTEAVFDYIATTTplrqaTSVDDFANSVL-LMASDLS 248
Cdd:cd05323   154 YSASKHGVVGFTRSLADLLeYKTGVRVNAICPGFTNTPLLPDLVAKEAEMLPSAPT-----QSPEVVAKAIVyLIEDDEK 228
                         250
                  ....*....|...
gi 1918264442 249 aaiTGQSIAVDGG 261
Cdd:cd05323   229 ---NGAIWIVDGG 238
PRK12747 PRK12747
short chain dehydrogenase; Provisional
12-261 7.70e-27

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 104.77  E-value: 7.70e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQ----GMANEVT 87
Cdd:PRK12747    2 LKGKVALVTGASRGIGRAIAKRLANDGALVAIHYGNRKEEAEETVYEIQSNGGSAFSIGANLESLHGVEalysSLDNELQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  88 ARYG--RIDILVNNALPGyqfnPSAdytSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKaqKTGKILNISTNLVYNPV 165
Cdd:PRK12747   82 NRTGstKFDILINNAGIG----PGA---FIEETTEQFFDRMVSVNAKAPFFIIQQALSRLR--DNSRIINISSAATRISL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 166 VTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT-TDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMA 244
Cdd:PRK12747  153 PDFIAYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTdMNAELLSDPMMKQYATTISAFNRLGEVEDIADTAAFLA 232
                         250
                  ....*....|....*..
gi 1918264442 245 SDLSAAITGQSIAVDGG 261
Cdd:PRK12747  233 SPDSRWVTGQLIDVSGG 249
PRK06181 PRK06181
SDR family oxidoreductase;
14-206 1.11e-26

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 104.29  E-value: 1.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNsQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRI 93
Cdd:PRK06181    1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARN-ETRLASLAQELADHGGEALVVPTDVSDAEACERLIEAAVARFGGI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  94 DILVNNAlpgyqfNPSADYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKtGKILNISTNLVYNPVVTYYDYTT 173
Cdd:PRK06181   80 DILVNNA------GITMWSRFDELTDLSVFERVMRVNYLGAVYCTHAALPHLKASR-GQIVVVSSLAGLTGVPTRSGYAA 152
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1918264442 174 AKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT 206
Cdd:PRK06181  153 SKHALHGFFDSLRIELADDGVAVTVVCPGFVAT 185
PRK06182 PRK06182
short chain dehydrogenase; Validated
15-206 2.26e-26

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 103.89  E-value: 2.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVnylnsqeAADTV--VADIVAAGGQAFAYqaDVTELEQMQGMANEVTARYGR 92
Cdd:PRK06182    4 KVALVTGASSGIGKATARRLAAQGYTVYG-------AARRVdkMEDLASLGVHPLSL--DVTDEASIKAAVDTIIAEEGR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  93 IDILVNNAlpGYqfnpsADYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNIST--NLVYNPVVTYYD 170
Cdd:PRK06182   75 IDVLVNNA--GY-----GSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSmgGKIYTPLGAWYH 147
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1918264442 171 YTtaKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT 206
Cdd:PRK06182  148 AT--KFALEGFSDALRLEVAPFGIDVVVIEPGGIKT 181
PRK07806 PRK07806
SDR family oxidoreductase;
12-112 2.77e-26

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 102.88  E-value: 2.77e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK07806    4 LPGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQKAPRANKVVAEIEAAGGRASAVGADLTDEESVAALMDTAREEFG 83
                          90       100
                  ....*....|....*....|.
gi 1918264442  92 RIDILVNNALPGYQFNPSADY 112
Cdd:PRK07806   84 GLDALVLNASGGMESGMDEDY 104
PRK07454 PRK07454
SDR family oxidoreductase;
15-244 3.18e-26

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 102.73  E-value: 3.18e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVnYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRID 94
Cdd:PRK07454    7 PRALITGASSGIGKATALAFAKAGWDLAL-VARSQDALEALAAELRSTGVKAAAYSIDLSNPEAIAPGIAELLEQFGCPD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  95 ILVNNAlpGYQFNPSADYTSIETVQWshfTQQIDgiVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDYTTA 174
Cdd:PRK07454   86 VLINNA--GMAYTGPLLEMPLSDWQW---VIQLN--LTSVFQCCSAVLPGMRARGGGLIINVSSIAARNAFPQWGAYCVS 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1918264442 175 KSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVFDyiatttplRQAT-SVDDFANSVLLMA 244
Cdd:PRK07454  159 KAALAAFTKCLAEEERSHGIRVCTITLGAVNTPLWDTETVQADFD--------RSAMlSPEQVAQTILHLA 221
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
16-264 3.43e-26

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


Pssm-ID: 131732 [Multi-domain]  Cd Length: 267  Bit Score: 103.08  E-value: 3.43e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  16 VVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAA-GGQAFAYQADVTE----LEQMQGMANEVTARY 90
Cdd:TIGR02685   3 AAVVTGAAKRIGSSIAVALHQEGYRVVLHYHRSAAAASTLAAELNARrPNSAVTCQADLSNsatlFSRCEAIIDACFRAF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  91 GRIDILVNNA--------LPGYQFNPSADYTSIETVQWSHFtqqidgivkgAVNAVQAVLPQMK-AQKTG---------- 151
Cdd:TIGR02685  83 GRCDVLVNNAsafyptplLRGDAGEGVGDKKSLEVQVAELF----------GSNAIAPYFLIKAfAQRQAgtraeqrstn 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 152 -KILNISTNLVYNPVVTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDAsrlTTEAVFDYIATTTPL-RQ 229
Cdd:TIGR02685 153 lSIVNLCDAMTDQPLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGLSLLPDA---MPFEVQEDYRRKVPLgQR 229
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1918264442 230 ATSVDDFANSVLLMASDLSAAITGQSIAVDGGLTM 264
Cdd:TIGR02685 230 EASAEQIADVVIFLVSPKAKYITGTCIKVDGGLSL 264
PRK07576 PRK07576
short chain dehydrogenase; Provisional
15-264 4.50e-26

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 102.73  E-value: 4.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNYlNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRID 94
Cdd:PRK07576   10 KNVVVVGGTSGINLGIAQAFARAGANVAVAS-RSQEKVDAAVAQLQQAGPEGLGVSADVRDYAAVEAAFAQIADEFGPID 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  95 ILVNNAlpGYQFNPSADYTSIetvqwSHFTQQIDGIVKGAVNAVQAVLPQMKaQKTGKILNISTNLVYNPVVTYYDYTTA 174
Cdd:PRK07576   89 VLVSGA--AGNFPAPAAGMSA-----NGFKTVVDIDLLGTFNVLKAAYPLLR-RPGASIIQISAPQAFVPMPMQAHVCAA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 175 KSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTD-ASRLT-TEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSAAIT 252
Cdd:PRK07576  161 KAGVDMLTRTLALEWGPEGIRVNSIVPGPIAGTEgMARLApSPELQAAVAQSVPLKRNGTKQDIANAALFLASDMASYIT 240
                         250
                  ....*....|..
gi 1918264442 253 GQSIAVDGGLTM 264
Cdd:PRK07576  241 GVVLPVDGGWSL 252
PRK06128 PRK06128
SDR family oxidoreductase;
12-265 5.30e-26

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 103.40  E-value: 5.30e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEA-ADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARY 90
Cdd:PRK06128   53 LQGRKALITGADSGIGRATAIAFAREGADIALNYLPEEEQdAAEVVQLIQAEGRKAVALPGDLKDEAFCRQLVERAVKEL 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  91 GRIDILVNNALPGYQFNPSADYTsietvqwshfTQQIDGIVKGAVNAV----QAVLPQMKAQKTgkILNISTNLVYNPVV 166
Cdd:PRK06128  133 GGLDILVNIAGKQTAVKDIADIT----------TEQFDATFKTNVYAMfwlcKAAIPHLPPGAS--IINTGSIQSYQPSP 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 167 TYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTT--DASRLTTEAVFDYiATTTPLRQATSVDDFANSVLLMA 244
Cdd:PRK06128  201 TLLDYASTKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPlqPSGGQPPEKIPDF-GSETPMKRPGQPVEMAPLYVLLA 279
                         250       260
                  ....*....|....*....|.
gi 1918264442 245 SDLSAAITGQSIAVDGGLTMP 265
Cdd:PRK06128  280 SQESSYVTGEVFGVTGGLLLS 300
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
15-196 5.53e-26

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: 101.95  E-value: 5.53e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVcvnYL--NSQEAADTVVADIVA---AGGQAFAY-QADVTELEQMQGMANEVTA 88
Cdd:cd08939     2 KHVLITGGSSGIGKALAKELVKEGANV---IIvaRSESKLEEAVEEIEAeanASGQKVSYiSADLSDYEEVEQAFAQAVE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  89 RYGRIDILVNNA---LPGYqfnpsadytsIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPV 165
Cdd:cd08939    79 KGGPPDLVVNCAgisIPGL----------FEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGI 148
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1918264442 166 VTYYDYTTAKSALIGLTRNLAAELGQYGIRV 196
Cdd:cd08939   149 YGYSAYCPSKFALRGLAESLRQELKPYNIRV 179
PRK09186 PRK09186
flagellin modification protein A; Provisional
11-264 5.79e-26

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 102.38  E-value: 5.79e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  11 FLLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFA-YQADVTELEQMQGMANEVTAR 89
Cdd:PRK09186    1 MLKGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEFKSKKLSlVELDITDQESLEEFLSKSAEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  90 YGRIDILVNNALPgyqfnPSADY-TSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNL-VYNPVVT 167
Cdd:PRK09186   81 YGKIDGAVNCAYP-----RNKDYgKKFFDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGGGNLVNISSIYgVVAPKFE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 168 YYD---------YTTAKSALIGLTRNLAAELGQYGIRVNLLA-GGLLKTTDasrlttEAVFDYIATTTPLRQATSVDDFA 237
Cdd:PRK09186  156 IYEgtsmtspveYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSpGGILDNQP------EAFLNAYKKCCNGKGMLDPDDIC 229
                         250       260
                  ....*....|....*....|....*..
gi 1918264442 238 NSVLLMASDLSAAITGQSIAVDGGLTM 264
Cdd:PRK09186  230 GTLVFLLSDQSKYITGQNIIVDDGFSL 256
PRK06701 PRK06701
short chain dehydrogenase; Provisional
12-264 6.06e-26

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 102.80  E-value: 6.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK06701   44 LKGKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEDANETKQRVEKEGVKCLLIPGDVSDEAFCKDAVEETVRELG 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpGYQFNPSadytSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKaqKTGKILNISTNLVYNPVVTYYDY 171
Cdd:PRK06701  124 RLDILVNNA--AFQYPQQ----SLEDITAEQLDKTFKTNIYSYFHMTKAALPHLK--QGSAIINTGSITGYEGNETLIDY 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 172 TTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTT-DASRLTTEAVFDYiATTTPLRQATSVDDFANSVLLMASDLSAA 250
Cdd:PRK06701  196 SATKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTPlIPSDFDEEKVSQF-GSNTPMQRPGQPEELAPAYVFLASPDSSY 274
                         250
                  ....*....|....
gi 1918264442 251 ITGQSIAVDGGLTM 264
Cdd:PRK06701  275 ITGQMLHVNGGVIV 288
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
15-265 7.35e-26

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 101.96  E-value: 7.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRID 94
Cdd:PRK12745    3 PVALVTGGRRGIGLGIARALAAAGFDLAINDRPDDEELAATQQELRALGVEVIFFPADVADLSAHEAMLDAAQAAWGRID 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  95 ILVNNAlpGYQFNPSADytsIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKT------GKILNISTnlvYNPVVTY 168
Cdd:PRK12745   83 CLVNNA--GVGVKVRGD---LLDLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEpeelphRSIVFVSS---VNAIMVS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 169 Y---DYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT--TDASRLTTEAVFDyiATTTPLRQATSVDDFANSVLLM 243
Cdd:PRK12745  155 PnrgEYCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTdmTAPVTAKYDALIA--KGLVPMPRWGEPEDVARAVAAL 232
                         250       260
                  ....*....|....*....|..
gi 1918264442 244 ASDLSAAITGQSIAVDGGLTMP 265
Cdd:PRK12745  233 ASGDLPYSTGQAIHVDGGLSIP 254
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
12-263 1.11e-25

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 101.38  E-value: 1.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVvADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK07523    8 LTGRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAA-ESLKGQGLSAHALAFDVTDHDAVRAAIDAFEAEIG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpGYQFNpsadyTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNIST--NLVYNPVVTyy 169
Cdd:PRK07523   87 PIDILVNNA--GMQFR-----TPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASvqSALARPGIA-- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 170 DYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVF-DYIATTTPLRQATSVDDFANSVLLMASDLS 248
Cdd:PRK07523  158 PYTATKGAVGNLTKGMATDWAKHGLQCNAIAPGYFDTPLNAALVADPEFsAWLEKRTPAGRWGKVEELVGACVFLASDAS 237
                         250
                  ....*....|....*
gi 1918264442 249 AAITGQSIAVDGGLT 263
Cdd:PRK07523  238 SFVNGHVLYVDGGIT 252
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
15-206 1.23e-25

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: 100.77  E-value: 1.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGaSVCVnYLNSQ--EAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGR 92
Cdd:cd05324     1 KVALVTGANRGIGFEIVRQLAKSG-PGTV-ILTARdvERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  93 IDILVNNAlpGYQFNPSADYTSietvqwshFTQQIDGIVK----GAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVvty 168
Cdd:cd05324    79 LDILVNNA--GIAFKGFDDSTP--------TREQARETMKtnffGTVDVTQALLPLLKKSPAGRIVNVSSGLGSLTS--- 145
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1918264442 169 yDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT 206
Cdd:cd05324   146 -AYGVSKAALNALTRILAKELKETGIKVNACCPGWVKT 182
PRK06179 PRK06179
short chain dehydrogenase; Provisional
14-206 2.07e-25

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 101.13  E-value: 2.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVcvnYLNSQEAADtvvadivAAGGQAFAYQA-DVTELEQMQGMANEVTARYGR 92
Cdd:PRK06179    4 SKVALVTGASSGIGRATAEKLARAGYRV---FGTSRNPAR-------AAPIPGVELLElDVTDDASVQAAVDEVIARAGR 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  93 IDILVNNAlpGYQFNPSADYTSIETVQwshftQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDYT 172
Cdd:PRK06179   74 IDVLVNNA--GVGLAGAAEESSIAQAQ-----ALFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVLGFLPAPYMALYA 146
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1918264442 173 TAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT 206
Cdd:PRK06179  147 ASKHAVEGYSESLDHEVRQFGIRVSLVEPAYTKT 180
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
13-262 2.93e-25

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: 100.31  E-value: 2.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  13 LNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVvADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGR 92
Cdd:cd08945     2 DSEVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTV-KELREAGVEADGRTCDVRSVPEIEALVAAAVARYGP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  93 IDILVNNA-LPGyqfnpSADYTSIETVQWshftqqiDGIVKGAVNAVQAVLPQ------MKAQKTGKILNISTNLVYNPV 165
Cdd:cd08945    81 IDVLVNNAgRSG-----GGATAELADELW-------LDVVETNLTGVFRVTKEvlkaggMLERGTGRIINIASTGGKQGV 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 166 VTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRL----------TTEAVFDYIATTTPLRQATSVDD 235
Cdd:cd08945   149 VHAAPYSASKHGVVGFTKALGLELARTGITVNAVCPGFVETPMAASVrehyadiwevSTEEAFDRITARVPLGRYVTPEE 228
                         250       260
                  ....*....|....*....|....*..
gi 1918264442 236 FANSVLLMASDLSAAITGQSIAVDGGL 262
Cdd:cd08945   229 VAGMVAYLIGDGAAAVTAQALNVCGGL 255
PRK06523 PRK06523
short chain dehydrogenase; Provisional
12-265 2.98e-25

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 100.36  E-value: 2.98e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVnylnsqeAADTVVADivAAGGQAFAyQADVTELEQMQGMANEVTARYG 91
Cdd:PRK06523    7 LAGKRALVTGGTKGIGAATVARLLEAGARVVT-------TARSRPDD--LPEGVEFV-AADLTTAEGCAAVARAVLERLG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpGYQFNPSADYTSIETVQWShftQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVvtyYD- 170
Cdd:PRK06523   77 GVDILVHVL--GGSSAPAGGFAALTDEEWQ---DELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSIQRRLPL---PEs 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 171 ---YTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRL----------TTEAVFDYIATTT---PLRQATSVD 234
Cdd:PRK06523  149 ttaYAAAKAALSTYSKSLSKEVAPKGVRVNTVSPGWIETEAAVALaerlaeaagtDYEGAKQIIMDSLggiPLGRPAEPE 228
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1918264442 235 DFANSVLLMASDLSAAITGQSIAVDGGlTMP 265
Cdd:PRK06523  229 EVAELIAFLASDRAASITGTEYVIDGG-TVP 258
PRK07577 PRK07577
SDR family oxidoreductase;
14-261 3.03e-25

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 99.80  E-value: 3.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVcvnylnsqeaadTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGrI 93
Cdd:PRK07577    3 SRTVLVTGATKGIGLALSLRLANLGHQV------------IGIARSAIDDFPGELFACDLADIEQTAATLAQINEIHP-V 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  94 DILVNN---ALPGyqfnpsadytSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNpVVTYYD 170
Cdd:PRK07577   70 DAIVNNvgiALPQ----------PLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNICSRAIFG-ALDRTS 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 171 YTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKtTDASRLTTEAVFD---YIATTTPLRQATSVDDFANSVLLMASDL 247
Cdd:PRK07577  139 YSAAKSALVGCTRTWALELAEYGITVNAVAPGPIE-TELFRQTRPVGSEeekRVLASIPMRRLGTPEEVAAAIAFLLSDD 217
                         250
                  ....*....|....
gi 1918264442 248 SAAITGQSIAVDGG 261
Cdd:PRK07577  218 AGFITGQVLGVDGG 231
PRK07791 PRK07791
short chain dehydrogenase; Provisional
15-261 3.12e-25

