NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|4503301|ref|NP_001350|]
View 

2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing], mitochondrial isoform 1 precursor [Homo sapiens]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10143283)

atypical SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase that 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, similar to human peroxisomal 2,4-dienoyl-CoA reductase, an auxiliary enzyme of beta-oxidation that catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA

CATH:  3.40.50.720
EC:  1.-.-.-
Gene Ontology:  GO:0070403|GO:0016491
PubMed:  12604210|19011750|19011748|19027726|20423462
SCOP:  4000029

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 57-303 3.83e-127

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: 363.83  E-value: 3.83e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   57 FQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAG 136
Cdd:cd05369   1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISSATGGRAHPIQCDVRDPEAVEAAVDETLKEFG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  137 HPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSASAKAG 216
Cdd:cd05369  81 KIDILINNAAGNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAKHGGSILNISATYAYTGSPFQVHSAAAKAG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  217 VEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAV 296
Cdd:cd05369 161 VDALTRSLAVEWGPYGIRVNAIAPGPIPTTEGMERLAPSGKSEKKMIERVPLGRLGTPEEIANLALFLLSDAASYINGTT 240


                ....*..
gi 4503301  297 IKFDGGE 303
Cdd:cd05369 241 LVVDGGQ 247
 
Name Accession Description Interval E-value
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 57-303 3.83e-127

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: 363.83  E-value: 3.83e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   57 FQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAG 136
Cdd:cd05369   1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISSATGGRAHPIQCDVRDPEAVEAAVDETLKEFG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  137 HPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSASAKAG 216
Cdd:cd05369  81 KIDILINNAAGNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAKHGGSILNISATYAYTGSPFQVHSAAAKAG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  217 VEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAV 296
Cdd:cd05369 161 VDALTRSLAVEWGPYGIRVNAIAPGPIPTTEGMERLAPSGKSEKKMIERVPLGRLGTPEEIANLALFLLSDAASYINGTT 240


                ....*..
gi 4503301  297 IKFDGGE 303
Cdd:cd05369 241 LVVDGGQ 247
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 79-303 1.48e-73

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 227.64  E-value: 1.48e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    79 LSSLGAQCVIASRKMDVLKATAEQISSQTGnKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSP 158
Cdd:PRK07677  21 FAEEGANVVITGRTKEKLEEAKLEIEQFPG-QVLTVQMDVRNPEDVQKMVEQIDEKFGRIDALINNAAGNFICPAEDLSV 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   159 NAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWG-KYGMRFNV 237
Cdd:PRK07677 100 NGWNSVIDIVLNGTFYCSQAVGKYWIEKGIKGNIINMVATYAWDAGPGVIHSAAAKAGVLAMTRTLAVEWGrKYGIRVNA 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503301   238 IQPGPIKTKGAFSRLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGGE 303
Cdd:PRK07677 180 IAPGPIERTGGADKLWESEEAAKRTIQSVPLGRLGTPEEIAGLAYFLLSDEAAYINGTCITMDGGQ 245
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 83-302 2.56e-60

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: 193.46  E-value: 2.56e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   83 GAQCVIASRKMDVLKATAEQISSQtGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAWK 162
Cdd:COG1028  30 GARVVITDRDAEALEAAAAELRAA-GGRALAVAADVTDEAAVEALVAAAVAAFGRLDILVNNAGITPPGPLEELTEEDWD 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  163 TITDIVLNGTAFVTLEIGKQLiKAQKGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGP 242
Cdd:COG1028 109 RVLDVNLKGPFLLTRAALPHM-RERGGGRIVNISSIAGLRGSPGQAAYAASKAAVVGLTRSLALELAPRGIRVNAVAPGP 187

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  243 IKTkGAFSRLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:COG1028 188 IDT-PMTRALLGAEEVREALAARIPLGRLGTPEEVAAAVLFLASDAASYITGQVLAVDGG 246
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 78-302 4.92e-51

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: 169.15  E-value: 4.92e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301     78 LLSSLGAQCVIASRKMDvLKATAEQISSQTGnkVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAA--GNFISPTER 155
Cdd:pfam13561  15 ALAEEGAEVVLTDLNEA-LAKRVEELAEELG--AAVLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGfaPKLKGPFLD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    156 LSPNAWKTITDIVLNGTAFVTLEIGKQLikaQKGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRF 235
Cdd:pfam13561  92 TSREDFDRALDVNLYSLFLLAKAALPLM---KEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVELGPRGIRV 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503301    236 NVIQPGPIKTkGAFSRLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:pfam13561 169 NAISPGPIKT-LAASGIPGFDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGG 234
kduD TIGR01832
2-deoxy-D-gluconate 3-dehydrogenase; This model describes 2-deoxy-D-gluconate 3-dehydrogenase ...
 56-302 3.89e-30

2-deoxy-D-gluconate 3-dehydrogenase; This model describes 2-deoxy-D-gluconate 3-dehydrogenase (also called 2-keto-3-deoxygluconate oxidoreductase), a member of the family of short-chain-alcohol dehydrogenases (pfam00106). This protein has been characterized in Erwinia chrysanthemi as an enzyme of pectin degradation. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 188170 [Multi-domain]  Cd Length: 248  Bit Score: 114.86  E-value: 3.89e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301     56 SFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKmdVLKATAEQISsQTGNKVHAIQCDVRDPDMVQNTVSELIKVA 135
Cdd:TIGR01832   2 SLEGKVALVTGANTGLGQGIAVGLAEAGADIVGAGRS--EPSETQQQVE-ALGRRFLSLTADLSDIEAIKALVDSAVEEF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    136 GHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFLSITTIYAETGsGFVVPSASA-K 214
Cdd:TIGR01832  79 GHIDILVNNAGIIRRADAEEFSEKDWDDVMNVNLKSVFFLTQAAAKHFLKQGRGGKIINIASMLSFQG-GIRVPSYTAsK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    215 AGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKG-AFSRLDPTGTfeKEMIGRIPCGRLGTVEELANLAAFLCSDYASWIN 293
Cdd:TIGR01832 158 HAVAGLTKLLANEWAAKGINVNAIAPGYMATNNtQALRADEDRN--AAILERIPAGRWGTPDDIGGPAVFLASSASDYVN 235


                  ....*....
gi 4503301    294 GAVIKFDGG 302
Cdd:TIGR01832 236 GYTLAVDGG 244
 
Name Accession Description Interval E-value
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 57-303 3.83e-127

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: 363.83  E-value: 3.83e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   57 FQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAG 136
Cdd:cd05369   1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISSATGGRAHPIQCDVRDPEAVEAAVDETLKEFG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  137 HPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSASAKAG 216
Cdd:cd05369  81 KIDILINNAAGNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAKHGGSILNISATYAYTGSPFQVHSAAAKAG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  217 VEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAV 296
Cdd:cd05369 161 VDALTRSLAVEWGPYGIRVNAIAPGPIPTTEGMERLAPSGKSEKKMIERVPLGRLGTPEEIANLALFLLSDAASYINGTT 240


                ....*..
gi 4503301  297 IKFDGGE 303
Cdd:cd05369 241 LVVDGGQ 247
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 79-303 1.48e-73

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 227.64  E-value: 1.48e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    79 LSSLGAQCVIASRKMDVLKATAEQISSQTGnKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSP 158
Cdd:PRK07677  21 FAEEGANVVITGRTKEKLEEAKLEIEQFPG-QVLTVQMDVRNPEDVQKMVEQIDEKFGRIDALINNAAGNFICPAEDLSV 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   159 NAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWG-KYGMRFNV 237
Cdd:PRK07677 100 NGWNSVIDIVLNGTFYCSQAVGKYWIEKGIKGNIINMVATYAWDAGPGVIHSAAAKAGVLAMTRTLAVEWGrKYGIRVNA 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503301   238 IQPGPIKTKGAFSRLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGGE 303
Cdd:PRK07677 180 IAPGPIERTGGADKLWESEEAAKRTIQSVPLGRLGTPEEIAGLAYFLLSDEAAYINGTCITMDGGQ 245
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 83-302 2.56e-60

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: 193.46  E-value: 2.56e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   83 GAQCVIASRKMDVLKATAEQISSQtGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAWK 162
Cdd:COG1028  30 GARVVITDRDAEALEAAAAELRAA-GGRALAVAADVTDEAAVEALVAAAVAAFGRLDILVNNAGITPPGPLEELTEEDWD 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  163 TITDIVLNGTAFVTLEIGKQLiKAQKGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGP 242
Cdd:COG1028 109 RVLDVNLKGPFLLTRAALPHM-RERGGGRIVNISSIAGLRGSPGQAAYAASKAAVVGLTRSLALELAPRGIRVNAVAPGP 187

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  243 IKTkGAFSRLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:COG1028 188 IDT-PMTRALLGAEEVREALAARIPLGRLGTPEEVAAAVLFLASDAASYITGQVLAVDGG 246
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 78-302 4.92e-51

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: 169.15  E-value: 4.92e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301     78 LLSSLGAQCVIASRKMDvLKATAEQISSQTGnkVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAA--GNFISPTER 155
Cdd:pfam13561  15 ALAEEGAEVVLTDLNEA-LAKRVEELAEELG--AAVLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGfaPKLKGPFLD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    156 LSPNAWKTITDIVLNGTAFVTLEIGKQLikaQKGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRF 235
Cdd:pfam13561  92 TSREDFDRALDVNLYSLFLLAKAALPLM---KEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVELGPRGIRV 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503301    236 NVIQPGPIKTkGAFSRLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:pfam13561 169 NAISPGPIKT-LAASGIPGFDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGG 234
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 78-300 8.89e-51

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: 168.62  E-value: 8.89e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   78 LLSSLGAQCVIASRKMDVLKATAEqiSSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLS 157
Cdd:cd05233  17 RLAREGAKVVLADRNEEALAELAA--IEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILVNNAGIARPGPLEELT 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  158 PNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFLsITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNV 237
Cdd:cd05233  95 DEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVN-ISSVAGLRPLPGQAAYAASKAALEGLTRSLALELAPYGIRVNA 173

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503301  238 IQPGPIKTKGAFSRLDPTGtfEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFD 300
Cdd:cd05233 174 VAPGLVDTPMLAKLGPEEA--EKELAAAIPLGRLGTPEEVAEAVVFLASDEASYITGQVIPVD 234
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
78-302 2.97e-50

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 167.64  E-value: 2.97e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    78 LLSSLGAQCVIASRKMDVLKATAEQISSQtGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLS 157
Cdd:PRK05653  24 RLAADGAKVVIYDSNEEAAEALAAELRAA-GGEARVLVFDVSDEAAVRALIEAAVEAFGALDILVNNAGITRDALLPRMS 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   158 PNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAaFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNV 237
Cdd:PRK05653 103 EEDWDRVIDVNLTGTFNVVRAALPPMIKARYGR-IVNISSVSGVTGNPGQTNYSAAKAGVIGFTKALALELASRGITVNA 181

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503301   238 IQPGPIKTkgafSRLDPTGTFEKEMIGR-IPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK05653 182 VAPGFIDT----DMTEGLPEEVKAEILKeIPLGRLGQPEEVANAVAFLASDAASYITGQVIPVNGG 243
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 57-302 3.08e-50

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 168.21  E-value: 3.08e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    57 FQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISsQTGNKVHAIQCDVRDPDMVQNTVSELIKVAG 136
Cdd:PRK07576   7 FAGKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVAQLQ-QAGPEGLGVSADVRDYAAVEAAFAQIADEFG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   137 HPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTaFVTLEIGKQLIKaQKGAAFLSITTIYAETGSGFVVPSASAKAG 216
Cdd:PRK07576  86 PIDVLVSGAAGNFPAPAAGMSANGFKTVVDIDLLGT-FNVLKAAYPLLR-RPGASIIQISAPQAFVPMPMQAHVCAAKAG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   217 VEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAV 296
Cdd:PRK07576 164 VDMLTRTLALEWGPEGIRVNSIVPGPIAGTEGMARLAPSPELQAAVAQSVPLKRNGTKQDIANAALFLASDMASYITGVV 243


                 ....*.
gi 4503301   297 IKFDGG 302
Cdd:PRK07576 244 LPVDGG 249
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 56-302 8.65e-43

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: 148.27  E-value: 8.65e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   56 SFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKaTAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVA 135
Cdd:cd05347   2 SLKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAE-EAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  136 GHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKaQKGAAFLSITTIYAETGSGFVVPSASAKA 215
Cdd:cd05347  81 GKIDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIK-QGHGKIINICSLLSELGGPPVPAYAASKG 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  216 GVEAMSKSLAAEWGKYGMRFNVIQPGPIKTK-GAFSRLDPtgTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWING 294
Cdd:cd05347 160 GVAGLTKALATEWARHGIQVNAIAPGYFATEmTEAVVADP--EFNDDILKRIPAGRWGQPEDLVGAAVFLASDASDYVNG 237


                ....*...
gi 4503301  295 AVIKFDGG 302
Cdd:cd05347 238 QIIFVDGG 245
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 56-302 3.78e-42

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 146.49  E-value: 3.78e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    56 SFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVA 135
Cdd:PRK05557   2 SLEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGAEALVAEIGALGGKALAVQGDVSDAESVERAVDEAKAEF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   136 GHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGaAFLSITTIYAETGSGFVVPSASAKA 215
Cdd:PRK05557  82 GGVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSG-RIINISSVVGLMGNPGQANYAASKA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   216 GVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKgAFSRLDPtgTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGA 295
Cdd:PRK05557 161 GVIGFTKSLARELASRGITVNAVAPGFIETD-MTDALPE--DVKEAILAQIPLGRLGQPEEIASAVAFLASDEAAYITGQ 237


                 ....*..
gi 4503301   296 VIKFDGG 302
Cdd:PRK05557 238 TLHVNGG 244
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 79-302 1.17e-41

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: 145.49  E-value: 1.17e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   79 LSSLGAQCVIASRKMDVLKATAEQISsQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSP 158
Cdd:cd05344  21 LAREGARVAICARNRENLERAASELR-AGGAGVLAVVADLTDPEDIDRLVEKAGDAFGRVDILVNNAGGPPPGPFAELTD 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  159 NAWKTITDIVLNGTAFVTLEIGKQLIKaQKGAAFLSITTIYA-ETGSGFVVpSASAKAGVEAMSKSLAAEWGKYGMRFNV 237
Cdd:cd05344 100 EDWLEAFDLKLLSVIRIVRAVLPGMKE-RGWGRIVNISSLTVkEPEPNLVL-SNVARAGLIGLVKTLSRELAPDGVTVNS 177

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503301  238 IQPGPIKT--------KGAFSRLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:cd05344 178 VLPGYIDTervrrlleARAEKEGISVEEAEKEVASQIPLGRVGKPEELAALIAFLASEKASYITGQAILVDGG 250
PRK12826 PRK12826
SDR family oxidoreductase;
56-303 8.61e-40

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 140.44  E-value: 8.61e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    56 SFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQtGNKVHAIQCDVRDPDMVQNTVSELIKVA 135
Cdd:PRK12826   3 DLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAA-GGKARARQVDVRDRAALKAAVAAGVEDF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   136 GHPNIVINNAAgnfISP---TERLSPNAWKTITDIVLNGTAFVTleigKQLIKAQKGAAFLSITTIYAETGSGFVVPS-- 210
Cdd:PRK12826  82 GRLDILVANAG---IFPltpFAEMDDEQWERVIDVNLTGTFLLT----QAALPALIRAGGGRIVLTSSVAGPRVGYPGla 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   211 --ASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTkgafSRLDPTGTFE--KEMIGRIPCGRLGTVEELANLAAFLCS 286
Cdd:PRK12826 155 hyAASKAGLVGFTRALALELAARNITVNSVHPGGVDT----PMAGNLGDAQwaEAIAAAIPLGRLGEPEDIAAAVLFLAS 230

                        250
                 ....*....|....*..
gi 4503301   287 DYASWINGAVIKFDGGE 303
Cdd:PRK12826 231 DEARYITGQTLPVDGGA 247
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 78-302 1.88e-39

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: 139.22  E-value: 1.88e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   78 LLSSLGAQCVIASRKMDVLKATAEQISSQtGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNA---AGNFIsptE 154
Cdd:cd05333  19 RLAAEGAKVAVTDRSEEAAAETVEEIKAL-GGNAAALEADVSDREAVEALVEKVEAEFGPVDILVNNAgitRDNLL---M 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  155 RLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAaFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMR 234
Cdd:cd05333  95 RMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGR-IINISSVVGLIGNPGQANYAASKAGVIGFTKSLAKELASRGIT 173

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4503301  235 FNVIQPGPIKTkgafsrlDPTGTFE----KEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:cd05333 174 VNAVAPGFIDT-------DMTDALPekvkEKILKQIPLGRLGTPEEVANAVAFLASDDASYITGQVLHVNGG 238
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 83-302 1.71e-38

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 137.39  E-value: 1.71e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    83 GAQCVIASRKMDVLKATAEQISSqTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAWK 162
Cdd:PRK08213  36 GARVVLSARKAEELEEAAAHLEA-LGIDALWIAADVADEADIERLAEETLERFGHVDILVNNAGATWGAPAEDHPVEAWD 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   163 TITDIVLNGTAFVTLEIGKQLIKAQKGAAFLSITTIYAETGS-----GFVVPSASaKAGVEAMSKSLAAEWGKYGMRFNV 237
Cdd:PRK08213 115 KVMNLNVRGLFLLSQAVAKRSMIPRGYGRIINVASVAGLGGNppevmDTIAYNTS-KGAVINFTRALAAEWGPHGIRVNA 193

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503301   238 IQPG--PIK-TKGAFSRLdptgtfEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK08213 194 IAPGffPTKmTRGTLERL------GEDLLAHTPLGRLGDDEDLKGAALLLASDASKHITGQILAVDGG 255
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 96-305 3.62e-38

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 136.15  E-value: 3.62e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    96 LKATAEQISsQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGtAFV 175
Cdd:PRK12825  44 AEELVEAVE-ALGRRAQAVQADVTDKAALEAAVAAAVERFGRIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSG-VFH 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   176 TLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTkgafSRLDPT 255
Cdd:PRK12825 122 LLRAVVPPMRKQRGGRIVNISSVAGLPGWPGRSNYAAAKAGLVGLTKALARELAEYGITVNMVAPGDIDT----DMKEAT 197

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 4503301   256 GTFEKEMI-GRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGGEEV 305
Cdd:PRK12825 198 IEEAREAKdAETPLGRSGTPEDIARAVAFLCSDASDYITGQVIEVTGGVDV 248
FabG-like PRK07231
SDR family oxidoreductase;
83-302 1.59e-37

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 134.57  E-value: 1.59e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    83 GAQCVIASRKMDVLKATAEQIssQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFI-SPTERLSPNAW 161
Cdd:PRK07231  29 GARVVVTDRNEEAAERVAAEI--LAGGRAIAVAADVSDEADVEAAVAAALERFGSVDILVNNAGTTHRnGPLLDVDEAEF 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   162 KTITDIVLNGTAFVTLEIGKQLiKAQKGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPG 241
Cdd:PRK07231 107 DRIFAVNVKSPYLWTQAAVPAM-RGEGGGAIVNVASTAGLRPRPGLGWYNASKGAVITLTKALAAELGPDKIRVNAVAPV 185

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4503301   242 PIKTKGAFSRL-DPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK07231 186 VVETGLLEAFMgEPTPENRAKFLATIPLGRLGTPEDIANAALFLASDEASWITGVTLVVDGG 247
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 56-302 1.12e-36

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 132.47  E-value: 1.12e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    56 SFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQTGnkvhAIQCDVRDPDMVQNTVSELIKVA 135
Cdd:PRK06841  12 DLSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGGNAK----GLVCDVSDSQSVEAAVAAVISAF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   136 GHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGaaflSITTIYAETGS----GFVVPSA 211
Cdd:PRK06841  88 GRIDILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGG----KIVNLASQAGVvaleRHVAYCA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   212 SaKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKT---KGAFSrldptGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDY 288
Cdd:PRK06841 164 S-KAGVVGMTKVLALEWGPYGITVNAISPTVVLTelgKKAWA-----GEKGERAKKLIPAGRFAYPEEIAAAALFLASDA 237

                        250
                 ....*....|....
gi 4503301   289 ASWINGAVIKFDGG 302
Cdd:PRK06841 238 AAMITGENLVIDGG 251
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
56-302 3.01e-36

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 131.40  E-value: 3.01e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    56 SFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKmDVLKATAEQISsQTGNKVHAIQCDVRDPDMVQNTVSELIKVA 135
Cdd:PRK06935  12 SLDGKVAIVTGGNTGLGQGYAVALAKAGADIIITTHG-TNWDETRRLIE-KEGRKVTFVQVDLTKPESAEKVVKEALEEF 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   136 GHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKaQKGAAFLSITTIYAETGSGFVVPSASAKA 215
Cdd:PRK06935  90 GKIDILVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAK-QGSGKIINIASMLSFQGGKFVPAYTASKH 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   216 GVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKG-AFSRLDPTGTfeKEMIGRIPCGRLGTVEELANLAAFLCSDYASWING 294
Cdd:PRK06935 169 GVAGLTKAFANELAAYNIQVNAIAPGYIKTANtAPIRADKNRN--DEILKRIPAGRWGEPDDLMGAAVFLASRASDYVNG 246


                 ....*...
gi 4503301   295 AVIKFDGG 302
Cdd:PRK06935 247 HILAVDGG 254
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 78-302 5.66e-36

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 130.35  E-value: 5.66e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    78 LLSSLGAQCVIASRK-MDVLKATAEQISSQtGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERL 156
Cdd:PRK05565  24 LLAKEGAKVVIAYDInEEAAQELLEEIKEE-GGDAIAVKADVSSEEDVENLVEQIVEKFGKIDILVNNAGISNFGLVTDM 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   157 SPNAWKTITDIVLNGTAFVTLEIGKQLIKaQKGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFN 236
Cdd:PRK05565 103 TDEEWDRVIDVNLTGVMLLTRYALPYMIK-RKSGVIVNISSIWGLIGASCEVLYSASKGAVNAFTKALAKELAPSGIRVN 181

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503301   237 VIQPGPIKTK-GAFSRLDptgtfEKEMIGR-IPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK05565 182 AVAPGAIDTEmWSSFSEE-----DKEGLAEeIPLGRLGKPEEIAKVVLFLASDDASYITGQIITVDGG 244
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 59-302 1.62e-35

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: 129.43  E-value: 1.62e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   59 GKVAFITGGGTGLGKGMTTLLSSLGAQCVIASR-KMDVLKATAEQISsQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGH 137
Cdd:cd05358   3 GKVALVTGASSGIGKAIAIRLATAGANVVVNYRsKEDAAEEVVEEIK-AVGGKAIAVQADVSKEEDVVALFQSAIKEFGT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  138 PNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSASAKAGV 217
Cdd:cd05358  82 LDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKIKGKIINMSSVHEKIPWPGHVNYAASKGGV 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  218 EAMSKSLAAEWGKYGMRFNVIQPGPIKTKgafSRLDPTGTFEKEM--IGRIPCGRLGTVEELANLAAFLCSDYASWINGA 295
Cdd:cd05358 162 KMMTKTLAQEYAPKGIRVNAIAPGAINTP---INAEAWDDPEQRAdlLSLIPMGRIGEPEEIAAAAAWLASDEASYVTGT 238


                ....*..
gi 4503301  296 VIKFDGG 302
Cdd:cd05358 239 TLFVDGG 245
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 55-306 6.30e-34

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 125.56  E-value: 6.30e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    55 NSFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISsqtGNKVHAIQCDVRDPDMVQNTVSELIKV 134
Cdd:PRK12829   7 KPLDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARLP---GAKVTATVADVADPAQVERVFDTAVER 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   135 AGHPNIVINNAaGNFiSPTER---LSPNAWKTITDIVLNGTaFVTLEIGKQLIKAQK-GAAFLSITTIYAETGSGFVVPS 210
Cdd:PRK12829  84 FGGLDVLVNNA-GIA-GPTGGideITPEQWEQTLAVNLNGQ-FYFARAAVPLLKASGhGGVIIALSSVAGRLGYPGRTPY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   211 ASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKG--------AFSRLDPTGTFEKEMIGRIPCGRLGTVEELANLAA 282
Cdd:PRK12829 161 AASKWAVVGLVKSLAIELGPLGIRVNAILPGIVRGPRmrrviearAQQLGIGLDEMEQEYLEKISLGRMVEPEDIAATAL 240

                        250       260
                 ....*....|....*....|....
gi 4503301   283 FLCSDYASWINGAVIKFDGGEEVL 306
Cdd:PRK12829 241 FLASPAARYITGQAISVDGNVEYL 264
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 100-302 1.07e-33

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: 124.37  E-value: 1.07e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  100 AEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEI 179
Cdd:cd05352  49 AEELAKKYGVKTKAYKCDVSSQESVEKTFKQIQKDFGKIDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAA 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  180 GKQLIKAQKGaaflSIttIYAETGSGFVV----PSAS---AKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTkgafsrl 252
Cdd:cd05352 129 AKIFKKQGKG----SL--IITASMSGTIVnrpqPQAAynaSKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDT------- 195

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 4503301  253 DPTGTFEKEMI----GRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:cd05352 196 DLTDFVDKELRkkweSYIPLKRIALPEELVGAYLYLASDASSYTTGSDLIIDGG 249
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 62-302 7.16e-33

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: 122.08  E-value: 7.16e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   62 AFITGGGTGLGKGMTTLLSSLGAQCVIASRK-MDVLKATAEQISSQtGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNI 140
Cdd:cd05359   1 ALVTGGSRGIGKAIALRLAERGADVVINYRKsKDAAAEVAAEIEEL-GGKAVVVRADVSQPQDVEEMFAAVKERFGRLDV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  141 VINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKqLIKAQKGAAFLSITTiyaeTGSGFVVPS----ASAKAG 216
Cdd:cd05359  80 LVSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAK-LMRERGGGRIVAISS----LGSIRALPNylavGTAKAA 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  217 VEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRLDPTGTfEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAV 296
Cdd:cd05359 155 LEALVRYLAVELGPRGIRVNAVSPGVIDTDALAHFPNREDL-LEAAAANTPAGRVGTPQDVADAVGFLCSDAARMITGQT 233


                ....*.
gi 4503301  297 IKFDGG 302
Cdd:cd05359 234 LVVDGG 239
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 53-302 1.86e-32

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 121.23  E-value: 1.86e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    53 PPNSFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQtGNKVHAIQCDVRDPDMVQNTVSELI 132
Cdd:PRK12939   1 MASNLAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAA-GGRAHAIAADLADPASVQRFFDAAA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   133 KVAGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLiKAQKGAAFLSITTIYAETGSGFVVPSAS 212
Cdd:PRK12939  80 AALGGLDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHL-RDSGRGRIVNLASDTALWGAPKLGAYVA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   213 AKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKgAFSRLdPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWI 292
Cdd:PRK12939 159 SKGAVIGMTRSLARELGGRGITVNAIAPGLTATE-ATAYV-PADERHAYYLKGRALERLQVPDDVAGAVLFLLSDAARFV 236