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 100.90  E-value: 3.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNYL--------NSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEV 86
Cdd:PRK07791    7 RVVIVTGAGGGIGRAHALAFAAEGARVVVNDIgvgldgsaSGGSAAQAVVDEIVAAGGEAVANGDDIADWDGAANLVDAA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  87 TARYGRIDILVNNAlpgyQFNPSADYTSIETVQWShftqqidgivkgAVNAVQ-----AVL--------PQMKAQKT--G 151
Cdd:PRK07791   87 VETFGGLDVLVNNA----GILRDRMIANMSEEEWD------------AVIAVHlkghfATLrhaaaywrAESKAGRAvdA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 152 KILNISTNLVYNPVVTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAggllkTTDASRLTTEAVFDYIATTtplrQAT 231
Cdd:PRK07791  151 RIINTSSGAGLQGSVGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIA-----PAARTRMTETVFAEMMAKP----EEG 221
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1918264442 232 SVDDFANS-----VLLMASDLSAAITGQSIAVDGG 261
Cdd:PRK07791  222 EFDAMAPEnvsplVVWLGSAESRDVTGKVFEVEGG 256
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
12-261 5.12e-25

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 99.59  E-value: 5.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGAS-VCVNYlnsQEAADTvvADIVAAGGQAFAY-QADVTELEQMQGMANEVTAR 89
Cdd:PRK12481    6 LNGKVAIITGCNTGLGQGMAIGLAKAGADiVGVGV---AEAPET--QAQVEALGRKFHFiTADLIQQKDIDSIVSQAVEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  90 YGRIDILVNNAlpgyQFNPSADYTSIETVQWSHFtqqIDGIVKGAVNAVQAVLPQMKAQKTG-KILNISTNLVYNPVVTY 168
Cdd:PRK12481   81 MGHIDILINNA----GIIRRQDLLEFGNKDWDDV---ININQKTVFFLSQAVAKQFVKQGNGgKIINIASMLSFQGGIRV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 169 YDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRL-TTEAVFDYIATTTPLRQATSVDDFANSVLLMASDL 247
Cdd:PRK12481  154 PSYTASKSAVMGLTRALATELSQYNINVNAIAPGYMATDNTAALrADTARNEAILERIPASRWGTPDDLAGPAIFLSSSA 233
                         250
                  ....*....|....
gi 1918264442 248 SAAITGQSIAVDGG 261
Cdd:PRK12481  234 SDYVTGYTLAVDGG 247
PRK06914 PRK06914
SDR family oxidoreductase;
14-206 6.54e-25

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 100.10  E-value: 6.54e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVcVNYLNSQEAADTVVADIVAAGGQA--FAYQADVTELEQMQGmANEVTARYG 91
Cdd:PRK06914    3 KKIAIVTGASSGFGLLTTLELAKKGYLV-IATMRNPEKQENLLSQATQLNLQQniKVQQLDVTDQNSIHN-FQLVLKEIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpGYqfnpsADYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNIS--TNLVYNPVvtYY 169
Cdd:PRK06914   81 RIDLLVNNA--GY-----ANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISsiSGRVGFPG--LS 151
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1918264442 170 DYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT 206
Cdd:PRK06914  152 PYVSSKYALEGFSESLRLELKPFGIDVALIEPGSYNT 188
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
13-264 6.95e-25

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: 99.46  E-value: 6.95e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  13 LNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADtvVADIVAA--GGQAFAYQADVTELEQMQGMANEVTARY 90
Cdd:cd05322     1 MNQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEK--VADEINAeyGEKAYGFGADATNEQSVIALSKGVDEIF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  91 GRIDILVNNAlpgyQFNPSADYTSIETVQWShFTQQIDgIVKGAVNAVQAVLPQMKAQKTGKILNISTNlvYNPVVTYYD 170
Cdd:cd05322    79 KRVDLLVYSA----GIAKSAKITDFELGDFD-RSLQVN-LVGYFLCAREFSKLMIRDGIQGRIIQINSK--SGKVGSKHN 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 171 --YTTAKSALIGLTRNLAAELGQYGIRVN-LLAGGLLKT--------TDASRL--TTEAVFDYIATTTPLRQATSVDDFA 237
Cdd:cd05322   151 sgYSAAKFGGVGLTQSLALDLAEHGITVNsLMLGNLLKSpmfqsllpQYAKKLgiKESEVEQYYIDKVPLKRGCDYQDVL 230
                         250       260
                  ....*....|....*....|....*..
gi 1918264442 238 NSVLLMASDLSAAITGQSIAVDGGLTM 264
Cdd:cd05322   231 NMLLFYASPKASYCTGQSINITGGQVM 257
PRK07062 PRK07062
SDR family oxidoreductase;
15-262 7.93e-25

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 99.35  E-value: 7.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASV--CVNylnSQEAADTVVADIVAA--GGQAFAYQADVTELEQMQGMANEVTARY 90
Cdd:PRK07062    9 RVAVVTGGSSGIGLATVELLLEAGASVaiCGR---DEERLASAEARLREKfpGARLLAARCDVLDEADVAAFAAAVEARF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  91 GRIDILVNNALPGYqFNPSADyTSIEtvQWSHftqQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNP----VV 166
Cdd:PRK07062   86 GGVDMLVNNAGQGR-VSTFAD-TTDD--AWRD---ELELKYFSVINPTRAFLPLLRASAAASIVCVNSLLALQPephmVA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 167 TyydyTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASR---------LTTEAVFDYIATT--TPLRQATSVDD 235
Cdd:PRK07062  159 T----SAARAGLLNLVKSLATELAPKGVRVNSILLGLVESGQWRRryearadpgQSWEAWTAALARKkgIPLGRLGRPDE 234
                         250       260
                  ....*....|....*....|....*..
gi 1918264442 236 FANSVLLMASDLSAAITGQSIAVDGGL 262
Cdd:PRK07062  235 AARALFFLASPLSSYTTGSHIDVSGGF 261
PRK07060 PRK07060
short chain dehydrogenase; Provisional
15-263 9.44e-25

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 98.63  E-value: 9.44e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCvnylnsqeAADTVVADIVAAGGQAFA--YQADVTEleqmQGMANEVTARYGR 92
Cdd:PRK07060   10 KSVLVTGASSGIGRACAVALAQRGARVV--------AAARNAAALDRLAGETGCepLRLDVGD----DAAIRAALAAAGA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  93 IDILVNNAlpgyqfnPSADYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQM-KAQKTGKILNISTNLVYNPVVTYYDY 171
Cdd:PRK07060   78 FDGLVNCA-------GIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMiAAGRGGSIVNVSSQAALVGLPDHLAY 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 172 TTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAV-FDYIATTTPLRQATSVDDFANSVLLMASDLSAA 250
Cdd:PRK07060  151 CASKAALDAITRVLCVELGPHGIRVNSVNPTVTLTPMAAEAWSDPQkSGPMLAAIPLGRFAEVDDVAAPILFLLSDAASM 230
                         250
                  ....*....|...
gi 1918264442 251 ITGQSIAVDGGLT 263
Cdd:PRK07060  231 VSGVSLPVDGGYT 243
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
12-261 9.85e-25

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 98.79  E-value: 9.85e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGAS-VCVNYLNSQEAadtvVADIVAAGGQAFAYQADVTELEQMQGMANEVTARY 90
Cdd:PRK08993    8 LEGKVAVVTGCDTGLGQGMALGLAEAGCDiVGINIVEPTET----IEQVTALGRRFLSLTADLRKIDGIPALLERAVAEF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  91 GRIDILVNNAlPGYQFNPSADYTSietvqwshftQQIDGIVKGAVNAV----QAVLPQMKAQ-KTGKILNISTNLVYNPV 165
Cdd:PRK08993   84 GHIDILVNNA-GLIRREDAIEFSE----------KDWDDVMNLNIKSVffmsQAAAKHFIAQgNGGKIINIASMLSFQGG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 166 VTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTE-----AVFDYIatttPLRQATSVDDFANSV 240
Cdd:PRK08993  153 IRVPSYTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATNNTQQLRADeqrsaEILDRI----PAGRWGLPSDLMGPV 228
                         250       260
                  ....*....|....*....|.
gi 1918264442 241 LLMASDLSAAITGQSIAVDGG 261
Cdd:PRK08993  229 VFLASSASDYINGYTIAVDGG 249
PRK07109 PRK07109
short chain dehydrogenase; Provisional
14-198 2.93e-24

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 99.23  E-value: 2.93e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVCVnYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRI 93
Cdd:PRK07109    8 RQVVVITGASAGVGRATARAFARRGAKVVL-LARGEEGLEALAAEIRAAGGEALAVVADVADAEAVQAAADRAEEELGPI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  94 DILVNNALPGYqFNPSADYTSIEtvqwshFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDYTT 173
Cdd:PRK07109   87 DTWVNNAMVTV-FGPFEDVTPEE------FRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALAYRSIPLQSAYCA 159
                         170       180
                  ....*....|....*....|....*
gi 1918264442 174 AKSALIGLTRNLAAELGQYGIRVNL 198
Cdd:PRK07109  160 AKHAIRGFTDSLRCELLHDGSPVSV 184
PRK06198 PRK06198
short chain dehydrogenase; Provisional
9-259 3.43e-24

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 97.77  E-value: 3.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442   9 PAFLLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTA 88
Cdd:PRK06198    1 MGRLDGKVALVTGGTQGLGAAIARAFAERGAAGLVICGRNAEKGEAQAAELEALGAKAVFVQADLSDVEDCRRVVAAADE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  89 RYGRIDILVNNAlpGYQFNPSADYTSIETvqwshFTQQIDGIVKGAVNAVQAVLPQMKAQKT-GKILNISTNLVYNPVVT 167
Cdd:PRK06198   81 AFGRLDALVNAA--GLTDRGTILDTSPEL-----FDRHFAVNVRAPFFLMQEAIKLMRRRKAeGTIVNIGSMSAHGGQPF 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 168 YYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT---TDASRLTTEAVFDYI---ATTTPLRQATSVDDFANSVL 241
Cdd:PRK06198  154 LAAYCASKGALATLTRNAAYALLRNRIRVNGLNIGWMATegeDRIQREFHGAPDDWLekaAATQPFGRLLDPDEVARAVA 233
                         250
                  ....*....|....*...
gi 1918264442 242 LMASDLSAAITGQSIAVD 259
Cdd:PRK06198  234 FLLSDESGLMTGSVIDFD 251
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
16-207 6.96e-24

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: 96.54  E-value: 6.96e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  16 VVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVaDIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRIDI 95
Cdd:cd05339     1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETAN-NVRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  96 LVNNA--LPGYQFNpSADYTSIETvqwshfTQQIDgiVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDYTT 173
Cdd:cd05339    80 LINNAgvVSGKKLL-ELPDEEIEK------TFEVN--TLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCA 150
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1918264442 174 AKSALIGLTRNLAAELGQY---GIRVNLLAGGLLKTT 207
Cdd:cd05339   151 SKAAAVGFHESLRLELKAYgkpGIKTTLVCPYFINTG 187
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
12-264 1.06e-23

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: 96.27  E-value: 1.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVAdivaAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:cd05348     2 LKGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRAD----FGDAVVGVEGDVRSLADNERAVARCVERFG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpgyqfnPSADY-TSIETVQWSHFTQQIDGI----VKGAVNAVQAVLPQMKAQKTGKILNIStNLVYNPVV 166
Cdd:cd05348    78 KLDCFIGNA-------GIWDYsTSLVDIPEEKLDEAFDELfhinVKGYILGAKAALPALYATEGSVIFTVS-NAGFYPGG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 167 TYYDYTTAKSALIGLTRNLAAELGQYgIRVNLLAGGLLKTT---------DASRLTTEAVFDYIATTTPLRQATSVDDFA 237
Cdd:cd05348   150 GGPLYTASKHAVVGLVKQLAYELAPH-IRVNGVAPGGMVTDlrgpaslgqGETSISTPPLDDMLKSILPLGFAPEPEDYT 228
                         250       260
                  ....*....|....*....|....*...
gi 1918264442 238 NSVLLMAS-DLSAAITGQSIAVDGGLTM 264
Cdd:cd05348   229 GAYVFLASrGDNRPATGTVINYDGGMGV 256
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
12-262 1.07e-23

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 96.36  E-value: 1.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNsQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK08085    7 LAGKNILITGSAQGIGFLLATGLAEYGAEIIINDIT-AERAELAVAKLRQEGIKAHAAPFNVTHKQEVEAAIEHIEKDIG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNA-----LPGYQFnPSADYTSIETV-QWSHFtqqidgIVKgavnavQAVLPQMKAQKTGKILNISTNLVYNPV 165
Cdd:PRK08085   86 PIDVLINNAgiqrrHPFTEF-PEQEWNDVIAVnQTAVF------LVS------QAVARYMVKRQAGKIINICSMQSELGR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 166 VTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVF-DYIATTTPLRQATSVDDFANSVLLMA 244
Cdd:PRK08085  153 DTITPYAASKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMTKALVEDEAFtAWLCKRTPAARWGDPQELIGAAVFLS 232
                         250
                  ....*....|....*...
gi 1918264442 245 SDLSAAITGQSIAVDGGL 262
Cdd:PRK08085  233 SKASDFVNGHLLFVDGGM 250
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
16-189 1.81e-23

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: 95.14  E-value: 1.81e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  16 VVIVTGASRGLGAQIAQKMAGAGASVcVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRIDI 95
Cdd:cd05360     2 VVVITGASSGIGRATALAFAERGAKV-VLAARSAEALHELAREVRELGGEAIAVVADVADAAQVERAADTAVERFGRIDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  96 LVNNALpgyqfnpSADYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDYTTAK 175
Cdd:cd05360    81 WVNNAG-------VAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRSAPLQAAYSASK 153
                         170
                  ....*....|....
gi 1918264442 176 SALIGLTRNLAAEL 189
Cdd:cd05360   154 HAVRGFTESLRAEL 167
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
12-264 2.02e-23

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: 95.38  E-value: 2.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSqEAADTVVADIvaaGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:cd05363     1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINL-EAARATAAEI---GPAACAISLDVTDQASIDRCVAALVDRWG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpgyqfnPSADYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQ-KTGKILNISTNLVYNPVVTYYD 170
Cdd:cd05363    77 SIDILVNNA-------ALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQgRGGKIINMASQAGRRGEALVGV 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 171 YTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT-----TDA-------------SRLTTEAVfdyiatttPLRQATS 232
Cdd:cd05363   150 YCATKAAVISLTQSAGLNLIRHGINVNAIAPGVVDGehwdgVDAkfaryenrprgekKRLVGEAV--------PFGRMGR 221
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1918264442 233 VDDFANSVLLMASDLSAAITGQSIAVDGGLTM 264
Cdd:cd05363   222 AEDLTGMAIFLASTDADYIVAQTYNVDGGNWM 253
PRK05855 PRK05855
SDR family oxidoreductase;
15-206 2.85e-23

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 98.51  E-value: 2.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVvADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRID 94
Cdd:PRK05855  316 KLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTA-ELIRAAGAVAHAYRVDVSDADAMEAFAEWVRAEHGVPD 394
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  95 ILVNNALPGyQFNPSADyTSIEtvQWshftQQIDGI-VKGAVNAVQAVLPQMKAQKT-GKILNISTNLVYNPVVTYYDYT 172
Cdd:PRK05855  395 IVVNNAGIG-MAGGFLD-TSAE--DW----DRVLDVnLWGVIHGCRLFGRQMVERGTgGHIVNVASAAAYAPSRSLPAYA 466
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1918264442 173 TAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT 206
Cdd:PRK05855  467 TSKAAVLMLSECLRAELAAAGIGVTAICPGFVDT 500
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
12-262 3.07e-23

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 95.02  E-value: 3.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLnSQEAADTVVADIvaaGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK06200    4 LHGQVALITGGGSGIGRALVERFLAEGARVAVLER-SAEKLASLRQRF---GDHVLVVEGDVTSYADNQRAVDQTVDAFG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpG-YQFnpsadYTSIETVQWSHFTQQIDGI----VKGAVNAVQAVLPQMKAQKTGKILNISTNlvynpvv 166
Cdd:PRK06200   80 KLDCFVGNA--GiWDY-----NTSLVDIPAETLDTAFDEIfnvnVKGYLLGAKAALPALKASGGSMIFTLSNS------- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 167 TYYD------YTTAKSALIGLTRNLAAELGQYgIRVNLLAGGLLKT---------TDASRLTT-EAVFDYIATTTPLRQA 230
Cdd:PRK06200  146 SFYPggggplYTASKHAVVGLVRQLAYELAPK-IRVNGVAPGGTVTdlrgpaslgQGETSISDsPGLADMIAAITPLQFA 224
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1918264442 231 TSVDDFANSVLLMASD-LSAAITGQSIAVDGGL 262
Cdd:PRK06200  225 PQPEDHTGPYVLLASRrNSRALTGVVINADGGL 257
PRK06125 PRK06125
short chain dehydrogenase; Provisional
12-263 3.29e-23

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 95.11  E-value: 3.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVcVNYLNSQEAADTVVADIVAAGGQAFAYQA-DVTELEQMQgmanEVTARY 90
Cdd:PRK06125    5 LAGKRVLITGASKGIGAAAAEAFAAEGCHL-HLVARDADALEALAADLRAAHGVDVAVHAlDLSSPEARE----QLAAEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  91 GRIDILVNNA--LPGyqfnpsADYTSIETVQWSHftqQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTY 168
Cdd:PRK06125   80 GDIDILVNNAgaIPG------GGLDDVDDAAWRA---GWELKVFGYIDLTRLAYPRMKARGSGVIVNVIGAAGENPDADY 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 169 YDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGG---------LLKTTDASRLTTEAVFDYIATTTPLRQATSVDDFANS 239
Cdd:PRK06125  151 ICGSAGNAALMAFTRALGGKSLDDGVRVVGVNPGpvatdrmltLLKGRARAELGDESRWQELLAGLPLGRPATPEEVADL 230
                         250       260
                  ....*....|....*....|....
gi 1918264442 240 VLLMASDLSAAITGQSIAVDGGLT 263
Cdd:PRK06125  231 VAFLASPRSGYTSGTVVTVDGGIS 254
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
12-264 4.11e-23

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 94.64  E-value: 4.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNsQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK08217    3 LKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLN-QEKLEEAVAECGALGTEVRGYAANVTDEEDVEATFAQIAEDFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNA--LPGYQFNPSADYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQM-KAQKTGKILNIS----------T 158
Cdd:PRK08217   82 QLNGLINNAgiLRDGLLVKAKDGKVTSKMSLEQFQSVIDVNLTGVFLCGREAAAKMiESGSKGVIINISsiaragnmgqT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 159 NlvynpvvtyydYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVfDYIATTTPLRQATSVDDFAN 238
Cdd:PRK08217  162 N-----------YSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTAAMKPEAL-ERLEKMIPVGRLGEPEEIAH 229
                         250       260
                  ....*....|....*....|....*..
gi 1918264442 239 SV-LLMASDLsaaITGQSIAVDGGLTM 264
Cdd:PRK08217  230 TVrFIIENDY---VTGRVLEIDGGLRL 253
PRK06500 PRK06500
SDR family oxidoreductase;
12-261 2.69e-22

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 92.33  E-value: 2.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNsqeaADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK06500    4 LQGKTALITGGTSGIGLETARQFLAEGARVAITGRD----PASLEAARAELGESALVIRADAGDVAAQKALAQALAEAFG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpgyqfnPSADYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMkAQKTGKILNISTN----LVYNPVvt 167
Cdd:PRK06500   80 RLDAVFINA-------GVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLL-ANPASIVLNGSINahigMPNSSV-- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 168 yydYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRL-----TTEAVFDYIATTTPLRQATSVDDFANSVLL 242
Cdd:PRK06500  150 ---YAASKAALLSLAKTLSGELLPRGIRVNAVSPGPVQTPLYGKLglpeaTLDAVAAQIQALVPLGRFGTPEEIAKAVLY 226
                         250
                  ....*....|....*....
gi 1918264442 243 MASDLSAAITGQSIAVDGG 261
Cdd:PRK06500  227 LASDESAFIVGSEIIVDGG 245
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
14-264 3.72e-22

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 91.56  E-value: 3.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVCvnylnsqeAADtvVADIVAAGGQAFAYQADVTelEQMQGMANEVtaryGRI 93
Cdd:PRK06550    5 TKTVLITGAASGIGLAQARAFLAQGAQVY--------GVD--KQDKPDLSGNFHFLQLDLS--DDLEPLFDWV----PSV 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  94 DILVNNA--LPGYQfnPSADyTSIETVQwshftQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDY 171
Cdd:PRK06550   69 DILCNTAgiLDDYK--PLLD-TSLEEWQ-----HIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAGGGGAAY 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 172 TTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT-TDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSAA 250
Cdd:PRK06550  141 TASKHALAGFTKQLALDYAKDGIQVFGIAPGAVKTpMTAADFEPGGLADWVARETPIKRWAEPEEVAELTLFLASGKADY 220
                         250
                  ....*....|....
gi 1918264442 251 ITGQSIAVDGGLTM 264
Cdd:PRK06550  221 MQGTIVPIDGGWTL 234
PRK07326 PRK07326
SDR family oxidoreductase;
11-196 4.11e-22

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 91.61  E-value: 4.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  11 FLLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADtvVADIVAAGGQAFAYQADVTELEQMQGMANEVTARY 90
Cdd:PRK07326    3 SLKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEE--AAAELNNKGNVLGLAADVRDEADVQRAVDAIVAAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  91 GRIDILVNNALPGYqFNPSADYTsIEtvQWShftQQIDGIVKGAVNAVQAVLPQMKAQKtGKILNISTNLVYNPVVTYYD 170
Cdd:PRK07326   81 GGLDVLIANAGVGH-FAPVEELT-PE--EWR---LVIDTNLTGAFYTIKAAVPALKRGG-GYIINISSLAGTNFFAGGAA 152
                         170       180
                  ....*....|....*....|....*.
gi 1918264442 171 YTTAKSALIGLTRNLAAELGQYGIRV 196
Cdd:PRK07326  153 YNASKFGLVGFSEAAMLDLRQYGIKV 178
PRK06057 PRK06057
short chain dehydrogenase; Provisional
12-263 6.75e-22

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 91.33  E-value: 6.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVcvnylnsqeaadtVVADIVAAGGQAFA-------YQADVTELEQMQGMAN 84
Cdd:PRK06057    5 LAGRVAVITGGGSGIGLATARRLAAEGATV-------------VVGDIDPEAGKAAAdevgglfVPTDVTDEDAVNALFD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  85 EVTARYGRIDILVNNAlpgyQFNPSADyTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNL-VYN 163
Cdd:PRK06057   72 TAAETYGSVDIAFNNA----GISPPED-DSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASFVaVMG 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 164 PVVTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT--------TDASRLTTEAVFdyiattTPLRQATSVDD 235
Cdd:PRK06057  147 SATSQISYTASKGGVLAMSRELGVQFARQGIRVNALCPGPVNTpllqelfaKDPERAARRLVH------VPMGRFAEPEE 220
                         250       260
                  ....*....|....*....|....*...
gi 1918264442 236 FANSVLLMASDLSAAITGQSIAVDGGLT 263
Cdd:PRK06057  221 IAAAVAFLASDDASFITASTFLVDGGIS 248
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
12-199 7.76e-22

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 90.90  E-value: 7.76e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGasVCVNYLNSQEAADTVVADIVAAGGQAFAYQ-ADVTELEQMQGMANEVTARY 90
Cdd:PRK07666    5 LQGKNALITGAGRGIGRAVAIALAKEG--VNVGLLARTEENLKAVAEEVEAYGVKVVIAtADVSDYEEVTAAIEQLKNEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  91 GRIDILVNNALPGyQFnpsADYTSIETVQWshfTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYD 170
Cdd:PRK07666   83 GSIDILINNAGIS-KF---GKFLELDPAEW---EKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKGAAVTSA 155
                         170       180
                  ....*....|....*....|....*....
gi 1918264442 171 YTTAKSALIGLTRNLAAELGQYGIRVNLL 199
Cdd:PRK07666  156 YSASKFGVLGLTESLMQEVRKHNIRVTAL 184
PRK05872 PRK05872
short chain dehydrogenase; Provisional
12-196 9.62e-22

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 91.57  E-value: 9.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNsqEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK05872    7 LAGKVVVVTGAARGIGAELARRLHARGAKLALVDLE--EAELAALAAELGGDDRVLTVVADVTDLAAMQAAAEEAVERFG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpGYqfnpsADYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKtGKILNISTNLVYNPVVTYYDY 171
Cdd:PRK05872   85 GIDVVVANA--GI-----ASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERR-GYVLQVSSLAAFAAAPGMAAY 156
                         170       180
                  ....*....|....*....|....*
gi 1918264442 172 TTAKSALIGLTRNLAAELGQYGIRV 196
Cdd:PRK05872  157 CASKAGVEAFANALRLEVAHHGVTV 181
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
11-261 1.34e-21

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


Pssm-ID: 187609 [Multi-domain]  Cd Length: 244  Bit Score: 90.22  E-value: 1.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  11 FLLNKVVIVTGASRGLGAQIAQKMAGAGASVcVNYLNSQEAADTVVADivAAGGQAFayQADVTELEQMQgmanEVTARY 90
Cdd:cd05351     4 DFAGKRALVTGAGKGIGRATVKALAKAGARV-VAVSRTQADLDSLVRE--CPGIEPV--CVDLSDWDATE----EALGSV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  91 GRIDILVNNAlpgyqfnPSADYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKT-GKILNISTNLVYNPVVTYY 169
Cdd:cd05351    75 GPVDLLVNNA-------AVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGVpGSIVNVSSQASQRALTNHT 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 170 DYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLkTTDASRLT------TEAVFDYIatttPLRQATSVDDFANSVLLM 243
Cdd:cd05351   148 VYCSTKAALDMLTKVMALELGPHKIRVNSVNPTVV-MTDMGRDNwsdpekAKKMLNRI----PLGKFAEVEDVVNAILFL 222
                         250
                  ....*....|....*...
gi 1918264442 244 ASDLSAAITGQSIAVDGG 261
Cdd:cd05351   223 LSDKSSMTTGSTLPVDGG 240
PRK07831 PRK07831
SDR family oxidoreductase;
12-258 1.44e-21

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 90.48  E-value: 1.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGAS-RGLGAQIAQKMAGAGASVCVNYLNSQ---EAADTVVADivAAGGQAFAYQADVTELEQMQGMANEVT 87
Cdd:PRK07831   15 LAGKVVLVTAAAgTGIGSATARRALEEGARVVISDIHERrlgETADELAAE--LGLGRVEAVVCDVTSEAQVDALIDAAV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  88 ARYGRIDILVNNALPGYQfNPSADYTSietVQWSHFtqqIDGIVKGAVNAVQAVLPQMKAQKT-GKILNISTNLVYNPVV 166
Cdd:PRK07831   93 ERLGRLDVLVNNAGLGGQ-TPVVDMTD---DEWSRV---LDVTLTGTFRATRAALRYMRARGHgGVIVNNASVLGWRAQH 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 167 TYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASD 246
Cdd:PRK07831  166 GQAHYAAAKAGVMALTRCSALEAAEYGVRINAVAPSIAMHPFLAKVTSAELLDELAAREAFGRAAEPWEVANVIAFLASD 245
                         250
                  ....*....|..
gi 1918264442 247 LSAAITGQSIAV 258
Cdd:PRK07831  246 YSSYLTGEVVSV 257
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
12-241 2.80e-21

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: 89.29  E-value: 2.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYlNSQEAADTVVADIVAAGgqafAYQADVTELEQMQGMANEVTARYG 91
Cdd:cd05370     3 LTGNTVLITGGTSGIGLALARKFLEAGNTVIITG-RREERLAEAKKELPNIH----TIVLDVGDAESVEALAEALLSEYP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNALPGYQFNPSADYTSIETVQwshftQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDY 171
Cdd:cd05370    78 NLDILINNAGIQRPIDLRDPASDLDKAD-----TEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANPVY 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 172 TTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTdasrLTTEAVFDYIATTTPLrqatSVDDFANSVL 241
Cdd:cd05370   153 CATKAALHSYTLALRHQLKDTGVEVVEIVPPAVDTE----LHEERRNPDGGTPRKM----PLDEFVDEVV 214
PRK05866 PRK05866
SDR family oxidoreductase;
9-206 3.68e-21

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 90.19  E-value: 3.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442   9 PAFLLNKVVIVTGASRGLGAQIAQKMAGAGASVCVnYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTA 88
Cdd:PRK05866   35 PVDLTGKRILLTGASSGIGEAAAEQFARRGATVVA-VARREDLLDAVADRITRAGGDAMAVPCDLSDLDAVDALVADVEK 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  89 RYGRIDILVNNAlpGYQF-NPSADytSIEtvQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVT 167
Cdd:PRK05866  114 RIGGVDILINNA--GRSIrRPLAE--SLD--RWHDVERTMVLNYYAPLRLIRGLAPGMLERGDGHIINVATWGVLSEASP 187
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1918264442 168 YYD-YTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT 206
Cdd:PRK05866  188 LFSvYNASKAALSAVSRVIETEWGDRGVHSTTLYYPLVAT 227
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
15-238 4.05e-21

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: 89.43  E-value: 4.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARY-GRI 93
Cdd:cd09763     4 KIALVTGASRGIGRGIALQLGEAGATVYITGRTILPQLPGTAEEIEARGGKCIPVRCDHSDDDEVEALFERVAREQqGRL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  94 DILVNNALPGYQfnpsADYTSIETVQWSHFTQQIDGIVKGAVNA-----VQAVlPQMKAQKTGKILNIST----NLVYNP 164
Cdd:cd09763    84 DILVNNAYAAVQ----LILVGVAKPFWEEPPTIWDDINNVGLRAhyacsVYAA-PLMVKAGKGLIVIISStgglEYLFNV 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1918264442 165 vvtYYDytTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKttdasrltTEAVFDYIATTTPLRQATSVDDFAN 238
Cdd:cd09763   159 ---AYG--VGKAAIDRMAADMAHELKPHGVAVVSLWPGFVR--------TELVLEMPEDDEGSWHAKERDAFLN 219
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
12-241 5.66e-21

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: 88.75  E-value: 5.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVnYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:cd08934     1 LQGKVALVTGASSGIGEATARALAAEGAAVAI-AARRVDRLEALADELEAEGGKALVLELDVTDEQQVDAAVERTVEALG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNALPGYqFNPsadytsIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDY 171
Cdd:cd08934    80 RLDILVNNAGIML-LGP------VEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVY 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1918264442 172 TTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRL----TTEAVFDYIATTTPLRQatsvDDFANSVL 241
Cdd:cd08934   153 NATKFGVNAFSEGLRQEVTERGVRVVVIEPGTVDTELRDHIthtiTKEAYEERISTIRKLQA----EDIAAAVR 222
PRK12744 PRK12744
SDR family oxidoreductase;
12-263 7.52e-21

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 88.64  E-value: 7.52e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNS---QEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTA 88
Cdd:PRK12744    6 LKGKVVLIAGGAKNLGGLIARDLAAQGAKAVAIHYNSaasKADAEETVAAVKAAGAKAVAFQADLTTAAAVEKLFDDAKA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  89 RYGRIDILVNNAlpGYQF-NPSADYTSIETVQWShftqqidgivkgAVNAVQAVLPQMKAQKT----GKILNISTNLV-- 161
Cdd:PRK12744   86 AFGRPDIAINTV--GKVLkKPIVEISEAEYDEMF------------AVNSKSAFFFIKEAGRHlndnGKIVTLVTSLLga 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 162 YNPVvtYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTT-DASRLTTEAVfDYIATTTPL-----RQATSVDD 235
Cdd:PRK12744  152 FTPF--YSAYAGSKAPVEHFTRAASKEFGARGISVTAVGPGPMDTPfFYPQEGAEAV-AYHKTAAALspfskTGLTDIED 228
                         250       260
                  ....*....|....*....|....*...
gi 1918264442 236 FANSVLLMASDlSAAITGQSIAVDGGLT 263
Cdd:PRK12744  229 IVPFIRFLVTD-GWWITGQTILINGGYT 255
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
15-261 1.14e-20

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 88.21  E-value: 1.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASR--GLGAQIAQKMAGAGASVCVNYLNSQEAA---------DTVVADIVAAGGQAFAY-QADVTELEQMQGM 82
Cdd:PRK12748    6 KIALVTGASRlnGIGAAVCRRLAAKGIDIFFTYWSPYDKTmpwgmhdkePVLLKEEIESYGVRCEHmEIDLSQPYAPNRV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  83 ANEVTARYGRIDILVNNALPGYQfnpsadyTSIETVQwshfTQQIDGivKGAVNA------VQAVLPQMKAQKTGKILNI 156
Cdd:PRK12748   86 FYAVSERLGDPSILINNAAYSTH-------TRLEELT----AEQLDK--HYAVNVratmllSSAFAKQYDGKAGGRIINL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 157 STNLVYNPVVTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDAsrltTEAVFDYIATTTPLRQATSVDDF 236
Cdd:PRK12748  153 TSGQSLGPMPDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDTGWI----TEELKHHLVPKFPQGRVGEPVDA 228
                         250       260
                  ....*....|....*....|....*
gi 1918264442 237 ANSVLLMASDLSAAITGQSIAVDGG 261
Cdd:PRK12748  229 ARLIAFLVSEEAKWITGQVIHSEGG 253
PRK07825 PRK07825
short chain dehydrogenase; Provisional
15-196 1.46e-20

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 88.07  E-value: 1.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNsQEAADTVVADIvaagGQAFAYQADVTELEQMQGMANEVTARYGRID 94
Cdd:PRK07825    6 KVVAITGGARGIGLATARALAALGARVAIGDLD-EALAKETAAEL----GLVVGGPLDVTDPASFAAFLDAVEADLGPID 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  95 ILVNNA--LPGYQFNPSADYTSietvqwshfTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNIST--NLVYNP-VVTyy 169
Cdd:PRK07825   81 VLVNNAgvMPVGPFLDEPDAVT---------RRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVASlaGKIPVPgMAT-- 149
                         170       180
                  ....*....|....*....|....*..
gi 1918264442 170 dYTTAKSALIGLTRNLAAELGQYGIRV 196
Cdd:PRK07825  150 -YCASKHAVVGFTDAARLELRGTGVHV 175
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
15-207 1.72e-20

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: 87.34  E-value: 1.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVC-----VNYLnsQEAADTVVADIvaaGGQAFAYQADVTELEQMQGMANEVTAR 89
Cdd:cd05346     1 KTVLITGASSGIGEATARRFAKAGAKLIltgrrAERL--QELADELGAKF---PVKVLPLQLDVSDRESIEAALENLPEE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  90 YGRIDILVNNA-----LPGYQfnpSADYTSIETVqwshftqqIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNP 164
Cdd:cd05346    76 FRDIDILVNNAglalgLDPAQ---EADLEDWETM--------IDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYP 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1918264442 165 VVTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTT 207
Cdd:cd05346   145 YAGGNVYCATKAAVRQFSLNLRKDLIGTGIRVTNIEPGLVETE 187
PRK06949 PRK06949
SDR family oxidoreductase;
12-262 2.03e-20

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 87.51  E-value: 2.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCvnyLNSQ--EAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTAR 89
Cdd:PRK06949    7 LEGKVALVTGASSGLGARFAQVLAQAGAKVV---LASRrvERLKELRAEIEAEGGAAHVVSLDVTDYQSIKAAVAHAETE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  90 YGRIDILVNNAlpgyqfnPSADYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQ--------KTGKILNISTNLV 161
Cdd:PRK06949   84 AGTIDILVNNS-------GVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIARakgagntkPGGRIINIASVAG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 162 YNPVVTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT--------TDASRLTTEAVfdyiatttPLRQATSV 233
Cdd:PRK06949  157 LRVLPQIGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTeinhhhweTEQGQKLVSML--------PRKRVGKP 228
                         250       260
                  ....*....|....*....|....*....
gi 1918264442 234 DDFANSVLLMASDLSAAITGQSIAVDGGL 262
Cdd:PRK06949  229 EDLDGLLLLLAADESQFINGAIISADDGF 257
PRK05875 PRK05875
short chain dehydrogenase; Provisional
12-261 2.14e-20