                        250
                 ....*....|
gi 4503301   293 NGAVIKFDGG 302
Cdd:PRK12939 237 TGQLLPVNGG 246
PRK07035 PRK07035
SDR family oxidoreductase;
59-302 5.07e-32

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 120.12  E-value: 5.07e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    59 GKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQtGNKVHAIQCDVRDPDMVQNTVSELIKVAGHP 138
Cdd:PRK07035   8 GKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIVAA-GGKAEALACHIGEMEQIDALFAHIRERHGRL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   139 NIVINNAAGN-FISPTERLSPNAWKTITDIVLNGTAFVTLEIGKqLIKAQKGAAFLSITTIYAETGSGFVVPSASAKAGV 217
Cdd:PRK07035  87 DILVNNAAANpYFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGK-LMKEQGGGSIVNVASVNGVSPGDFQGIYSITKAAV 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   218 EAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAfSRLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVI 297
Cdd:PRK07035 166 ISMTKAFAKECAPFGIRVNALLPGLTDTKFA-SALFKNDAILKQALAHIPLRRHAEPSEMAGAVLYLASDASSYTTGECL 244


                 ....*
gi 4503301   298 KFDGG 302
Cdd:PRK07035 245 NVDGG 249
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 56-302 1.40e-31

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: 119.48  E-value: 1.40e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   56 SFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISsQTGNKVHAIQCDVRDPDMVQNTVSELIKVA 135
Cdd:cd08935   2 SLKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEIT-ALGGRAIALAADVLDRASLERAREEIVAQF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  136 GHPNIVINNAAGNFISPT---ERLSPN-----------AWKTITDIVLNGTAFVTLEIGKQLIKaQKGAAFLSITTIYAE 201
Cdd:cd08935  81 GTVDILINGAGGNHPDATtdpEHYEPEteqnffdldeeGWEFVFDLNLNGSFLPSQVFGKDMLE-QKGGSIINISSMNAF 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  202 TGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRL-DPTGTFE---KEMIGRIPCGRLGTVEEL 277
Cdd:cd08935 160 SPLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQNRKLLiNPDGSYTdrsNKILGRTPMGRFGKPEEL 239

                       250       260
                ....*....|....*....|....*.
gi 4503301  278 ANLAAFLCSD-YASWINGAVIKFDGG 302
Cdd:cd08935 240 LGALLFLASEkASSFVTGVVIPVDGG 265
PRK06949 PRK06949
SDR family oxidoreductase;
57-302 2.07e-31

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 118.71  E-value: 2.07e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    57 FQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQTGNkVHAIQCDVRDPDMVQNTVSELIKVAG 136
Cdd:PRK06949   7 LEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIEAEGGA-AHVVSLDVTDYQSIKAAVAHAETEAG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   137 HPNIVINNAAgnfISPTERL---SPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGA--AFLSITTIYAETGSGF-VVPS 210
Cdd:PRK06949  86 TIDILVNNSG---VSTTQKLvdvTPADFDFVFDTNTRGAFFVAQEVAKRMIARAKGAgnTKPGGRIINIASVAGLrVLPQ 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   211 ----ASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRLDPTGTfeKEMIGRIPCGRLGTVEELANLAAFLCS 286
Cdd:PRK06949 163 iglyCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINHHHWETEQG--QKLVSMLPRKRVGKPEDLDGLLLLLAA 240

                        250
                 ....*....|....*.
gi 4503301   287 DYASWINGAVIKFDGG 302
Cdd:PRK06949 241 DESQFINGAIISADDG 256
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 79-303 2.66e-31

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 118.75  E-value: 2.66e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    79 LSSLGAQCVIASRKMDVLKATAEQISSQTG-NKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGN-FISPTERL 156
Cdd:PRK05875  27 LVAAGAAVMIVGRNPDKLAAAAEEIEALKGaGAVRYEPADVTDEDQVARAVDAATAWHGRLHGVVHCAGGSeTIGPITQI 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   157 SPNAWKTITDIVLNGTAFVTLEIGKQLIKAqKGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFN 236
Cdd:PRK05875 107 DSDAWRRTVDLNVNGTMYVLKHAARELVRG-GGGSFVGISSIAASNTHRWFGAYGVTKSAVDHLMKLAADELGPSWVRVN 185

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503301   237 VIQPGPIKTKGAFSRLDpTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGGE 303
Cdd:PRK05875 186 SIRPGLIRTDLVAPITE-SPELSADYRACTPLPRVGEVEDVANLAMFLLSDAASWITGQVINVDGGH 251
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 78-287 3.12e-31

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


Pssm-ID: 443365 [Multi-domain]  Cd Length: 240  Bit Score: 117.59  E-value: 3.12e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   78 LLSSLGAQCVIASRKMDVLKATAEQIssqtGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLS 157
Cdd:COG4221  24 ALAAAGARVVLAARRAERLEALAAEL----GGRALAVPLDVTDEAAVEAAVAAAVAEFGRLDVLVNNAGVALLGPLEELD 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  158 PNAWKTITDIVLNGTAFVTLEIGKQLiKAQKGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNV 237
Cdd:COG4221 100 PEDWDRMIDVNVKGVLYVTRAALPAM-RARGSGHIVNISSIAGLRPYPGGAVYAATKAAVRGLSESLRAELRPTGIRVTV 178

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 4503301  238 IQPGPIKTkgAFSRLDPTGTFEKEMIGRIPCGRLgTVEELANLAAFLCSD 287
Cdd:COG4221 179 IEPGAVDT--EFLDSVFDGDAEAAAAVYEGLEPL-TPEDVAEAVLFALTQ 225
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 79-302 1.64e-30

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: 116.01  E-value: 1.64e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   79 LSSLGAQCVIASRKMDVLKATAEQISSQtGNKVHAIQCDV---RDPDMVQNTVSEliKVAGHPNIVINNAAGNFISPTER 155
Cdd:cd05329  26 LAGLGAEVYTCARNQKELDECLTEWREK-GFKVEGSVCDVssrSERQELMDTVAS--HFGGKLNILVNNAGTNIRKEAKD 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  156 LSPNAWKTITDIVLNgTAFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRF 235
Cdd:cd05329 103 YTEEDYSLIMSTNFE-AAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGATKGALNQLTRSLACEWAKDNIRV 181

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503301  236 NVIQPGPIKTKGAFSRLDPTGTFEKeMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:cd05329 182 NAVAPWVIATPLVEPVIQQKENLDK-VIERTPLKRFGEPEEVAALVAFLCMPAASYITGQIIAVDGG 247
PRK06484 PRK06484
short chain dehydrogenase; Validated
 58-302 2.58e-30

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 120.34  E-value: 2.58e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    58 QGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMdvlkATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGH 137
Cdd:PRK06484   4 QSRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNV----ERARERADSLGPDHHALAMDVSDEAQIREGFEQLHREFGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   138 PNIVINNAA--GNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSASAKA 215
Cdd:PRK06484  80 IDVLVNNAGvtDPTMTATLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGHGAAIVNVASGAGLVALPKRTAYSASKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   216 GVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKgAFSRLDPTGTFEKEMI-GRIPCGRLGTVEELANLAAFLCSDYASWING 294
Cdd:PRK06484 160 AVISLTRSLACEWAAKGIRVNAVLPGYVRTQ-MVAELERAGKLDPSAVrSRIPLGRLGRPEEIAEAVFFLASDQASYITG 238


                 ....*...
gi 4503301   295 AVIKFDGG 302
Cdd:PRK06484 239 STLVVDGG 246
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 79-245 3.44e-30

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 113.48  E-value: 3.44e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301     79 LSSLGAQCVIASRKMDVLKATAEQISsQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSP 158
Cdd:pfam00106  20 LAKEGAKVVLVDRSEEKLEAVAKELG-ALGGKALFIQGDVTDRAQVKALVEQAVERLGRLDILVNNAGITGLGPFSELSD 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    159 NAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAfLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVI 238
Cdd:pfam00106  99 EDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRI-VNISSVAGLVPYPGGSAYSASKAAVIGFTRSLALELAPHGIRVNAV 177


                  ....*..
gi 4503301    239 QPGPIKT 245
Cdd:pfam00106 178 APGGVDT 184
kduD TIGR01832
2-deoxy-D-gluconate 3-dehydrogenase; This model describes 2-deoxy-D-gluconate 3-dehydrogenase ...
 56-302 3.89e-30

2-deoxy-D-gluconate 3-dehydrogenase; This model describes 2-deoxy-D-gluconate 3-dehydrogenase (also called 2-keto-3-deoxygluconate oxidoreductase), a member of the family of short-chain-alcohol dehydrogenases (pfam00106). This protein has been characterized in Erwinia chrysanthemi as an enzyme of pectin degradation. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 188170 [Multi-domain]  Cd Length: 248  Bit Score: 114.86  E-value: 3.89e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301     56 SFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKmdVLKATAEQISsQTGNKVHAIQCDVRDPDMVQNTVSELIKVA 135
Cdd:TIGR01832   2 SLEGKVALVTGANTGLGQGIAVGLAEAGADIVGAGRS--EPSETQQQVE-ALGRRFLSLTADLSDIEAIKALVDSAVEEF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    136 GHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFLSITTIYAETGsGFVVPSASA-K 214
Cdd:TIGR01832  79 GHIDILVNNAGIIRRADAEEFSEKDWDDVMNVNLKSVFFLTQAAAKHFLKQGRGGKIINIASMLSFQG-GIRVPSYTAsK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    215 AGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKG-AFSRLDPTGTfeKEMIGRIPCGRLGTVEELANLAAFLCSDYASWIN 293
Cdd:TIGR01832 158 HAVAGLTKLLANEWAAKGINVNAIAPGYMATNNtQALRADEDRN--AAILERIPAGRWGTPDDIGGPAVFLASSASDYVN 235


                  ....*....
gi 4503301    294 GAVIKFDGG 302
Cdd:TIGR01832 236 GYTLAVDGG 244
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 56-302 5.15e-30

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 114.82  E-value: 5.15e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    56 SFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVI----ASRKMDVLKATAEQISSQtGNKVHAIQCDVRDPDMVQNTVSEL 131
Cdd:PRK12827   3 SLDSRRVLITGGSGGLGRAIAVRLAADGADVIVldihPMRGRAEADAVAAGIEAA-GGKALGLAFDVRDFAATRAALDAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   132 IKVAGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSA 211
Cdd:PRK12827  82 VEEFGRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRARRGGRIVNIASVAGVRGNRGQVNYA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   212 SAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAfSRLDPTGTFEKEMigriPCGRLGTVEELANLAAFLCSDYASW 291
Cdd:PRK12827 162 ASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPMA-DNAAPTEHLLNPV----PVQRLGEPDEVAALVAFLVSDAASY 236

                        250
                 ....*....|.
gi 4503301   292 INGAVIKFDGG 302
Cdd:PRK12827 237 VTGQVIPVDGG 247
PRK07774 PRK07774
SDR family oxidoreductase;
57-303 7.37e-30

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 114.46  E-value: 7.37e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    57 FQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQTGNKVHaIQCDVRDPD----MVQNTVSELi 132
Cdd:PRK07774   4 FDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGGTAIA-VQVDVSDPDsakaMADATVSAF- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   133 kvaGHPNIVINNAA---GNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKaQKGAAFLSITTIYAETGSGFVvp 209
Cdd:PRK07774  82 ---GGIDYLVNNAAiygGMKLDLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAK-RGGGAIVNQSSTAAWLYSNFY-- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   210 sASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKgAFSRLDPtGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYA 289
Cdd:PRK07774 156 -GLAKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTE-ATRTVTP-KEFVADMVKGIPLSRMGTPEDLVGMCLFLLSDEA 232

                        250
                 ....*....|....
gi 4503301   290 SWINGAVIKFDGGE 303
Cdd:PRK07774 233 SWITGQIFNVDGGQ 246
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 58-302 2.68e-29

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: 112.75  E-value: 2.68e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   58 QGKVAFITGGGTGLGKGMTTLLSSLGAQCVI--ASRKmDVLKATAEQISSQtGNKVHAIQCDVRDPDMVQNTVSELIKVA 135
Cdd:cd05362   2 AGKVALVTGASRGIGRAIAKRLARDGASVVVnyASSK-AAAEEVVAEIEAA-GGKAIAVQADVSDPSQVARLFDAAEKAF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  136 GHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLikaQKGAAFLSITTIYAETGSGFVVPSASAKA 215
Cdd:cd05362  80 GGVDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRL---RDGGRIINISSSLTAAYTPNYGAYAGSKA 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  216 GVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRLDPTGT-FEKEMIgriPCGRLGTVEELANLAAFLCSDYASWING 294
Cdd:cd05362 157 AVEAFTRVLAKELGGRGITVNAVAPGPVDTDMFYAGKTEEAVeGYAKMS---PLGRLGEPEDIAPVVAFLASPDGRWVNG 233


                ....*...
gi 4503301  295 AVIKFDGG 302
Cdd:cd05362 234 QVIRANGG 241
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 58-302 5.11e-29

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 112.29  E-value: 5.11e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    58 QGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQtGNKVHAIQCDVRDPDMVQNTVSELIKVAGH 137
Cdd:PRK12429   3 KGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALQKA-GGKAIGVAMDVTDEEAINAGIDYAVETFGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   138 PNIVINNAAGNFISPTERLSPNAWKTITDIVLNGtAFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSASAKAGV 217
Cdd:PRK12429  82 VDILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDG-AFLTTKAALPIMKAQGGGRIINMASVHGLVGSAGKAAYVSAKHGL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   218 EAMSKSLAAEWGKYGMRFNVIQPGPIKT---------KGAFSRLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDY 288
Cdd:PRK12429 161 IGLTKVVALEGATHGVTVNAICPGYVDTplvrkqipdLAKERGISEEEVLEDVLLPLVPQKRFTTVEEIADYALFLASFA 240

                        250
                 ....*....|....
gi 4503301   289 ASWINGAVIKFDGG 302
Cdd:PRK12429 241 AKGVTGQAWVVDGG 254
PRK06484 PRK06484
short chain dehydrogenase; Validated
 78-302 8.19e-29

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 116.10  E-value: 8.19e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    78 LLSSLGAQCVIASRKMDVLKATAEQIssqtGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFI-SPTERL 156
Cdd:PRK06484 288 RFAAAGDRLLIIDRDAEGAKKLAEAL----GDEHLSVQADITDEAAVESAFAQIQARWGRLDVLVNNAGIAEVfKPSLEQ 363

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   157 SPNAWKTITDIVLNGTAFVTLEIGKQLikaQKGAAFLSITTIyaeTGSGFVVPS---ASAKAGVEAMSKSLAAEWGKYGM 233
Cdd:PRK06484 364 SAEDFTRVYDVNLSGAFACARAAARLM---SQGGVIVNLGSI---ASLLALPPRnayCASKAAVTMLSRSLACEWAPAGI 437

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   234 RFNVIQPGPIKTKGAfSRLDPTGTFEKEMI-GRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK06484 438 RVNTVAPGYIETPAV-LALKASGRADFDSIrRRIPLGRLGDPEEVAEAIAFLASPAASYVNGATLTVDGG 506
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 58-302 1.87e-28

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: 110.50  E-value: 1.87e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   58 QGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGH 137
Cdd:cd08930   1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKNRVIALELDITSKESIKELIESYLEKFGR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  138 PNIVINNAAGNF---ISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKaQKGAAFLSITTIYAETGSGF-------- 206
Cdd:cd08930  81 IDILINNAYPSPkvwGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKK-QGKGSIINIASIYGVIAPDFriyentqm 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  207 ---VVPSAsAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSrldptgtFEKEMIGRIPCGRLGTVEELANLAAF 283
Cdd:cd08930 160 yspVEYSV-IKAGIIHLTKYLAKYYADTGIRVNAISPGGILNNQPSE-------FLEKYTKKCPLKRMLNPEDLRGAIIF 231

                       250
                ....*....|....*....
gi 4503301  284 LCSDYASWINGAVIKFDGG 302
Cdd:cd08930 232 LLSDASSYVTGQNLVIDGG 250
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 51-302 1.89e-28

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 111.15  E-value: 1.89e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    51 MLPPN-SFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQtGNKVHAIQCDVRDPDMVQNTVS 129
Cdd:PRK08277   1 MMPNLfSLKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAA-GGEALAVKADVLDKESLEQARQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   130 ELIKVAGHPNIVINNAAGN------------FISPTER---LSPNAWKTITDIVLNGTAFVTLEIGKQLIKaQKGAAFLS 194
Cdd:PRK08277  80 QILEDFGPCDILINGAGGNhpkattdnefheLIEPTKTffdLDEEGFEFVFDLNLLGTLLPTQVFAKDMVG-RKGGNIIN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   195 ITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRL-DPTGTFE---KEMIGRIPCGR 270
Cdd:PRK08277 159 ISSMNAFTPLTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTEQNRALLfNEDGSLTeraNKILAHTPMGR 238

                        250       260       270
                 ....*....|....*....|....*....|...
gi 4503301   271 LGTVEELANLAAFLCSD-YASWINGAVIKFDGG 302
Cdd:PRK08277 239 FGKPEELLGTLLWLADEkASSFVTGVVLPVDGG 271
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
78-245 3.63e-28

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 109.57  E-value: 3.63e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   78 LLSSLGAQCVIASRKMDVLKATAEQISSQtGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLS 157
Cdd:COG0300  24 ALAARGARVVLVARDAERLEALAAELRAA-GARVEVVALDVTDPDAVAALAEAVLARFGPIDVLVNNAGVGGGGPFEELD 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  158 PNAWKTITDIVLNGTAFVTLEIGKQLiKAQKGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNV 237
Cdd:COG0300 103 LEDLRRVFEVNVFGPVRLTRALLPLM-RARGRGRIVNVSSVAGLRGLPGMAAYAASKAALEGFSESLRAELAPTGVRVTA 181


                ....*...
gi 4503301  238 IQPGPIKT 245
Cdd:COG0300 182 VCPGPVDT 189
PRK07063 PRK07063
SDR family oxidoreductase;
54-306 6.01e-28

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 109.37  E-value: 6.01e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    54 PNSFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQI-SSQTGNKVHAIQCDVRDPDMVQNTVSELI 132
Cdd:PRK07063   2 MNRLAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIaRDVAGARVLAVPADVTDAASVAAAVAAAE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   133 KVAGHPNIVINNAAGN-FISPTErLSPNAWKTITDIVLNGTAFVTLEIGKQLIkAQKGAAFLSITTIYAETGSGFVVPSA 211
Cdd:PRK07063  82 EAFGPLDVLVNNAGINvFADPLA-MTDEDWRRCFAVDLDGAWNGCRAVLPGMV-ERGRGSIVNIASTHAFKIIPGCFPYP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   212 SAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAF----SRLDPTGTfEKEMIGRIPCGRLGTVEELANLAAFLCSD 287
Cdd:PRK07063 160 VAKHGLLGLTRALGIEYAARNVRVNAIAPGYIETQLTEdwwnAQPDPAAA-RAETLALQPMKRIGRPEEVAMTAVFLASD 238

                        250
                 ....*....|....*....
gi 4503301   288 YASWINGAVIKFDGGEEVL 306
Cdd:PRK07063 239 EAPFINATCITIDGGRSVL 257
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 97-302 1.51e-27

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: 107.93  E-value: 1.51e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   97 KATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFispteRLSPNAWKTITDIV-------L 169
Cdd:cd05349  35 TESAEAVAAEAGERAIAIQADVRDRDQVQAMIEEAKNHFGPVDTIVNNALIDF-----PFDPDQRKTFDTIDwedyqqqL 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  170 NGT---AFVTLEIGKQLIKAQKGAAFLSITTIYAETGsgfVVP---SASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPI 243
Cdd:cd05349 110 EGAvkgALNLLQAVLPDFKERGSGRVINIGTNLFQNP---VVPyhdYTTAKAALLGFTRNMAKELGPYGITVNMVSGGLL 186

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4503301  244 KTKGAfSRLDPTGTFEKeMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:cd05349 187 KVTDA-SAATPKEVFDA-IAQTTPLGKVTTPQDIADAVLFFASPWARAVTGQNLVVDGG 243
PRK09242 PRK09242
SDR family oxidoreductase;
79-302 1.97e-27

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 107.91  E-value: 1.97e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    79 LSSLGAQCVIASRKMDVLKATAEQISSQ-TGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLS 157
Cdd:PRK09242  29 FLGLGADVLIVARDADALAQARDELAEEfPEREVHGLAADVSDDEDRRAILDWVEDHWDGLHILVNNAGGNIRKAAIDYT 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   158 PNAWKTITDIVLngtaFVTLEIGKQ---LIKAQKGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMR 234
Cdd:PRK09242 109 EDEWRGIFETNL----FSAFELSRYahpLLKQHASSAIVNIGSVSGLTHVRSGAPYGMTKAALLQMTRNLAVEWAEDGIR 184

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503301   235 FNVIQPGPIKTKGAFSRLDPTGTFEkEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK09242 185 VNAVAPWYIRTPLTSGPLSDPDYYE-QVIERTPMRRVGEPEEVAAAVAFLCMPAASYITGQCIAVDGG 251
PRK05867 PRK05867
SDR family oxidoreductase;
51-302 2.21e-27

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 107.81  E-value: 2.21e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    51 MLPPNSFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSqTGNKVHAIQCDVRDPDMVQNTVSE 130
Cdd:PRK05867   1 VLDLFDLHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIGT-SGGKVVPVCCDVSQHQQVTSMLDQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   131 LIKVAGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAflsITTIYAETGSGFVVPS 210
Cdd:PRK05867  80 VTAELGGIDIAVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQGQGGV---IINTASMSGHIINVPQ 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   211 -----ASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKgafsRLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLC 285
Cdd:PRK05867 157 qvshyCASKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTE----LVEPYTEYQPLWEPKIPLGRLGRPEELAGLYLYLA 232

                        250
                 ....*....|....*..
gi 4503301   286 SDYASWINGAVIKFDGG 302
Cdd:PRK05867 233 SEASSYMTGSDIVIDGG 249
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 79-302 3.99e-27

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: 106.88  E-value: 3.99e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   79 LSSLGAQCVIASRKMDVLKATAEQISsQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNfiSPTERLSP 158
Cdd:cd05365  19 LAKAGASVVIADLKSEGAEAVAAAIQ-QAGGQAIGLECNVTSEQDLEAVVKATVSQFGGITILVNNAGGG--GPKPFDMP 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  159 nawKTITDIV----LNGTAFVTLE--IGKQLIKAQkGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYG 232
Cdd:cd05365  96 ---MTEEDFEwafkLNLFSAFRLSqlCAPHMQKAG-GGAILNISSMSSENKNVRIAAYGSSKAAVNHMTRNLAFDLGPKG 171

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  233 MRFNVIQPGPIKTKGAFSRLDPTgtFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:cd05365 172 IRVNAVAPGAVKTDALASVLTPE--IERAMLKHTPLGRLGEPEDIANAALFLCSPASAWVSGQVLTVSGG 239
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 51-302 5.42e-27

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 106.85  E-value: 5.42e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    51 MLPPNSFQ--GKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQtGNKVHAIQCDVRDPDMVQNTV 128
Cdd:PRK06113   1 MFNSDNLRldGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQL-GGQAFACRCDITSEQELSALA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   129 SELIKVAGHPNIVINNAAGNFISPTER-LSPNAWKtitdIVLNGTAFVTL-EIGKQLIKAQKGAAFLSITTIYAETGSGF 206
Cdd:PRK06113  80 DFALSKLGKVDILVNNAGGGGPKPFDMpMADFRRA----YELNVFSFFHLsQLVAPEMEKNGGGVILTITSMAAENKNIN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   207 VVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRLDPTgtFEKEMIGRIPCGRLGTVEELANLAAFLCS 286
Cdd:PRK06113 156 MTSYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTDALKSVITPE--IEQKMLQHTPIRRLGQPQDIANAALFLCS 233

                        250
                 ....*....|....*.
gi 4503301   287 DYASWINGAVIKFDGG 302
Cdd:PRK06113 234 PAASWVSGQILTVSGG 249
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 57-303 7.57e-27

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: 106.45  E-value: 7.57e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   57 FQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQTGN-KVHAIQCDVRDPDMVQNTVSELIKVA 135
Cdd:cd05330   1 FKDKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEIAPDaEVLLIKADVSDEAQVEAYVDATVEQF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  136 GHPNIVINNAA--GNfISPTERLSPNAWKTITDIVLNGTaFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSASA 213
Cdd:cd05330  81 GRIDGFFNNAGieGK-QNLTEDFGADEFDKVVSINLRGV-FYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQSGYAAA 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  214 KAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKT---KGAFSRLDPTG--TFEKEMIGRIPCGRLGTVEELANLAAFLCSDY 288
Cdd:cd05330 159 KHGVVGLTRNSAVEYGQYGIRINAIAPGAILTpmvEGSLKQLGPENpeEAGEEFVSVNPMKRFGEPEEVAAVVAFLLSDD 238

                       250
                ....*....|....*
gi 4503301  289 ASWINGAVIKFDGGE 303
Cdd:cd05330 239 AGYVNAAVVPIDGGQ 253
PRK12743 PRK12743
SDR family oxidoreductase;
97-302 1.87e-26

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 105.12  E-value: 1.87e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    97 KATAEQISsQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGtAFVT 176
Cdd:PRK12743  41 KETAEEVR-SHGVRAEIRQLDLSDLPEGAQALDKLIQRLGRIDVLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDG-AFLC 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   177 LEIG-KQLIKAQKGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTkgAFSRLDPT 255
Cdd:PRK12743 119 SQIAaRHMVKQGQGGRIINITSVHEHTPLPGASAYTAAKHALGGLTKAMALELVEHGILVNAVAPGAIAT--PMNGMDDS 196

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 4503301   256 GTFEKEMIGrIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK12743 197 DVKPDSRPG-IPLGRPGDTHEIASLVAWLCSEGASYTTGQSLIVDGG 242
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 79-302 2.54e-26

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 104.85  E-value: 2.54e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    79 LSSLGAQCVIASRKMDVLKATAEQISSQtGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSP 158
Cdd:PRK07523  30 LAQAGAEVILNGRDPAKLAAAAESLKGQ-GLSAHALAFDVTDHDAVRAAIDAFEAEIGPIDILVNNAGMQFRTPLEDFPA 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   159 NAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAaFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVI 238
Cdd:PRK07523 109 DAFERLLRTNISSVFYVGQAVARHMIARGAGK-IINIASVQSALARPGIAPYTATKGAVGNLTKGMATDWAKHGLQCNAI 187