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 87.94  E-value: 2.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQ-ADVTELEQMQGMANEVTARY 90
Cdd:PRK05875    5 FQDRTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEIEALKGAGAVRYEpADVTDEDQVARAVDAATAWH 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  91 GRIDILVNNALPGYQFNPsadYTSIETVQWShftQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYD 170
Cdd:PRK05875   85 GRLHGVVHCAGGSETIGP---ITQIDSDAWR---RTVDLNVNGTMYVLKHAARELVRGGGGSFVGISSIAASNTHRWFGA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 171 YTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTT-DASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSA 249
Cdd:PRK05875  159 YGVTKSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDlVAPITESPELSADYRACTPLPRVGEVEDVANLAMFLLSDAAS 238
                         250
                  ....*....|..
gi 1918264442 250 AITGQSIAVDGG 261
Cdd:PRK05875  239 WITGQVINVDGG 250
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
16-264 3.07e-20

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


Pssm-ID: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 86.48  E-value: 3.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  16 VVIVTGASRGLGAQIAQKMAGAGASV-CVnylnsqeaaDTVVADivAAGGQAFAyqadvTELEQMQGMANE--------V 86
Cdd:cd05361     3 IALVTHARHFAGPASAEALTEDGYTVvCH---------DASFAD--AAERQAFE-----SENPGTKALSEQkpeelvdaV 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  87 TARYGRIDILVNNALPGYQFNPSADYTSIEtvqwshFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVV 166
Cdd:cd05361    67 LQAGGAIDVLVSNDYIPRPMNPIDGTSEAD------IRQAFEALSIFPFALLQAAIAQMKKAGGGSIIFITSAVPKKPLA 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 167 TYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTD---ASRLTTE-AVFDYIATTTPLRQATSVDDFANSVLL 242
Cdd:cd05361   141 YNSLYGPARAAAVALAESLAKELSRDNILVYAIGPNFFNSPTyfpTSDWENNpELRERVKRDVPLGRLGRPDEMGALVAF 220
                         250       260
                  ....*....|....*....|..
gi 1918264442 243 MASDLSAAITGQSIAVDGGLTM 264
Cdd:cd05361   221 LASRRADPITGQFFAFAGGYLP 242
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
15-258 3.38e-20

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: 86.26  E-value: 3.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVvadivAAGGQAFAYQADVTELEQMQGMANEVTARYGRID 94
Cdd:cd08932     1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALS-----ASGGDVEAVPYDARDPEDARALVDALRDRFGRID 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  95 ILVNNALPGYQfnpsadyTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNI---STNLVYNPVVTyydY 171
Cdd:cd08932    76 VLVHNAGIGRP-------TTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLnslSGKRVLAGNAG---Y 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 172 TTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVFDYIATTTPlrqatsvDDFANSVlLMASDLSAAI 251
Cdd:cd08932   146 SASKFALRALAHALRQEGWDHGVRVSAVCPGFVDTPMAQGLTLVGAFPPEEMIQP-------KDIANLV-RMVIELPENI 217

                  ....*..
gi 1918264442 252 TgqSIAV 258
Cdd:cd08932   218 T--SVAV 222
PRK08278 PRK08278
SDR family oxidoreductase;
12-255 3.51e-20

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 86.88  E-value: 3.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAAD------TVVADIVAAGGQAFAYQADVTELEQMQGMANE 85
Cdd:PRK08278    4 LSGKTLFITGASRGIGLAIALRAARDGANIVIAAKTAEPHPKlpgtihTAAEEIEAAGGQALPLVGDVRDEDQVAAAVAK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  86 VTARYGRIDILVNNAlpgyqfnpSA-DYTSIETVQWSHF--TQQIDgiVKGAVNAVQAVLPQMKAQKTGKILNISTNLVY 162
Cdd:PRK08278   84 AVERFGGIDICVNNA--------SAiNLTGTEDTPMKRFdlMQQIN--VRGTFLVSQACLPHLKKSENPHILTLSPPLNL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 163 NP--VVTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLaggLLKTTDAsrltTEAVFDYIATTTPLRQATSVDDFANSV 240
Cdd:PRK08278  154 DPkwFAPHTAYTMAKYGMSLCTLGLAEEFRDDGIAVNAL---WPRTTIA----TAAVRNLLGGDEAMRRSRTPEIMADAA 226
                         250
                  ....*....|....*
gi 1918264442 241 LLMASDLSAAITGQS 255
Cdd:PRK08278  227 YEILSRPAREFTGNF 241
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
12-264 5.86e-20

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 85.83  E-value: 5.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK12938    1 MSQRIAYVTGGMGGIGTSICQRLHKDGFKVVAGCGPNSPRRVKWLEDQKALGFDFIASEGNVGDWDSTKAAFDKVKAEVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpgyQFNPSADYTSIETVQWshfTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDY 171
Cdd:PRK12938   81 EIDVLVNNA----GITRDVVFRKMTREDW---TAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFGQTNY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 172 TTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLkTTDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSAAI 251
Cdd:PRK12938  154 STAKAGIHGFTMSLAQEVATKGVTVNTVSPGYI-GTDMVKAIRPDVLEKIVATIPVRRLGSPDEIGSIVAWLASEESGFS 232
                         250
                  ....*....|...
gi 1918264442 252 TGQSIAVDGGLTM 264
Cdd:PRK12938  233 TGADFSLNGGLHM 245
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
30-261 7.24e-20

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


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 86.34  E-value: 7.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  30 IAQKMAGAGASVCVNYLNsqEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRIDILVNNAlpgyQFNP- 108
Cdd:PRK08415   23 IAKACFEQGAELAFTYLN--EALKKRVEPIAQELGSDYVYELDVSKPEHFKSLAESLKKDLGKIDFIVHSV----AFAPk 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 109 -SADYTSIETVQwSHFTQQIDGIVKGAVNAVQAVLPQMKaqKTGKILNISTNLVYNPVVTYYDYTTAKSALIGLTRNLAA 187
Cdd:PRK08415   97 eALEGSFLETSK-EAFNIAMEISVYSLIELTRALLPLLN--DGASVLTLSYLGGVKYVPHYNVMGVAKAALESSVRYLAV 173
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1918264442 188 ELGQYGIRVNLLAGGLLKTTDASRLTT-EAVFDYIATTTPLRQATSVDDFANSVLLMASDLSAAITGQSIAVDGG 261
Cdd:PRK08415  174 DLGKKGIRVNAISAGPIKTLAASGIGDfRMILKWNEINAPLKKNVSIEEVGNSGMYLLSDLSSGVTGEIHYVDAG 248
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
17-206 7.36e-20

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: 85.46  E-value: 7.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  17 VIVTGASRGLGAQIAQKMAGAGASVCVNYLNSqEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRIDIL 96
Cdd:cd05350     1 VLITGASSGIGRALAREFAKAGYNVALAARRT-DRLDELKAELLNPNPSVEVEILDVTDEERNQLVIAELEAELGGLDLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  97 VNNAlpgyqfnpsADY--TSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDYTTA 174
Cdd:cd05350    80 IINA---------GVGkgTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAYSAS 150
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1918264442 175 KSALIGLTRNLAAELGQYGIRVNLLAGGLLKT 206
Cdd:cd05350   151 KAALSSLAESLRYDVKKRGIRVTVINPGFIDT 182
PRK07775 PRK07775
SDR family oxidoreductase;
17-252 9.17e-20

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 85.96  E-value: 9.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  17 VIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADtVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRIDIL 96
Cdd:PRK07775   13 ALVAGASSGIGAATAIELAAAGFPVALGARRVEKCEE-LVDKIRADGGEAVAFPLDVTDPDSVKSFVAQAEEALGEIEVL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  97 VNNAlpGYQFNPSADYTSIETvqwshFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDYTTAKS 176
Cdd:PRK07775   92 VSGA--GDTYFGKLHEISTEQ-----FESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALRQRPHMGAYGAAKA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 177 ALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVfdyiatttplrqATSVDDFA------NSVLLMASDLSAA 250
Cdd:PRK07775  165 GLEAMVTNLQMELEGTGVRASIVHPGPTLTGMGWSLPAEVI------------GPMLEDWAkwgqarHDYFLRASDLARA 232

                  ..
gi 1918264442 251 IT 252
Cdd:PRK07775  233 IT 234
PRK08263 PRK08263
short chain dehydrogenase; Provisional
14-202 1.08e-19

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 85.86  E-value: 1.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVCVNylnsqeAADTV-VADIVAA-GGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK08263    3 EKVWFITGASRGFGRAWTEAALERGDRVVAT------ARDTAtLADLAEKyGDRLLPLALDVTDRAAVFAAVETAVEHFG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpGY-QFNPsadytsIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNIST--NLVYNPVVTY 168
Cdd:PRK08263   77 RLDIVVNNA--GYgLFGM------IEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSigGISAFPMSGI 148
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1918264442 169 ydYTTAKSALIGLTRNLAAELGQYGIRVNLLAGG 202
Cdd:PRK08263  149 --YHASKWALEGMSEALAQEVAEFGIKVTLVEPG 180
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
15-254 1.58e-19

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: 85.35  E-value: 1.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASV---CvnylNSQEAADTVVADIVAAGG--QAFAYQADVTELEQMQGMANEVTAR 89
Cdd:cd05327     2 KVVVITGANSGIGKETARELAKRGAHViiaC----RNEEKGEEAAAEIKKETGnaKVEVIQLDLSSLASVRQFAEEFLAR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  90 YGRIDILVNNAlpGYqFNPSADYTS--IEtvqwSHFtqqidgivkgAVNAV------QAVLPQMKAQKTGKILNIS---- 157
Cdd:cd05327    78 FPRLDILINNA--GI-MAPPRRLTKdgFE----LQF----------AVNYLghflltNLLLPVLKASAPSRIVNVSsiah 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 158 ------TNLVYNPVVTYYDYTTA----KSALIGLTRNLAAELGQYGIRVNLLAGGLLKTT----DASRLTTEAVFDYIAT 223
Cdd:cd05327   141 ragpidFNDLDLENNKEYSPYKAygqsKLANILFTRELARRLEGTGVTVNALHPGVVRTEllrrNGSFFLLYKLLRPFLK 220
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1918264442 224 TTPLRQAtsvddfANSVLLMASDLSAAITGQ 254
Cdd:cd05327   221 KSPEQGA------QTALYAATSPELEGVSGK 245
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
12-261 4.00e-19

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 84.83  E-value: 4.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMAnEVTARYG 91
Cdd:PRK07792   10 LSGKVAVVTGAAAGLGRAEALGLARLGATVVVNDVASALDASDVLDEIRAAGAKAVAVAGDISQRATADELV-ATAVGLG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpGYQ-----FNPS-ADYTSIETVQW-SHFTqqidgIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNP 164
Cdd:PRK07792   89 GLDIVVNNA--GITrdrmlFNMSdEEWDAVIAVHLrGHFL-----LTRNAAAYWRAKAKAAGGPVYGRIVNTSSEAGLVG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 165 VVTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAggllktTDASRLTTEAVFdyiaTTTPLRQATSVDDF-----ANS 239
Cdd:PRK07792  162 PVGQANYGAAKAGITALTLSAARALGRYGVRANAIC------PRARTAMTADVF----GDAPDVEAGGIDPLspehvVPL 231
                         250       260
                  ....*....|....*....|..
gi 1918264442 240 VLLMASDLSAAITGQSIAVDGG 261
Cdd:PRK07792  232 VQFLASPAAAEVNGQVFIVYGP 253
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
12-199 1.04e-18

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: 82.49  E-value: 1.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVnylnSQEAAD----------TVVADIVAAGGQAFAYQADVTELEQMQG 81
Cdd:cd09762     1 LAGKTLFITGASRGIGKAIALKAARDGANVVI----AAKTAEphpklpgtiyTAAEEIEAAGGKALPCIVDIRDEDQVRA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  82 MANEVTARYGRIDILVNNA----LPGYQFNPSADYTSIETVQwshftqqidgiVKGAVNAVQAVLPQMKAQKTGKILNIS 157
Cdd:cd09762    77 AVEKAVEKFGGIDILVNNAsaisLTGTLDTPMKRYDLMMGVN-----------TRGTYLCSKACLPYLKKSKNPHILNLS 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1918264442 158 TNLVYNPV--VTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLL 199
Cdd:cd09762   146 PPLNLNPKwfKNHTAYTMAKYGMSMCVLGMAEEFKPGGIAVNAL 189
PRK05717 PRK05717
SDR family oxidoreductase;
15-263 1.34e-18

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 82.63  E-value: 1.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADtvVADivAAGGQAFAYQADVTELEQMQGMANEVTARYGRID 94
Cdd:PRK05717   11 RVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSK--VAK--ALGENAWFIAMDVADEAQVAAGVAEVLGQFGRLD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  95 ILVNNALPGYQFNpsadyTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKtGKILNISTNLVYNPVVTYYDYTTA 174
Cdd:PRK05717   87 ALVCNAAIADPHN-----TTLESLSLAHWNRVLAVNLTGPMLLAKHCAPYLRAHN-GAIVNLASTRARQSEPDTEAYAAS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 175 KSALIGLTRNLAAELGQyGIRVNLLAGGLLKTTDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSAAITGQ 254
Cdd:PRK05717  161 KGGLLALTHALAISLGP-EIRVNAVSPGWIDARDPSQRRAEPLSEADHAQHPAGRVGTVEDVAAMVAWLLSRQAGFVTGQ 239

                  ....*....
gi 1918264442 255 SIAVDGGLT 263
Cdd:PRK05717  240 EFVVDGGMT 248
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
12-261 1.49e-18

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 82.53  E-value: 1.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASR--GLGAQIAQKMAGAGASVCVNYL----------NSQEAADTVVADIVAAGGQAFAYQADVTELEQM 79
Cdd:PRK12859    4 LKNKVAVVTGVSRldGIGAAICKELAEAGADIFFTYWtaydkempwgVDQDEQIQLQEELLKNGVKVSSMELDLTQNDAP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  80 QGMANEVTARYGRIDILVNNALpgyqFNPSADYTSIETVQW-SHFTQQIDGIVKGAVNAVQavlpQMKAQKTGKILNIST 158
Cdd:PRK12859   84 KELLNKVTEQLGYPHILVNNAA----YSTNNDFSNLTAEELdKHYMVNVRATTLLSSQFAR----GFDKKSGGRIINMTS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 159 NLVYNPVVTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGllkTTDASRLTTEaVFDYIATTTPLRQATSVDDFAN 238
Cdd:PRK12859  156 GQFQGPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPG---PTDTGWMTEE-IKQGLLPMFPFGRIGEPKDAAR 231
                         250       260
                  ....*....|....*....|...
gi 1918264442 239 SVLLMASDLSAAITGQSIAVDGG 261
Cdd:PRK12859  232 LIKFLASEEAEWITGQIIHSEGG 254
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
12-264 2.30e-18

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 81.50  E-value: 2.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVnYLNSQEAADTVVADIvaaGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK12936    4 LSGRKALVTGASGGIGEEIARLLHAQGAIVGL-HGTRVEKLEALAAEL---GERVKIFPANLSDRDEVKALGQKAEADLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpgyQFNPSADYTSIETVQWshftqqiDGIVKGAVNAV----QAVLPQMKAQKTGKILNIST--NLVYNPV 165
Cdd:PRK12936   80 GVDILVNNA----GITKDGLFVRMSDEDW-------DSVLEVNLTATfrltRELTHPMMRRRYGRIINITSvvGVTGNPG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 166 VTyyDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVfDYIATTTPLRQATSVDDFANSVLLMAS 245
Cdd:PRK12936  149 QA--NYCASKAGMIGFSKSLAQEIATRNVTVNCVAPGFIESAMTGKLNDKQK-EAIMGAIPMKRMGTGAEVASAVAYLAS 225
                         250
                  ....*....|....*....
gi 1918264442 246 DLSAAITGQSIAVDGGLTM 264
Cdd:PRK12936  226 SEAAYVTGQTIHVNGGMAM 244
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
15-201 9.42e-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: 79.47  E-value: 9.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADivaaGGQAFAYQADVTELEQMQGMANEVTARYGRID 94
Cdd:cd08929     1 KAALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQE----LEGVLGLAGDVRDEADVRRAVDAMEEAFGGLD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  95 ILVNNALPGYqfnpsadYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDYTTA 174
Cdd:cd08929    77 ALVNNAGVGV-------MKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNAS 149
                         170       180
                  ....*....|....*....|....*...
gi 1918264442 175 KSALIGLTRNLAAELGQYGIRV-NLLAG 201
Cdd:cd08929   150 KFGLLGLSEAAMLDLREANIRVvNVMPG 177
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
12-261 1.07e-17

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 80.14  E-value: 1.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGAS--RGLGAQIAQKMAGAGASVCVNYLNSQEAA-DTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTA 88
Cdd:PRK07370    4 LTGKKALVTGIAnnRSIAWGIAQQLHAAGAELGITYLPDEKGRfEKKVRELTEPLNPSLFLPCDVQDDAQIEETFETIKQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  89 RYGRIDILVNNALPGYQFNPSADYTSIETvqwSHFTQQIDGIVKGAVNAVQAVLPQMKaqKTGKILNIsTNLVYNPVVTY 168
Cdd:PRK07370   84 KWGKLDILVHCLAFAGKEELIGDFSATSR---EGFARALEISAYSLAPLCKAAKPLMS--EGGSIVTL-TYLGGVRAIPN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 169 YDYT-TAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTteAVFDYI---ATTTPLRQATSVDDFANSVLLMA 244
Cdd:PRK07370  158 YNVMgVAKAALEASVRYLAAELGPKNIRVNAISAGPIRTLASSAVG--GILDMIhhvEEKAPLRRTVTQTEVGNTAAFLL 235
                         250
                  ....*....|....*..
gi 1918264442 245 SDLSAAITGQSIAVDGG 261
Cdd:PRK07370  236 SDLASGITGQTIYVDAG 252
PRK07832 PRK07832
SDR family oxidoreductase;
15-206 1.65e-17