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503301   239 QPGPIKTK-GAFSRLDP--TGTFEKemigRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK07523 188 APGYFDTPlNAALVADPefSAWLEK----RTPAGRWGKVEELVGACVFLASDASSFVNGHVLYVDGG 250
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 56-302 6.30e-26

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 103.99  E-value: 6.30e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    56 SFQGKVAFITGGGTGLGKGMTTLLSSLGAQCV---IASRKMD-VLKATAEQissqtGNKVHAIQCDVRDPDMVQNTVSEL 131
Cdd:PRK07097   7 SLKGKIALITGASYGIGFAIAKAYAKAGATIVfndINQELVDkGLAAYREL-----GIEAHGYVCDVTDEDGVQAMVSQI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   132 IKVAGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAaFLSITTIYAETGSGFVVPSA 211
Cdd:PRK07097  82 EKEVGVIDILVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGK-IINICSMMSELGRETVSAYA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   212 SAKAGVEAMSKSLAAEWGKYGMRFNVIQPG--------PIKTKGAFSRLDPtgtFEKEMIGRIPCGRLGTVEELANLAAF 283
Cdd:PRK07097 161 AAKGGLKMLTKNIASEYGEANIQCNGIGPGyiatpqtaPLRELQADGSRHP---FDQFIIAKTPAARWGDPEDLAGPAVF 237

                        250
                 ....*....|....*....
gi 4503301   284 LCSDYASWINGAVIKFDGG 302
Cdd:PRK07097 238 LASDASNFVNGHILYVDGG 256
PRK06172 PRK06172
SDR family oxidoreductase;
57-302 1.66e-25

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 102.52  E-value: 1.66e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    57 FQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISsQTGNKVHAIQCDVRDPDMVQNTVSELIKVAG 136
Cdd:PRK06172   5 FSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALIR-EAGGEALFVACDVTRDAEVKALVEQTIAAYG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   137 HPNIVINNAA-GNFISPTERLSPNAWKTITDIVLNGTaFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSASAKA 215
Cdd:PRK06172  84 RLDYAFNNAGiEIEQGRLAEGSEAEFDAIMGVNVKGV-WLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPKMSIYAASKH 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   216 GVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKgAFSRLDPTGTFEKEMI-GRIPCGRLGTVEELANLAAFLCSDYASWING 294
Cdd:PRK06172 163 AVIGLTKSAAIEYAKKGIRVNAVCPAVIDTD-MFRRAYEADPRKAEFAaAMHPVGRIGKVEEVASAVLYLCSDGASFTTG 241


                 ....*...
gi 4503301   295 AVIKFDGG 302
Cdd:PRK06172 242 HALMVDGG 249
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 55-302 1.86e-25

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: 102.46  E-value: 1.86e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   55 NSFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIAsrkmDVLKATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKV 134
Cdd:cd05341   1 NRLKGKVAIVTGGARGLGLAHARLLVAEGAKVVLS----DILDEEGQAAAAELGDAARFFHLDVTDEDGWTAVVDTAREA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  135 AGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTaFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSASAK 214
Cdd:cd05341  77 FGRLDVLVNNAGILTGGTVETTTLEEWRRLLDINLTGV-FLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALAAYNASK 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  215 AGVEAMSKSLAAEWGK--YGMRFNVIQPGPIKTKGAFSRLDPTGtfEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWI 292
Cdd:cd05341 156 GAVRGLTKSAALECATqgYGIRVNSVHPGYIYTPMTDELLIAQG--EMGNYPNTPMGRAGEPDEIAYAVVYLASDESSFV 233

                       250
                ....*....|
gi 4503301  293 NGAVIKFDGG 302
Cdd:cd05341 234 TGSELVVDGG 243
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 57-302 2.42e-25

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: 102.18  E-value: 2.42e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   57 FQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSqtgnkvHAIQC--DVRDPDMVQNTVSELIKV 134
Cdd:cd08944   1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAG------GALALrvDVTDEQQVAALFERAVEE 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  135 AGHPNIVINNAAGNFISPT-ERLSPNAWKTITDIVLNGTaFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSASA 213
Cdd:cd08944  75 FGGLDLLVNNAGAMHLTPAiIDTDLAVWDQTMAINLRGT-FLCCRHAAPRMIARGGGSIVNLSSIAGQSGDPGYGAYGAS 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  214 KAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKT-------KGAFSRLDPTGtfEKEMIGRIPcGRLGTVEELANLAAFLCS 286
Cdd:cd08944 154 KAAIRNLTRTLAAELRHAGIRCNALAPGLIDTplllaklAGFEGALGPGG--FHLLIHQLQ-GRLGRPEDVAAAVVFLLS 230

                       250
                ....*....|....*.
gi 4503301  287 DYASWINGAVIKFDGG 302
Cdd:cd08944 231 DDASFITGQVLCVDGG 246
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 55-302 3.59e-25

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 101.90  E-value: 3.59e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    55 NSFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISsQTGNKVHAIQCDVRDPDMVQNTVSELIKV 134
Cdd:PRK13394   3 SNLNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEIN-KAGGKAIGVAMDVTNEDAVNAGIDKVAER 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   135 AGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSASAK 214
Cdd:PRK13394  82 FGSVDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   215 AGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRLDPT----GTFEKE-----MIGRIPCGRLGTVEELANLAAFLC 285
Cdd:PRK13394 162 HGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDKQIPEQakelGISEEEvvkkvMLGKTVDGVFTTVEDVAQTVLFLS 241

                        250
                 ....*....|....*..
gi 4503301   286 SDYASWINGAVIKFDGG 302
Cdd:PRK13394 242 SFPSAALTGQSFVVSHG 258
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
59-302 4.91e-25

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 101.80  E-value: 4.91e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    59 GKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKaTAEQISSQtGNKVHAIQCDVRDPDMVQNTVSELIKVAGHP 138
Cdd:PRK08226   6 GKTALITGALQGIGEGIARVFARHGANLILLDISPEIEK-LADELCGR-GHRCTAVVADVRDPASVAAAIKRAKEKEGRI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   139 NIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFL--SIT-TIYAETGSgfvVPSASAKA 215
Cdd:PRK08226  84 DILVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMmsSVTgDMVADPGE---TAYALTKA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   216 GVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGA-----FSRLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYAS 290
Cdd:PRK08226 161 AIVGLTKSLAVEYAQSGIRVNAICPGYVRTPMAesiarQSNPEDPESVLTEMAKAIPLRRLADPLEVGELAAFLASDESS 240

                        250
                 ....*....|..
gi 4503301   291 WINGAVIKFDGG 302
Cdd:PRK08226 241 YLTGTQNVIDGG 252
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 55-302 5.96e-25

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: 100.93  E-value: 5.96e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   55 NSFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIAsrkmDVLKATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKV 134
Cdd:cd05345   1 MRLEGKVAIVTGAGSGFGEGIARRFAQEGARVVIA----DINADGAERVAADIGEAAIAIQADVTKRADVEAMVEAALSK 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  135 AGHPNIVINNAA-GNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLiKAQKGAAFLSIttiyAETGS-----GFVV 208
Cdd:cd05345  77 FGRLDILVNNAGiTHRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHM-EEQGGGVIINI----ASTAGlrprpGLTW 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  209 PSASaKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRLDP-TGTFEKEMIGRIPCGRLGTVEELANLAAFLCSD 287
Cdd:cd05345 152 YNAS-KGWVVTATKAMAVELAPRNIRVNCLCPVAGETPLLSMFMGEdTPENRAKFRATIPLGRLSTPDDIANAALYLASD 230

                       250
                ....*....|....*
gi 4503301  288 YASWINGAVIKFDGG 302
Cdd:cd05345 231 EASFITGVALEVDGG 245
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
57-307 1.15e-24

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 100.18  E-value: 1.15e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    57 FQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIA-SRKMDVLKATAEQISsQTGNKVHAIQCDVRDPDMVQNTVSELIKVA 135
Cdd:PRK08063   2 FSGKVALVTGSSRGIGKAIALRLAEEGYDIAVNyARSRKAAEETAEEIE-ALGRKALAVKANVGDVEKIKEMFAQIDEEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   136 GHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKaQKGAAFLSITTIyaetGSGFVVPSASA-- 213
Cdd:PRK08063  81 GRLDVFVNNAASGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEK-VGGGKIISLSSL----GSIRYLENYTTvg 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   214 --KAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTkgafsrlDPTGTFE------KEMIGRIPCGRLGTVEELANLAAFLC 285
Cdd:PRK08063 156 vsKAALEALTRYLAVELAPKGIAVNAVSGGAVDT-------DALKHFPnreellEDARAKTPAGRMVEPEDVANAVLFLC 228

                        250       260
                 ....*....|....*....|..
gi 4503301   286 SDYASWINGAVIKFDGGEEVLI 307
Cdd:PRK08063 229 SPEADMIRGQTIIVDGGRSLLV 250
PRK07856 PRK07856
SDR family oxidoreductase;
83-304 1.21e-24

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 100.39  E-value: 1.21e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    83 GAQCVIASRKmdvlkataeQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAWK 162
Cdd:PRK07856  30 GATVVVCGRR---------APETVDGRPAEFHAADVRDPDQVAALVDAIVERHGRLDVLVNNAGGSPYALAAEASPRFHE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   163 TITDIVLNGTAFVTLEIGKQLIKAQKGAAFLSITTIYAETGS-GFVVPSAsAKAGVEAMSKSLAAEWGKyGMRFNVIQPG 241
Cdd:PRK07856 101 KIVELNLLAPLLVAQAANAVMQQQPGGGSIVNIGSVSGRRPSpGTAAYGA-AKAGLLNLTRSLAVEWAP-KVRVNAVVVG 178

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4503301   242 PIKTKGAFSRL-DPTGTfekEMIGR-IPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGGEE 304
Cdd:PRK07856 179 LVRTEQSELHYgDAEGI---AAVAAtVPLGRLATPADIAWACLFLASDLASYVSGANLEVHGGGE 240
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 56-302 2.03e-24

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 99.40  E-value: 2.03e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    56 SFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSqtgnkvHAIQCDVRDPDMVQNTVSElikvA 135
Cdd:PRK07060   6 DFSGKSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGC------EPLRLDVGDDAAIRAALAA----A 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   136 GHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSASAKA 215
Cdd:PRK07060  76 GAFDGLVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAAGRGGSIVNVSSQAALVGLPDHLAYCASKA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   216 GVEAMSKSLAAEWGKYGMRFNVIQPGPIKTK-GAFSRLDPTGTfeKEMIGRIPCGRLGTVEELANLAAFLCSDYASWING 294
Cdd:PRK07060 156 ALDAITRVLCVELGPHGIRVNSVNPTVTLTPmAAEAWSDPQKS--GPMLAAIPLGRFAEVDDVAAPILFLLSDAASMVSG 233


                 ....*...
gi 4503301   295 AVIKFDGG 302
Cdd:PRK07060 234 VSLPVDGG 241
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
99-302 3.83e-24

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 98.82  E-value: 3.83e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    99 TAEQISSqTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLE 178
Cdd:PRK12481  46 TQAQVEA-LGRKFHFITADLIQQKDIDSIVSQAVEVMGHIDILINNAGIIRRQDLLEFGNKDWDDVININQKTVFFLSQA 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   179 IGKQLIKAQKGAAFLSITTIYAETGsGFVVPSASA-KAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAfSRLDPTGT 257
Cdd:PRK12481 125 VAKQFVKQGNGGKIINIASMLSFQG-GIRVPSYTAsKSAVMGLTRALATELSQYNINVNAIAPGYMATDNT-AALRADTA 202

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 4503301   258 FEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK12481 203 RNEAILERIPASRWGTPDDLAGPAIFLSSSASDYVTGYTLAVDGG 247
PRK06124 PRK06124
SDR family oxidoreductase;
50-302 8.21e-24

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 98.25  E-value: 8.21e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    50 AMLPPNSFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISsQTGNKVHAIQCDVRDPDMVQNTVS 129
Cdd:PRK06124   2 SILQRFSLAGQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALR-AAGGAAEALAFDIADEEAVAAAFA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   130 ELIKVAGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLngTAFVTL-EIGKQLIKAQKGAAFLSITTIYAE-TGSGFV 207
Cdd:PRK06124  81 RIDAEHGRLDILVNNVGARDRRPLAELDDAAIRALLETDL--VAPILLsRLAAQRMKRQGYGRIIAITSIAGQvARAGDA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   208 VPSAsAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTK-GAFSRLDPTgtFEKEMIGRIPCGRLGTVEELANLAAFLCS 286
Cdd:PRK06124 159 VYPA-AKQGLTGLMRALAAEFGPHGITSNAIAPGYFATEtNAAMAADPA--VGPWLAQRTPLGRWGRPEEIAGAAVFLAS 235

                        250
                 ....*....|....*.
gi 4503301   287 DYASWINGAVIKFDGG 302
Cdd:PRK06124 236 PAASYVNGHVLAVDGG 251
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 83-302 8.56e-24

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: 97.94  E-value: 8.56e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   83 GAQCVIASRKMDVLKATAEQISsqTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAWK 162
Cdd:cd08942  30 GARVIISARKAEACADAAEELS--AYGECIAIPADLSSEEGIEALVARVAERSDRLDVLVNNAGATWGAPLEAFPESGWD 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  163 TITDIVLNGTAFVTLEIGKQLIK---AQKGAAFLSITTIYAETGSGFVVPSASA-KAGVEAMSKSLAAEWGKYGMRFNVI 238
Cdd:cd08942 108 KVMDINVKSVFFLTQALLPLLRAaatAENPARVINIGSIAGIVVSGLENYSYGAsKAAVHQLTRKLAKELAGEHITVNAI 187

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503301  239 QPGPIKTKGAFSRLDPTGTFEKEMiGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:cd08942 188 APGRFPSKMTAFLLNDPAALEAEE-KSIPLGRWGRPEDMAGLAIMLASRAGAYLTGAVIPVDGG 250
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
56-302 1.80e-23

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 97.25  E-value: 1.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    56 SFQGKVAFITGGGTGLGKGMTTLLSSLGaqCVIASRKMDVLKATAEQISsQTGNKVHAIQCDVRDPDMVQNTVSELIKVA 135
Cdd:PRK08993   7 SLEGKVAVVTGCDTGLGQGMALGLAEAG--CDIVGINIVEPTETIEQVT-ALGRRFLSLTADLRKIDGIPALLERAVAEF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   136 GHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFLSITTIYAETGsGFVVPSASA-K 214
Cdd:PRK08993  84 GHIDILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQGNGGKIINIASMLSFQG-GIRVPSYTAsK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   215 AGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAfSRLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWING 294
Cdd:PRK08993 163 SGVMGVTRLMANEWAKHNINVNAIAPGYMATNNT-QQLRADEQRSAEILDRIPAGRWGLPSDLMGPVVFLASSASDYING 241


                 ....*...
gi 4503301   295 AVIKFDGG 302
Cdd:PRK08993 242 YTIAVDGG 249
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
107-302 2.29e-23

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 96.76  E-value: 2.29e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   107 TGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQlIKA 186
Cdd:PRK12824  50 TEDQVRLKELDVTDTEECAEALAEIEEEEGPVDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAA-MCE 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   187 QKGAAFLSITTIYAETGSgFVVPSASA-KAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAfsrldptGTFEKEMIGR 265
Cdd:PRK12824 129 QGYGRIINISSVNGLKGQ-FGQTNYSAaKAGMIGFTKALASEGARYGITVNCIAPGYIATPMV-------EQMGPEVLQS 200

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 4503301   266 ----IPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK12824 201 ivnqIPMKRLGTPEEIAAAVAFLVSEAAGFITGETISINGG 241
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 79-302 3.16e-23

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 96.57  E-value: 3.16e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    79 LSSLGAQCVIASRKMDVLKATAEQISSQtGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAA----GNFISP-- 152
Cdd:PRK08217  25 LAQKGAKLALIDLNQEKLEEAVAECGAL-GTEVRGYAANVTDEEDVEATFAQIAEDFGQLNGLINNAGilrdGLLVKAkd 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   153 ---TERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFLSITTIyAETGSGFVVPSASAKAGVEAMSKSLAAEWG 229
Cdd:PRK08217 104 gkvTSKMSLEQFQSVIDVNLTGVFLCGREAAAKMIESGSKGVIINISSI-ARAGNMGQTNYSASKAGVAAMTVTWAKELA 182

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503301   230 KYGMRFNVIQPGPIKTkgafsrlDPTGTFEKEMIGR----IPCGRLGTVEELANLAAF-LCSDYaswINGAVIKFDGG 302
Cdd:PRK08217 183 RYGIRVAAIAPGVIET-------EMTAAMKPEALERlekmIPVGRLGEPEEIAHTVRFiIENDY---VTGRVLEIDGG 250
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 58-302 3.18e-23

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: 96.37  E-value: 3.18e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   58 QGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQTGNKVHaiqCDVRDPDMVQNTVSELIKVAGH 137
Cdd:cd05326   3 DGKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGDPDISFVH---CDVTVEADVRAAVDTAVARFGR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  138 PNIVINNAA--GNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGaAFLSITTIYAETGSGFVVPSASAKA 215
Cdd:cd05326  80 LDIMFNNAGvlGAPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKG-SIVSVASVAGVVGGLGPHAYTASKH 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  216 GVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRLDPtgtfEKEMIGRI------PCGRLGTVEELANLAAFLCSDYA 289
Cdd:cd05326 159 AVLGLTRSAATELGEHGIRVNCVSPYGVATPLLTAGFGV----EDEAIEEAvrgaanLKGTALRPEDIAAAVLYLASDDS 234

                       250
                ....*....|...
gi 4503301  290 SWINGAVIKFDGG 302
Cdd:cd05326 235 RYVSGQNLVVDGG 247
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 57-302 1.41e-22

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 94.85  E-value: 1.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    57 FQGKVAFITGGGTGLGKGMTTLLSSLGAqcviasrKMDVLKATAEQISSQTGNK-VHAIQCDVRDPDMVQNTVSELIKVA 135
Cdd:PRK06463   5 FKGKVALITGGTRGIGRAIAEAFLREGA-------KVAVLYNSAENEAKELREKgVFTIKCDVGNRDQVKKSKEVVEKEF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   136 GHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIgKQLIKAQKGAAFLSI------------TTIYAETg 203
Cdd:PRK06463  78 GRVDVLVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEF-LPLLKLSKNGAIVNIasnagigtaaegTTFYAIT- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   204 sgfvvpsasaKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRLDP--TGTFEKEMIGRIPCGRLGTVEELANLA 281
Cdd:PRK06463 156 ----------KAGIIILTRRLAFELGKYGIRVNAVAPGWVETDMTLSGKSQeeAEKLRELFRNKTVLKTTGKPEDIANIV 225

                        250       260
                 ....*....|....*....|.
gi 4503301   282 AFLCSDYASWINGAVIKFDGG 302
Cdd:PRK06463 226 LFLASDDARYITGQVIVADGG 246
PRK06114 PRK06114
SDR family oxidoreductase;
56-302 2.33e-22

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 94.08  E-value: 2.33e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    56 SFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMD-VLKATAEQISSqTGNKVHAIQCDVRDPDMVQNTVSELIKV 134
Cdd:PRK06114   5 DLDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDdGLAETAEHIEA-AGRRAIQIAADVTSKADLRAAVARTEAE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   135 AGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTaFVTLEIGKQLIKAQKGAAFLSITTIyaetgSGFVVPSA--- 211
Cdd:PRK06114  84 LGALTLAVNAAGIANANPAEEMEEEQWQTVMDINLTGV-FLSCQAEARAMLENGGGSIVNIASM-----SGIIVNRGllq 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   212 ----SAKAGVEAMSKSLAAEWGKYGMRFNVIQPG----PIKTKGAFSRLdpTGTFEKEMigriPCGRLGTVEELANLAAF 283
Cdd:PRK06114 158 ahynASKAGVIHLSKSLAMEWVGRGIRVNSISPGytatPMNTRPEMVHQ--TKLFEEQT----PMQRMAKVDEMVGPAVF 231

                        250
                 ....*....|....*....
gi 4503301   284 LCSDYASWINGAVIKFDGG 302
Cdd:PRK06114 232 LLSDAASFCTGVDLLVDGG 250
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 83-302 2.98e-22

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 94.00  E-value: 2.98e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    83 GAQCVIASRKMdvlKATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHP-NIVINNAAGNFispteRLSPNAW 161
Cdd:PRK08642  29 GARVVVNYHQS---EDAAEALADELGDRAIALQADVTDREQVQAMFATATEHFGKPiTTVVNNALADF-----SFDGDAR 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   162 KTITDIV-------LNGT---AFVTLEIGKQLIKAQKGAAFLSI-TTIYAETgsgfVVP---SASAKAGVEAMSKSLAAE 227
Cdd:PRK08642 101 KKADDITwedfqqqLEGSvkgALNTIQAALPGMREQGFGRIINIgTNLFQNP----VVPyhdYTTAKAALLGLTRNLAAE 176

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503301   228 WGKYGMRFNVIQPGPIKTKGAfSRLDPTGTFekEMIGR-IPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK08642 177 LGPYGITVNMVSGGLLRTTDA-SAATPDEVF--DLIAAtTPLRKVTTPQEFADAVLFFASPWARAVTGQNLVVDGG 249
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 57-311 4.74e-22

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 93.26  E-value: 4.74e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    57 FQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQTgnkvhaIQCDVRDPDMVQNTVSELIKVAG 136
Cdd:PRK06057   5 LAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEVGGLF------VPTDVTDEDAVNALFDTAAETYG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   137 HPNIVINNAAgnfISPTERLS-----PNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAaFLSITTIYAETGSGFVVPSA 211
Cdd:PRK06057  79 SVDIAFNNAG---ISPPEDDSilntgLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGS-IINTASFVAVMGSATSQISY 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   212 SA-KAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKT---KGAFSRlDPtgtfekEMIGR----IPCGRLGTVEELANLAAF 283
Cdd:PRK06057 155 TAsKGGVLAMSRELGVQFARQGIRVNALCPGPVNTpllQELFAK-DP------ERAARrlvhVPMGRFAEPEEIAAAVAF 227

                        250       260
                 ....*....|....*....|....*...
gi 4503301   284 LCSDYASWINGAVIKFDGGeevlISGEF 311
Cdd:PRK06057 228 LASDDASFITASTFLVDGG----ISGAY 251
PRK07074 PRK07074
SDR family oxidoreductase;
94-302 7.18e-22

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 92.91  E-value: 7.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    94 DVLKATAEQISSQTG-NKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGt 172
Cdd:PRK07074  33 DIDAAALAAFADALGdARFVPVACDLTDAASLAAALANAAAERGPVDVLVANAGAARAASLHDTTPASWRADNALNLEA- 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   173 AFVTLE-IGKQLIKAQKGaaflSITTIYAETG-SGFVVPSAS-AKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAF 249
Cdd:PRK07074 112 AYLCVEaVLEGMLKRSRG----AVVNIGSVNGmAALGHPAYSaAKAGLIHYTKLLAVEYGRFGIRANAVAPGTVKTQAWE 187

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 4503301   250 SRLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK07074 188 ARVAANPQVFEELKKWYPLQDFATPDDVANAVLFLASPAARAITGVCLPVDGG 240
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
83-302 7.23e-22

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 92.78  E-value: 7.23e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    83 GAQCVIASRKMDVLKATAEQIssqtGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAWK 162
Cdd:PRK07067  30 GARVVIADIKPARARLAALEI----GPAAIAVSLDVTRQDSIDRIVAAAVERFGGIDILFNNAALFDMAPILDISRDSYD 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   163 TITDIVLNGTAFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGP 242
Cdd:PRK07067 106 RLFAVNVKGLFFLMQAVARHMVEQGRGGKIINMASQAGRRGEALVSHYCATKAAVISYTQSAALALIRHGINVNAIAPGV 185

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503301   243 IKTK------GAFSRLD--PTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK07067 186 VDTPmwdqvdALFARYEnrPPGEKKRLVGEAVPLGRMGVPDDLTGMALFLASADADYIVAQTYNVDGG 253
PRK09135 PRK09135
pteridine reductase; Provisional
 83-302 1.13e-21

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 92.30  E-value: 1.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    83 GAQCVI-ASRKMDVLKATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAW 161
Cdd:PRK09135  30 GYRVAIhYHRSAAEADALAAELNALRPGSAAALQADLLDPDALPELVAACVAAFGRLDALVNNASSFYPTPLGSITEAQW 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   162 KTITDIVLNGTAFVTLEIGKQLiKAQKGaAFLSITTIYAETG-SGFVVPSAsAKAGVEAMSKSLAAEWGKyGMRFNVIQP 240
Cdd:PRK09135 110 DDLFASNLKAPFFLSQAAAPQL-RKQRG-AIVNITDIHAERPlKGYPVYCA-AKAALEMLTRSLALELAP-EVRVNAVAP 185

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4503301   241 GPIKTKGAFSRLDPTGtfEKEMIGRIPCGRLGTVEELANLAAFLCSDyASWINGAVIKFDGG 302
Cdd:PRK09135 186 GAILWPEDGNSFDEEA--RQAILARTPLKRIGTPEDIAEAVRFLLAD-ASFITGQILAVDGG 244
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 57-302 1.25e-21

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: 92.30  E-value: 1.25e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   57 FQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQIssqtGNKVHAIQCDVRDPDMVQNTVSELIKVAG 136
Cdd:cd05363   1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEI----GPAACAISLDVTDQASIDRCVAALVDRWG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  137 HPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSASAKAG 216
Cdd:cd05363  77 SIDILVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQGRGGKIINMASQAGRRGEALVGVYCATKAA 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  217 VEAMSKSLAAEWGKYGMRFNVIQPGPIKTK------GAFSRLD--PTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDY 288
Cdd:cd05363 157 VISLTQSAGLNLIRHGINVNAIAPGVVDGEhwdgvdAKFARYEnrPRGEKKRLVGEAVPFGRMGRAEDLTGMAIFLASTD 236

                       250
                ....*....|....
gi 4503301  289 ASWINGAVIKFDGG 302
Cdd:cd05363 237 ADYIVAQTYNVDGG 250
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 57-302 2.05e-21

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: 91.70  E-value: 2.05e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   57 FQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQI--SSQTGNKVHAIQCDVRDPDMVQNTVSELIKV 134
Cdd:cd05364   1 LSGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSClqAGVSEKKILLVVADLTEEEGQDRIISTTLAK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  135 AGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAqKGAaFLSITTIYAETGSGFVVPSASAK 214
Cdd:cd05364  81 FGRLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKT-KGE-IVNVSSVAGGRSFPGVLYYCISK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  215 AGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTkGAFSRL----DPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYAS 290
Cdd:cd05364 159 AALDQFTRCTALELAPKGVRVNSVSPGVIVT-GFHRRMgmpeEQYIKFLSRAKETHPLGRPGTVDEVAEAIAFLASDASS 237

                       250
                ....*....|..
gi 4503301  291 WINGAVIKFDGG 302
Cdd:cd05364 238 FITGQLLPVDGG 249
PRK06500 PRK06500
SDR family oxidoreductase;
83-302 3.60e-21

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 90.79  E-value: 3.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    83 GAQCVIASRKMDVLKATAEQIssqtGNKVHAIQCDVRDPDmVQNTVSELIKVA-GHPNIVINNAAGNFISPTERLSPNAW 161
Cdd:PRK06500  30 GARVAITGRDPASLEAARAEL----GESALVIRADAGDVA-AQKALAQALAEAfGRLDAVFINAGVAKFAPLEDWDEAMF 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   162 KTITDIVLNGTAFvtleigkqLIKA-----QKGAAFLSITTIYAETGsgfvVPSASA----KAGVEAMSKSLAAEWGKYG 232
Cdd:PRK06500 105 DRSFNTNVKGPYF--------LIQAllpllANPASIVLNGSINAHIG----MPNSSVyaasKAALLSLAKTLSGELLPRG 172

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503301   233 MRFNVIQPGPIKTKgAFSRLDPTGTFEKEM----IGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK06500 173 IRVNAVSPGPVQTP-LYGKLGLPEATLDAVaaqiQALVPLGRFGTPEEIAKAVLYLASDESAFIVGSEIIVDGG 245
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
47-302 3.60e-21

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 94.14  E-value: 3.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    47 LQKaMLPPNSFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQtgNKVHAIQCDVRDPDMVQN 126
Cdd:PRK08324 411 LQR-MPKPKPLAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGP--DRALGVACDVTDEAAVQA 487

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   127 TVSELIKVAGHPNIVINNaAGNFIS-PTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFLSITT---IYAet 202
Cdd:PRK08324 488 AFEEAALAFGGVDIVVSN-AGIAISgPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGLGGSIVFIASknaVNP-- 564

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   203 GSGFvVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIktkgaFSRldpTGTFEKEMI-GR-----IPCGRLG---- 272
Cdd:PRK08324 565 GPNF-GAYGAAKAAELHLVRQLALELGPDGIRVNGVNPDAV-----VRG---SGIWTGEWIeARaaaygLSEEELEefyr 635

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 4503301   273 ---------TVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK08324 636 arnllkrevTPEDVAEAVVFLASGLLSKTTGAIITVDGG 674
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 51-303 3.73e-21

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 90.73  E-value: 3.73e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    51 MLPPNSFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMdvlkataeqiSSQTGNKVHAIQCDVRDPDMVQNTVSE 130
Cdd:PRK06523   1 MSFFLELAGKRALVTGGTKGIGAATVARLLEAGARVVTTARSR----------PDDLPEGVEFVAADLTTAEGCAAVARA 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   131 LIKVAGHPNIVINNA------AGNFISpterLSPNAWktITDIVLNGTAFVTLEIG--KQLIKAQKGAAfLSITTI---- 198
Cdd:PRK06523  71 VLERLGGVDILVHVLggssapAGGFAA----LTDEEW--QDELNLNLLAAVRLDRAllPGMIARGSGVI-IHVTSIqrrl 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   199 --YAETgsgfvVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGA---FSRL-DPTGTFE---KEMI----GR 265
Cdd:PRK06523 144 plPEST-----TAYAAAKAALSTYSKSLSKEVAPKGVRVNTVSPGWIETEAAvalAERLaEAAGTDYegaKQIImdslGG 218

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 4503301   266 IPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGGE 303
Cdd:PRK06523 219 IPLGRPAEPEEVAELIAFLASDRAASITGTEYVIDGGT 256
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 55-302 3.81e-21

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 90.63  E-value: 3.81e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    55 NSFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSqTGNKVHAIqcDVRDPDMVQNTVSELIKV 134
Cdd:PRK12828   3 HSLQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGVPA-DALRIGGI--DLVDPQAARRAVDEVNRQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   135 AGHPNIVINNaAGNFISPT-ERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFL--SITTIYAETGSGfvvPSA 211
Cdd:PRK12828  80 FGRLDALVNI-AGAFVWGTiADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNigAGAALKAGPGMG---AYA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   212 SAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKgafsrldptgTFEKEMigriPCGRLG---TVEELANLAAFLCSDY 288
Cdd:PRK12828 156 AAKAGVARLTEALAAELLDRGITVNAVLPSIIDTP----------PNRADM----PDADFSrwvTPEQIAAVIAFLLSDE 221

                        250
                 ....*....|....
gi 4503301   289 ASWINGAVIKFDGG 302
Cdd:PRK12828 222 AQAITGASIPVDGG 235
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
 83-302 4.41e-21

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: 90.47  E-value: 4.41e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   83 GAQCVIASRKmDVLKATAEQISSQTGNKVhAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAgnFiSPTERLSpnawK 162
Cdd:COG0623  31 GAELAFTYQG-EALKKRVEPLAEELGSAL-VLPCDVTDDEQIDALFDEIKEKWGKLDFLVHSIA--F-APKEELG----G 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  163 TITDIVLNGTAfVTLEIG----KQLIKA-----QKGAAFLSITTIyaetGSGFVVPS----ASAKAGVEAMSKSLAAEWG 229
Cdd:COG0623 102 RFLDTSREGFL-LAMDISayslVALAKAaeplmNEGGSIVTLTYL----GAERVVPNynvmGVAKAALEASVRYLAADLG 176

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503301  230 KYGMRFNVIQPGPIKTKgAFSRLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:COG0623 177 PKGIRVNAISAGPIKTL-AASGIPGFDKLLDYAEERAPLGRNVTIEEVGNAAAFLLSDLASGITGEIIYVDGG 248
PRK08589 PRK08589
SDR family oxidoreductase;
60-302 4.56e-21

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 90.99  E-value: 4.56e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    60 KVAFITGGGTGLGKGMTTLLSSLGAQcVIASRKMDVLKATAEQISSqTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPN 139
Cdd:PRK08589   7 KVAVITGASTGIGQASAIALAQEGAY-VLAVDIAEAVSETVDKIKS-NGGKAKAYHVDISDEQQVKDFASEIKEQFGRVD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   140 IVINNA----AGNFIS--PTErlspnAWKTITDIVLNGTAFVTleigKQLIK--AQKGAAFLSITTIYAETG----SGFv 207
Cdd:PRK08589  85 VLFNNAgvdnAAGRIHeyPVD-----VFDKIMAVDMRGTFLMT----KMLLPlmMEQGGSIINTSSFSGQAAdlyrSGY- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   208 vpsASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTkgafSRLDP-TGTFEKEMiGR---------IPCGRLGTVEEL 277
Cdd:PRK08589 155 ---NAAKGAVINFTKSIAIEYGRDGIRANAIAPGTIET----PLVDKlTGTSEDEA-GKtfrenqkwmTPLGRLGKPEEV 226

                        250       260
                 ....*....|....*....|....*
gi 4503301   278 ANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK08589 227 AKLVVFLASDDSSFITGETIRIDGG 251
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 83-303 5.14e-21

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 90.40  E-value: 5.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    83 GAQCVIASRKMDVLKATAEQISSqTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAA--GNFiSPTERLSPNA 160
Cdd:PRK07890  29 GADVVLAARTAERLDEVAAEIDD-LGRRALAVPTDITDEDQCANLVALALERFGRVDALVNNAFrvPSM-KPLADADFAH 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   161 WKTITDIVLNGTAFVTLEIGKQLiKAQKGAAFLSITTIYAETGSGFVvPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQP 240
Cdd:PRK07890 107 WRAVIELNVLGTLRLTQAFTPAL-AESGGSIVMINSMVLRHSQPKYG-AYKMAKGALLAASQSLATELGPQGIRVNSVAP 184

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4503301   241 GPI---KTKGAFSRLDPT-GTFEKEMI----GRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGGE 303
Cdd:PRK07890 185 GYIwgdPLKGYFRHQAGKyGVTVEQIYaetaANSDLKRLPTDDEVASAVLFLASDLARAITGQTLDVNCGE 255
PRK07831 PRK07831
SDR family oxidoreductase;
83-297 9.84e-21

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 89.71  E-value: 9.84e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    83 GAQCVIASRKMDVLKATAEQISSQTG-NKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAW 161
Cdd:PRK07831  42 GARVVISDIHERRLGETADELAAELGlGRVEAVVCDVTSEAQVDALIDAAVERLGRLDVLVNNAGLGGQTPVVDMTDDEW 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   162 KTITDIVLNGTAFVTLEIGKQLIKAQKGAAFL---SITTIYAETGSGFVvpsASAKAGVEAMSKSLAAEWGKYGMRFNVI 238
Cdd:PRK07831 122 SRVLDVTLTGTFRATRAALRYMRARGHGGVIVnnaSVLGWRAQHGQAHY---AAAKAGVMALTRCSALEAAEYGVRINAV 198

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503301   239 QPgpiktkgAFSR---LDPTGTFE--KEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVI 297
Cdd:PRK07831 199 AP-------SIAMhpfLAKVTSAEllDELAAREAFGRAAEPWEVANVIAFLASDYSSYLTGEVV 255
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 108-302 1.70e-20

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: 88.68  E-value: 1.70e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  108 GNKVHAIQCDVRDPDMVQNTVSELikvaGHPNIVINNAA----GNFISPTErlspNAWKTITDIVLNGTAFVTLEIGKQL 183
Cdd:cd05368  45 GPGITTRVLDVTDKEQVAALAKEE----GRIDVLFNCAGfvhhGSILDCED----DDWDFAMNLNVRSMYLMIKAVLPKM 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  184 IKAQKGaaflSITTIYAETGSGFVVPS----ASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRLDPTGTFE 259
Cdd:cd05368 117 LARKDG----SIINMSSVASSIKGVPNrfvySTTKAAVIGLTKSVAADFAQQGIRCNAICPGTVDTPSLEERIQAQPDPE 192

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 4503301  260 ---KEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:cd05368 193 ealKAFAARQPLGRLATPEEVAALAVYLASDESAYVTGTAVVIDGG 238
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 55-302 1.79e-20

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 89.01  E-value: 1.79e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    55 NSFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRK-MDVLKATAEQISSQTGNKVhAIQCDVRDPDMVQNTVSELIK 133
Cdd:PRK08936   3 SDLEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSdEEEANDVAEEIKKAGGEAI-AVKGDVTVESDVVNLIQTAVK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   134 VAGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSASA 213
Cdd:PRK08936  82 EFGTLDVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHDIKGNIINMSSVHEQIPWPLFVHYAAS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   214 KAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTK-GAFSRLDPTGtfEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWI 292
Cdd:PRK08936 162 KGGVKLMTETLAMEYAPKGIRVNNIGPGAINTPiNAEKFADPKQ--RADVESMIPMGYIGKPEEIAAVAAWLASSEASYV 239

                        250
                 ....*....|
gi 4503301   293 NGAVIKFDGG 302
Cdd:PRK08936 240 TGITLFADGG 249
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 58-302 2.36e-20

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 88.26  E-value: 2.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    58 QGKVAFITGGGTGLGKGMTTLLSSLGAQCVIA-SRKMDVLKATAEQISSQTGNKVhAIQCDVRDPDMVQNTVSELIKVAG 136
Cdd:PRK12937   4 SNKVAIVTGASRGIGAAIARRLAADGFAVAVNyAGSAAAADELVAEIEAAGGRAI-AVQADVADAAAVTRLFDAAETAFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   137 HPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTaFVTLeiGKQLIKAQKGAAFLSITT----IYAETGSgfvvPSAS 212
Cdd:PRK12937  83 RIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGA-FVVL--REAARHLGQGGRIINLSTsviaLPLPGYG----PYAA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   213 AKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRLDPTgtFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWI 292
Cdd:PRK12937 156 SKAAVEGLVHVLANELRGRGITVNAVAPGPVATELFFNGKSAE--QIDQLAGLAPLERLGTPEEIAAAVAFLAGPDGAWV 233

                        250
                 ....*....|
gi 4503301   293 NGAVIKFDGG 302
Cdd:PRK12937 234 NGQVLRVNGG 243
PRK06398 PRK06398
aldose dehydrogenase; Validated
 103-307 2.86e-20

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 88.35  E-value: 2.86e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   103 ISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQ 182
Cdd:PRK06398  38 IKEPSYNDVDYFKVDVSNKEQVIKGIDYVISKYGRIDILVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPY 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   183 LIKAQKGAaFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYgMRFNVIQPGPIKT----KGAFSRL--DPTG 256
Cdd:PRK06398 118 MLKQDKGV-IINIASVQSFAVTRNAAAYVTSKHAVLGLTRSIAVDYAPT-IRCVAVCPGSIRTplleWAAELEVgkDPEH 195

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 4503301   257 TFEK-EMIGRI-PCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGGEEVLI 307
Cdd:PRK06398 196 VERKiREWGEMhPMKRVGKPEEVAYVVAFLASDLASFITGECVTVDGGLRALI 248
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 56-302 3.11e-20

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 88.14  E-value: 3.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    56 SFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIasrKMDVLKATAEQISSQ---TGNKVHAIQCDVRDPDMVQNTVSELI 132
Cdd:PRK12935   3 QLNGKVAIVTGGAKGIGKAITVALAQEGAKVVI---NYNSSKEAAENLVNElgkEGHDVYAVQADVSKVEDANRLVEEAV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   133 KVAGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNgTAFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSAS 212
Cdd:PRK12935  80 NHFGKVDILVNNAGITRDRTFKKLNREDWERVIDVNLS-SVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFGQTNYSA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   213 AKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRldPTGTFEKeMIGRIPCGRLGTVEELANLAAFLCSDYAsWI 292
Cdd:PRK12935 159 AKAGMLGFTKSLALELAKTNVTVNAICPGFIDTEMVAEV--PEEVRQK-IVAKIPKKRFGQADEIAKGVVYLCRDGA-YI 234

                        250
                 ....*....|
gi 4503301   293 NGAVIKFDGG 302
Cdd:PRK12935 235 TGQQLNINGG 244
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 59-302 4.04e-20

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: 88.20  E-value: 4.04e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   59 GKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHP 138
Cdd:cd05366   2 SKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEAAKSTIQEISEAGYNAVAVGADVTDKDDVEALIDQAVEKFGSF 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  139 NIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSASAKAGVE 218
Cdd:cd05366  82 DVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGHGGKIINASSIAGVQGFPNLGAYSASKFAVR 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  219 AMSKSLAAEWGKYGMRFNVIQPGPIKTK------GAFSRLD--PTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYAS 290
Cdd:cd05366 162 GLTQTAAQELAPKGITVNAYAPGIVKTEmwdyidEEVGEIAgkPEGEGFAEFSSSIPLGRLSEPEDVAGLVSFLASEDSD 241

                       250
                ....*....|..
gi 4503301  291 WINGAVIKFDGG 302
Cdd:cd05366 242 YITGQTILVDGG 253
PRK07814 PRK07814
SDR family oxidoreductase;
59-302 9.78e-20

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 87.14  E-value: 9.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    59 GKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQIsSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHP 138
Cdd:PRK07814  10 DQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQI-RAAGRRAHVVAADLAHPEATAGLAGQAVEAFGRL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   139 NIVINNAAGNFISPTERLSPNAWK-TITDIVLNGTAFVTLEIgKQLIKAQKGAAFLSITTIYAET-GSGFVVpSASAKAG 216
Cdd:PRK07814  89 DIVVNNVGGTMPNPLLSTSTKDLAdAFTFNVATAHALTVAAV-PLMLEHSGGGSVINISSTMGRLaGRGFAA-YGTAKAA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   217 VEAMSKSLAAEWGKYgMRFNVIQPGPIKTKgAFSRLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAV 296
Cdd:PRK07814 167 LAHYTRLAALDLCPR-IRVNAIAPGSILTS-ALEVVAANDELRAPMEKATPLRRLGDPEDIAAAAVYLASPAGSYLTGKT 244


                 ....*.
gi 4503301   297 IKFDGG 302
Cdd:PRK07814 245 LEVDGG 250
PRK07577 PRK07577
SDR family oxidoreductase;
114-302 1.09e-19

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 86.32  E-value: 1.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   114 IQCDVRDPdmvQNTVSELIKVAGHPNI--VINNAAGNFISPTERLSPNAWKTITDivLNGTAFVtlEIGKQLIKAQKGAA 191
Cdd:PRK07577  46 FACDLADI---EQTAATLAQINEIHPVdaIVNNVGIALPQPLGKIDLAALQDVYD--LNVRAAV--QVTQAFLEGMKLRE 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   192 FLSITTIYAET--GSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKgAFSRLDPTGT-FEKEMIGRIPC 268
Cdd:PRK07577 119 QGRIVNICSRAifGALDRTSYSAAKSALVGCTRTWALELAEYGITVNAVAPGPIETE-LFRQTRPVGSeEEKRVLASIPM 197

                        170       180       190
                 ....*....|....*....|....*....|....
gi 4503301   269 GRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK07577 198 RRLGTPEEVAAAIAFLLSDDAGFITGQVLGVDGG 231
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 83-302 1.17e-19

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: 86.48  E-value: 1.17e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   83 GAQCVIASRKmDVLKATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAgnfISPTERL------ 156
Cdd:cd05372  27 GAELAFTYQP-EALRKRVEKLAERLGESALVLPCDVSNDEEIKELFAEVKKDWGKLDGLVHSIA---FAPKVQLkgpfld 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  157 -SPNAWKTITDIvlNGTAFVTL--EIGKQLikaQKGAAFLSITTIyaetGSGFVVPS----ASAKAGVEAMSKSLAAEWG 229
Cdd:cd05372 103 tSRKGFLKALDI--SAYSLVSLakAALPIM---NPGGSIVTLSYL----GSERVVPGynvmGVAKAALESSVRYLAYELG 173

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503301  230 KYGMRFNVIQPGPIKTKGAFSrldptGTFEKEMIG----RIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:cd05372 174 RKGIRVNAISAGPIKTLAASG-----ITGFDKMLEyseqRAPLGRNVTAEEVGNTAAFLLSDLSSGITGEIIYVDGG 245
PRK06138 PRK06138
SDR family oxidoreductase;
58-302 1.27e-19

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 86.74  E-value: 1.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    58 QGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSqtGNKVHAIQCDVRDPDMVQNTVSELIKVAGH 137
Cdd:PRK06138   4 AGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAA--GGRAFARQGDVGSAEAVEALVDFVAARWGR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   138 PNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTaFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSASAKAGV 217
Cdd:PRK06138  82 LDVLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGV-FLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGRAAYVASKGAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   218 EAMSKSLAAEWGKYGMRFNVIQPGPIKT---KGAFSRLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWING 294
Cdd:PRK06138 161 ASLTRAMALDHATDGIRVNAVAPGTIDTpyfRRIFARHADPEALREALRARHPMNRFGTAEEVAQAALFLASDESSFATG 240


                 ....*...
gi 4503301   295 AVIKFDGG 302
Cdd:PRK06138 241 TTLVVDGG 248
PRK08340 PRK08340
SDR family oxidoreductase;
79-301 1.73e-19

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 86.40  E-value: 1.73e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    79 LSSLGAQCVIASRKMDVLKATAEQISSQTGnkVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISP--TERL 156
Cdd:PRK08340  20 LLKKGARVVISSRNEENLEKALKELKEYGE--VYAVKADLSDKDDLKNLVKEAWELLGGIDALVWNAGNVRCEPcmLHEA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   157 SPNAWKTITDIVLNGTAFVT-LEIGKQLIKAQKGA-AFLSITTIYAETGSgfVVPSASAKAGVEAMSKSLAAEWGKYGMR 234
Cdd:PRK08340  98 GYSDWLEAALLHLVAPGYLTtLLIQAWLEKKMKGVlVYLSSVSVKEPMPP--LVLADVTRAGLVQLAKGVSRTYGGKGIR 175

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503301   235 FNVIQPGPIKTKGAFSRL---------DPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDG 301
Cdd:PRK08340 176 AYTVLLGSFDTPGARENLariaeergvSFEETWEREVLERTPLKRTGRWEELGSLIAFLLSENAEYMLGSTIVFDG 251
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 104-302 1.79e-19

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 86.22  E-value: 1.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   104 SSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNF----ISPTE-----RLSPNAWKTITDIVLNGTAF 174
Cdd:PRK06171  44 GDGQHENYQFVPTDVSSAEEVNHTVAEIIEKFGRIDGLVNNAGINIprllVDEKDpagkyELNEAAFDKMFNINQKGVFL 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   175 VTLEIGKQLIKAQKGAaflsITTIYAETGS----GFVVPSASaKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKG--- 247
Cdd:PRK06171 124 MSQAVARQMVKQHDGV----IVNMSSEAGLegseGQSCYAAT-KAALNSFTRSWAKELGKHNIRVVGVAPGILEATGlrt 198

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503301   248 -------AFSRldpTGTFEKEMIG-----RIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK06171 199 peyeealAYTR---GITVEQLRAGytktsTIPLGRSGKLSEVADLVCYLLSDRASYITGVTTNIAGG 262
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 59-302 2.11e-19

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: 85.96  E-value: 2.11e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   59 GKVAFITGGGTGLGKGMTTLLSSLGAQCVIAS-RKMDVLKATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGH 137
Cdd:cd08940   2 GKVALVTGSTSGIGLGIARALAAAGANIVLNGfGDAAEIEAVRAGLAAKHGVKVLYHGADLSKPAAIEDMVAYAQRQFGG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  138 PNIVINNAAGNFISPTERLSPNAWKTItdIVLNGTA-FVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSASAKAG 216
Cdd:cd08940  82 VDILVNNAGIQHVAPIEDFPTEKWDAI--IALNLSAvFHTTRLALPHMKKQGWGRIINIASVHGLVASANKSAYVAAKHG 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  217 VEAMSKSLAAEWGKYGMRFNVIQPGPIKTK--------GAFSRLDPTGTFEKEMIG-RIPCGRLGTVEELANLAAFLCSD 287
Cdd:cd08940 160 VVGLTKVVALETAGTGVTCNAICPGWVLTPlvekqisaLAQKNGVPQEQAARELLLeKQPSKQFVTPEQLGDTAVFLASD 239

                       250
                ....*....|....*
gi 4503301  288 YASWINGAVIKFDGG 302
Cdd:cd08940 240 AASQITGTAVSVDGG 254
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 58-245 2.25e-19

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: 85.67  E-value: 2.25e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   58 QGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQtGNKVHAIQCDVRDP----DMVQNTVSELik 133
Cdd:cd08934   2 QGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELEAE-GGKALVLELDVTDEqqvdAAVERTVEAL-- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  134 vaGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTlEIGKQLIKAQKGAAFLSITTIYAE-TGSGFVVPSAS 212
Cdd:cd08934  79 --GRLDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTT-HAALPHHLLRNKGTIVNISSVAGRvAVRNSAVYNAT 155

                       170       180       190
                ....*....|....*....|....*....|...
gi 4503301  213 aKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKT 245
Cdd:cd08934 156 -KFGVNAFSEGLRQEVTERGVRVVVIEPGTVDT 187
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 59-302 3.59e-19

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 85.68  E-value: 3.59e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    59 GKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVaGHP 138
Cdd:PRK08339   8 GKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSESNVDVSYIVADLTKREDLERTVKELKNI-GEP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   139 NIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVpSASAKAGVE 218
Cdd:PRK08339  87 DIFFFSTGGPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSVAIKEPIPNIAL-SNVVRISMA 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   219 AMSKSLAAEWGKYGMRFNVIQPGPIKT----KGAFSRLDPTG-TFE---KEMIGRIPCGRLGTVEELANLAAFLCSDYAS 290
Cdd:PRK08339 166 GLVRTLAKELGPKGITVNGIMPGIIRTdrviQLAQDRAKREGkSVEealQEYAKPIPLGRLGEPEEIGYLVAFLASDLGS 245

                        250
                 ....*....|..
gi 4503301   291 WINGAVIKFDGG 302
Cdd:PRK08339 246 YINGAMIPVDGG 257
PRK06940 PRK06940
short chain dehydrogenase; Provisional
 81-302 8.22e-19

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 84.69  E-value: 8.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    81 SLGAQCVIASRKMDVLKATAEQISsQTGNKVHAIQCDVRDPDMVQNtvseLIKVA---GHPNIVINnAAGnfISPTERlS 157
Cdd:PRK06940  22 GAGKKVLLADYNEENLEAAAKTLR-EAGFDVSTQEVDVSSRESVKA----LAATAqtlGPVTGLVH-TAG--VSPSQA-S 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   158 PnawKTITDIVLNGTAFVTLEIGKqlIKAQKGAAflsiTTIYAEtgSGFVVPSASAK------------------AGVEA 219
Cdd:PRK06940  93 P---EAILKVDLYGTALVLEEFGK--VIAPGGAG----VVIASQ--SGHRLPALTAEqeralattpteellslpfLQPDA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   220 MSKSLAA-----------------EWGKYGMRFNVIQPGPIKTKGAFSRLD-PTGTFEKEMIGRIPCGRLGTVEELANLA 281
Cdd:PRK06940 162 IEDSLHAyqiakranalrvmaeavKWGERGARINSISPGIISTPLAQDELNgPRGDGYRNMFAKSPAGRPGTPDEIAALA 241

                        250       260
                 ....*....|....*....|.
gi 4503301   282 AFLCSDYASWINGAVIKFDGG 302
Cdd:PRK06940 242 EFLMGPRGSFITGSDFLVDGG 262
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 108-302 1.64e-18

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 83.59  E-value: 1.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   108 GNKVHAIQCDVRDPD----MVQNTVSELikvaGHPNIVINNAAgnfispteRLSPNAWKTITDIVLNGTAFV----TLEI 179
Cdd:PRK12748  66 GVRCEHMEIDLSQPYapnrVFYAVSERL----GDPSILINNAA--------YSTHTRLEELTAEQLDKHYAVnvraTMLL 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   180 GKQLIKAQKGAAFLSITTIyaeTGSGFV------VPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAfsrld 253
Cdd:PRK12748 134 SSAFAKQYDGKAGGRIINL---TSGQSLgpmpdeLAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDTGWI----- 205

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 4503301   254 pTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK12748 206 -TEELKHHLVPKFPQGRVGEPVDAARLIAFLVSEEAKWITGQVIHSEGG 253
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 57-303 2.51e-18