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 79.70  E-value: 1.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVcvnYLNSQEAA--DTVVADIVAAGGQAFAYQA-DVTELEQMQGMANEVTARYG 91
Cdd:PRK07832    1 KRCFVTGAASGIGRATALRLAAQGAEL---FLTDRDADglAQTVADARALGGTVPEHRAlDISDYDAVAAFAADIHAAHG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpgyqfnPSADYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQM-KAQKTGKILNIST--NLVYNPvvTY 168
Cdd:PRK07832   78 SMDVVMNIA-------GISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMvAAGRGGHLVNVSSaaGLVALP--WH 148
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1918264442 169 YDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT 206
Cdd:PRK07832  149 AAYSASKFGLRGLSEVLRFDLARHGIGVSVVVPGAVKT 186
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
14-202 1.68e-17

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: 79.50  E-value: 1.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVcVNYLNSQEAADTVVADIVAAG-GQAFAYQADVTELEQMQGMANEVTARYGR 92
Cdd:cd08933     9 DKVVIVTGGSRGIGRGIVRAFVENGAKV-VFCARGEAAGQALESELNRAGpGSCKFVPCDVTKEEDIKTLISVTVERFGR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  93 IDILVNNAlpGYQFNP-SADYTSIEtvqwsHFTQQIDGIVKGAVNAVQAVLPQMKaQKTGKILNISTNLVYNPVVTYYDY 171
Cdd:cd08933    88 IDCLVNNA--GWHPPHqTTDETSAQ-----EFRDLLNLNLISYFLASKYALPHLR-KSQGNIINLSSLVGSIGQKQAAPY 159
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1918264442 172 TTAKSALIGLTRNLAAELGQYGIRVNLLAGG 202
Cdd:cd08933   160 VATKGAITAMTKALAVDESRYGVRVNCISPG 190
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
14-265 2.53e-17

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: 78.87  E-value: 2.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAadtvvADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRI 93
Cdd:cd05371     2 GLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPG-----ETVAKLGDNCRFVPVDVTSEKDVKAALALAKAKFGRL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  94 DILVNNALPGYQFNpSADYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQ------KTGKILNISTnlvynpvVT 167
Cdd:cd05371    77 DIVVNCAGIAVAAK-TYNKKGQQPHSLELFQRVINVNLIGTFNVIRLAAGAMGKNepdqggERGVIINTAS-------VA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 168 YYD-------YTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLtTEAVFDYIATTTP-LRQATSVDDFANS 239
Cdd:cd05371   149 AFEgqigqaaYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLAGL-PEKVRDFLAKQVPfPSRLGDPAEYAHL 227
                         250       260
                  ....*....|....*....|....*.
gi 1918264442 240 VLLMASDlsAAITGQSIAVDGGLTMP 265
Cdd:cd05371   228 VQHIIEN--PYLNGEVIRLDGAIRMP 251
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
17-206 3.27e-17

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: 78.11  E-value: 3.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  17 VIVTGASRGLGAQIAQKMAGAGAS-VCVNYLNSQEAADtvVADIVAAGGQAFAYQADVTELeqMQGMANEVTARYG--RI 93
Cdd:cd05325     1 VLITGASRGIGLELVRQLLARGNNtVIATCRDPSAATE--LAALGASHSRLHILELDVTDE--IAESAEAVAERLGdaGL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  94 DILVNNAlpgyqfNPSADYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNIST---NLVYNPVVTYYD 170
Cdd:cd05325    77 DVLINNA------GILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSrvgSIGDNTSGGWYS 150
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1918264442 171 YTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT 206
Cdd:cd05325   151 YRASKAALNMLTKSLAVELKRDGITVVSLHPGWVRT 186
PRK07985 PRK07985
SDR family oxidoreductase;
12-261 8.51e-17

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 78.11  E-value: 8.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYL-NSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARY 90
Cdd:PRK07985   47 LKDRKALVTGGDSGIGRAAAIAYAREGADVAISYLpVEEEDAQDVKKIIEECGRKAVLLPGDLSDEKFARSLVHEAHKAL 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  91 GRIDILVNNALPGYQFNPSADYTSietvqwSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTgkILNISTNLVYNPVVTYYD 170
Cdd:PRK07985  127 GGLDIMALVAGKQVAIPDIADLTS------EQFQKTFAINVFALFWLTQEAIPLLPKGAS--IITTSSIQAYQPSPHLLD 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 171 YTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTT-DASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSA 249
Cdd:PRK07985  199 YAATKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTAlQISGGQTQDKIPQFGQQTPMKRAGQPAELAPVYVYLASQESS 278
                         250
                  ....*....|..
gi 1918264442 250 AITGQSIAVDGG 261
Cdd:PRK07985  279 YVTAEVHGVCGG 290
PRK12742 PRK12742
SDR family oxidoreductase;
14-261 1.24e-16

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 76.72  E-value: 1.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADivaAGGQAFayQADVTELEQMQgmanEVTARYGRI 93
Cdd:PRK12742    6 GKKVLVLGGSRGIGAAIVRRFVTDGANVRFTYAGSKDAAERLAQE---TGATAV--QTDSADRDAVI----DVVRKSGAL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  94 DILVNNALPGYQFNP-SADYTSIEtvqwshftQQIDGIVKGAVNAVQAVLPQMKaqKTGKILNI-STNLVYNPVVTYYDY 171
Cdd:PRK12742   77 DILVVNAGIAVFGDAlELDADDID--------RLFKINIHAPYHASVEAARQMP--EGGRIIIIgSVNGDRMPVAGMAAY 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 172 TTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT--TDASRLTTEAVFDYIAtttpLRQATSVDDFANSVLLMASDLSA 249
Cdd:PRK12742  147 AASKSALQGMARGLARDFGPRGITINVVQPGPIDTdaNPANGPMKDMMHSFMA----IKRHGRPEEVAGMVAWLAGPEAS 222
                         250
                  ....*....|..
gi 1918264442 250 AITGQSIAVDGG 261
Cdd:PRK12742  223 FVTGAMHTIDGA 234
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
12-255 1.62e-16

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


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 76.46  E-value: 1.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVnyLNSQEAADTVVADIVAAGGQA----FAYQADVTELEQMQGMANEVT 87
Cdd:cd05340     2 LNDRIILVTGASDGIGREAALTYARYGATVIL--LGRNEEKLRQVADHINEEGGRqpqwFILDLLTCTSENCQQLAQRIA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  88 ARYGRIDILVNNALPGYQFNPSADYTSietvqwSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVT 167
Cdd:cd05340    80 VNYPRLDGVLHNAGLLGDVCPLSEQNP------QVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRAN 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 168 YYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTtdASRLTTeavfdyIATTTPLRQATSVDDFANSVLLMASDl 247
Cdd:cd05340   154 WGAYAVSKFATEGL*QVLADEYQQRNLRVNCINPGGTRT--AMRASA------FPTEDPQKLKTPADIMPLYLWLMGDD- 224

                  ....*...
gi 1918264442 248 SAAITGQS 255
Cdd:cd05340   225 SRRKTGMT 232
PRK07533 PRK07533
enoyl-[acyl-carrier-protein] reductase FabI;
31-262 2.84e-16

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


Pssm-ID: 181020 [Multi-domain]  Cd Length: 258  Bit Score: 76.13  E-value: 2.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  31 AQKMAGAGASVCVNYLNsqEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRIDILVNNAlpgyQFNPSA 110
Cdd:PRK07533   29 ARAFRALGAELAVTYLN--DKARPYVEPLAEELDAPIFLPLDVREPGQLEAVFARIAEEWGRLDFLLHSI----AFAPKE 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 111 DY------TSIETvqwshFTQQIDGIVKGAVNAVQAVLPQMKaqKTGKILNIStnlvY---NPVVTYYDYT-TAKSALIG 180
Cdd:PRK07533  103 DLhgrvvdCSREG-----FALAMDVSCHSFIRMARLAEPLMT--NGGSLLTMS----YygaEKVVENYNLMgPVKAALES 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 181 LTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTT-EAVFDYIATTTPLRQATSVDDFANSVLLMASDLSAAITGQSIAVD 259
Cdd:PRK07533  172 SVRYLAAELGPKGIRVHAISPGPLKTRAASGIDDfDALLEDAAERAPLRRLVDIDDVGAVAAFLASDAARRLTGNTLYID 251

                  ...
gi 1918264442 260 GGL 262
Cdd:PRK07533  252 GGY 254
PRK08690 PRK08690
enoyl-[acyl-carrier-protein] reductase FabI;
11-264 1.45e-15

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


Pssm-ID: 169553 [Multi-domain]  Cd Length: 261  Bit Score: 74.23  E-value: 1.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  11 FLLNKVVIVTG--ASRGLGAQIAQKMAGAGASVCVNYLNsqEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTA 88
Cdd:PRK08690    3 FLQGKKILITGmiSERSIAYGIAKACREQGAELAFTYVV--DKLEERVRKMAAELDSELVFRCDVASDDEINQVFADLGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  89 RYGRIDILVNN-------ALPGyQFnpsADYTSIETVQWSHftqQIDGIVKGAVnaVQAVLPQMKAQKtGKILNISTNLV 161
Cdd:PRK08690   81 HWDGLDGLVHSigfapkeALSG-DF---LDSISREAFNTAH---EISAYSLPAL--AKAARPMMRGRN-SAIVALSYLGA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 162 YNPVVTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTT-EAVFDYIATTTPLRQATSVDDFANSV 240
Cdd:PRK08690  151 VRAIPNYNVMGMAKASLEAGIRFTAACLGKEGIRCNGISAGPIKTLAASGIADfGKLLGHVAAHNPLRRNVTIEEVGNTA 230
                         250       260
                  ....*....|....*....|....
gi 1918264442 241 LLMASDLSAAITGQSIAVDGGLTM 264
Cdd:PRK08690  231 AFLLSDLSSGITGEITYVDGGYSI 254
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
14-241 9.35e-15

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: 71.77  E-value: 9.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVcVNYLNSQEAADTVVADIVAAGGQA-FAYQADVTELEQMQGMANEVTARYGR 92
Cdd:cd05343     6 GRVALVTGASVGIGAAVARALVQHGMKV-VGCARRVDKIEALAAECQSAGYPTlFPYQCDLSNEEQILSMFSAIRTQHQG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  93 IDILVNNALPGYQfNPSADYTsieTVQWShftQQIDGIVKGAVNAVQAVLPQMKAQKT--GKILNISTNL--VYNPVVTY 168
Cdd:cd05343    85 VDVCINNAGLARP-EPLLSGK---TEGWK---EMFDVNVLALSICTREAYQSMKERNVddGHIININSMSghRVPPVSVF 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1918264442 169 YDYTTAKSALIGLTRNLAAEL--GQYGIRVNLLAGGLLKTTDASRLtTEAVFDYIATTTPLRQATSVDDFANSVL 241
Cdd:cd05343   158 HFYAATKHAVTALTEGLRQELreAKTHIRATSISPGLVETEFAFKL-HDNDPEKAAATYESIPCLKPEDVANAVL 231
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
12-196 1.13e-14

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


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 71.35  E-value: 1.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQeaadtVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:COG3967     3 LTGNTILITGGTSGIGLALAKRLHARGNTVIITGRREE-----KLEEAAAANPGLHTIVLDVADPASIAALAEQVTAEFP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpGYQFNPSADytsIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDY 171
Cdd:COG3967    78 DLNVLINNA--GIMRAEDLL---DEAEDLADAEREITTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGLAFVPLAVTPTY 152
                         170       180
                  ....*....|....*....|....*
gi 1918264442 172 TTAKSALIGLTRNLAAELGQYGIRV 196
Cdd:COG3967   153 SATKAALHSYTQSLRHQLKDTSVKV 177
PRK08339 PRK08339
short chain dehydrogenase; Provisional
12-261 1.30e-14

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 71.42  E-value: 1.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTaRYG 91
Cdd:PRK08339    6 LSGKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSESNVDVSYIVADLTKREDLERTVKELK-NIG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDIL---VNNALPGYQFNPSADytsietvQWShftQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTY 168
Cdd:PRK08339   85 EPDIFffsTGGPKPGYFMEMSME-------DWE---GAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSVAIKEPIPNI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 169 YDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRL----------TTEAVFDYIATTTPLRQATSVDDFAN 238
Cdd:PRK08339  155 ALSNVVRISMAGLVRTLAKELGPKGITVNGIMPGIIRTDRVIQLaqdrakregkSVEEALQEYAKPIPLGRLGEPEEIGY 234
                         250       260
                  ....*....|....*....|...
gi 1918264442 239 SVLLMASDLSAAITGQSIAVDGG 261
Cdd:PRK08339  235 LVAFLASDLGSYINGAMIPVDGG 257
PRK07984 PRK07984
enoyl-ACP reductase FabI;
11-264 1.37e-14

enoyl-ACP reductase FabI;


Pssm-ID: 181187 [Multi-domain]  Cd Length: 262  Bit Score: 71.47  E-value: 1.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  11 FLLNKVVIVTG--ASRGLGAQIAQKMAGAGASVCVNYLNsqEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTA 88
Cdd:PRK07984    3 FLSGKRILVTGvaSKLSIAYGIAQAMHREGAELAFTYQN--DKLKGRVEEFAAQLGSDIVLPCDVAEDASIDAMFAELGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  89 RYGRIDILVNNA--LPGYQFNpsADYTSIETVQWSHFTQQIDGIVKGAVnavqavlpqmkAQKTGKILNISTNLVY---- 162
Cdd:PRK07984   81 VWPKFDGFVHSIgfAPGDQLD--GDYVNAVTREGFKIAHDISSYSFVAM-----------AKACRSMLNPGSALLTlsyl 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 163 ---NPVVTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTT-EAVFDYIATTTPLRQATSVDDFAN 238
Cdd:PRK07984  148 gaeRAIPNYNVMGLAKASLEANVRYMANAMGPEGVRVNAISAGPIRTLAASGIKDfRKMLAHCEAVTPIRRTVTIEDVGN 227
                         250       260
                  ....*....|....*....|....*.
gi 1918264442 239 SVLLMASDLSAAITGQSIAVDGGLTM 264
Cdd:PRK07984  228 SAAFLCSDLSAGISGEVVHVDGGFSI 253
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
14-196 1.56e-14

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: 70.90  E-value: 1.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADivaAGGQAFAYQADVTELEQMQGMANEVTarygRI 93
Cdd:cd05354     3 DKTVLVTGANRGIGKAFVESLLAHGAKKVYAAVRDPGSAAHLVAK---YGDKVVPLRLDVTDPESIKAAAAQAK----DV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  94 DILVNNALPGYQFNPSADyTSIETVQwshftQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDYTT 173
Cdd:cd05354    76 DVVINNAGVLKPATLLEE-GALEALK-----QEMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKNFPAMGTYSA 149
                         170       180
                  ....*....|....*....|...
gi 1918264442 174 AKSALIGLTRNLAAELGQYGIRV 196
Cdd:cd05354   150 SKSAAYSLTQGLRAELAAQGTLV 172
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
14-206 2.12e-14

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: 70.71  E-value: 2.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVCVnYLNSQEAADTVVADIVAAGG-QAFAYQADVTELEQ-MQGMANEVTARyg 91
Cdd:cd05356     1 GTWAVVTGATDGIGKAYAEELAKRGFNVIL-ISRTQEKLDAVAKEIEEKYGvETKTIAADFSAGDDiYERIEKELEGL-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNA-----LPGYQFN-PSADYTSIETVqwshftqqidgIVKGAVNAVQAVLPQMKAQKTGKILNIS--TNLVYN 163
Cdd:cd05356    78 DIGILVNNVgishsIPEYFLEtPEDELQDIINV-----------NVMATLKMTRLILPGMVKRKKGAIVNISsfAGLIPT 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1918264442 164 PVVTYYDYTtaKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT 206
Cdd:cd05356   147 PLLATYSAS--KAFLDFFSRALYEEYKSQGIDVQSLLPYLVAT 187
PRK06997 PRK06997
enoyl-[acyl-carrier-protein] reductase FabI;
11-261 3.51e-14

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


Pssm-ID: 180789 [Multi-domain]  Cd Length: 260  Bit Score: 70.24  E-value: 3.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  11 FLLNKVVIVTG--ASRGLGAQIAQKMAGAGASVCVNYLNsqEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTA 88
Cdd:PRK06997    3 FLAGKRILITGllSNRSIAYGIAKACKREGAELAFTYVG--DRFKDRITEFAAEFGSDLVFPCDVASDEQIDALFASLGQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  89 RYGRIDILVNNAlpgyQFNP----SADYTSIETVQWSHFTQQIDGIVKGAVnaVQAVLPQMkaQKTGKILNISTNLVYNP 164
Cdd:PRK06997   81 HWDGLDGLVHSI----GFAPreaiAGDFLDGLSRENFRIAHDISAYSFPAL--AKAALPML--SDDASLLTLSYLGAERV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 165 VVTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTT-EAVFDYIATTTPLRQATSVDDFANSVLLM 243
Cdd:PRK06997  153 VPNYNTMGLAKASLEASVRYLAVSLGPKGIRANGISAGPIKTLAASGIKDfGKILDFVESNAPLRRNVTIEEVGNVAAFL 232
                         250
                  ....*....|....*...
gi 1918264442 244 ASDLSAAITGQSIAVDGG 261
Cdd:PRK06997  233 LSDLASGVTGEITHVDSG 250
PRK05693 PRK05693
SDR family oxidoreductase;
15-241 4.32e-14

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 70.20  E-value: 4.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVcvnYLNSQEAADtvVADIVAAGGQAFayQADVTELEQMQGMANEVTARYGRID 94
Cdd:PRK05693    2 PVVLITGCSSGIGRALADAFKAAGYEV---WATARKAED--VEALAAAGFTAV--QLDVNDGAALARLAEELEAEHGGLD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  95 ILVNNAlpGY-QFNPSADyTSIETVQwshftQQIDGIVKGAVNAVQAVLPQMKaQKTGKILNISTnlVYNPVVTYY--DY 171
Cdd:PRK05693   75 VLINNA--GYgAMGPLLD-GGVEAMR-----RQFETNVFAVVGVTRALFPLLR-RSRGLVVNIGS--VSGVLVTPFagAY 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 172 TTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEA--VFDYIATTTPLR------------QATSVDDFA 237
Cdd:PRK05693  144 CASKAAVHALSDALRLELAPFGVQVMEVQPGAIASQFASNASREAeqLLAEQSPWWPLRehiqararasqdNPTPAAEFA 223

                  ....
gi 1918264442 238 NSVL 241
Cdd:PRK05693  224 RQLL 227
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
12-260 7.64e-14

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 70.64  E-value: 7.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASV-CVNYLNSQEAADTVVADIvaaGGQAFAYqaDVTELEQMQGMANEVTARY 90
Cdd:PRK08261  208 LAGKVALVTGAARGIGAAIAEVLARDGAHVvCLDVPAAGEALAAVANRV---GGTALAL--DITAPDAPARIAEHLAERH 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  91 GRIDILVNNAlpgyqfnpsadytsietvqwshftqqidGIVK---------GAVNAVQAVlpQMKAQ------------- 148
Cdd:PRK08261  283 GGLDIVVHNA----------------------------GITRdktlanmdeARWDSVLAV--NLLAPlriteallaagal 332
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 149 -KTGKILNIS-----------TNlvynpvvtyydYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT--TDASRLTT 214
Cdd:PRK08261  333 gDGGRIVGVSsisgiagnrgqTN-----------YAASKAGVIGLVQALAPLLAERGITINAVAPGFIETqmTAAIPFAT 401
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1918264442 215 EAVFDYIATttpLRQATSVDDFANSVLLMASDLSAAITGQSIAVDG 260
Cdd:PRK08261  402 REAGRRMNS---LQQGGLPVDVAETIAWLASPASGGVTGNVVRVCG 444
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
12-261 1.88e-13

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 67.86  E-value: 1.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADtvVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK05786    3 LKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKR--MKKTLSKYGNIHYVVGDVSSTESARNVIEKAAKVLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlPGYQFNPSADYTSIETVQWSHftqqidgiVKGAVNAVQAVLPQMKAQKTgKILNISTNLVYNPVVTYYDY 171
Cdd:PRK05786   81 AIDGLVVTV-GGYVEDTVEEFSGLEEMLTNH--------IKIPLYAVNASLRFLKEGSS-IVLVSSMSGIYKASPDQLSY 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 172 TTAKSALIGLTRNLAAELGQYGIRVNLLA-GGLLKTTDASRltteavfDYiATTTPLRQATS-VDDFANSVLLMASDLSA 249
Cdd:PRK05786  151 AVAKAGLAKAVEILASELLGRGIRVNGIApTTISGDFEPER-------NW-KKLRKLGDDMApPEDFAKVIIWLLTDEAD 222
                         250
                  ....*....|..
gi 1918264442 250 AITGQSIAVDGG 261
Cdd:PRK05786  223 WVDGVVIPVDGG 234
PRK08159 PRK08159
enoyl-[acyl-carrier-protein] reductase FabI;
30-261 1.93e-13

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


Pssm-ID: 181260 [Multi-domain]  Cd Length: 272  Bit Score: 68.24  E-value: 1.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  30 IAQKMAGAGASVCVNYlnSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRIDILVNNAlpGYQFNPS 109
Cdd:PRK08159   28 IAKACRAAGAELAFTY--QGDALKKRVEPLAAELGAFVAGHCDVTDEASIDAVFETLEKKWGKLDFVVHAI--GFSDKDE 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 110 ADYTSIETVQwSHFTQQIDGivkgAVNAVQAVlpqmkAQKTGKILNISTNLVynpVVTYY-------DYTT---AKSALI 179
Cdd:PRK08159  104 LTGRYVDTSR-DNFTMTMDI----SVYSFTAV-----AQRAEKLMTDGGSIL---TLTYYgaekvmpHYNVmgvAKAALE 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 180 GLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTeavFDYIAT----TTPLRQATSVDDFANSVLLMASDLSAAITGQS 255
Cdd:PRK08159  171 ASVKYLAVDLGPKNIRVNAISAGPIKTLAASGIGD---FRYILKwneyNAPLRRTVTIEEVGDSALYLLSDLSRGVTGEV 247

                  ....*.
gi 1918264442 256 IAVDGG 261
Cdd:PRK08159  248 HHVDSG 253
PRK06194 PRK06194
hypothetical protein; Provisional
14-196 2.05e-13

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 68.50  E-value: 2.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNsQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRI 93
Cdd:PRK06194    6 GKVAVITGAASGFGLAFARIGAALGMKLVLADVQ-QDALDRAVAELRAQGAEVLGVRTDVSDAAQVEALADAALERFGAV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  94 DILVNNA---LPGYQF-NPSADYtsietvQWShftqqIDGIVKGAVNAVQAVLPQMKAQKT------GKILNIST--NLV 161
Cdd:PRK06194   85 HLLFNNAgvgAGGLVWeNSLADW------EWV-----LGVNLWGVIHGVRAFTPLMLAAAEkdpayeGHIVNTASmaGLL 153
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1918264442 162 YNPVVTYYDYTtaKSALIGLTRNLAAELGQYGIRV 196
Cdd:PRK06194  154 APPAMGIYNVS--KHAVVSLTETLYQDLSLVTDQV 186
PRK08303 PRK08303
short chain dehydrogenase; Provisional
12-193 5.91e-13

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 67.33  E-value: 5.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTV--------VADIV-AAGGQAFAYQADVTELEQMQGM 82
Cdd:PRK08303    6 LRGKVALVAGATRGAGRGIAVELGAAGATVYVTGRSTRARRSEYdrpetieeTAELVtAAGGRGIAVQVDHLVPEQVRAL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  83 ANEVTARYGRIDILVNNALPGYQFnpsadyTSIETVQWSHFTQQIDGIVKGAVNA----VQAVLPQMKAQKTGKILNIS- 157
Cdd:PRK08303   86 VERIDREQGRLDILVNDIWGGEKL------FEWGKPVWEHSLDKGLRMLRLAIDThlitSHFALPLLIRRPGGLVVEITd 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1918264442 158 ----TNLVYNPVVTYYDYttAKSALIGLTRNLAAELGQYG 193
Cdd:PRK08303  160 gtaeYNATHYRLSVFYDL--AKTSVNRLAFSLAHELAPHG 197
PRK06505 PRK06505
enoyl-[acyl-carrier-protein] reductase FabI;
30-265 7.70e-13

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


Pssm-ID: 180596 [Multi-domain]  Cd Length: 271  Bit Score: 66.69  E-value: 7.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  30 IAQKMAGAGASVCVNYlnSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRIDILVN-------NALP 102
Cdd:PRK06505   25 IAKQLAAQGAELAFTY--QGEALGKRVKPLAESLGSDFVLPCDVEDIASVDAVFEALEKKWGKLDFVVHaigfsdkNELK 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 103 G-YQFNPSADYTSIETVQWSHFTQqidgIVKGAVnavqAVLPQmkaqkTGKILNISTNLVYNPVVTYYDYTTAKSALIGL 181
Cdd:PRK06505  103 GrYADTTRENFSRTMVISCFSFTE----IAKRAA----KLMPD-----GGSMLTLTYGGSTRVMPNYNVMGVAKAALEAS 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 182 TRNLAAELGQYGIRVNLLAGGLLKTTDASRLT-TEAVFDYIATTTPLRQATSVDDFANSVLLMASDLSAAITGQSIAVDG 260
Cdd:PRK06505  170 VRYLAADYGPQGIRVNAISAGPVRTLAGAGIGdARAIFSYQQRNSPLRRTVTIDEVGGSALYLLSDLSSGVTGEIHFVDS 249

                  ....*...
gi 1918264442 261 G---LTMP 265
Cdd:PRK06505  250 GyniVSMP 257
PRK06139 PRK06139
SDR family oxidoreductase;
12-192 9.02e-13

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 67.05  E-value: 9.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVcVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK06139    5 LHGAVVVITGASSGIGQATAEAFARRGARL-VLAARDEEALQAVAEECRALGAEVLVVPTDVTDADQVKALATQAASFGG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNALPGY--QFnpsaDYTSIEtvqwSHfTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILN-IST-NLVYNPVVT 167
Cdd:PRK06139   84 RIDVWVNNVGVGAvgRF----EETPIE----AH-EQVIQTNLIGYMRDAHAALPIFKKQGHGIFINmISLgGFAAQPYAA 154
                         170       180
                  ....*....|....*....|....*
gi 1918264442 168 yyDYTTAKSALIGLTRNLAAELGQY 192
Cdd:PRK06139  155 --AYSASKFGLRGFSEALRGELADH 177
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
15-206 1.11e-12

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: 65.94  E-value: 1.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGAS---VCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARyg 91
Cdd:cd09806     1 TVVLITGCSSGIGLHLAVRLASDPSKrfkVYATMRDLKKKGRLWEAAGALAGGTLETLQLDVCDSKSVAAAVERVTER-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNALPGYqFNPsadytsIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNIST-----NLVYNPVv 166
Cdd:cd09806    79 HVDVLVCNAGVGL-LGP------LEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSvgglqGLPFNDV- 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1918264442 167 tyydYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT 206
Cdd:cd09806   151 ----YCASKFALEGLCESLAVQLLPFNVHLSLIECGPVHT 186
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
16-206 2.07e-12

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: 65.00  E-value: 2.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  16 VVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRIDI 95
Cdd:cd05367     1 VIILTGASRGIGRALAEELLKRGSPSVVVLLARSEEPLQELKEELRPGLRVTTVKADLSDAAGVEQLLEAIRKLDGERDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  96 LVNNALPGYQFNPSADyTSIETVQwSHFTQQidgiVKGAVNAVQAVLPQMKAQKT-GKILNISTNLVYNPVVTYYDYTTA 174
Cdd:cd05367    81 LINNAGSLGPVSKIEF-IDLDELQ-KYFDLN----LTSPVCLTSTLLRAFKKRGLkKTVVNVSSGAAVNPFKGWGLYCSS 154
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1918264442 175 KSALIGLTRNLAAELgqYGIRVNLLAGGLLKT 206
Cdd:cd05367   155 KAARDMFFRVLAAEE--PDVRVLSYAPGVVDT 184
PLN02730 PLN02730
enoyl-[acyl-carrier-protein] reductase
83-262 2.35e-12

enoyl-[acyl-carrier-protein] reductase


Pssm-ID: 178331 [Multi-domain]  Cd Length: 303  Bit Score: 65.57  E-value: 2.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  83 ANEVTARYGRIDILVNNALPGyqfnPSADYTSIETVQwSHFTQQIDGIVKGAVNAVQAVLPQMKaqKTGKILNIsTNLVY 162
Cdd:PLN02730  111 AESVKADFGSIDILVHSLANG----PEVTKPLLETSR-KGYLAAISASSYSFVSLLQHFGPIMN--PGGASISL-TYIAS 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 163 NPVVTYYD--YTTAKSALIGLTRNLAAELG-QYGIRVNLLAGGLLKTTDASRLT-TEAVFDYIATTTPLRQATSVDDFAN 238
Cdd:PLN02730  183 ERIIPGYGggMSSAKAALESDTRVLAFEAGrKYKIRVNTISAGPLGSRAAKAIGfIDDMIEYSYANAPLQKELTADEVGN 262
                         170       180
                  ....*....|....*....|....
gi 1918264442 239 SVLLMASDLSAAITGQSIAVDGGL 262
Cdd:PLN02730  263 AAAFLASPLASAITGATIYVDNGL 286
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
16-262 2.52e-12

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: 64.82  E-value: 2.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  16 VVIVTGASRGLGAQIAQKMAGAGASVcvnylnsqeaadtVVADIvaagGQAFAyQADVTELEQMQGMANEVTARY-GRID 94
Cdd:cd05328     1 TIVITGAASGIGAATAELLEDAGHTV-------------IGIDL----READV-IADLSTPEGRAAAIADVLARCsGVLD 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  95 ILVNNA-LPGyqfnpSADYTSIETVQWShftqqidgivkGAVNAVQAVLPQMKAQKTGKILNISTNLVY------NPVV- 166
Cdd:cd05328    63 GLVNCAgVGG-----TTVAGLVLKVNYF-----------GLRALMEALLPRLRKGHGPAAVVVSSIAGAgwaqdkLELAk 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 167 --------------------TYYDYTTAKSALIGLTRNLAAE-LGQYGIRVNLLAGG-----LLKTTDASRLTTEAVfdy 220
Cdd:cd05328   127 alaagtearavalaehagqpGYLAYAGSKEALTVWTRRRAATwLYGAGVRVNTVAPGpvetpILQAFLQDPRGGESV--- 203
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1918264442 221 IATTTPLRQATSVDDFANSVLLMASDLSAAITGQSIAVDGGL 262
Cdd:cd05328   204 DAFVTPMGRRAEPDEIAPVIAFLASDAASWINGANLFVDGGL 245
PRK09072 PRK09072
SDR family oxidoreductase;
12-200 2.81e-12

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 64.96  E-value: 2.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVnyLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQgMANEVTARYG 91
Cdd:PRK09072    3 LKDKRVLLTGASGGIGQALAEALAAAGARLLL--VGRNAEKLEALAARLPYPGRHRWVVADLTSEAGRE-AVLARAREMG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpGY-QFNPSADYTSietvqwSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNI-ST--NLVYnPvvT 167
Cdd:PRK09072   80 GINVLINNA--GVnHFALLEDQDP------EAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVgSTfgSIGY-P--G 148
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1918264442 168 YYDYTTAKSALIGLTRNLAAELGQYGIRVNLLA 200
Cdd:PRK09072  149 YASYCASKFALRGFSEALRRELADTGVRVLYLA 181
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
15-260 5.12e-12

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


Pssm-ID: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 63.50  E-value: 5.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADtvvADIVAAGGQAFayqadvteLEQMQGMANEVTARYGRID 94
Cdd:cd05334     2 RVVLVYGGRGALGSAVVQAFKSRGWWVASIDLAENEEAD---ASIIVLDSDSF--------TEQAKQVVASVARLSGKVD 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  95 ILVNNAlPGYQFNPSADYTSIETVQwshftQQIDGIVKGAVNAVQAVLPQMKaqKTGKILNISTNLVYNPVVTYYDYTTA 174
Cdd:cd05334    71 ALICVA-GGWAGGSAKSKSFVKNWD-----LMWKQNLWTSFIASHLATKHLL--SGGLLVLTGAKAALEPTPGMIGYGAA 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 175 KSALIGLTRNLAAELG--QYGIRVNLLAGGLLKTTDASRLTTEAVFDyiaTTTPLRQATSVddfansVLLMASDLSAAIT 252
Cdd:cd05334   143 KAAVHQLTQSLAAENSglPAGSTANAILPVTLDTPANRKAMPDADFS---SWTPLEFIAEL------ILFWASGAARPKS 213

                  ....*...
gi 1918264442 253 GQSIAVDG 260
Cdd:cd05334   214 GSLIPVVT 221
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
16-196 5.99e-12

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: 63.56  E-value: 5.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  16 VVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRIDI 95
Cdd:cd05373     1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLVDIIRDAGGSAKAVPTDARDEDEVIALFDLIEEEIGPLEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  96 LVNNALPGYQF----NPSADYTSIETVqwSHFtqqidgivkGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDY 171
Cdd:cd05373    81 LVYNAGANVWFpileTTPRVFEKVWEM--AAF---------GGFLAAREAAKRMLARGRGTIIFTGATASLRGRAGFAAF 149
                         170       180
                  ....*....|....*....|....*
gi 1918264442 172 TTAKSALIGLTRNLAAELGQYGIRV 196
Cdd:cd05373   150 AGAKFALRALAQSMARELGPKGIHV 174
PRK08267 PRK08267
SDR family oxidoreductase;
15-196 1.33e-11

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 63.03  E-value: 1.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNsQEAADTVVADIvaAGGQAFAYQADVTELEQMQG-MANEVTARYGRI 93
Cdd:PRK08267    2 KSIFITGAASGIGRATALLFAAEGWRVGAYDIN-EAGLAALAAEL--GAGNAWTGALDVTDRAAWDAaLADFAAATGGRL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  94 DILVNNA--LPGYQFNpSADYTSIEtvqwshftQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNI-STNLVYN-PVVTYY 169
Cdd:PRK08267   79 DVLFNNAgiLRGGPFE-DIPLEAHD--------RVIDINVKGVLNGAHAALPYLKATPGARVINTsSASAIYGqPGLAVY 149
                         170       180
                  ....*....|....*....|....*..
gi 1918264442 170 DYTtaKSALIGLTRNLAAELGQYGIRV 196
Cdd:PRK08267  150 SAT--KFAVRGLTEALDLEWRRHGIRV 174
PRK06482 PRK06482
SDR family oxidoreductase;
19-224 1.34e-11

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 63.21  E-value: 1.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  19 VTGASRGLGAQIAQKMAGAGASVcvnylnsqeaADTV-----VADIVAAGGQAF-AYQADVTELEQMQGMANEVTARYGR 92
Cdd:PRK06482    7 ITGASSGFGRGMTERLLARGDRV----------AATVrrpdaLDDLKARYGDRLwVLQLDVTDSAAVRAVVDRAFAALGR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  93 IDILVNNAlpGYQFNPSADYTSIETVQwshftQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDYT 172
Cdd:PRK06482   77 IDVVVSNA--GYGLFGAAEELSDAQIR-----RQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQIAYPGFSLYH 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1918264442 173 TAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVFDYIATT 224
Cdd:PRK06482  150 ATKWGIEGFVEAVAQEVAPFGIEFTIVEPGPARTNFGAGLDRGAPLDAYDDT 201
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
16-245 2.40e-11

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 62.08  E-value: 2.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  16 VVIVTGASRGLGAQIAQKMAGAGASVcVNYLNSQEAADTVVADIvaaGGQAFAYQADVTELEQMQGMANEVTARYGRIDI 95
Cdd:PRK10538    2 IVLVTGATAGFGECITRRFIQQGHKV-IATGRRQERLQELKDEL---GDNLYIAQLDVRNRAAIEEMLASLPAEWRNIDV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  96 LVNNALPGYQFNPsADYTSIEtvQWShftQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDYTTAK 175
Cdd:PRK10538   78 LVNNAGLALGLEP-AHKASVE--DWE---TMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATK 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 176 SALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTTEAVFDYIATTTPLRQATSVDDFANSVLLMAS 245
Cdd:PRK10538  152 AFVRQFSLNLRTDLHGTAVRVTDIEPGLVGGTEFSNVRFKGDDGKAEKTYQNTVALTPEDVSEAVWWVAT 221
PRK08703 PRK08703
SDR family oxidoreductase;
9-202 6.24e-11