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: 82.96  E-value: 2.51e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   57 FQGKVAFITGGGTGLGKGMTTLLSSLGAqCVIASRKMDVLKATAEQISSqTGNKVHAIQCDVRDPDMVQNTVSELIKVAG 136
Cdd:cd08937   2 FEGKVVVVTGAAQGIGRGVAERLAGEGA-RVLLVDRSELVHEVLAEILA-AGDAAHVHTADLETYAGAQGVVRAAVERFG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  137 HPNIVINNAAGNFIS-PTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAaFLSITTIyaETGSGFVVPSASAKA 215
Cdd:cd08937  80 RVDVLINNVGGTIWAkPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGV-IVNVSSI--ATRGIYRIPYSAAKG 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  216 GVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRLDPTGTFEKE----------MIGRIPCGRLGTVEELANLAAFLC 285
Cdd:cd08937 157 GVNALTASLAFEHARDGIRVNAVAPGGTEAPPRKIPRNAAPMSEQEkvwyqrivdqTLDSSLMGRYGTIDEQVRAILFLA 236

                       250
                ....*....|....*...
gi 4503301  286 SDYASWINGAVIKFDGGE 303
Cdd:cd08937 237 SDEASYITGTVLPVGGGD 254
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 55-302 2.80e-18

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 82.67  E-value: 2.80e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    55 NSFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQtGNKVHAIQCDVRDPDMVQNTVSELIKV 134
Cdd:PRK07478   2 MRLNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIRAE-GGEAVALAGDVRDEAYAKALVALAVER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   135 AGHPNIVINNAAGN-FISPTERLSPNAWKTITDIVLNGtAFVTleiGKQLIKA--QKGAAFLSITTIYAETGSGF--VVP 209
Cdd:PRK07478  81 FGGLDIAFNNAGTLgEMGPVAEMSLEGWRETLATNLTS-AFLG---AKHQIPAmlARGGGSLIFTSTFVGHTAGFpgMAA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   210 SASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKgAFSRLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYA 289
Cdd:PRK07478 157 YAASKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTP-MGRAMGDTPEALAFVAGLHALKRMAQPEEIAQAALFLASDAA 235

                        250
                 ....*....|...
gi 4503301   290 SWINGAVIKFDGG 302
Cdd:PRK07478 236 SFVTGTALLVDGG 248
PRK08416 PRK08416
enoyl-ACP reductase;
100-302 4.08e-18

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 82.51  E-value: 4.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   100 AEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNA-------AGNFiSPTERLSPNAWKTITDIVLNgt 172
Cdd:PRK08416  50 AEDLEQKYGIKAKAYPLNILEPETYKELFKKIDEDFDRVDFFISNAiisgravVGGY-TKFMRLKPKGLNNIYTATVN-- 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   173 AFV--TLEIGKQLIKAqKGAAFLSITT----IYAETGSGfvvpSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTK 246
Cdd:PRK08416 127 AFVvgAQEAAKRMEKV-GGGSIISLSStgnlVYIENYAG----HGTSKAAVETMVKYAATELGEKNIRVNAVSGGPIDTD 201

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 4503301   247 G--AFSRLDPTgtfEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK08416 202 AlkAFTNYEEV---KAKTEELSPLNRMGQPEDLAGACLFLCSEKASWLTGQTIVVDGG 256
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 59-257 5.76e-18

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: 81.67  E-value: 5.76e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   59 GKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMD------------VLKATAEQISSQtGNKVHAIQCDVRDPDMVQN 126
Cdd:cd05338   3 GKVAFVTGASRGIGRAIALRLAKAGATVVVAAKTASegdngsakslpgTIEETAEEIEAA-GGQALPIVVDVRDEDQVRA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  127 TVSELIKVAGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGaaflSITTIYAETGSGF 206
Cdd:cd05338  82 LVEATVDQFGRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQG----HILNISPPLSLRP 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 4503301  207 V---VPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRLDPTGT 257
Cdd:cd05338 158 ArgdVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPSTAIETPAATELSGGSD 211
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 57-305 8.68e-18

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: 81.81  E-value: 8.68e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   57 FQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAG 136
Cdd:cd08933   7 YADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAGPGSCKFVPCDVTKEEDIKTLISVTVERFG 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  137 HPNIVINNAAGNFI-SPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQkgAAFLSITTIYAETGSGFVVPSASAKA 215
Cdd:cd08933  87 RIDCLVNNAGWHPPhQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQ--GNIINLSSLVGSIGQKQAAPYVATKG 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  216 GVEAMSKSLAAEWGKYGMRFNVIQPGPIKT----KGAFSRLDPTGTFEKEMIGRiPCGRLGTVEELANLAAFLCSDyASW 291
Cdd:cd08933 165 AITAMTKALAVDESRYGVRVNCISPGNIWTplweELAAQTPDTLATIKEGELAQ-LLGRMGTEAESGLAALFLAAE-ATF 242

                       250
                ....*....|....
gi 4503301  292 INGAVIKFDGGEEV 305
Cdd:cd08933 243 CTGIDLLLSGGAEL 256
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 56-302 9.01e-18

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: 81.36  E-value: 9.01e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   56 SFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSqtgnkVHAIQCDVRDPDMVQNtvseliKVA 135
Cdd:cd05351   4 DFAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVRECPG-----IEPVCVDLSDWDATEE------ALG 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  136 GHP--NIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSASA 213
Cdd:cd05351  73 SVGpvDLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGVPGSIVNVSSQASQRALTNHTVYCST 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  214 KAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTK-GAFSRLDPTgtFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWI 292
Cdd:cd05351 153 KAALDMLTKVMALELGPHKIRVNSVNPTVVMTDmGRDNWSDPE--KAKKMLNRIPLGKFAEVEDVVNAILFLLSDKSSMT 230

                       250
                ....*....|
gi 4503301  293 NGAVIKFDGG 302
Cdd:cd05351 231 TGSTLPVDGG 240
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 106-302 1.37e-17

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 80.99  E-value: 1.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   106 QTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIK 185
Cdd:PRK12859  65 KNGVKVSSMELDLTQNDAPKELLNKVTEQLGYPHILVNNAAYSTNNDFSNLTAEELDKHYMVNVRATTLLSSQFARGFDK 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   186 AQKGaaflSITTIYAETGSGFVVPS---ASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRLdptgtfEKEM 262
Cdd:PRK12859 145 KSGG----RIINMTSGQFQGPMVGElayAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDTGWMTEEI------KQGL 214

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 4503301   263 IGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK12859 215 LPMFPFGRIGEPKDAARLIKFLASEEAEWITGQIIHSEGG 254
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 83-303 1.83e-17

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: 80.80  E-value: 1.83e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   83 GAQCVIA--SRKMDVLKATAEQISsQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPT-ERLSPN 159
Cdd:cd05355  50 GADVAINylPEEEDDAEETKKLIE-EEGRKCLLIPGDLGDESFCRDLVKEVVKEFGKLDILVNNAAYQHPQESiEDITTE 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  160 AWKTITDIVLNGTAFVTLEIGKQLikaQKGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQ 239
Cdd:cd05355 129 QLEKTFRTNIFSMFYLTKAALPHL---KKGSSIINTTSVTAYKGSPHLLDYAATKGAIVAFTRGLSLQLAEKGIRVNAVA 205

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503301  240 PGPIKTKgafsrLDPtGTFEKEMIG----RIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGGE 303
Cdd:cd05355 206 PGPIWTP-----LIP-SSFPEEKVSefgsQVPMGRAGQPAEVAPAYVFLASQDSSYVTGQVLHVNGGE 267
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 87-245 3.21e-17

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: 79.58  E-value: 3.21e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   87 VIA-SRKMDVLKATAEQISSQtgnkVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAWKTIT 165
Cdd:cd05374  27 VIAtARNPDKLESLGELLNDN----LEVLELDVTDEESIKAAVKEVIERFGRIDVLVNNAGYGLFGPLEETSIEEVRELF 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  166 DIVLNGTAFVTLEIGKQLIKAQKGaaflSITTIyaetGS--GFVV-----PSASAKAGVEAMSKSLAAEWGKYGMRFNVI 238
Cdd:cd05374 103 EVNVFGPLRVTRAFLPLMRKQGSG----RIVNV----SSvaGLVPtpflgPYCASKAALEALSESLRLELAPFGIKVTII 174


                ....*..
gi 4503301  239 QPGPIKT 245
Cdd:cd05374 175 EPGPVRT 181
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 100-302 3.46e-17

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: 79.44  E-value: 3.46e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  100 AEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVInNAAGNFI-SPTERLSPNAWKTITDIVLNGtAFVTLE 178
Cdd:cd05331  31 PFVLLLEYGDPLRLTPLDVADAAAVREVCSRLLAEHGPIDALV-NCAGVLRpGATDPLSTEDWEQTFAVNVTG-VFNLLQ 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  179 IGKQLIKAQKGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKT----------KGA 248
Cdd:cd05331 109 AVAPHMKDRRTGAIVTVASNAAHVPRISMAAYGASKAALASLSKCLGLELAPYGVRCNVVSPGSTDTamqrtlwhdeDGA 188

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 4503301  249 FSRLdpTGTFEKEMIGrIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:cd05331 189 AQVI--AGVPEQFRLG-IPLGKIAQPADIANAVLFLASDQAGHITMHDLVVDGG 239
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 106-302 5.03e-17

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 80.08  E-value: 5.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   106 QTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAgnFISPTERLspnawKTITDIVLNGTaFVTLEIGK-QLI 184
Cdd:PRK06701  93 KEGVKCLLIPGDVSDEAFCKDAVEETVRELGRLDILVNNAA--FQYPQQSL-----EDITAEQLDKT-FKTNIYSYfHMT 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   185 KA-----QKGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKgafsrLDPTgTFE 259
Cdd:PRK06701 165 KAalphlKQGSAIINTGSITGYEGNETLIDYSATKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTP-----LIPS-DFD 238

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 4503301   260 KEMIG----RIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK06701 239 EEKVSqfgsNTPMQRPGQPEELAPAYVFLASPDSSYITGQMLHVNGG 285
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 79-302 6.02e-17

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: 78.97  E-value: 6.02e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   79 LSSLGAqCVIAsrkMDVLKATAEQISSQTGNKVHA--IQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERL 156
Cdd:cd08943  21 LAAEGA-AVVV---ADIDPEIAEKVAEAAQGGPRAlgVQCDVTSEAQVQSAFEQAVLEFGGLDIVVSNAGIATSSPIAET 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  157 SPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFL---SITTIYAetGSGFvVPSASAKAGVEAMSKSLAAEWGKYGM 233
Cdd:cd08943  97 SLEDWNRSMDINLTGHFLVSREAFRIMKSQGIGGNIVfnaSKNAVAP--GPNA-AAYSAAKAAEAHLARCLALEGGEDGI 173

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503301  234 RFNVIQPGPIKTKGAFS-------RLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:cd08943 174 RVNTVNPDAVFRGSKIWegvwraaRAKAYGLLEEEYRTRNLLKREVLPEDVAEAVVAMASEDFGKTTGAIVTVDGG 249
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 59-302 1.36e-16

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: 78.00  E-value: 1.36e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   59 GKVAFITGGGTGLGKGMTTLLSSLGAQCVIAsrkmDVLKATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHP 138
Cdd:cd09761   1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFA----DIDEERGADFAEAEGPNLFFVHGDVADETLVKFVVYAMLEKLGRI 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  139 NIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKaqKGAAFLSITTIYAETGSGFVVPSASAKAGVE 218
Cdd:cd09761  77 DVLVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIK--NKGRIINIASTRAFQSEPDSEAYAASKGGLV 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  219 AMSKSLAAEWGKYgMRFNVIQPGPIKTKGAFSRldPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIK 298
Cdd:cd09761 155 ALTHALAMSLGPD-IRVNCISPGWINTTEQQEF--TAAPLTQEDHAQHPAGRVGTPKDIANLVLFLCQQDAGFITGETFI 231


                ....
gi 4503301  299 FDGG 302
Cdd:cd09761 232 VDGG 235
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 51-302 1.37e-16

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: 77.97  E-value: 1.37e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   51 MLPPNSFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQtGNKVHAIQCDVRDPDMVQNTVSE 130
Cdd:cd08936   2 VTRRDPLANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGE-GLSVTGTVCHVGKAEDRERLVAT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  131 LIKVAGHPNIVINNAA-----GNFISPTERlspnAWKTITDIVLNGTAFVTLEIGKQLIKaQKGAAFLSITTIYAETGSG 205
Cdd:cd08936  81 AVNLHGGVDILVSNAAvnpffGNILDSTEE----VWDKILDVNVKATALMTKAVVPEMEK-RGGGSVVIVSSVAAFHPFP 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  206 FVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKgaFSR-LDPTGTFEKEMIGRIPCGRLGTVEELANLAAFL 284
Cdd:cd08936 156 GLGPYNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTS--FSSaLWMDKAVEESMKETLRIRRLGQPEDCAGIVSFL 233

                       250
                ....*....|....*...
gi 4503301  285 CSDYASWINGAVIKFDGG 302
Cdd:cd08936 234 CSEDASYITGETVVVGGG 251
PRK07533 PRK07533
enoyl-[acyl-carrier-protein] reductase FabI;
213-302 2.01e-16

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


Pssm-ID: 181020 [Multi-domain]  Cd Length: 258  Bit Score: 77.67  E-value: 2.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   213 AKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAfSRLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWI 292
Cdd:PRK07533 165 VKAALESSVRYLAAELGPKGIRVHAISPGPLKTRAA-SGIDDFDALLEDAAERAPLRRLVDIDDVGAVAAFLASDAARRL 243

                         90
                 ....*....|
gi 4503301   293 NGAVIKFDGG 302
Cdd:PRK07533 244 TGNTLYIDGG 253
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 101-302 2.97e-16

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 76.93  E-value: 2.97e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   101 EQISSQTGNkVHAIQCDVRDPdmvqntVSELIKVAGHPNIVINNAAgnfI----SPTERLSPNAWKTITDIVLNGTAFVT 176
Cdd:PRK06550  38 QDKPDLSGN-FHFLQLDLSDD------LEPLFDWVPSVDILCNTAG---IlddyKPLLDTSLEEWQHIFDTNLTSTFLLT 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   177 LEIGKQLIKAQKGAaFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRLDPtG 256
Cdd:PRK06550 108 RAYLPQMLERKSGI-IINMCSIASFVAGGGGAAYTASKHALAGFTKQLALDYAKDGIQVFGIAPGAVKTPMTAADFEP-G 185

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 4503301   257 TFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK06550 186 GLADWVARETPIKRWAEPEEVAELTLFLASGKADYMQGTIVPIDGG 231
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 58-306 4.87e-16

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 76.59  E-value: 4.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    58 QGKVAFITGGGTGLGKGMTTLLSSLGAQCVIAsrkmDVLKATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGH 137
Cdd:PRK08265   5 AGKVAIVTGGATLIGAAVARALVAAGARVAIV----DIDADNGAAVAASLGERARFIATDITDDAAIERAVATVVARFGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   138 PNIVINNAAgNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLiKAQKGAA--FLSITTIYAETGSgFVVPsaSAKA 215
Cdd:PRK08265  81 VDILVNLAC-TYLDDGLASSRADWLAALDVNLVSAAMLAQAAHPHL-ARGGGAIvnFTSISAKFAQTGR-WLYP--ASKA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   216 GVEAMSKSLAAEWGKYGMRFNVIQPG----PIK---TKGAFSRLDPTG-TFEkemigriPCGRLGTVEELANLAAFLCSD 287
Cdd:PRK08265 156 AIRQLTRSMAMDLAPDGIRVNSVSPGwtwsRVMdelSGGDRAKADRVAaPFH-------LLGRVGDPEEVAQVVAFLCSD 228

                        250
                 ....*....|....*....
gi 4503301   288 YASWINGAVIKFDGGEEVL 306
Cdd:PRK08265 229 AASFVTGADYAVDGGYSAL 247
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 83-303 7.74e-16

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 76.24  E-value: 7.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    83 GAQCVIASRKMDVLKATAEQISSQTGNKVHAIQCDVRDPDmvqnTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAWK 162
Cdd:PRK06125  31 GCHLHLVARDADALEALAADLRAAHGVDVAVHALDLSSPE----AREQLAAEAGDIDILVNNAGAIPGGGLDDVDDAAWR 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   163 TITDIVLNGtaFVTLeiGKQLIKAQKGAAFLSITTIYAETGSGF---VVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQ 239
Cdd:PRK06125 107 AGWELKVFG--YIDL--TRLAYPRMKARGSGVIVNVIGAAGENPdadYICGSAGNAALMAFTRALGGKSLDDGVRVVGVN 182

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4503301   240 PGPIKT-------KGAFSRLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGGE 303
Cdd:PRK06125 183 PGPVATdrmltllKGRARAELGDESRWQELLAGLPLGRPATPEEVADLVAFLASPRSGYTSGTVVTVDGGI 253
PRK07062 PRK07062
SDR family oxidoreductase;
78-302 1.38e-15

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 75.46  E-value: 1.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    78 LLSSLGAQCVIASRKMDVLKATAEQISSQ-TGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERL 156
Cdd:PRK07062  27 LLLEAGASVAICGRDEERLASAEARLREKfPGARLLAARCDVLDEADVAAFAAAVEARFGGVDMLVNNAGQGRVSTFADT 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   157 SPNAWKTITDI----VLNGT-AFVTLeigkqlIKAQKGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKY 231
Cdd:PRK07062 107 TDDAWRDELELkyfsVINPTrAFLPL------LRASAAASIVCVNSLLALQPEPHMVATSAARAGLLNLVKSLATELAPK 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   232 GMRFNVIQPGPIKT---KGAF-SRLDPTGTFEK--EMIGR---IPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK07062 181 GVRVNSILLGLVESgqwRRRYeARADPGQSWEAwtAALARkkgIPLGRLGRPDEAARALFFLASPLSSYTTGSHIDVSGG 260
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 58-302 1.78e-15

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: 74.88  E-value: 1.78e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   58 QGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQtGNKVHAIQCDVRDPDMVQNTVSELIKVAGH 137
Cdd:cd08945   2 DSEVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELREA-GVEADGRTCDVRSVPEIEALVAAAVARYGP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  138 PNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAA-FLSITTIYAETGSGFVVPSASAKAG 216
Cdd:cd08945  81 IDVLVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKAGGMLERGTGrIINIASTGGKQGVVHAAPYSASKHG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  217 VEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFS----RLDPTGTFEKEMIGRI----PCGRLGTVEELANLAAFLCSDY 288
Cdd:cd08945 161 VVGFTKALGLELARTGITVNAVCPGFVETPMAASvrehYADIWEVSTEEAFDRItarvPLGRYVTPEEVAGMVAYLIGDG 240

                       250
                ....*....|....
gi 4503301  289 ASWINGAVIKFDGG 302
Cdd:cd08945 241 AAAVTAQALNVCGG 254
PLN02253 PLN02253
xanthoxin dehydrogenase
 50-302 1.87e-15

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 75.24  E-value: 1.87e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    50 AMLPPNSFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIAsrkmDVLKATAEQISSQTGNK--VHAIQCDVRDPDMVQNT 127
Cdd:PLN02253   9 SSLPSQRLLGKVALVTGGATGIGESIVRLFHKHGAKVCIV----DLQDDLGQNVCDSLGGEpnVCFFHCDVTVEDDVSRA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   128 VSELIKVAGHPNIVINNA--AGNFISPTERLSPNAWKTITDIVLNGtAFVTLEIGKQLIKAQKGAAFLSITTIYAETGSg 205
Cdd:PLN02253  85 VDFTVDKFGTLDIMVNNAglTGPPCPDIRNVELSEFEKVFDVNVKG-VFLGMKHAARIMIPLKKGSIVSLCSVASAIGG- 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   206 fVVPSA--SAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRLDPTGTFEKEMIG-RIPCGRLG-------TVE 275
Cdd:PLN02253 163 -LGPHAytGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALALAHLPEDERTEDALAGfRAFAGKNAnlkgvelTVD 241

                        250       260
                 ....*....|....*....|....*..
gi 4503301   276 ELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PLN02253 242 DVANAVLFLASDEARYISGLNLMIDGG 268
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 79-302 2.03e-15

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 74.79  E-value: 2.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    79 LSSLGAQCVIAsrkmDVLKATAEQISS---QTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTER 155
Cdd:PRK08085  29 LAEYGAEIIIN----DITAERAELAVAklrQEGIKAHAAPFNVTHKQEVEAAIEHIEKDIGPIDVLINNAGIQRRHPFTE 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   156 LSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAaFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRF 235
Cdd:PRK08085 105 FPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGK-IINICSMQSELGRDTITPYAASKGAVKMLTRGMCVELARHNIQV 183

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503301   236 NVIQPGPIKTKGAFSRLDpTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK08085 184 NGIAPGYFKTEMTKALVE-DEAFTAWLCKRTPAARWGDPQELIGAAVFLSSKASDFVNGHLLFVDGG 249
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 78-247 2.37e-15

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: 74.21  E-value: 2.37e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   78 LLSSLGAQCVIASRKMDVLKATAEQISS---QTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTE 154
Cdd:cd08939  20 ELVKEGANVIIVARSESKLEEAVEEIEAeanASGQKVSYISADLSDYEEVEQAFAQAVEKGGPPDLVVNCAGISIPGLFE 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  155 RLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKG--------AAFLSittIYAETgsgfvvPSASAKAGVEAMSKSLAA 226
Cdd:cd08939 100 DLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGhivfvssqAALVG---IYGYS------AYCPSKFALRGLAESLRQ 170

                       170       180
                ....*....|....*....|.
gi 4503301  227 EWGKYGMRFNVIQPGPIKTKG 247
Cdd:cd08939 171 ELKPYNIRVSVVYPPDTDTPG 191
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 54-300 4.68e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 73.89  E-value: 4.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    54 PNSFQGKVAFITGGGTGLGKGMTTLLSSLGAQC-VIASRKMDVLKATAEQISSqTGNKVHAIQCDVRDPDMVQNTVSELI 132
Cdd:PRK06198   1 MGRLDGKVALVTGGTQGLGAAIARAFAERGAAGlVICGRNAEKGEAQAAELEA-LGAKAVFVQADLSDVEDCRRVVAAAD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   133 KVAGHPNIVINnAAGNfispTER-----LSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFV 207
Cdd:PRK06198  80 EAFGRLDALVN-AAGL----TDRgtildTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKAEGTIVNIGSMSAHGGQPFL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   208 VPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKG------AFSRlDPTGTFEKEMiGRIPCGRLGTVEELANLA 281
Cdd:PRK06198 155 AAYCASKGALATLTRNAAYALLRNRIRVNGLNIGWMATEGedriqrEFHG-APDDWLEKAA-ATQPFGRLLDPDEVARAV 232

                        250
                 ....*....|....*....
gi 4503301   282 AFLCSDYASWINGAVIKFD 300
Cdd:PRK06198 233 AFLLSDESGLMTGSVIDFD 251
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 56-250 7.71e-15

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 72.80  E-value: 7.71e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    56 SFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQIsSQTGNKVHAIQCDVRDPDMVQNTVSELIKVA 135
Cdd:PRK07666   4 SLQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEV-EAYGVKVVIATADVSDYEEVTAAIEQLKNEL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   136 GHPNIVINNAA-GNFISPTErLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGaaflSITTIYAETG-SGFVVPSA-- 211
Cdd:PRK07666  83 GSIDILINNAGiSKFGKFLE-LDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSG----DIINISSTAGqKGAAVTSAys 157

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 4503301   212 SAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFS 250
Cdd:PRK07666 158 ASKFGVLGLTESLMQEVRKHNIRVTALTPSTVATDMAVD 196
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
79-302 8.22e-15

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


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 73.22  E-value: 8.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    79 LSSLGAQCVIASRKMDVLKATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAgnfISPTERLSP 158
Cdd:PRK08594  29 LHNAGAKLVFTYAGERLEKEVRELADTLEGQESLLLPCDVTSDEEITACFETIKEEVGVIHGVAHCIA---FANKEDLRG 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   159 NAWKTITDIVL---NGTAFVTLEIGKQLIK-AQKGAAFLSITTIYAEtgsgFVVPSAS----AKAGVEAMSKSLAAEWGK 230
Cdd:PRK08594 106 EFLETSRDGFLlaqNISAYSLTAVAREAKKlMTEGGSIVTLTYLGGE----RVVQNYNvmgvAKASLEASVKYLANDLGK 181

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503301   231 YGMRFNVIQPGPIKT---KGafsrldpTGTFE---KEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK08594 182 DGIRVNAISAGPIRTlsaKG-------VGGFNsilKEIEERAPLRRTTTQEEVGDTAAFLFSDLSRGVTGENIHVDSG 252
PRK07326 PRK07326
SDR family oxidoreductase;
55-245 8.53e-15

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 72.74  E-value: 8.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    55 NSFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSqtGNKVHAIQCDVRDPDMVQNTVSELIKV 134
Cdd:PRK07326   2 MSLKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNN--KGNVLGLAADVRDEADVQRAVDAIVAA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   135 AGHPNIVINNAA-GNFiSPTERLSPNAWKTITDIVLNGtAFVTLEIGKQLIKAQKGaAFLSITTI----YAETGSGFvvp 209
Cdd:PRK07326  80 FGGLDVLIANAGvGHF-APVEELTPEEWRLVIDTNLTG-AFYTIKAAVPALKRGGG-YIINISSLagtnFFAGGAAY--- 153

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 4503301   210 SASaKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKT 245
Cdd:PRK07326 154 NAS-KFGLVGFSEAAMLDLRQYGIKVSTIMPGSVAT 188
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 114-307 1.54e-14

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


Pssm-ID: 187589 [Multi-domain]  Cd Length: 250  Bit Score: 72.14  E-value: 1.54e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  114 IQCDVRDPDMVQNTVSE-----------LIKVAG--HPNIVINNAAGNFISPTE-------RLSPN---AWKTITDIVLN 170
Cdd:cd05328  36 VIADLSTPEGRAAAIADvlarcsgvldgLVNCAGvgGTTVAGLVLKVNYFGLRAlmeallpRLRKGhgpAAVVVSSIAGA 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  171 GTAFVTLEIGKQLIkaqkgAAFLSITTIYAETGSGFVVPS-ASAKAGVEAMSKSLAAEWG-KYGMRFNVIQPGPIKTK-- 246
Cdd:cd05328 116 GWAQDKLELAKALA-----AGTEARAVALAEHAGQPGYLAyAGSKEALTVWTRRRAATWLyGAGVRVNTVAPGPVETPil 190

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503301  247 GAFsRLDPTGtfeKEMIGRI--PCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGGEEVLI 307
Cdd:cd05328 191 QAF-LQDPRG---GESVDAFvtPMGRRAEPDEIAPVIAFLASDAASWINGANLFVDGGLDASM 249
PRK07069 PRK07069
short chain dehydrogenase; Validated
 94-302 1.67e-14