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 60.72  E-value: 6.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442   9 PAFLLNKVVIVTGASRGLGAQIAQKMAGAGASVcVNYLNSQEAADTVVADIVAAGG-QAFAYQADV--TELEQMQGMANE 85
Cdd:PRK08703    1 MATLSDKTILVTGASQGLGEQVAKAYAAAGATV-ILVARHQKKLEKVYDAIVEAGHpEPFAIRFDLmsAEEKEFEQFAAT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  86 VT-ARYGRIDILVNNALPGYQFNPSADYTSIETVQwshfTQQIDGIVKGAVnaVQAVLPQMKAQKTGKILNISTNLVYNP 164
Cdd:PRK08703   80 IAeATQGKLDGIVHCAGYFYALSPLDFQTVAEWVN----QYRINTVAPMGL--TRALFPLLKQSPDASVIFVGESHGETP 153
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1918264442 165 VVTYYDYTTAKSALIGLTRNLAAELGQYG-IRVNLLAGG 202
Cdd:PRK08703  154 KAYWGGFGASKAALNYLCKVAADEWERFGnLRANVLVPG 192
PRK05993 PRK05993
SDR family oxidoreductase;
14-216 1.10e-10

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 60.43  E-value: 1.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVcvnYLNSQEAADtvVADIVAAGGQAFayQADVTELEQMQGMANEVTARY-GR 92
Cdd:PRK05993    4 KRSILITGCSSGIGAYCARALQSDGWRV---FATCRKEED--VAALEAEGLEAF--QLDYAEPESIAALVAQVLELSgGR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  93 IDILVNNALPGyqfNPSAdytsIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDYT 172
Cdd:PRK05993   77 LDALFNNGAYG---QPGA----VEDLPTEALRAQFEANFFGWHDLTRRVIPVMRKQGQGRIVQCSSILGLVPMKYRGAYN 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1918264442 173 TAKSALIGLTRNLAAELGQYGIRVNLLAGGLLkttdASRLTTEA 216
Cdd:PRK05993  150 ASKFAIEGLSLTLRMELQGSGIHVSLIEPGPI----ETRFRANA 189
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
12-261 1.26e-10

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


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 60.13  E-value: 1.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGAS--RGLGAQIAQKMAGAGASVCVNYlnSQEAADTVVADIVAA--GGQAFAYQADVTELEQMQGMANEVT 87
Cdd:PRK08594    5 LEGKTYVVMGVAnkRSIAWGIARSLHNAGAKLVFTY--AGERLEKEVRELADTleGQESLLLPCDVTSDEEITACFETIK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  88 ARYGRIDILVNnalpgyqfnpSADYTSIETVQWSHFTQQIDG------IVKGAVNAV-QAVLPQMKaqKTGKILNIsTNL 160
Cdd:PRK08594   83 EEVGVIHGVAH----------CIAFANKEDLRGEFLETSRDGfllaqnISAYSLTAVaREAKKLMT--EGGSIVTL-TYL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 161 VYNPVVTYYDYT-TAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRLTT-EAVFDYIATTTPLRQATSVDDFAN 238
Cdd:PRK08594  150 GGERVVQNYNVMgVAKASLEASVKYLANDLGKDGIRVNAISAGPIRTLSAKGVGGfNSILKEIEERAPLRRTTTQEEVGD 229
                         250       260
                  ....*....|....*....|...
gi 1918264442 239 SVLLMASDLSAAITGQSIAVDGG 261
Cdd:PRK08594  230 TAAFLFSDLSRGVTGENIHVDSG 252
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
15-206 1.72e-10

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: 59.39  E-value: 1.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADtVVADIvaAGGQAFAYQADVTELEQMQG-MANEVTARYGRI 93
Cdd:cd08931     1 KAIFITGAASGIGRETALLFARNGWFVGLYDIDEDGLAA-LAAEL--GAENVVAGALDVTDRAAWAAaLADFAAATGGRL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  94 DILVNNALPGyQFNPsadytsIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNI--STNLVYNPVVTYYDY 171
Cdd:cd08931    78 DALFNNAGVG-RGGP------FEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTasSSAIYGQPDLAVYSA 150
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1918264442 172 TtaKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT 206
Cdd:cd08931   151 T--KFAVRGLTEALDVEWARHGIRVADVWPWFVDT 183
PRK07889 PRK07889
enoyl-[acyl-carrier-protein] reductase FabI;
72-261 1.91e-10

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


Pssm-ID: 236124 [Multi-domain]  Cd Length: 256  Bit Score: 59.57  E-value: 1.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  72 DVTELEQMQGMANEVTARYGRIDILVN-------NALPGYQFN-PSADY-TSIETVQWSHftqqidgivkgaVNAVQAVL 142
Cdd:PRK07889   65 DVTNEEHLASLADRVREHVDGLDGVVHsigfapqSALGGNFLDaPWEDVaTALHVSAYSL------------KSLAKALL 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 143 PQMkaQKTGKILNistnLVYNPVVTY--YDY-TTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASRL----TTE 215
Cdd:PRK07889  133 PLM--NEGGSIVG----LDFDATVAWpaYDWmGVAKAALESTNRYLARDLGPRGIRVNLVAAGPIRTLAAKAIpgfeLLE 206
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1918264442 216 AVFDYIAtttPLrqATSVDD---FANSVLLMASDLSAAITGQSIAVDGG 261
Cdd:PRK07889  207 EGWDERA---PL--GWDVKDptpVARAVVALLSDWFPATTGEIVHVDGG 250
PRK06603 PRK06603
enoyl-[acyl-carrier-protein] reductase FabI;
18-261 6.07e-10

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


Pssm-ID: 168626 [Multi-domain]  Cd Length: 260  Bit Score: 58.10  E-value: 6.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  18 IVTGASRGLGAQ--IAQKMAGAGASVCVNYlnSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRIDI 95
Cdd:PRK06603   12 LITGIANNMSISwaIAQLAKKHGAELWFTY--QSEVLEKRVKPLAEEIGCNFVSELDVTNPKSISNLFDDIKEKWGSFDF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  96 LVN-------NALPGYQFNpsadyTSIEtvqwsHFTQQIDGIVKGAVNAVQAVLPQMkaQKTGKILNISTNLVYNPVVTY 168
Cdd:PRK06603   90 LLHgmafadkNELKGRYVD-----TSLE-----NFHNSLHISCYSLLELSRSAEALM--HDGGSIVTLTYYGAEKVIPNY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 169 YDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTtdasrLTTEAVFDYI------ATTTPLRQATSVDDFANSVLL 242
Cdd:PRK06603  158 NVMGVAKAALEASVKYLANDMGENNIRVNAISAGPIKT-----LASSAIGDFStmlkshAATAPLKRNTTQEDVGGAAVY 232
                         250
                  ....*....|....*....
gi 1918264442 243 MASDLSAAITGQSIAVDGG 261
Cdd:PRK06603  233 LFSELSKGVTGEIHYVDCG 251
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
15-206 6.13e-10

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: 58.25  E-value: 6.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASV---CVNYLNSQEAADTVVADIvaAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:cd09807     2 KTVIITGANTGIGKETARELARRGARVimaCRDMAKCEEAAAEIRRDT--LNHEVIVRHLDLASLKSIRAFAAEFLAEED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpGYQFNP---SAD--YTSIETVQWSHF--TQQIDGIVKGAVNAvQAVLPQMKAQKTGKI--LNISTNLVY 162
Cdd:cd09807    80 RLDVLINNA--GVMRCPyskTEDgfEMQFGVNHLGHFllTNLLLDLLKKSAPS-RIVNVSSLAHKAGKInfDDLNSEKSY 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1918264442 163 NpvvTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT 206
Cdd:cd09807   157 N---TGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRT 197
PRK06300 PRK06300
enoyl-(acyl carrier protein) reductase; Provisional
12-262 1.12e-09

enoyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 235776 [Multi-domain]  Cd Length: 299  Bit Score: 57.91  E-value: 1.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGAS--RGLGAQIAQKMAGAGASVCVN--------YLNSQEAADTVVADIVAAGG-----QAFAYQADVTEL 76
Cdd:PRK06300    6 LTGKIAFIAGIGddQGYGWGIAKALAEAGATILVGtwvpiykiFSQSLELGKFDASRKLSNGSlltfaKIYPMDASFDTP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  77 EQ------------------MQGMANEVTARYGRIDILVNNALPGyqfnPSADYTSIETVQwSHFTQQIDGIVKGAVNAV 138
Cdd:PRK06300   86 EDvpeeirenkrykdlsgytISEVAEQVKKDFGHIDILVHSLANS----PEISKPLLETSR-KGYLAALSTSSYSFVSLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 139 QAVLPQMKAQKTGKILnisTNLVYNPVVTYYD--YTTAKSALIGLTRNLAAELG-QYGIRVNLLAGGLLKTTDASRLT-T 214
Cdd:PRK06300  161 SHFGPIMNPGGSTISL---TYLASMRAVPGYGggMSSAKAALESDTKVLAWEAGrRWGIRVNTISAGPLASRAGKAIGfI 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1918264442 215 EAVFDYIATTTPLRQATSVDDFANSVLLMASDLSAAITGQSIAVDGGL 262
Cdd:PRK06300  238 ERMVDYYQDWAPLPEPMEAEQVGAAAAFLVSPLASAITGETLYVDHGA 285
PRK06197 PRK06197
short chain dehydrogenase; Provisional
15-100 2.45e-09

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 56.57  E-value: 2.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTvVADIVAAGGQA-FAYQA-DVTELEQMQGMANEVTARYGR 92
Cdd:PRK06197   17 RVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAA-AARITAATPGAdVTLQElDLTSLASVRAAADALRAAYPR 95

                  ....*...
gi 1918264442  93 IDILVNNA 100
Cdd:PRK06197   96 IDLLINNA 103
PRK05876 PRK05876
short chain dehydrogenase; Provisional
18-206 7.70e-09

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 54.96  E-value: 7.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  18 IVTGASRGLGAQIAQKMAGAGASVCVNYLNsQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRIDILV 97
Cdd:PRK05876   10 VITGGASGIGLATGTEFARRGARVVLGDVD-KPGLRQAVNHLRAEGFDVHGVMCDVRHREEVTHLADEAFRLLGHVDVVF 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  98 NNA---LPGyqfnPSADYTSiETVQWShftqqIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLV-YNPVVTYYDYTT 173
Cdd:PRK05876   89 SNAgivVGG----PIVEMTH-DDWRWV-----IDVDLWGSIHTVEAFLPRLLEQGTGGHVVFTASFAgLVPNAGLGAYGV 158
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1918264442 174 AKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT 206
Cdd:PRK05876  159 AKYGVVGLAETLAREVTADGIGVSVLCPMVVET 191
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
17-259 2.71e-08

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


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 52.58  E-value: 2.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  17 VIVTGASRGLGAQIAQKMAGAGASVcvnylnsqeaadtvvadiVAAGGQAFAYQADVTELEQMQGMANEVtaryGRIDIL 96
Cdd:cd11731     1 IIVIGATGTIGLAVAQLLSAHGHEV------------------ITAGRSSGDYQVDITDEASIKALFEKV----GHFDAI 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  97 VNNAlpgyqfnpsadyTSIETVQWSHFTQQ-----IDGIVKGAVNAVQAVLPQMKaqKTGKILNISTNLVYNPVVTYYDY 171
Cdd:cd11731    59 VSTA------------GDAEFAPLAELTDAdfqrgLNSKLLGQINLVRHGLPYLN--DGGSITLTSGILAQRPIPGGAAA 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 172 TTAKSALIGLTRNLAAELGQyGIRVNLLAGGLLKTtdasrlTTEAVFDYIATTTPLRQATSVDDFANSVllmasdlSAAI 251
Cdd:cd11731   125 ATVNGALEGFVRAAAIELPR-GIRINAVSPGVVEE------SLEAYGDFFPGFEPVPAEDVAKAYVRSV-------EGAF 190

                  ....*...
gi 1918264442 252 TGQSIAVD 259
Cdd:cd11731   191 TGQVLHVD 198
PRK08340 PRK08340
SDR family oxidoreductase;
17-263 2.85e-08

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 53.27  E-value: 2.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  17 VIVTGASRGLGAQIAQKMAGAGASVCVNylNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYGRIDIL 96
Cdd:PRK08340    3 VLVTASSRGIGFNVARELLKKGARVVIS--SRNEENLEKALKELKEYGEVYAVKADLSDKDDLKNLVKEAWELLGGIDAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  97 VNNAlPGYQFNP----SADYtsietvqwshftqqIDGIVKGAVNAV-----QAVLPQ--MKAQKTGKILNISTNLVYNPV 165
Cdd:PRK08340   81 VWNA-GNVRCEPcmlhEAGY--------------SDWLEAALLHLVapgylTTLLIQawLEKKMKGVLVYLSSVSVKEPM 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 166 VTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASR----------LTTEAVFDY-IATTTPLRQATSVD 234
Cdd:PRK08340  146 PPLVLADVTRAGLVQLAKGVSRTYGGKGIRAYTVLLGSFDTPGAREnlariaeergVSFEETWEReVLERTPLKRTGRWE 225
                         250       260
                  ....*....|....*....|....*....
gi 1918264442 235 DFANSVLLMASDLSAAITGQSIAVDGGLT 263
Cdd:PRK08340  226 ELGSLIAFLLSENAEYMLGSTIVFDGAMT 254
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
12-256 7.55e-08

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 51.80  E-value: 7.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVnyLNSQEAADTVVAD-IVAAGG-QAFAYQAD---VTElEQMQGMANEV 86
Cdd:PRK08945   10 LKDRIILVTGAGDGIGREAALTYARHGATVIL--LGRTEEKLEAVYDeIEAAGGpQPAIIPLDlltATP-QNYQQLADTI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  87 TARYGRIDILVNNA-LPGyqfnpsadytsiETVQWSHFTQQI-DGIVKGAVNAV----QAVLPQMKAQKTGKILNISTNL 160
Cdd:PRK08945   87 EEQFGRLDGVLHNAgLLG------------ELGPMEQQDPEVwQDVMQVNVNATfmltQALLPLLLKSPAASLVFTSSSV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 161 VYNPVVTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTT-DASRLTTEavfdyiattTPLRQATSVDDFANS 239
Cdd:PRK08945  155 GRQGRANWGAYAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRTAmRASAFPGE---------DPQKLKTPEDIMPLY 225
                         250
                  ....*....|....*..
gi 1918264442 240 VLLMASDlSAAITGQSI 256
Cdd:PRK08945  226 LYLMGDD-SRRKNGQSF 241
PRK06196 PRK06196
oxidoreductase; Provisional
12-100 1.93e-07

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 51.22  E-value: 1.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNyLNSQEAADTVVADIVAAGGQAFayqaDVTELEQMQGMANEVTARYG 91
Cdd:PRK06196   24 LSGKTAIVTGGYSGLGLETTRALAQAGAHVIVP-ARRPDVAREALAGIDGVEVVML----DLADLESVRAFAERFLDSGR 98

                  ....*....
gi 1918264442  92 RIDILVNNA 100
Cdd:PRK06196   99 RIDILINNA 107
PRK07024 PRK07024
SDR family oxidoreductase;
17-206 3.05e-07

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 50.31  E-value: 3.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  17 VIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVAdiVAAGGQAFAYQADVTELEQMQGMANEVTARYGRIDIL 96
Cdd:PRK07024    5 VFITGASSGIGQALAREYARQGATLGLVARRTDALQAFAAR--LPKAARVSVYAADVRDADALAAAAADFIAAHGLPDVV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  97 VNNA------LPGYQfnpsADYTSIETVqwshftqqIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYD 170
Cdd:PRK07024   83 IANAgisvgtLTEER----EDLAVFREV--------MDTNYFGMVATFQPFIAPMRAARRGTLVGIASVAGVRGLPGAGA 150
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1918264442 171 YTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT 206
Cdd:PRK07024  151 YSASKAAAIKYLESLRVELRPAGVRVVTIAPGYIRT 186
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
15-144 4.85e-07

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: 48.63  E-value: 4.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442   15 KVVIVTGASRGLGAQIAQKMAGAGASVCVnyLNS-----QEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTAR 89
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGARRLV--LLSrsgpdAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAV 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1918264442   90 YGRIDILVNNALpgyqfnpSADYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQ 144
Cdd:smart00822  79 EGPLTGVIHAAG-------VLDDGVLASLTPERFAAVLAPKAAGAWNLHELTADL 126
PRK08264 PRK08264
SDR family oxidoreductase;
14-196 5.32e-07

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 49.12  E-value: 5.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVADIVAAggqafayQADVTELEQMQGMANEVtaryGRI 93
Cdd:PRK08264    6 GKVVLVTGANRGIGRAFVEQLLARGAAKVYAAARDPESVTDLGPRVVPL-------QLDVTDPASVAAAAEAA----SDV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  94 DILVNNALPGYQFNPSADyTSIETVQwshftQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNISTNLVYNPVVTYYDYTT 173
Cdd:PRK08264   75 TILVNNAGIFRTGSLLLE-GDEDALR-----AEMETNYFGPLAMARAFAPVLAANGGGAIVNVLSVLSWVNFPNLGTYSA 148
                         170       180
                  ....*....|....*....|...
gi 1918264442 174 AKSALIGLTRNLAAELGQYGIRV 196
Cdd:PRK08264  149 SKAAAWSLTQALRAELAPQGTRV 171
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
15-211 1.51e-06

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: 48.36  E-value: 1.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASV---CVNYLNSQEAADTVVADIVAAGGQAFAYqaDVTELEQMQGMANEVTARYG 91
Cdd:cd09809     2 KVIIITGANSGIGFETARSFALHGAHVilaCRNMSRASAAVSRILEEWHKARVEAMTL--DLASLRSVQRFAEAFKAKNS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNA----LPgYQFNPSADYTSIETVQWSHF--TQQIDGIVKGAVNAVQAVLPQmKAQKTGKILNISTNLVYN-- 163
Cdd:cd09809    80 PLHVLVCNAavfaLP-WTLTEDGLETTFQVNHLGHFylVQLLEDVLRRSAPARVIVVSS-ESHRFTDLPDSCGNLDFSll 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1918264442 164 --PVVTYYD---YTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDASR 211
Cdd:cd09809   158 spPKKKYWSmlaYNRAKLCNILFSNELHRRLSPRGITSNSLHPGNMMYSSIHR 210
PRK08862 PRK08862
SDR family oxidoreductase;
14-196 1.77e-06