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 72.05  E-value: 1.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    94 DVLKATAEQISSQTGNKV-HAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGT 172
Cdd:PRK07069  35 AGLDAFAAEINAAHGEGVaFAAVQDVTDEAQWQALLAQAADAMGGLSVLVNNAGVGSFGAIEQIELDEWRRVMAINVESI 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   173 aFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGM--RFNVIQPGPIKT---KG 247
Cdd:PRK07069 115 -FLGCKHALPYLRASQPASIVNISSVAAFKAEPDYTAYNASKAAVASLTKSIALDCARRGLdvRCNSIHPTFIRTgivDP 193

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 4503301   248 AFSRLDPTGTFEKeMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK07069 194 IFQRLGEEEATRK-LARGVPLGRLGEPDDVAHAVLYLASDESRFVTGAELVIDGG 247
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 101-302 1.69e-14

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 71.87  E-value: 1.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   101 EQISSQTGNKVHAIQCDVRDPDMV----QNTVSELIKVaghpNIVINNAA----GNFIspteRLSPNAWKTITDIVLNGT 172
Cdd:PRK12936  44 EALAAELGERVKIFPANLSDRDEVkalgQKAEADLEGV----DILVNNAGitkdGLFV----RMSDEDWDSVLEVNLTAT 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   173 AFVTLEIGKQLIKAQKGAaFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTkgafSRL 252
Cdd:PRK12936 116 FRLTRELTHPMMRRRYGR-IINITSVVGVTGNPGQANYCASKAGMIGFSKSLAQEIATRNVTVNCVAPGFIES----AMT 190

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 4503301   253 DPTGTFEKEMI-GRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK12936 191 GKLNDKQKEAImGAIPMKRMGTGAEVASAVAYLASSEAAYVTGQTIHVNGG 241
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 59-304 6.51e-14

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 70.45  E-value: 6.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    59 GKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQTGN-KVHAIQCDVRDPDMVQNTVSELIKVAGH 137
Cdd:PRK12384   2 NQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINAEYGEgMAYGFGADATSEQSVLALSRGVDEIFGR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   138 PNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSASAKAGV 217
Cdd:PRK12384  82 VDLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDGIQGRIIQINSKSGKVGSKHNSGYSAAKFGG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   218 EAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRLDPT-----GTFEKEM----IGRIPCGRLGTVEELANLAAFLCSDY 288
Cdd:PRK12384 162 VGLTQSLALDLAEYGITVHSLMLGNLLKSPMFQSLLPQyakklGIKPDEVeqyyIDKVPLKRGCDYQDVLNMLLFYASPK 241

                        250
                 ....*....|....*.
gi 4503301   289 ASWINGAVIKFDGGEE 304
Cdd:PRK12384 242 ASYCTGQSINVTGGQV 257
PRK06947 PRK06947
SDR family oxidoreductase;
98-302 9.29e-14

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 69.83  E-value: 9.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    98 ATAEQISS---QTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAgnFISPTERL---SPNAWKTITDIVLNG 171
Cdd:PRK06947  38 AAAEETADavrAAGGRACVVAGDVANEADVIAMFDAVQSAFGRLDALVNNAG--IVAPSMPLadmDAARLRRMFDTNVLG 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   172 TAFVTLEIGKQLIKAQKGA--AFLSITTIYAETGSGF-VVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGA 248
Cdd:PRK06947 116 AYLCAREAARRLSTDRGGRggAIVNVSSIASRLGSPNeYVDYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEIH 195

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 4503301   249 FSRLDPTGTfeKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK06947 196 ASGGQPGRA--ARLGAQTPLGRAGEADEVAETIVWLLSDAASYVTGALLDVGGG 247
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
116-306 1.33e-13

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 69.74  E-value: 1.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   116 CDVRDPDMVQNTVSELIKVAGHPNIVINNAAgnfISPTERLSPNawktITDIVLNGTAfVTLEIGK----QLIKAQK--- 188
Cdd:PRK07370  66 CDVQDDAQIEETFETIKQKWGKLDILVHCLA---FAGKEELIGD----FSATSREGFA-RALEISAyslaPLCKAAKplm 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   189 --GAAFLSITTIyaetGSGFVVPS----ASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAfsrlDPTGTFeKEM 262
Cdd:PRK07370 138 seGGSIVTLTYL----GGVRAIPNynvmGVAKAALEASVRYLAAELGPKNIRVNAISAGPIRTLAS----SAVGGI-LDM 208

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 4503301   263 IGRI----PCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGGEEVL 306
Cdd:PRK07370 209 IHHVeekaPLRRTVTQTEVGNTAAFLLSDLASGITGQTIYVDAGYCIM 256
PRK08690 PRK08690
enoyl-[acyl-carrier-protein] reductase FabI;
94-305 1.74e-13

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


Pssm-ID: 169553 [Multi-domain]  Cd Length: 261  Bit Score: 69.23  E-value: 1.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    94 DVLKATAEQISSQTGNKVhAIQCDVRDPDMVQNTVSELIK-----------VAGHPNIVInnaAGNFIsptERLSPNAWK 162
Cdd:PRK08690  42 DKLEERVRKMAAELDSEL-VFRCDVASDDEINQVFADLGKhwdgldglvhsIGFAPKEAL---SGDFL---DSISREAFN 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   163 TITDIvlNGTAFVTLEIGKQLIKAQKGAAFLSITTIyaetGSGFVVPSAS----AKAGVEAMSKSLAAEWGKYGMRFNVI 238
Cdd:PRK08690 115 TAHEI--SAYSLPALAKAARPMMRGRNSAIVALSYL----GAVRAIPNYNvmgmAKASLEAGIRFTAACLGKEGIRCNGI 188

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503301   239 QPGPIKTKGAfSRLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGGEEV 305
Cdd:PRK08690 189 SAGPIKTLAA-SGIADFGKLLGHVAAHNPLRRNVTIEEVGNTAAFLLSDLSSGITGEITYVDGGYSI 254
PRK12742 PRK12742
SDR family oxidoreductase;
97-302 2.65e-13

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 68.25  E-value: 2.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    97 KATAEQISSQTGNKvhAIQCDVRDPDMVQNTVSElikvAGHPNI-VINNAAGNFISPTErLSPNAWKTITDIVLNGTAFV 175
Cdd:PRK12742  41 KDAAERLAQETGAT--AVQTDSADRDAVIDVVRK----SGALDIlVVNAGIAVFGDALE-LDADDIDRLFKINIHAPYHA 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   176 TLEIGKQLIKAQKgaaflsITTIYAETGSGFVVPSASA----KAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKgafsr 251
Cdd:PRK12742 114 SVEAARQMPEGGR------IIIIGSVNGDRMPVAGMAAyaasKSALQGMARGLARDFGPRGITINVVQPGPIDTD----- 182

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 4503301   252 LDPTGTFEKEMI-GRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK12742 183 ANPANGPMKDMMhSFMAIKRHGRPEEVAGMVAWLAGPEASFVTGAMHTIDGA 234
PRK09730 PRK09730
SDR family oxidoreductase;
101-302 3.16e-13

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 68.34  E-value: 3.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   101 EQISSQtGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPT-ERLSPNAWKTITDIVLNGTAFVTLEI 179
Cdd:PRK09730  44 NLITQA-GGKAFVLQADISDENQVVAMFTAIDQHDEPLAALVNNAGILFTQCTvENLTAERINRVLSTNVTGYFLCCREA 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   180 GKQLIKAQ--KGAAFLSITTIYAETGS-GFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTK-----GAFSR 251
Cdd:PRK09730 123 VKRMALKHggSGGAIVNVSSAASRLGApGEYVDYAASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEmhasgGEPGR 202

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 4503301   252 LDptgtfekEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK09730 203 VD-------RVKSNIPMQRGGQPEEVAQAIVWLLSDKASYVTGSFIDLAGG 246
PRK06123 PRK06123
SDR family oxidoreductase;
84-302 3.30e-13

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 68.27  E-value: 3.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    84 AQCVIASRKMDVLKATAEQISSQTGNKVhAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAgnFISPTERLSPNAWKT 163
Cdd:PRK06123  28 AVCLNYLRNRDAAEAVVQAIRRQGGEAL-AVAADVADEADVLRLFEAVDRELGRLDALVNNAG--ILEAQMRLEQMDAAR 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   164 ITDIVLN---GTAFVTLEIGKQLIKAQ--KGAAFLSITTIYAETGS-GFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNV 237
Cdd:PRK06123 105 LTRIFATnvvGSFLCAREAVKRMSTRHggRGGAIVNVSSMAARLGSpGEYIDYAASKGAIDTMTIGLAKEVAAEGIRVNA 184

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4503301   238 IQPGPIKTKGAFSRLDPtGTFEKeMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK06123 185 VRPGVIYTEIHASGGEP-GRVDR-VKAGIPMGRGGTAEEVARAILWLLSDEASYTTGTFIDVSGG 247
PRK08628 PRK08628
SDR family oxidoreductase;
78-302 3.56e-13

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 68.45  E-value: 3.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    78 LLSSLGAQCVIASRKMDVLkATAEQISSQTGnKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGN--------- 148
Cdd:PRK08628  26 RLAEEGAIPVIFGRSAPDD-EFAEELRALQP-RAEFVQVDLTDDAQCRDAVEQTVAKFGRIDGLVNNAGVNdgvgleagr 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   149 --FISPTERlspNAWKTitdivlngtaFVTLEIGKQLIKAQKGAaFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAA 226
Cdd:PRK08628 104 eaFVASLER---NLIHY----------YVMAHYCLPHLKASRGA-IVNISSKTALTGQGGTSGYAAAKGAQLALTREWAV 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   227 EWGKYGMRFNVIQPGPIKTKGAFSRLDptgTFE------KEMIGRIPCG-RLGTVEELANLAAFLCSDYASWINGAVIKF 299
Cdd:PRK08628 170 ALAKDGVRVNAVIPAEVMTPLYENWIA---TFDdpeaklAAITAKIPLGhRMTTAEEIADTAVFLLSERSSHTTGQWLFV 246


                 ...
gi 4503301   300 DGG 302
Cdd:PRK08628 247 DGG 249
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 57-280 4.91e-13

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: 68.00  E-value: 4.91e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   57 FQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAG 136
Cdd:cd05332   1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELGAPSPHVVPLDMSDLEDAEQVVEEALKLFG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  137 HPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGaAFLSITTIYAETGSGFVVPSASAKAG 216
Cdd:cd05332  81 GLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQG-SIVVVSSIAGKIGVPFRTAYAASKHA 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503301  217 VEAMSKSLAAEWGKYGMRFNVIQPGPIKTKgaFSRLDPTGTFEKEMIGRIPCGRLGTVEELANL 280
Cdd:cd05332 160 LQGFFDSLRAELSEPNISVTVVCPGLIDTN--IAMNALSGDGSMSAKMDDTTANGMSPEECALE 221
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 78-245 6.90e-13

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: 67.41  E-value: 6.90e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   78 LLSSLGAQCVIASRKMDVLKATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLS 157
Cdd:cd05373  18 RFAAEGFSVALAARREAKLEALLVDIIRDAGGSAKAVPTDARDEDEVIALFDLIEEEIGPLEVLVYNAGANVWFPILETT 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  158 PNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVpSASAKAGVEAMSKSLAAEWGKYGMRF-N 236
Cdd:cd05373  98 PRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASLRGRAGFAA-FAGAKFALRALAQSMARELGPKGIHVaH 176


                ....*....
gi 4503301  237 VIQPGPIKT 245
Cdd:cd05373 177 VIIDGGIDT 185
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 70-245 8.38e-13

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: 66.97  E-value: 8.38e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   70 GLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQTgNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNF 149
Cdd:cd05350   9 GIGRALAREFAKAGYNVALAARRTDRLDELKAELLNPN-PSVEVEILDVTDEERNQLVIAELEAELGGLDLVIINAGVGK 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  150 ISPTERLSPNAWKTITDIVLNGtAFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWG 229
Cdd:cd05350  88 GTSLGDLSFKAFRETIDTNLLG-AAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKAALSSLAESLRYDVK 166

                       170
                ....*....|....*.
gi 4503301  230 KYGMRFNVIQPGPIKT 245
Cdd:cd05350 167 KRGIRVTVINPGFIDT 182
PRK07984 PRK07984
enoyl-ACP reductase FabI;
94-302 8.42e-13

enoyl-ACP reductase FabI;


Pssm-ID: 181187 [Multi-domain]  Cd Length: 262  Bit Score: 67.23  E-value: 8.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    94 DVLKATAEQISSQTGNKVhAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAgnfISPTERLSPNAWKTIT----DIVL 169
Cdd:PRK07984  42 DKLKGRVEEFAAQLGSDI-VLPCDVAEDASIDAMFAELGKVWPKFDGFVHSIG---FAPGDQLDGDYVNAVTregfKIAH 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   170 NGTAFVTLEIGKQLIKA-QKGAAFLSITTIYAETGsgfvVPSAS----AKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIK 244
Cdd:PRK07984 118 DISSYSFVAMAKACRSMlNPGSALLTLSYLGAERA----IPNYNvmglAKASLEANVRYMANAMGPEGVRVNAISAGPIR 193

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4503301   245 TKGAFSRLDptgtFEKeMIGR----IPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK07984 194 TLAASGIKD----FRK-MLAHceavTPIRRTVTIEDVGNSAAFLCSDLSAGISGEVVHVDGG 250
PRK06997 PRK06997
enoyl-[acyl-carrier-protein] reductase FabI;
190-310 1.00e-12

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


Pssm-ID: 180789 [Multi-domain]  Cd Length: 260  Bit Score: 67.15  E-value: 1.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   190 AAFLSITTIYAETgsgfVVPSAS----AKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAfSRLDPTGTFEKEMIGR 265
Cdd:PRK06997 139 ASLLTLSYLGAER----VVPNYNtmglAKASLEASVRYLAVSLGPKGIRANGISAGPIKTLAA-SGIKDFGKILDFVESN 213

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 4503301   266 IPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGGEEVLISGE 310
Cdd:PRK06997 214 APLRRNVTIEEVGNVAAFLLSDLASGVTGEITHVDSGFNAVVGGM 258
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 96-302 1.43e-12

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: 66.15  E-value: 1.43e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   96 LKATAEQIssqtGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFV 175
Cdd:cd05357  41 LKDELNAL----RNSAVLVQADLSDFAACADLVAAAFRAFGRCDVLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLL 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  176 TLEIGKQLIKAQKGaAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYgMRFNVIQPGPIktkgAFSRLDPT 255
Cdd:cd05357 117 IQAFARRLAGSRNG-SIINIIDAMTDRPLTGYFAYCMSKAALEGLTRSAALELAPN-IRVNGIAPGLI----LLPEDMDA 190

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 4503301  256 GTFEkEMIGRIPCGRLGTVEELANLAAFLC-SDYaswINGAVIKFDGG 302
Cdd:cd05357 191 EYRE-NALRKVPLKRRPSAEEIADAVIFLLdSNY---ITGQIIKVDGG 234
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 83-250 2.27e-12

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: 65.76  E-value: 2.27e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   83 GAQCVIASRKMDVLKATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNA---AGnfISPTERLSPN 159
Cdd:cd05346  24 GAKLILTGRRAERLQELADELGAKFPVKVLPLQLDVSDRESIEAALENLPEEFRDIDILVNNAglaLG--LDPAQEADLE 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  160 AWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAF--LSITTIYAETGSGfvVPSASaKAGVEAMSKSLAAEWGKYGMRFNV 237
Cdd:cd05346 102 DWETMIDTNVKGLLNVTRLILPIMIARNQGHIInlGSIAGRYPYAGGN--VYCAT-KAAVRQFSLNLRKDLIGTGIRVTN 178

                       170
                ....*....|...
gi 4503301  238 IQPGPIKTKgaFS 250
Cdd:cd05346 179 IEPGLVETE--FS 189
PRK05717 PRK05717
SDR family oxidoreductase;
59-302 3.06e-12

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 65.68  E-value: 3.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    59 GKVAFITGGGTGLGKGMTTLLSSLGAQCVIAsrkmDVLKATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHP 138
Cdd:PRK05717  10 GRVALVTGAARGIGLGIAAWLIAEGWQVVLA----DLDRERGSKVAKALGENAWFIAMDVADEAQVAAGVAEVLGQFGRL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   139 NIVINNA--AGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLiKAQKGAaFLSITTIYAETGSGFVVPSASAKAG 216
Cdd:PRK05717  86 DALVCNAaiADPHNTTLESLSLAHWNRVLAVNLTGPMLLAKHCAPYL-RAHNGA-IVNLASTRARQSEPDTEAYAASKGG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   217 VEAMSKSLAAEWGKyGMRFNVIQPGPIKTKG-AFSRLDPTGTFEKemiGRIPCGRLGTVEELANLAAFLCSDYASWINGA 295
Cdd:PRK05717 164 LLALTHALAISLGP-EIRVNAVSPGWIDARDpSQRRAEPLSEADH---AQHPAGRVGTVEDVAAMVAWLLSRQAGFVTGQ 239


                 ....*..
gi 4503301   296 VIKFDGG 302
Cdd:PRK05717 240 EFVVDGG 246
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 58-303 3.80e-12

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: 65.56  E-value: 3.80e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   58 QGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGH 137
Cdd:cd05322   1 MNQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAEYGEKAYGFGADATNEQSVIALSKGVDEIFKR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  138 PNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSASAKAGV 217
Cdd:cd05322  81 VDLLVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDGIQGRIIQINSKSGKVGSKHNSGYSAAKFGG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  218 EAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRLDPT-----GTFEKEM----IGRIPCGRLGTVEELANLAAFLCSDY 288
Cdd:cd05322 161 VGLTQSLALDLAEHGITVNSLMLGNLLKSPMFQSLLPQyakklGIKESEVeqyyIDKVPLKRGCDYQDVLNMLLFYASPK 240

                       250
                ....*....|....*
gi 4503301  289 ASWINGAVIKFDGGE 303
Cdd:cd05322 241 ASYCTGQSINITGGQ 255
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 51-267 8.11e-12

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 64.99  E-value: 8.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    51 MLPPNSFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISsqTGNKVHAIQCDVRDPDMVQNTVSE 130
Cdd:PRK05872   1 GPPMTSLAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAELG--GDDRVLTVVADVTDLAAMQAAAEE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   131 LIKVAGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNG---TAFVTLEigkQLIkAQKGaAFLSITTIYAETGSGFV 207
Cdd:PRK05872  79 AVERFGGIDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGvfhTVRATLP---ALI-ERRG-YVLQVSSLAAFAAAPGM 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503301   208 VPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKT---KGAFSRLdPTGtfeKEMIGRIP 267
Cdd:PRK05872 154 AAYCASKAGVEAFANALRLEVAHHGVTVGSAYLSWIDTdlvRDADADL-PAF---RELRARLP 212
PRK06128 PRK06128
SDR family oxidoreductase;
108-302 9.69e-12

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 64.88  E-value: 9.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   108 GNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGN-FISPTERLSPNAWktitDIVLNGTAFVTLEIGKQLIKA 186
Cdd:PRK06128 105 GRKAVALPGDLKDEAFCRQLVERAVKELGGLDILVNIAGKQtAVKDIADITTEQF----DATFKTNVYAMFWLCKAAIPH 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   187 QK-GAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKgafsrLDPTGTFEKEMI-- 263
Cdd:PRK06128 181 LPpGASIINTGSIQSYQPSPTLLDYASTKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTP-----LQPSGGQPPEKIpd 255

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 4503301   264 --GRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK06128 256 fgSETPMKRPGQPVEMAPLYVLLASQESSYVTGEVFGVTGG 296
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 108-302 1.53e-11

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: 63.64  E-value: 1.53e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  108 GNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAgnfISPTER-----LSPNAWKTITDIVLNGTAFVTLEIGKQ 182
Cdd:cd05337  50 GRRAIYFQADIGELSDHEALLDQAWEDFGRLDCLVNNAG---IAVRPRgdlldLTEDSFDRLIAINLRGPFFLTQAVARR 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  183 LIKAQKGAAFLS-----ITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTkgafSRLDPTGT 257
Cdd:cd05337 127 MVEQPDRFDGPHrsiifVTSINAYLVSPNRGEYCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHT----DMTAPVKE 202

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 4503301  258 FEKEMI--GRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:cd05337 203 KYDELIaaGLVPIRRWGQPEDIAKAVRTLASGLLPYSTGQPINIDGG 249
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
88-302 1.70e-11

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 63.59  E-value: 1.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    88 IASRKMDVLKATAEQISSQTGNKVhAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAWKTITDI 167
Cdd:PRK08643  31 IVDYNEETAQAAADKLSKDGGKAI-AVKADVSDRDQVFAAVRQVVDTFGDLNVVVNNAGVAPTTPIETITEEQFDKVYNI 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   168 VLNGT---------AFVTLEIGKQLIKAQKGAAflsittiyAETGSGFVVPSASaKAGVEAMSKSLAAEWGKYGMRFNVI 238
Cdd:PRK08643 110 NVGGViwgiqaaqeAFKKLGHGGKIINATSQAG--------VVGNPELAVYSST-KFAVRGLTQTAARDLASEGITVNAY 180

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4503301   239 QPGPIKT--------KGAFSRLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK08643 181 APGIVKTpmmfdiahQVGENAGKPDEWGMEQFAKDITLGRLSEPEDVANCVSFLAGPDSDYITGQTIIVDGG 252
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 54-302 1.72e-11

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 63.43  E-value: 1.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    54 PNSFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISsqTGNKVHAIQCDVRDPDMVQNTVSELIK 133
Cdd:PRK12823   3 NQRFAGKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRSELVHEVAAELRA--AGGEALALTADLETYAGAQAAMAAAVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   134 VAGHPNIVINNAAGnfispTERLSPNAWKTITDIV--LNGTAFVTL----EIGKQLIKAQKGaAFLSITTIyaETGSGFV 207
Cdd:PRK12823  81 AFGRIDVLINNVGG-----TIWAKPFEEYEEEQIEaeIRRSLFPTLwccrAVLPHMLAQGGG-AIVNVSSI--ATRGINR 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   208 VPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKtkgAFSRLDPTGTF-----EKEMIGRI--------PCGRLGTV 274
Cdd:PRK12823 153 VPYSAAKGGVNALTASLAFEYAEHGIRVNAVAPGGTE---APPRRVPRNAApqseqEKAWYQQIvdqtldssLMKRYGTI 229

                        250       260
                 ....*....|....*....|....*...
gi 4503301   275 EELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK12823 230 DEQVAAILFLASDEASYITGTVLPVGGG 257
PRK06079 PRK06079
enoyl-[acyl-carrier-protein] reductase FabI;
83-302 1.82e-11

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


Pssm-ID: 235694 [Multi-domain]  Cd Length: 252  Bit Score: 63.20  E-value: 1.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    83 GAQcVIASRKMDVLKataEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAgnfISPTERLSPNawk 162
Cdd:PRK06079  33 GAT-VIYTYQNDRMK---KSLQKLVDEEDLLVECDVASDESIERAFATIKERVGKIDGIVHAIA---YAKKEELGGN--- 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   163 tITDIVLNGTAFVTLEIGKQLIKAQKGAAFL-----SITTIyAETGSGFVVPSAS----AKAGVEAMSKSLAAEWGKYGM 233
Cdd:PRK06079 103 -VTDTSRDGYALAQDISAYSLIAVAKYARPLlnpgaSIVTL-TYFGSERAIPNYNvmgiAKAALESSVRYLARDLGKKGI 180

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4503301   234 RFNVIQPGPIKTKgAFSRLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK06079 181 RVNAISAGAVKTL-AVTGIKGHKDLLKESDSRTVDGVGVTIEEVGNTAAFLLSDLSTGVTGDIIYVDKG 248
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 60-302 1.94e-11

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 63.44  E-value: 1.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    60 KVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPN 139
Cdd:PRK12745   3 PVALVTGGRRGIGLGIARALAAAGFDLAINDRPDDEELAATQQELRALGVEVIFFPADVADLSAHEAMLDAAQAAWGRID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   140 IVINNAAgnfISPTER-----LSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFL--SITTIyAETGSGFVVPSAS 212
Cdd:PRK12745  83 CLVNNAG---VGVKVRgdlldLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEPEELPhrSIVFV-SSVNAIMVSPNRG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   213 ----AKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIK---TKGAFSRLDptGTFEKemiGRIPCGRLGTVEELANLAAFLC 285
Cdd:PRK12745 159 eyciSKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKtdmTAPVTAKYD--ALIAK---GLVPMPRWGEPEDVARAVAALA 233

                        250
                 ....*....|....*..
gi 4503301   286 SDYASWINGAVIKFDGG 302
Cdd:PRK12745 234 SGDLPYSTGQAIHVDGG 250
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 79-245 2.50e-11

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: 62.64  E-value: 2.50e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   79 LSSLGAQCVIASRKMDVLKATAEQISsQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAA---GNFISPTER 155
Cdd:cd05339  19 FAKRGAKVVILDINEKGAEETANNVR-KAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTILINNAGvvsGKKLLELPD 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  156 lsPNAWKTItDIVLNGTAFVTLEIGKQLIKAQKGaAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAE---WGKYG 232
Cdd:cd05339  98 --EEIEKTF-EVNTLAHFWTTKAFLPDMLERNHG-HIVTIASVAGLISPAGLADYCASKAAAVGFHESLRLElkaYGKPG 173

                       170
                ....*....|...
gi 4503301  233 MRFNVIQPGPIKT 245
Cdd:cd05339 174 IKTTLVCPYFINT 186
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
113-302 3.29e-11

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 62.72  E-value: 3.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   113 AIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTleigKQLIK--AQKG- 189
Cdd:PRK12938  57 ASEGNVGDWDSTKAAFDKVKAEVGEIDVLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVT----KQVIDgmVERGw 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   190 AAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFS-RLDptgTFEKeMIGRIPC 268
Cdd:PRK12938 133 GRIINISSVNGQKGQFGQTNYSTAKAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDMVKAiRPD---VLEK-IVATIPV 208

                        170       180       190
                 ....*....|....*....|....*....|....
gi 4503301   269 GRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK12938 209 RRLGSPDEIGSIVAWLASEESGFSTGADFSLNGG 242
PRK07454 PRK07454
SDR family oxidoreductase;
90-245 3.97e-11

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 62.28  E-value: 3.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    90 SRKMDVLKATAEQISSqTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAWKTITDIVL 169
Cdd:PRK07454  37 ARSQDALEALAAELRS-TGVKAAAYSIDLSNPEAIAPGIAELLEQFGCPDVLINNAGMAYTGPLLEMPLSDWQWVIQLNL 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   170 NGTAFVTLEIGKQLiKAQKGAAFLSITTIYAETgsgfVVPSASA----KAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKT 245
Cdd:PRK07454 116 TSVFQCCSAVLPGM-RARGGGLIINVSSIAARN----AFPQWGAycvsKAALAAFTKCLAEEERSHGIRVCTITLGAVNT 190
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
94-327 5.60e-11

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


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 62.07  E-value: 5.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    94 DVLKATAEQISSQTGNKvHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAgnfISPTERLSP---NAWKTITDIVLN 170
Cdd:PRK08415  41 EALKKRVEPIAQELGSD-YVYELDVSKPEHFKSLAESLKKDLGKIDFIVHSVA---FAPKEALEGsflETSKEAFNIAME 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   171 GTAFVTLEIGKQLIKA-QKGAAFLSITTIyaetGSGFVVPSAS----AKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKT 245
Cdd:PRK08415 117 ISVYSLIELTRALLPLlNDGASVLTLSYL----GGVKYVPHYNvmgvAKAALESSVRYLAVDLGKKGIRVNAISAGPIKT 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   246 KGAfsrldpTGTFEKEMIGR-----IPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGGEEVLISG--EFNDLRKvT 318
Cdd:PRK08415 193 LAA------SGIGDFRMILKwneinAPLKKNVSIEEVGNSGMYLLSDLSSGVTGEIHYVDAGYNIMGMGavEKEEDGK-T 265


                 ....*....
gi 4503301   319 KEQWDTIEE 327
Cdd:PRK08415 266 VLAWDLQKE 274
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 78-245 5.70e-11

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: 61.37  E-value: 5.70e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   78 LLSSLGAQCVIASRKmdvlKATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLS 157
Cdd:cd08929  19 LLHAEGYRVGICARD----EARLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEAFGGLDALVNNAGVGVMKPVEELT 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  158 PNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAaflsITTIYAETG----SGFVVPSASaKAGVEAMSKSLAAEWGKYGM 233
Cdd:cd08929  95 PEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGT----IVNVGSLAGknafKGGAAYNAS-KFGLLGLSEAAMLDLREANI 169

                       170
                ....*....|..
gi 4503301  234 RFNVIQPGPIKT 245
Cdd:cd08929 170 RVVNVMPGSVDT 181
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 83-302 1.13e-10

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 60.93  E-value: 1.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    83 GAQCVIASRKMDVLKATAEQISSQtgNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSpnawk 162
Cdd:PRK05786  29 GAQVCINSRNENKLKRMKKTLSKY--GNIHYVVGDVSSTESARNVIEKAAKVLNAIDGLVVTVGGYVEDTVEEFS----- 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   163 TITDIVLNGTAFVTLEIGKQLIKAQKGAaflSITTIYAETGSGFVVPS----ASAKAGVEAMSKSLAAEWGKYGMRFNVI 238
Cdd:PRK05786 102 GLEEMLTNHIKIPLYAVNASLRFLKEGS---SIVLVSSMSGIYKASPDqlsyAVAKAGLAKAVEILASELLGRGIRVNGI 178

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503301   239 QPGPIktkgafsrldpTGTFEKEMIGRIPcGRLGTV----EELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK05786 179 APTTI-----------SGDFEPERNWKKL-RKLGDDmappEDFAKVIIWLLTDEADWVDGVVIPVDGG 234
PRK05855 PRK05855
SDR family oxidoreductase;
53-245 2.14e-10

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 61.54  E-value: 2.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    53 PPNSFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQIsSQTGNKVHAIQCDVRDPDMVQNTVSELI 132
Cdd:PRK05855 309 PRGPFSGKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAELI-RAAGAVAHAYRVDVSDADAMEAFAEWVR 387

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   133 KVAGHPNIVINNA----AGNFISPTERlspnAWKTITDI----VLNGT-AFvtleiGKQLIKAQKGAAFLSITTIYAETG 203
Cdd:PRK05855 388 AEHGVPDIVVNNAgigmAGGFLDTSAE----DWDRVLDVnlwgVIHGCrLF-----GRQMVERGTGGHIVNVASAAAYAP 458

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 4503301   204 SGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKT 245
Cdd:PRK05855 459 SRSLPAYATSKAAVLMLSECLRAELAAAGIGVTAICPGFVDT 500
PRK05650 PRK05650
SDR family oxidoreductase;
83-266 2.71e-10

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 60.05  E-value: 2.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    83 GAQCVIASRKMDVLKATAEQISSQtGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINN---AAGNFIsptERLSPN 159
Cdd:PRK05650  24 GWRLALADVNEEGGEETLKLLREA-GGDGFYQRCDVRDYSQLTALAQACEEKWGGIDVIVNNagvASGGFF---EELSLE 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   160 AWKTITDIVLNGT-----AFVTleigkqLIKAQKGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMR 234
Cdd:PRK05650 100 DWDWQIAINLMGVvkgckAFLP------LFKRQKSGRIVNIASMAGLMQGPAMSSYNVAKAGVVALSETLLVELADDEIG 173

                        170       180       190
                 ....*....|....*....|....*....|..
gi 4503301   235 FNVIQPGPIKTKGAFSRLDPTGTFeKEMIGRI 266
Cdd:PRK05650 174 VHVVCPSFFQTNLLDSFRGPNPAM-KAQVGKL 204
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 106-302 3.76e-10

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 59.51  E-value: 3.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   106 QTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINnAAGNF-ISPTERLSPNAWKTItdivLNGTAFVTLEIGKQLI 184
Cdd:PRK08220  45 QEDYPFATFVLDVSDAAAVAQVCQRLLAETGPLDVLVN-AAGILrMGATDSLSDEDWQQT----FAVNAGGAFNLFRAVM 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   185 ---KAQKGAAFLSITTIYAEtgsgfvVP-------SASaKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTkgAFSRL-- 252
Cdd:PRK08220 120 pqfRRQRSGAIVTVGSNAAH------VPrigmaayGAS-KAALTSLAKCVGLELAPYGVRCNVVSPGSTDT--DMQRTlw 190

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   253 -DPTGtfEKEMI---------GrIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK08220 191 vDEDG--EQQVIagfpeqfklG-IPLGKIARPQEIANAVLFLASDLASHITLQDIVVDGG 247
PLN02730 PLN02730
enoyl-[acyl-carrier-protein] reductase
 188-302 4.02e-10

enoyl-[acyl-carrier-protein] reductase


Pssm-ID: 178331 [Multi-domain]  Cd Length: 303  Bit Score: 59.79  E-value: 4.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   188 KGAAFLSITTIYAETgsgfVVPS-----ASAKAGVEAMSKSLAAEWG-KYGMRFNVIQPGPIKTKGAfsrlDPTGtFEKE 261
Cdd:PLN02730 170 PGGASISLTYIASER----IIPGygggmSSAKAALESDTRVLAFEAGrKYKIRVNTISAGPLGSRAA----KAIG-FIDD 240

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 4503301   262 MI----GRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PLN02730 241 MIeysyANAPLQKELTADEVGNAAAFLASPLASAITGATIYVDNG 285
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 57-224 4.47e-10

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: 59.02  E-value: 4.47e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   57 FQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSqtgnkVHAIQCDVRDPDMVQNTVSELIkvAG 136
Cdd:COG3967   3 LTGNTILITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEAAAANPG-----LHTIVLDVADPASIAALAEQVT--AE 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  137 HP--NIVINNAAgnfISPTERLS--PNAWKTITDIV---LNGT-----AFVTleigkqLIKAQKGAAFLSITTIYAetgs 204
Cdd:COG3967  76 FPdlNVLINNAG---IMRAEDLLdeAEDLADAEREIttnLLGPirltaAFLP------HLKAQPEAAIVNVSSGLA---- 142

                       170       180
                ....*....|....*....|....*.
gi 4503301  205 gfVVPSASA------KAGVEAMSKSL 224
Cdd:COG3967 143 --FVPLAVTptysatKAALHSYTQSL 166
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 60-302 4.90e-10

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


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 58.85  E-value: 4.90e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   60 KVAFITGGGTGLGKGMTTLLSSLGAQCVIASRkMDVLKATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPN 139
Cdd:cd05323   1 KVAIITGGASGIGLATAKLLLKKGAKVAILDR-NENPGAAAELQAINPKVKATFVQCDVTSWEQLAAAFKKAIEKFGRVD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  140 IVINNAAGN---FISPTERLSPNaWKTITDIVLNGTAFVTLEIGKQLIKAQ--KGAAFLSITTIYA-ETGSGFVVPSASa 213
Cdd:cd05323  80 ILINNAGILdekSYLFAGKLPPP-WEKTIDVNLTGVINTTYLALHYMDKNKggKGGVIVNIGSVAGlYPAPQFPVYSAS- 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  214 KAGVEAMSKSLA-AEWGKYGMRFNVIQPGPIKTkgafSRLDPTGTFEKEMIGRIPCgrlGTVEELANLAAFLCSDYASwi 292
Cdd:cd05323 158 KHGVVGFTRSLAdLLEYKTGVRVNAICPGFTNT----PLLPDLVAKEAEMLPSAPT---QSPEVVAKAIVYLIEDDEK-- 228

                       250
                ....*....|
gi 4503301  293 NGAVIKFDGG 302
Cdd:cd05323 229 NGAIWIVDGG 238
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 184-302 5.16e-10

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: 59.13  E-value: 5.16e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  184 IKAQKGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFsrldPTGTFE---- 259
Cdd:cd05361 119 MKKAGGGSIIFITSAVPKKPLAYNSLYGPARAAAVALAESLAKELSRDNILVYAIGPNFFNSPTYF----PTSDWEnnpe 194

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 4503301  260 -KEMIGR-IPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:cd05361 195 lRERVKRdVPLGRLGRPDEMGALVAFLASRRADPITGQFFAFAGG 239
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 83-245 5.16e-10

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: 58.74  E-value: 5.16e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   83 GAQCVIASRKMDVLKATAEQISSQTGNKVHAIQCDVRD--PDMVQNTVSELIKVAGHPNIVINNAAGNF-ISPTERLSPN 159
Cdd:cd05340  28 GATVILLGRNEEKLRQVADHINEEGGRQPQWFILDLLTctSENCQQLAQRIAVNYPRLDGVLHNAGLLGdVCPLSEQNPQ 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  160 AWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFLSITTIyAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQ 239
Cdd:cd05340 108 VWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSV-GRQGRANWGAYAVSKFATEGL*QVLADEYQQRNLRVNCIN 186


                ....*.
gi 4503301  240 PGPIKT 245
Cdd:cd05340 187 PGGTRT 192
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
228-302 6.38e-10

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 58.47  E-value: 6.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   228 WGKYGMRFNVIQPGPIKTK--GAF------SRLDPTGTfekemigriPCGRLGTVEELANLAAFLCSDYASWINGAVIKF 299
Cdd:PRK12428 156 FGARGIRVNCVAPGPVFTPilGDFrsmlgqERVDSDAK---------RMGRPATADEQAAVLVFLCSDAARWINGVNLPV 226


                 ...
gi 4503301   300 DGG 302
Cdd:PRK12428 227 DGG 229
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 83-245 8.12e-10

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 58.90  E-value: 8.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    83 GAQCVIASRKMDVLKATAEQIssqtGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAWK 162
Cdd:PRK08263  27 GDRVVATARDTATLADLAEKY----GDRLLPLALDVTDRAAVFAAVETAVEHFGRLDIVVNNAGYGLFGMIEEVTESEAR 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   163 TITDIVLNGTAFVTleigkQ----LIKAQKGAAFLSITTIyaETGSGFvvPS----ASAKAGVEAMSKSLAAEWGKYGMR 234
Cdd:PRK08263 103 AQIDTNFFGALWVT-----QavlpYLREQRSGHIIQISSI--GGISAF--PMsgiyHASKWALEGMSEALAQEVAEFGIK 173

                        170
                 ....*....|.
gi 4503301   235 FNVIQPGPIKT 245
Cdd:PRK08263 174 VTLVEPGGYST 184
PRK05866 PRK05866
SDR family oxidoreductase;
50-232 8.45e-10

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 58.98  E-value: 8.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    50 AMLPPNSFQ--------------GKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSqTGNKVHAIQ 115
Cdd:PRK05866  17 GMRPPISPQllinrpprqpvdltGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITR-AGGDAMAVP 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   116 CDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERlSPNAWKTIT-DIVLN--GTAFVTLEIGKQLIKAQKGaAF 192
Cdd:PRK05866  96 CDLSDLDAVDALVADVEKRIGGVDILINNAGRSIRRPLAE-SLDRWHDVErTMVLNyyAPLRLIRGLAPGMLERGDG-HI 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 4503301   193 LSITT--IYAETGSGFVVPSASaKAGVEAMSKSLAAEWGKYG 232
Cdd:PRK05866 174 INVATwgVLSEASPLFSVYNAS-KAALSAVSRVIETEWGDRG 214
PRK12744 PRK12744
SDR family oxidoreductase;
56-302 1.97e-09

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 57.44  E-value: 1.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    56 SFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQ---TGNKVHAIQCDVRDPDMVQNTVSELI 132
Cdd:PRK12744   5 SLKGKVVLIAGGAKNLGGLIARDLAAQGAKAVAIHYNSAASKADAEETVAAvkaAGAKAVAFQADLTTAAAVEKLFDDAK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   133 KVAGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLikaQKGAAFLSITTIYAETGSGFVVPSAS 212
Cdd:PRK12744  85 AAFGRPDIAINTVGKVLKKPIVEISEAEYDEMFAVNSKSAFFFIKEAGRHL---NDNGKIVTLVTSLLGAFTPFYSAYAG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   213 AKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRLDPTGT-FEKE--MIGRIPCGRLGTVEELANLAAFLCSDyA 289
Cdd:PRK12744 162 SKAPVEHFTRAASKEFGARGISVTAVGPGPMDTPFFYPQEGAEAVaYHKTaaALSPFSKTGLTDIEDIVPFIRFLVTD-G 240

                        250
                 ....*....|...
gi 4503301   290 SWINGAVIKFDGG 302
Cdd:PRK12744 241 WWITGQTILINGG 253
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 78-297 2.23e-09

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: 56.60  E-value: 2.23e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   78 LLSSLGAQCVIASRKMDVLKATaeqisSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLS 157
Cdd:cd08932  19 ALARDGYRVSLGLRNPEDLAAL-----SASGGDVEAVPYDARDPEDARALVDALRDRFGRIDVLVHNAGIGRPTTLREGS 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  158 PNAWKTITDIvlngTAFVTLEIGKQLIKAQKGAAflSITTIYAETGSG-FVVPSASA----KAGVEAMSKSLAAEWGKYG 232
Cdd:cd08932  94 DAELEAHFSI----NVIAPAELTRALLPALREAG--SGRVVFLNSLSGkRVLAGNAGysasKFALRALAHALRQEGWDHG 167

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503301  233 MRFNVIQPGPIKTKGAfsrldptgtfEKEM-IGRIPCGRLGTVEELANLAAFLCSDYASWINGAVI 297
Cdd:cd08932 168 VRVSAVCPGFVDTPMA----------QGLTlVGAFPPEEMIQPKDIANLVRMVIELPENITSVAVL 223
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 83-253 2.32e-09

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: 57.01  E-value: 2.32e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   83 GAQCVIASRKMDVLKATAEQISsQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAWK 162
Cdd:cd05360  24 GAKVVLAARSAEALHELAREVR-ELGGEAIAVVADVADAAQVERAADTAVERFGRIDTWVNNAGVAVFGRFEDVTPEEFR 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  163 TITDIVLNGTAFVTLEIGKQLIKAQKGaAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNV--IQP 240
Cdd:cd05360 103 RVFDVNYLGHVYGTLAALPHLRRRGGG-ALINVGSLLGYRSAPLQAAYSASKHAVRGFTESLRAELAHDGAPISVtlVQP 181

                       170
                ....*....|....*.
gi 4503301  241 GPIKTKG---AFSRLD 253
Cdd:cd05360 182 TAMNTPFfghARSYMG 197
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 92-271 2.35e-09

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: 57.08  E-value: 2.35e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   92 KMDVLKATAEQISSQTgnkVHAIQCDVRDPDMVQNTVSELikVAGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNG 171
Cdd:cd09806  39 KKGRLWEAAGALAGGT---LETLQLDVCDSKSVAAAVERV--TERHVDVLVCNAGVGLLGPLEALSEDAMASVFDVNVFG 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  172 TAFVTLEIGKQLIKAQKGaAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKgafsr 251
Cdd:cd09806 114 TVRMLQAFLPDMKRRGSG-RILVTSSVGGLQGLPFNDVYCASKFALEGLCESLAVQLLPFNVHLSLIECGPVHTA----- 187

                       170       180
                ....*....|....*....|
gi 4503301  252 ldptgtFEKEMIGRIPCGRL 271
Cdd:cd09806 188 ------FMEKVLGSPEEVLD 201
PRK06300 PRK06300
enoyl-(acyl carrier protein) reductase; Provisional
 189-306 5.19e-09

enoyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 235776 [Multi-domain]  Cd Length: 299  Bit Score: 56.36  E-value: 5.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   189 GAAFLSITTIYAETgsgfVVPS-----ASAKAGVEAMSKSLAAEWG-KYGMRFNVIQPGPIKtkgafSRLDPTGTFEKEM 262
Cdd:PRK06300 170 GGSTISLTYLASMR----AVPGygggmSSAKAALESDTKVLAWEAGrRWGIRVNTISAGPLA-----SRAGKAIGFIERM 240

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 4503301   263 I----GRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGGEEVL 306
Cdd:PRK06300 241 VdyyqDWAPLPEPMEAEQVGAAAAFLVSPLASAITGETLYVDHGANVM 288
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 59-302 5.19e-09

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


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 56.14  E-value: 5.19e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   59 GKVAFITGGGTGLGKGMTTLLSSLGAQCVIasrkMDVLKATAEQIsSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHP 138
Cdd:cd05371   2 GLVAVVTGGASGLGLATVERLLAQGAKVVI----LDLPNSPGETV-AKLGDNCRFVPVDVTSEKDVKAALALAKAKFGRL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  139 NIVInNAAGnfISPTERL---------SPNAWKTITDIVLNGTAFVT----LEIGKQ--LIKAQKG--------AAFlsi 195
Cdd:cd05371  77 DIVV-NCAG--IAVAAKTynkkgqqphSLELFQRVINVNLIGTFNVIrlaaGAMGKNepDQGGERGviintasvAAF--- 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  196 ttiyaETGSGFVVPSASaKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRLDPTGTFEKEMIgrIPCGRLGTVE 275
Cdd:cd05371 151 -----EGQIGQAAYSAS-KGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLAGLPEKVRDFLAKQV--PFPSRLGDPA 222

                       250       260
                ....*....|....*....|....*..
gi 4503301  276 ELANLAAFLCSDyaSWINGAVIKFDGG 302
Cdd:cd05371 223 EYAHLVQHIIEN--PYLNGEVIRLDGA 247
PRK07985 PRK07985
SDR family oxidoreductase;
188-305 5.77e-09

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 56.54  E-value: 5.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   188 KGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKgafsrLDPTGTFEKEMI---- 263
Cdd:PRK07985 177 KGASIITTSSIQAYQPSPHLLDYAATKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTA-----LQISGGQTQDKIpqfg 251

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 4503301   264 GRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGGEEV 305
Cdd:PRK07985 252 QQTPMKRAGQPAELAPVYVYLASQESSYVTAEVHGVCGGEHL 293
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 139-284 7.16e-09

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


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 54.83  E-value: 7.16e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  139 NIVINNAAGNFISPTERLSPNAWKTITDIVLNGTaFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSASAKAGVE 218
Cdd:cd02266  33 DVVVHNAAILDDGRLIDLTGSRIERAIRANVVGT-RRLLEAARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAALD 111

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503301  219 AMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRLdptGTFEKEMIGRIPCGRLGTVEELANLAAFL 284
Cdd:cd02266 112 GLAQQWASEGWGNGLPATAVACGTWAGSGMAKGP---VAPEEILGNRRHGVRTMPPEEVARALLNA 174
PRK07041 PRK07041
SDR family oxidoreductase;
81-302 7.61e-09

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 55.43  E-value: 7.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    81 SLGAQCVIASRKMDVLKATAEQIssQTGNKVHAIQCDVRDPDMVQNTVSElikvAGHPNIVINNAAGNFISPTERLSPNA 160
Cdd:PRK07041  19 AEGARVTIASRSRDRLAAAARAL--GGGAPVRTAALDITDEAAVDAFFAE----AGPFDHVVITAADTPGGPVRALPLAA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   161 WKTITDIVLNGTAFVTleigkqliKAQKGAAFLSITTIyaetgSGF--VVPSASA------KAGVEAMSKSLAAEWGKyg 232
Cdd:PRK07041  93 AQAAMDSKFWGAYRVA--------RAARIAPGGSLTFV-----SGFaaVRPSASGvlqgaiNAALEALARGLALELAP-- 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503301   233 MRFNVIQPGPIKTKgAFSRLDPTG---TFEKeMIGRIPCGRLGTVEELANLAAFLCSDyaSWINGAVIKFDGG 302
Cdd:PRK07041 158 VRVNTVSPGLVDTP-LWSKLAGDAreaMFAA-AAERLPARRVGQPEDVANAILFLAAN--GFTTGSTVLVDGG 226
PRK08159 PRK08159
enoyl-[acyl-carrier-protein] reductase FabI;
94-306 8.55e-09

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


Pssm-ID: 181260 [Multi-domain]  Cd Length: 272  Bit Score: 55.53  E-value: 8.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    94 DVLKATAEQISSQTGNKVhAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAA--------GNFISPTERlspNAWKTIT 165
Cdd:PRK08159  46 DALKKRVEPLAAELGAFV-AGHCDVTDEASIDAVFETLEKKWGKLDFVVHAIGfsdkdeltGRYVDTSRD---NFTMTMD 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   166 DIVLNGTAFVTleigkqliKAQK----GAAFLSITTIYAETgsgfVVPSAS----AKAGVEAMSKSLAAEWGKYGMRFNV 237
Cdd:PRK08159 122 ISVYSFTAVAQ--------RAEKlmtdGGSILTLTYYGAEK----VMPHYNvmgvAKAALEASVKYLAVDLGPKNIRVNA 189

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4503301   238 IQPGPIKTKGAfsrlDPTGTFE---KEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGGEEVL 306
Cdd:PRK08159 190 ISAGPIKTLAA----SGIGDFRyilKWNEYNAPLRRTVTIEEVGDSALYLLSDLSRGVTGEVHHVDSGYHVV 257
PRK07775 PRK07775
SDR family oxidoreductase;
79-245 9.23e-09

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 55.53  E-value: 9.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    79 LSSLGAQCVIASRKMDVLKATAEQISSQTGNKVhAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSP 158
Cdd:PRK07775  30 LAAAGFPVALGARRVEKCEELVDKIRADGGEAV-AFPLDVTDPDSVKSFVAQAEEALGEIEVLVSGAGDTYFGKLHEIST 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   159 NAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAaFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVI 238
Cdd:PRK07775 109 EQFESQVQIHLVGANRLATAVLPGMIERRRGD-LIFVGSDVALRQRPHMGAYGAAKAGLEAMVTNLQMELEGTGVRASIV 187


                 ....*..
gi 4503301   239 QPGPIKT 245
Cdd:PRK07775 188 HPGPTLT 194
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 114-246 9.82e-09

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 55.29  E-value: 9.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   114 IQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLiKAQKGAAFL 193
Cdd:PRK06179  50 LELDVTDDASVQAAVDEVIARAGRIDVLVNNAGVGLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHM-RAQGSGRII 128

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 4503301   194 SITTIYaetgsGFvVPS------ASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTK 246
Cdd:PRK06179 129 NISSVL-----GF-LPApymalyAASKHAVEGYSESLDHEVRQFGIRVSLVEPAYTKTN 181
PRK06505 PRK06505
enoyl-[acyl-carrier-protein] reductase FabI;
186-321 2.44e-08

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


Pssm-ID: 180596 [Multi-domain]  Cd Length: 271  Bit Score: 54.37  E-value: 2.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   186 AQKGAAFLS-----ITTIYAetGSGFVVPSAS----AKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRLDPTG 256
Cdd:PRK06505 128 AKRAAKLMPdggsmLTLTYG--GSTRVMPNYNvmgvAKAALEASVRYLAADYGPQGIRVNAISAGPVRTLAGAGIGDARA 205

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4503301   257 TFEKEMiGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGGEEVLISGEFNDLRKVTKEQ 321
Cdd:PRK06505 206 IFSYQQ-RNSPLRRTVTIDEVGGSALYLLSDLSSGVTGEIHFVDSGYNIVSMPTLEELKSSDEER 269
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 59-245 4.08e-08

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: 53.60  E-value: 4.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   59 GKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDV-LKATAEQIsSQTGNKVHAIQCDVRDPDMVQNTVSELIK-VAG 136
Cdd:cd09763   3 GKIALVTGASRGIGRGIALQLGEAGATVYITGRTILPqLPGTAEEI-EARGGKCIPVRCDHSDDDEVEALFERVAReQQG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  137 HPNIVINNAAG-------NFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAfLSITTIYAETGSgFVVP 209
Cdd:cd09763  82 RLDILVNNAYAavqlilvGVAKPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAGKGLI-VIISSTGGLEYL-FNVA 159

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 4503301  210 SASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKT 245
Cdd:cd09763 160 YGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRT 195
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 55-246 4.82e-08

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 53.42  E-value: 4.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    55 NSFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQtGNKVHAIQCDVRDPDMVQNTVSELIKV 134
Cdd:PRK05876   2 DGFPGRGAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLRAE-GFDVHGVMCDVRHREEVTHLADEAFRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   135 AGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGaAFLSITTIYAEtgsgfVVPSAS-- 212
Cdd:PRK05876  81 LGHVDVVFSNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEQGTG-GHVVFTASFAG-----LVPNAGlg 154

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 4503301   213 ----AKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTK 246
Cdd:PRK05876 155 aygvAKYGVVGLAETLAREVTADGIGVSVLCPMVVETN 192
PRK12746 PRK12746
SDR family oxidoreductase;
56-302 8.25e-08

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 52.73  E-value: 8.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    56 SFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIA-SRKMDVLKATAEQISSQTGnKVHAIQCDVRDPDMVQNTVSEL--- 131
Cdd:PRK12746   3 NLDGKVALVTGASRGIGRAIAMRLANDGALVAIHyGRNKQAADETIREIESNGG-KAFLIEADLNSIDGVKKLVEQLkne 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   132 --IKVA-GHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVtLEIGKQLIKAQkgAAFLSITTIYAETGSGFVV 208
Cdd:PRK12746  82 lqIRVGtSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFL-IQQTLPLLRAE--GRVINISSAEVRLGFTGSI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   209 PSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRLDPTgTFEKEMIGRIPCGRLGTVEELANLAAFLCSDY 288
Cdd:PRK12746 159 AYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDINAKLLDDP-EIRNFATNSSVFGRIGQVEDIADAVAFLASSD 237

                        250
                 ....*....|....
gi 4503301   289 ASWINGAVIKFDGG 302
Cdd:PRK12746 238 SRWVTGQIIDVSGG 251
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 213-302 9.21e-08