SDR family oxidoreductase;


Pssm-ID: 236342 [Multi-domain]  Cd Length: 227  Bit Score: 47.80  E-value: 1.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADTVVAdIVAAGGQAFAYQADVTELEQMQGMANEVTARYGR- 92
Cdd:PRK08862    5 SSIILITSAGSVLGRTISCHFARLGATLILCDQDQSALKDTYEQ-CSALTDNVYSFQLKDFSQESIRHLFDAIEQQFNRa 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  93 IDILVNNalpgYQFNPSADYTSIETVqwSHFTQQIDGIVKGAVNAVQAVLPQMKAQKT-GKILN-ISTNLVYNPVVTyyd 170
Cdd:PRK08862   84 PDVLVNN----WTSSPLPSLFDEQPS--ESFIQQLSSLASTLFTYGQVAAERMRKRNKkGVIVNvISHDDHQDLTGV--- 154
                         170       180
                  ....*....|....*....|....*.
gi 1918264442 171 yTTAKSALIGLTRNLAAELGQYGIRV 196
Cdd:PRK08862  155 -ESSNALVSGFTHSWAKELTPFNIRV 179
PRK06720 PRK06720
hypothetical protein; Provisional
12-100 1.81e-06

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 46.89  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNsQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARYG 91
Cdd:PRK06720   14 LAGKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDID-QESGQATVEEITNLGGEALFVSYDMEKQGDWQRVISITLNAFS 92

                  ....*....
gi 1918264442  92 RIDILVNNA 100
Cdd:PRK06720   93 RIDMLFQNA 101
PRK06079 PRK06079
enoyl-[acyl-carrier-protein] reductase FabI;
11-261 2.25e-06

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


Pssm-ID: 235694 [Multi-domain]  Cd Length: 252  Bit Score: 47.41  E-value: 2.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  11 FLLNKVVIVTGAS--RGLGAQIAQKMAGAGASVCVNYLNS--QEAADTVVADIVAAggqafaYQADVTELEQMQGMANEV 86
Cdd:PRK06079    4 ILSGKKIVVMGVAnkRSIAWGCAQAIKDQGATVIYTYQNDrmKKSLQKLVDEEDLL------VECDVASDESIERAFATI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  87 TARYGRIDILVNnalpgyqfnpsadytSIETVQWSHFTQQIDGIVKGAVNAVQ--AVLPQMKAQKTGK-ILNISTNLVyn 163
Cdd:PRK06079   78 KERVGKIDGIVH---------------AIAYAKKEELGGNVTDTSRDGYALAQdiSAYSLIAVAKYARpLLNPGASIV-- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 164 pVVTYY-------DYTT---AKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTtdasrLTTEAVFDY------IATTTPL 227
Cdd:PRK06079  141 -TLTYFgseraipNYNVmgiAKAALESSVRYLARDLGKKGIRVNAISAGAVKT-----LAVTGIKGHkdllkeSDSRTVD 214
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1918264442 228 RQATSVDDFANSVLLMASDLSAAITGQSIAVDGG 261
Cdd:PRK06079  215 GVGVTIEEVGNTAAFLLSDLSTGVTGDIIYVDKG 248
PRK09291 PRK09291
SDR family oxidoreductase;
15-196 1.03e-05

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 45.76  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGasvcvnylnsqeaaDTVVADiVAAGGQAFAYQADVTELeqmqGMANEV-----TAR 89
Cdd:PRK09291    3 KTILITGAGSGFGREVALRLARKG--------------HNVIAG-VQIAPQVTALRAEAARR----GLALRVekldlTDA 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  90 YGR-------IDILVNNALPGyQFNPSADyTSIETVQwshftQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNIST--NL 160
Cdd:PRK09291   64 IDRaqaaewdVDVLLNNAGIG-EAGAVVD-IPVELVR-----ELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSmaGL 136
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1918264442 161 VYNPVVTYYDYTtaKSALIGLTRNLAAELGQYGIRV 196
Cdd:PRK09291  137 ITGPFTGAYCAS--KHALEAIAEAMHAELKPFGIQV 170
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
163-262 1.14e-05

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 45.38  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 163 NPVVTYYDYTTAKSALIGLT-RNLAAELGQYGIRVNLLAGGLLKTTDASRLTT---EAVFDYIATttPLRQATSVDDFAN 238
Cdd:PRK12428  129 HPVALATGYQLSKEALILWTmRQAQPWFGARGIRVNCVAPGPVFTPILGDFRSmlgQERVDSDAK--RMGRPATADEQAA 206
                          90       100
                  ....*....|....*....|....
gi 1918264442 239 SVLLMASDLSAAITGQSIAVDGGL 262
Cdd:PRK12428  207 VLVFLCSDAARWINGVNLPVDGGL 230
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
15-100 1.23e-05

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: 45.59  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGA----SVCVNYLNSQEAAdtvvADIVAAGGQAFAYQADVTELEQMQGMANEVTARY 90
Cdd:cd09810     2 GTVVITGASSGLGLAAAKALARRGEwhvvMACRDFLKAEQAA----QEVGMPKDSYSVLHCDLASLDSVRQFVDNFRRTG 77
                          90
                  ....*....|
gi 1918264442  91 GRIDILVNNA 100
Cdd:cd09810    78 RPLDALVCNA 87
PRK08017 PRK08017
SDR family oxidoreductase;
13-206 2.22e-05

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 44.69  E-value: 2.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  13 LNKVVIVTGASRGLGAQIAQKMAGAGASVcvnYLNSQEAADtvVADIVAAGGQAFayQADVTELEQMQGMANEVTA-RYG 91
Cdd:PRK08017    1 MQKSVLITGCSSGIGLEAALELKRRGYRV---LAACRKPDD--VARMNSLGFTGI--LLDLDDPESVERAADEVIAlTDN 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  92 RIDILVNNAlpGYQFnpsadYTSIETVQWSHFTQQIDGIVKGAVNAVQAVLPQMKAQKTGKILNIST--NLVYNPvvTYY 169
Cdd:PRK08017   74 RLYGLFNNA--GFGV-----YGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGEGRIVMTSSvmGLISTP--GRG 144
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1918264442 170 DYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT 206
Cdd:PRK08017  145 AYAASKYALEAWSDALRMELRHSGIKVSLIEPGPIRT 181
PRK05854 PRK05854
SDR family oxidoreductase;
12-100 2.72e-05

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 44.67  E-value: 2.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  12 LLNKVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQ--EAAdtvVADIVAAGGQAFA--YQADVTELEQMQGMANEVT 87
Cdd:PRK05854   12 LSGKRAVVTGASDGLGLGLARRLAAAGAEVILPVRNRAkgEAA---VAAIRTAVPDAKLslRALDLSSLASVAALGEQLR 88
                          90
                  ....*....|...
gi 1918264442  88 ARYGRIDILVNNA 100
Cdd:PRK05854   89 AEGRPIHLLINNA 101
PRK08219 PRK08219
SDR family oxidoreductase;
15-188 2.88e-05

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 44.15  E-value: 2.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAG-----AGASvcvnylnSQEAADTVVADIVAAGgqafAYQADVTELEQMQGmaneVTAR 89
Cdd:PRK08219    4 PTALITGASRGIGAAIARELAPthtllLGGR-------PAERLDELAAELPGAT----PFPVDLTDPEAIAA----AVEQ 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  90 YGRIDILVNNAlpgyqfnPSADYTSIETV---QWSHftqQIDGIVKGAVNAVQAVLPQMKAQKtGKILNISTNLVYNPVV 166
Cdd:PRK08219   69 LGRLDVLVHNA-------GVADLGPVAEStvdEWRA---TLEVNVVAPAELTRLLLPALRAAH-GHVVFINSGAGLRANP 137
                         170       180
                  ....*....|....*....|..
gi 1918264442 167 TYYDYTTAKSALIGLTRNLAAE 188
Cdd:PRK08219  138 GWGSYAASKFALRALADALREE 159
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
17-100 2.99e-05

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: 44.41  E-value: 2.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  17 VIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADtvVADIVAAGgqAFAYQADVTELEQMQGMANEVTArYGRIDIL 96
Cdd:cd08951    10 IFITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAAD--AKAACPGA--AGVLIGDLSSLAETRKLADQVNA-IGRFDAV 84

                  ....
gi 1918264442  97 VNNA 100
Cdd:cd08951    85 IHNA 88
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
17-261 5.88e-05

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 43.38  E-value: 5.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  17 VIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAadtvVADIVAAGgqAFAYQADVTELEQMQGMANEVTARYGRIDIL 96
Cdd:PRK06483    5 ILITGAGQRIGLALAWHLLAQGQPVIVSYRTHYPA----IDGLRQAG--AQCIQADFSTNAGIMAFIDELKQHTDGLRAI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  97 VNNAlpgyqfnpS---ADYTSIETVQWSHFTQQIDGIVKGAVNavQAVLPQMKAQKTGK--ILNISTNLVYNPVVTYYDY 171
Cdd:PRK06483   79 IHNA--------SdwlAEKPGAPLADVLARMMQIHVNAPYLLN--LALEDLLRGHGHAAsdIIHITDYVVEKGSDKHIAY 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 172 TTAKSALIGLTRNLAAELGQYgIRVNLLAGGLL------------KTTDASRLTTEAVFDYIatttplrqATSVDdfans 239
Cdd:PRK06483  149 AASKAALDNMTLSFAAKLAPE-VKVNSIAPALIlfnegddaayrqKALAKSLLKIEPGEEEI--------IDLVD----- 214
                         250       260
                  ....*....|....*....|..
gi 1918264442 240 vLLMASDLsaaITGQSIAVDGG 261
Cdd:PRK06483  215 -YLLTSCY---VTGRSLPVDGG 232
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
15-131 3.15e-04

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: 41.22  E-value: 3.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKM-----AGAGASVCV---NYLNSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEV 86
Cdd:cd08941     2 KVVLVTGANSGLGLAICERLlaeddENPELTLILacrNLQRAEAACRALLASHPDARVVFDYVLVDLSNMVSVFAAAKEL 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1918264442  87 TARYGRIDILVNNAlpGYQFNPSADYTS---------IETVQWSHFTQQIDGIV 131
Cdd:cd08941    82 KKRYPRLDYLYLNA--GIMPNPGIDWIGaikevltnpLFAVTNPTYKIQAEGLL 133
PRK06940 PRK06940
short chain dehydrogenase; Provisional
14-263 3.19e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 41.16  E-value: 3.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  14 NKVVIVTGASrGLGAQIAQKMaGAGASVCVNYLNsQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEvTARYGRI 93
Cdd:PRK06940    2 KEVVVVIGAG-GIGQAIARRV-GAGKKVLLADYN-EENLEAAAKTLREAGFDVSTQEVDVSSRESVKALAAT-AQTLGPV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  94 DILVNNAlpgyQFNPSAdyTSIET----------VQWSHFTQQIDGIVKGAVNAVQA--VLPQMKAQK--------TGKI 153
Cdd:PRK06940   78 TGLVHTA----GVSPSQ--ASPEAilkvdlygtaLVLEEFGKVIAPGGAGVVIASQSghRLPALTAEQeralattpTEEL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 154 LNISTNLVYNPVVTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKTTDA-SRLTTE--AVFDYIATTTPLRQA 230
Cdd:PRK06940  152 LSLPFLQPDAIEDSLHAYQIAKRANALRVMAEAVKWGERGARINSISPGIISTPLAqDELNGPrgDGYRNMFAKSPAGRP 231
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1918264442 231 TSVDDFANSVLLMASDLSAAITGQSIAVDGGLT 263
Cdd:PRK06940  232 GTPDEIAALAEFLMGPRGSFITGSDFLVDGGAT 264
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
15-206 3.59e-04

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: 41.11  E-value: 3.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASV---CVNyLNSQEAAD---------TVVadivaaggqafayQADVTELEQMQGM 82
Cdd:cd09805     1 KAVLITGCDSGFGNLLAKKLDSLGFTVlagCLT-KNGPGAKElrrvcsdrlRTL-------------QLDVTKPEQIKRA 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  83 ANEVTARYGRIDI--LVNNAlpGYQFNPS-ADYTSIETvqwshFTQQIDGIVKGAVNAVQAVLPQMKAQKtGKILNISTN 159
Cdd:cd09805    67 AQWVKEHVGEKGLwgLVNNA--GILGFGGdEELLPMDD-----YRKCMEVNLFGTVEVTKAFLPLLRRAK-GRVVNVSSM 138
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1918264442 160 LVYNPVVTYYDYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT 206
Cdd:cd09805   139 GGRVPFPAGGAYCASKAAVEAFSDSLRRELQPWGVKVSIIEPGNFKT 185
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
16-94 1.44e-03

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: 39.66  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  16 VVIVTGASRGLGAQIAQKMAGAGASVCVnyL-------NSQEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTA 88
Cdd:cd08953   207 VYLVTGGAGGIGRALARALARRYGARLV--LlgrsplpPEEEWKAQTLAALEALGARVLYISADVTDAAAVRRLLEKVRE 284

                  ....*.
gi 1918264442  89 RYGRID 94
Cdd:cd08953   285 RYGAID 290
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
15-206 1.79e-03

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 38.90  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASV-CVNYLNSQEAADtvVADIvaAGGQAFAYQADVTELEQMQGMANEV-----TA 88
Cdd:PRK06924    2 RYVIITGTSQGLGEAIANQLLEKGTHViSISRTENKELTK--LAEQ--YNSNLTFHSLDLQDVHELETNFNEIlssiqED 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  89 RYGRIdILVNNAlpgyqfnpsADYTSIETVQWSHFTQQIDGIvkgAVNAVQAVL------PQMKAQKTGK-ILNISTNLV 161
Cdd:PRK06924   78 NVSSI-HLINNA---------GMVAPIKPIEKAESEELITNV---HLNLLAPMIltstfmKHTKDWKVDKrVINISSGAA 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1918264442 162 YNPVVTYYDYTTAKSALIGLTRNLAAE--LGQYGIRVNLLAGGLLKT 206
Cdd:PRK06924  145 KNPYFGWSAYCSSKAGLDMFTQTVATEqeEEEYPVKIVAFSPGVMDT 191
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
16-93 1.89e-03

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: 38.31  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  16 VVIVTGASRGLGAQIAQKMAGAGASVCVnyLNS-----QEAADTVVADIVAAGGQAFAYQADVTELEQMQGMANEVTARY 90
Cdd:pfam08659   2 TYLITGGLGGLGRELARWLAERGARHLV--LLSrsaapRPDAQALIAELEARGVEVVVVACDVSDPDAVAALLAEIKAEG 79

                  ...
gi 1918264442  91 GRI 93
Cdd:pfam08659  80 PPI 82
PRK08177 PRK08177
SDR family oxidoreductase;
15-206 2.82e-03

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 38.09  E-value: 2.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEAADtvvadiVAAGGQAFAYQADVTELEQMQGMANEVTARygRID 94
Cdd:PRK08177    2 RTALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQDTA------LQALPGVHIEKLDMNDPASLDQLLQRLQGQ--RFD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  95 ILVNNA-LPGYQFNPSADYTSIETVQWsHFTQQIDGI-----VKGAVNAVQAVLPQMKAQKTGKILNISTNLVYnpvvty 168
Cdd:PRK08177   74 LLFVNAgISGPAHQSAADATAAEIGQL-FLTNAIAPIrlarrLLGQVRPGQGVLAFMSSQLGSVELPDGGEMPL------ 146
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1918264442 169 ydYTTAKSALIGLTRNLAAELGQYGIRVNLLAGGLLKT 206
Cdd:PRK08177  147 --YKASKAALNSMTRSFVAELGEPTLTVLSMHPGWVKT 182
PRK05884 PRK05884
SDR family oxidoreductase;
17-261 4.57e-03

SDR family oxidoreductase;


Pssm-ID: 135642 [Multi-domain]  Cd Length: 223  Bit Score: 37.48  E-value: 4.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  17 VIVTGASRGLGAQIAQKMAGAGASVCVNYLNSQEA--------ADTVVADIvaaggqafayqADVTELEQMQGMANEvta 88
Cdd:PRK05884    3 VLVTGGDTDLGRTIAEGFRNDGHKVTLVGARRDDLevaakeldVDAIVCDN-----------TDPASLEEARGLFPH--- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  89 rygRIDILVNNALPGYQFNPSADYTSIETVqwSHFTQQIDGIVKGAVNAVQAVLPQMKAqkTGKILNISTNLVYNPVVTy 168
Cdd:PRK05884   69 ---HLDTIVNVPAPSWDAGDPRTYSLADTA--NAWRNALDATVLSAVLTVQSVGDHLRS--GGSIISVVPENPPAGSAE- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442 169 ydyTTAKSALIGLTRNLAAELGQYGIRVNLLAGGllkttdasrLTTEAVFDYIATTTPlrqaTSVDDFANSVLLMASDLS 248
Cdd:PRK05884  141 ---AAIKAALSNWTAGQAAVFGTRGITINAVACG---------RSVQPGYDGLSRTPP----PVAAEIARLALFLTTPAA 204
                         250
                  ....*....|...
gi 1918264442 249 AAITGQSIAVDGG 261
Cdd:PRK05884  205 RHITGQTLHVSHG 217
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
15-100 8.03e-03

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: 36.80  E-value: 8.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918264442  15 KVVIVTGASRGLGAQIAQKMAGAGASV---CVNylnsQEAADTVVADIVAAGG--QAFAYQADVTELEQMQGMANEVTAR 89
Cdd:cd09808     2 RSFLITGANSGIGKAAALAIAKRGGTVhmvCRN----QTRAEEARKEIETESGnqNIFLHIVDMSDPKQVWEFVEEFKEE 77
                          90
                  ....*....|.
gi 1918264442  90 YGRIDILVNNA 100
Cdd:cd09808    78 GKKLHVLINNA 88
 
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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