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: 52.62  E-value: 9.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    213 AKAGVEAMSKSLAAEWGKYGMRFNVIQPGpiktkgaFSRLDPTGTFE--KEMIGRIPCG-RLGTVEELANLAAFLCSDYA 289
Cdd:TIGR02685 176 AKHALEGLTRSAALELAPLQIRVNGVAPG-------LSLLPDAMPFEvqEDYRRKVPLGqREASAEQIADVVIFLVSPKA 248

                          90
                  ....*....|...
gi 4503301    290 SWINGAVIKFDGG 302
Cdd:TIGR02685 249 KYITGTCIKVDGG 261
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 57-302 1.44e-07

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 52.00  E-value: 1.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    57 FQGKVAFITGGGTGLGKGMTTLLSSLGAQCVI--ASRKMDVlKATAEQISSQtGNKVHAIQCDVRDPDMVQNTVS----E 130
Cdd:PRK12747   2 LKGKVALVTGASRGIGRAIAKRLANDGALVAIhyGNRKEEA-EETVYEIQSN-GGSAFSIGANLESLHGVEALYSsldnE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   131 LIKVAGHP--NIVINNAA---GNFIsptERLSPNAWKTITDIVLNGTAFVtleIGKQLIKAQKGAAFLSITTIYAETGSG 205
Cdd:PRK12747  80 LQNRTGSTkfDILINNAGigpGAFI---EETTEQFFDRMVSVNAKAPFFI---IQQALSRLRDNSRIINISSAATRISLP 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   206 FVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRL-DPTGTFEKEMIGRIpcGRLGTVEELANLAAFL 284
Cdd:PRK12747 154 DFIAYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMNAELLsDPMMKQYATTISAF--NRLGEVEDIADTAAFL 231

                        250
                 ....*....|....*...
gi 4503301   285 CSDYASWINGAVIKFDGG 302
Cdd:PRK12747 232 ASPDSRWVTGQLIDVSGG 249
PRK07201 PRK07201
SDR family oxidoreductase;
83-145 1.59e-07

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 52.65  E-value: 1.59e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503301    83 GAQCVIASRKMDVLKATAEQISSQtGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNA 145
Cdd:PRK07201 395 GATVFLVARNGEALDELVAEIRAK-GGTAHAYTCDLTDSAAVDHTVKDILAEHGHVDYLVNNA 456
PRK07889 PRK07889
enoyl-[acyl-carrier-protein] reductase FabI;
213-302 7.35e-07

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


Pssm-ID: 236124 [Multi-domain]  Cd Length: 256  Bit Score: 49.55  E-value: 7.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   213 AKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSrLDPTGTFEKEMIGRIPCG-RLGTVEELANLAAFLCSDYASW 291
Cdd:PRK07889 161 AKAALESTNRYLARDLGPRGIRVNLVAAGPIRTLAAKA-IPGFELLEEGWDERAPLGwDVKDPTPVARAVVALLSDWFPA 239

                         90
                 ....*....|.
gi 4503301   292 INGAVIKFDGG 302
Cdd:PRK07889 240 TTGEIVHVDGG 250
PRK08267 PRK08267
SDR family oxidoreductase;
96-245 9.18e-07

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 49.55  E-value: 9.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    96 LKATAEQIssqTGNKVHAIQCDVRDPDMVQNTVSELIKV-AGHPNIVINNA----AGNFisptERLSPNAWKTITDI--- 167
Cdd:PRK08267  38 LAALAAEL---GAGNAWTGALDVTDRAAWDAALADFAAAtGGRLDVLFNNAgilrGGPF----EDIPLEAHDRVIDInvk 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   168 -VLNGT--AFVTLeigkqliKAQKGAAFLSITTIYAETGS-GFVVPSASaKAGVEAMSKSLAAEWGKYGMRFNVIQPGPI 243
Cdd:PRK08267 111 gVLNGAhaALPYL-------KATPGARVINTSSASAIYGQpGLAVYSAT-KFAVRGLTEALDLEWRRHGIRVADVMPLFV 182


                 ..
gi 4503301   244 KT 245
Cdd:PRK08267 183 DT 184
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 59-268 9.31e-07

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: 49.43  E-value: 9.31e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   59 GKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHP 138
Cdd:cd05343   6 GRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAGYPTLFPYQCDLSNEEQILSMFSAIRTQHQGV 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  139 NIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLikAQKGAAFLSITTIyaETGSGFVVPSAS------ 212
Cdd:cd05343  86 DVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSM--KERNVDDGHIINI--NSMSGHRVPPVSvfhfya 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4503301  213 -AKAGVEAMSKSLAAE--WGKYGMRFNVIQPGPIKTKGAFSRLDPTGTFEKEMIGRIPC 268
Cdd:cd05343 162 aTKHAVTALTEGLRQElrEAKTHIRATSISPGLVETEFAFKLHDNDPEKAAATYESIPC 220
PRK06482 PRK06482
SDR family oxidoreductase;
87-245 1.30e-06

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 48.96  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    87 VIAS-RKMDVLkataEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAWKTIT 165
Cdd:PRK06482  29 VAATvRRPDAL----DDLKARYGDRLWVLQLDVTDSAAVRAVVDRAFAALGRIDVVVSNAGYGLFGAAEELSDAQIRRQI 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   166 DIVLNGTAfvtleigkQLIKA-------QKGAAFLSITTiyaETGS----GFVVPSASaKAGVEAMSKSLAAEWGKYGMR 234
Cdd:PRK06482 105 DTNLIGSI--------QVIRAalphlrrQGGGRIVQVSS---EGGQiaypGFSLYHAT-KWGIEGFVEAVAQEVAPFGIE 172

                        170
                 ....*....|.
gi 4503301   235 FNVIQPGPIKT 245
Cdd:PRK06482 173 FTIVEPGPART 183
PRK08278 PRK08278
SDR family oxidoreductase;
99-240 1.30e-06

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 49.13  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    99 TAEQISsQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTle 178
Cdd:PRK08278  53 AAEEIE-AAGGQALPLVGDVRDEDQVAAAVAKAVERFGGIDICVNNASAINLTGTEDTPMKRFDLMQQINVRGTFLVS-- 129

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503301   179 igKQLIKAQKGAAFLSITTI-----YAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQP 240
Cdd:PRK08278 130 --QACLPHLKKSENPHILTLspplnLDPKWFAPHTAYTMAKYGMSLCTLGLAEEFRDDGIAVNALWP 194
PRK06914 PRK06914
SDR family oxidoreductase;
59-262 1.46e-06

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 48.87  E-value: 1.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    59 GKVAFITGGGTGLGKGMTTLLSSLGAQcVIAS----RKMDVLKATAEQISSQTgnKVHAIQCDVRDPDMVQNtVSELIKV 134
Cdd:PRK06914   3 KKIAIVTGASSGFGLLTTLELAKKGYL-VIATmrnpEKQENLLSQATQLNLQQ--NIKVQQLDVTDQNSIHN-FQLVLKE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   135 AGHPNIVINNA---AGNFIsptERLSPNAWKTITDIVLNGTAFVTlEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSA 211
Cdd:PRK06914  79 IGRIDLLVNNAgyaNGGFV---EEIPVEEYRKQFETNVFGAISVT-QAVLPYMRKQKSGKIINISSISGRVGFPGLSPYV 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 4503301   212 SAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKT-------KGAFSRLDPTGTFEKEM 262
Cdd:PRK06914 155 SSKYALEGFSESLRLELKPFGIDVALIEPGSYNTniwevgkQLAENQSETTSPYKEYM 212
PRK06603 PRK06603
enoyl-[acyl-carrier-protein] reductase FabI;
189-308 2.44e-06

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


Pssm-ID: 168626 [Multi-domain]  Cd Length: 260  Bit Score: 48.08  E-value: 2.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   189 GAAFLSITTIYAETgsgfVVPSAS----AKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKgAFSRLDPTGTFEKEMIG 264
Cdd:PRK06603 139 GGSIVTLTYYGAEK----VIPNYNvmgvAKAALEASVKYLANDMGENNIRVNAISAGPIKTL-ASSAIGDFSTMLKSHAA 213

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 4503301   265 RIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGGEEVLIS 308
Cdd:PRK06603 214 TAPLKRNTTQEDVGGAAVYLFSELSKGVTGEIHYVDCGYNIMGS 257
PRK07832 PRK07832
SDR family oxidoreductase;
60-245 3.14e-06

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 47.73  E-value: 3.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    60 KVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPN 139
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARALGGTVPEHRALDISDYDAVAAFAADIHAAHGSMD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   140 IVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFLSITtiyaeTGSGFV-VP-----SASa 213
Cdd:PRK07832  81 VVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMVAAGRGGHLVNVS-----SAAGLVaLPwhaaySAS- 154

                        170       180       190
                 ....*....|....*....|....*....|..
gi 4503301   214 KAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKT 245
Cdd:PRK07832 155 KFGLRGLSEVLRFDLARHGIGVSVVVPGAVKT 186
PRK09186 PRK09186
flagellin modification protein A; Provisional
 59-302 3.41e-06

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 47.68  E-value: 3.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    59 GKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQTGNKVHA-IQCDVRDPDMVQNTVSELIKVAGH 137
Cdd:PRK09186   4 GKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEFKSKKLSlVELDITDQESLEEFLSKSAEKYGK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   138 PNIVINNAagnfiSPTerlsPNAWKT------ITDIVLN-----GTAFVTLEIGKQLIKAQKGAAFLSITTIYaetgsGF 206
Cdd:PRK09186  84 IDGAVNCA-----YPR----NKDYGKkffdvsLDDFNENlslhlGSSFLFSQQFAKYFKKQGGGNLVNISSIY-----GV 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   207 VVPS---------------ASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRLDptgTFEKEmigripCGRL 271
Cdd:PRK09186 150 VAPKfeiyegtsmtspveyAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPGGILDNQPEAFLN---AYKKC------CNGK 220

                        250       260       270
                 ....*....|....*....|....*....|...
gi 4503301   272 G--TVEELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK09186 221 GmlDPDDICGTLVFLLSDQSKYITGQNIIVDDG 253
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 50-327 3.84e-06

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 47.85  E-value: 3.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    50 AMLPPNSFQGKVAFITGGGTGLGKGMTTLLSSLGAQCV---IASrKMDVlKATAEQISSqTGNKVHAIQCDVRDpdmvQN 126
Cdd:PRK07792   3 RTTNTTDLSGKVAVVTGAAAGLGRAEALGLARLGATVVvndVAS-ALDA-SDVLDEIRA-AGAKAVAVAGDISQ----RA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   127 TVSELIKVA---GHPNIVINNAAgnfISPTERL---SPNAWKTITDIVLNGTAFVTLEIG---KQLIKAQKGAAFLSITT 197
Cdd:PRK07792  76 TADELVATAvglGGLDIVVNNAG---ITRDRMLfnmSDEEWDAVIAVHLRGHFLLTRNAAaywRAKAKAAGGPVYGRIVN 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   198 IYAETG-SGFVVPS--ASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGP--IKTKGAFsrldptGTFEKEMIGRI-PCgrl 271
Cdd:PRK07792 153 TSSEAGlVGPVGQAnyGAAKAGITALTLSAARALGRYGVRANAICPRArtAMTADVF------GDAPDVEAGGIdPL--- 223

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 4503301   272 gTVEELANLAAFLCSDYASWINGAVIKFDGGEEVLISgefndlRKVTKEQWDTIEE 327
Cdd:PRK07792 224 -SPEHVVPLVQFLASPAAAEVNGQVFIVYGPMVTLVA------APVVERRFDADGD 272
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 117-302 4.45e-06

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 47.36  E-value: 4.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   117 DVRDPDMVQNTVSELIKVAGHPNIVINNAA----GNFISPTErlspNAWKTITDIVLNGtAFVTLEIGKQLIKAQ-KGAA 191
Cdd:PRK07791  72 DIADWDGAANLVDAAVETFGGLDVLVNNAGilrdRMIANMSE----EEWDAVIAVHLKG-HFATLRHAAAYWRAEsKAGR 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   192 FLSITTIYAETGSGfVVPS------ASAKAGVEAMSKSLAAEWGKYGMRFNVIQPgpiktkGAFSRLdpTGTFEKEMIGR 265
Cdd:PRK07791 147 AVDARIINTSSGAG-LQGSvgqgnySAAKAGIAALTLVAAAELGRYGVTVNAIAP------AARTRM--TETVFAEMMAK 217

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 4503301   266 IPCGRLGTV--EELANLAAFLCSDYASWINGAVIKFDGG 302
Cdd:PRK07791 218 PEEGEFDAMapENVSPLVVWLGSAESRDVTGKVFEVEGG 256
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 100-245 5.65e-06

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: 47.27  E-value: 5.65e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  100 AEQISSQTGNKVHAIQCDVRDPDMVQNTVSeliKVAGHPNI-----VINNAA-GNFISPTERLSPNAWKTITDIVLNGTA 173
Cdd:cd09805  39 AKELRRVCSDRLRTLQLDVTKPEQIKRAAQ---WVKEHVGEkglwgLVNNAGiLGFGGDEELLPMDDYRKCMEVNLFGTV 115

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4503301  174 FVTLEIgKQLIKAQKGAaFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKT 245
Cdd:cd09805 116 EVTKAF-LPLLRRAKGR-VVNVSSMGGRVPFPAGGAYCASKAAVEAFSDSLRRELQPWGVKVSIIEPGNFKT 185
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 96-245 5.99e-06

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: 46.68  E-value: 5.99e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   96 LKATAEQISsqtGNKVHAIQCDVRDPDMVQNTVSELI-KVAGHPNIVINNAAGNFISPTERLSPNAWKTITDI----VLN 170
Cdd:cd08931  37 LAALAAELG---AENVVAGALDVTDRAAWAAALADFAaATGGRLDALFNNAGVGRGGPFEDVPLAAHDRMVDInvkgVLN 113

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503301  171 G--TAFvtleigkQLIKAQKGAAFLSITTIYAETGS-GFVVPSASaKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKT 245
Cdd:cd08931 114 GayAAL-------PYLKATPGARVINTASSSAIYGQpDLAVYSAT-KFAVRGLTEALDVEWARHGIRVADVWPWFVDT 183
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 58-302 6.33e-06

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: 46.96  E-value: 6.33e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   58 QGKVAFITGGGtglgkgmttllSSLGAQCV----IASRKMDVLKATAEQIS---SQTGNKVHAIQCDVRDPDMVQNTVSE 130
Cdd:cd05348   3 KGEVALITGGG-----------SGLGRALVerfvAEGAKVAVLDRSAEKVAelrADFGDAVVGVEGDVRSLADNERAVAR 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  131 LIKVAGHPNIVINNAA--GNFIS----PTERLSPnAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAF-LSITTIYAetG 203
Cdd:cd05348  72 CVERFGKLDCFIGNAGiwDYSTSlvdiPEEKLDE-AFDELFHINVKGYILGAKAALPALYATEGSVIFtVSNAGFYP--G 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  204 SGFVVPSASaKAGVEAMSKSLAAEWGKYgMRFNVIQPGPIKT--KGAFSRLDPTGTFEK----EMIGRI-PCGRLGTVEE 276
Cdd:cd05348 149 GGGPLYTAS-KHAVVGLVKQLAYELAPH-IRVNGVAPGGMVTdlRGPASLGQGETSISTppldDMLKSIlPLGFAPEPED 226

                       250       260
                ....*....|....*....|....*..
gi 4503301  277 LANLAAFLCS-DYASWINGAVIKFDGG 302
Cdd:cd05348 227 YTGAYVFLASrGDNRPATGTVINYDGG 253
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 56-224 9.74e-06

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: 46.15  E-value: 9.74e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   56 SFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSqtgnkVHAIQCDVRDPDMVQNTVSELIKva 135
Cdd:cd05370   2 KLTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELPN-----IHTIVLDVGDAESVEALAEALLS-- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  136 GHP--NIVINNaAG-----NFISPTERLspNAWKTITDIVLNGTAFVTLEIGKQLiKAQKGAAFLSITtiyaeTGSGFV- 207
Cdd:cd05370  75 EYPnlDILINN-AGiqrpiDLRDPASDL--DKADTEIDTNLIGPIRLIKAFLPHL-KKQPEATIVNVS-----SGLAFVp 145

                       170       180
                ....*....|....*....|.
gi 4503301  208 ---VPSASA-KAGVEAMSKSL 224
Cdd:cd05370 146 maaNPVYCAtKAALHSYTLAL 166
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 87-245 1.33e-05

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: 45.74  E-value: 1.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   87 VIASRKMDVLKATAEQIssQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAG-NFISPTERLSPNAWKTIT 165
Cdd:cd05367  29 VLLARSEEPLQELKEEL--RPGLRVTTVKADLSDAAGVEQLLEAIRKLDGERDLLINNAGSlGPVSKIEFIDLDELQKYF 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  166 DIVLngtaFVTLEIGKQLIKAQKGaAFLSITTIYAETGSGF-VVPSASA----KAGVEAMSKSLAAEwgKYGMRFNVIQP 240
Cdd:cd05367 107 DLNL----TSPVCLTSTLLRAFKK-RGLKKTVVNVSSGAAVnPFKGWGLycssKAARDMFFRVLAAE--EPDVRVLSYAP 179


                ....*
gi 4503301  241 GPIKT 245
Cdd:cd05367 180 GVVDT 184
PRK09072 PRK09072
SDR family oxidoreductase;
79-227 1.33e-05

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 46.09  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    79 LSSLGAQCVIASRKMDVLKATAEQISSQtgNKVHAIQCDVRDPDMVQnTVSELIKVAGHPNIVINNAAGNFISPTERLSP 158
Cdd:PRK09072  25 LAAAGARLLLVGRNAEKLEALAARLPYP--GRHRWVVADLTSEAGRE-AVLARAREMGGINVLINNAGVNHFALLEDQDP 101

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503301   159 NAwktITDIV-LNGTAfvTLEIGKQLI---KAQKGAAFLSITTIYAETG-SGFVVPSASaKAGV----EAMSKSLAAE 227
Cdd:PRK09072 102 EA---IERLLaLNLTA--PMQLTRALLpllRAQPSAMVVNVGSTFGSIGyPGYASYCAS-KFALrgfsEALRRELADT 173
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 59-161 1.54e-05

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: 45.68  E-value: 1.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   59 GKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQTGN-KVHAIQCDVRDPDMVQNTVSELIKVAGH 137
Cdd:cd05327   1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIKKETGNaKVEVIQLDLSSLASVRQFAEEFLARFPR 80

                        90       100
                ....*....|....*....|....
gi 4503301  138 PNIVINNAAGNfiSPTERLSPNAW 161
Cdd:cd05327  81 LDILINNAGIM--APPRRLTKDGF 102
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 56-241 1.68e-05

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


Pssm-ID: 187611 [Multi-domain]  Cd Length: 250  Bit Score: 45.39  E-value: 1.68e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   56 SFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVI-----------ASRKMdvLKATAEQISSQTGNKVhAIQCDVRDPDMV 124
Cdd:cd05353   2 RFDGRVVLVTGAGGGLGRAYALAFAERGAKVVVndlggdrkgsgKSSSA--ADKVVDEIKAAGGKAV-ANYDSVEDGEKI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  125 QNTVselIKVAGHPNIVINNAA----GNFISPTERlspnAWKTITDIVLNGTaFVTLEIGKQLIKAQKGAAFLSITT--- 197
Cdd:cd05353  79 VKTA---IDAFGRVDILVNNAGilrdRSFAKMSEE----DWDLVMRVHLKGS-FKVTRAAWPYMRKQKFGRIINTSSaag 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 4503301  198 IYAETGSGfvvPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPG 241
Cdd:cd05353 151 LYGNFGQA---NYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPA 191
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 60-245 2.25e-05

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: 44.92  E-value: 2.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   60 KVAFITGGGTGLGKGMTTLLSSLGAQCVI-ASRKMDVLKATAEQISSQtGNKVHAIQCDVRDPDMVQNTVSELIKVAGHP 138
Cdd:cd05324   1 KVALVTGANRGIGFEIVRQLAKSGPGTVIlTARDVERGQAAVEKLRAE-GLSVRFHQLDVTDDASIEAAADFVEEKYGGL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  139 NIVINNAAGNFIS-PTERLSPNAWKTITDIVLNGTAFVTLEIgKQLIKAQKGAAFLSITTIYAETGSGFVVpsasAKAGV 217
Cdd:cd05324  80 DILVNNAGIAFKGfDDSTPTREQARETMKTNFFGTVDVTQAL-LPLLKKSPAGRIVNVSSGLGSLTSAYGV----SKAAL 154

                       170       180
                ....*....|....*....|....*...
gi 4503301  218 EAMSKSLAAEWGKYGMRFNVIQPGPIKT 245
Cdd:cd05324 155 NALTRILAKELKETGIKVNACCPGWVKT 182
PRK06181 PRK06181
SDR family oxidoreductase;
59-145 2.84e-05

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 44.97  E-value: 2.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    59 GKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQtGNKVHAIQCDVRDPDMVQNTVSELIKVAGHP 138
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADH-GGEALVVPTDVSDAEACERLIEAAVARFGGI 79


                 ....*..
gi 4503301   139 NIVINNA 145
Cdd:PRK06181  80 DILVNNA 86
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 95-305 2.86e-05

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 44.95  E-value: 2.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    95 VLKATAEQ---ISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAA-GNFISPTERLSPN----AWKTITD 166
Cdd:PRK06200  35 VLERSAEKlasLRQRFGDHVLVVEGDVTSYADNQRAVDQTVDAFGKLDCFVGNAGiWDYNTSLVDIPAEtldtAFDEIFN 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   167 IVLNGTAFVTLEIGKQLiKAQKGaaflSIttIYAETGSGFV-----VPSASAKAGVEAMSKSLAAEWGKYgMRFNVIQPG 241
Cdd:PRK06200 115 VNVKGYLLGAKAALPAL-KASGG----SM--IFTLSNSSFYpggggPLYTASKHAVVGLVRQLAYELAPK-IRVNGVAPG 186

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503301   242 PIKT--KGAFS------RLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYAS-WINGAVIKFDGGEEV 305
Cdd:PRK06200 187 GTVTdlRGPASlgqgetSISDSPGLADMIAAITPLQFAPQPEDHTGPYVLLASRRNSrALTGVVINADGGLGI 259
PRK06194 PRK06194
hypothetical protein; Provisional
 57-150 5.07e-05

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 44.24  E-value: 5.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    57 FQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQtGNKVHAIQCDVRDPDMVQNTVSELIKVAG 136
Cdd:PRK06194   4 FAGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELRAQ-GAEVLGVRTDVSDAAQVEALADAALERFG 82

                         90
                 ....*....|....*..
gi 4503301   137 HPNIVINNA---AGNFI 150
Cdd:PRK06194  83 AVHLLFNNAgvgAGGLV 99
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 79-303 5.99e-05

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 43.94  E-value: 5.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    79 LSSLGAQCVI-ASRKMDVLKATAEQISSQTGNKVhAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLS 157
Cdd:PRK06077  26 LAKEGSLVVVnAKKRAEEMNETLKMVKENGGEGI-GVLADVSTREGCETLAKATIDRYGVADILVNNAGLGLFSPFLNVD 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   158 PNAWKTITDIVLNGTAFVTLEIGKQLikaQKGAAFLSITTIYAetgsgfVVPS------ASAKAGVEAMSKSLAAEWGKY 231
Cdd:PRK06077 105 DKLIDKHISTDFKSVIYCSQELAKEM---REGGAIVNIASVAG------IRPAyglsiyGAMKAAVINLTKYLALELAPK 175

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503301   232 gMRFNVIQPGPIKTKGAFSRLDPTGTFEKEMIGRIP-CGRLGTVEELANLAAFLCSDYAswINGAVIKFDGGE 303
Cdd:PRK06077 176 -IRVNAIAPGFVKTKLGESLFKVLGMSEKEFAEKFTlMGKILDPEEVAEFVAAILKIES--ITGQVFVLDSGE 245
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 83-177 7.27e-05

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 44.14  E-value: 7.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    83 GAQCVIASRKMDVLKATAEQISSQtGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAWK 162
Cdd:PRK07109  32 GAKVVLLARGEEGLEALAAEIRAA-GGEALAVVADVADAEAVQAAADRAEEELGPIDTWVNNAMVTVFGPFEDVTPEEFR 110

                         90
                 ....*....|....*
gi 4503301   163 TITDIVLNGTAFVTL 177
Cdd:PRK07109 111 RVTEVTYLGVVHGTL 125
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 57-246 1.52e-04

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: 42.39  E-value: 1.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   57 FQGKVAFITGGGTGLGKGMTTLLSSLGAQCV-IASRKMdvlkATAEQISSQTGNKVHAIQCDVRDPDmvqnTVSELIKVA 135
Cdd:cd05354   1 IKDKTVLVTGANRGIGKAFVESLLAHGAKKVyAAVRDP----GSAAHLVAKYGDKVVPLRLDVTDPE----SIKAAAAQA 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  136 GHPNIVINNA-AGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGkQLIKAQKGAAFLSITTIYA-ETGSGFVVPSASa 213
Cdd:cd05354  73 KDVDVVINNAgVLKPATLLEEGALEALKQEMDVNVFGLLRLAQAFA-PVLKANGGGAIVNLNSVASlKNFPAMGTYSAS- 150

                       170       180       190
                ....*....|....*....|....*....|...
gi 4503301  214 KAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTK 246
Cdd:cd05354 151 KSAAYSLTQGLRAELAAQGTLVLSVHPGPIDTR 183
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 83-246 1.61e-04

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 42.55  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    83 GAQCVIASRKMDVLKATAEQISSQTGNKVHAIQCDVR--DPDMVQNTVSELIKVAGHPNIVINNAA--GNfISPTERLSP 158
Cdd:PRK08945  36 GATVILLGRTEEKLEAVYDEIEAAGGPQPAIIPLDLLtaTPQNYQQLADTIEEQFGRLDGVLHNAGllGE-LGPMEQQDP 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   159 NAWKTITDIVLNGTAFVTLEIGKQLIKAQKGA-AFLSITTiyAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNV 237
Cdd:PRK08945 115 EVWQDVMQVNVNATFMLTQALLPLLLKSPAASlVFTSSSV--GRQGRANWGAYAVSKFATEGMMQVLADEYQGTNLRVNC 192


                 ....*....
gi 4503301   238 IQPGPIKTK 246
Cdd:PRK08945 193 INPGGTRTA 201
PRK07024 PRK07024
SDR family oxidoreductase;
83-245 2.03e-04

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 42.22  E-value: 2.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    83 GAQCVIASRKMDVLKATAEQIssQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNA---AGNFISPTERLSpn 159
Cdd:PRK07024  26 GATLGLVARRTDALQAFAARL--PKAARVSVYAADVRDADALAAAAADFIAAHGLPDVVIANAgisVGTLTEEREDLA-- 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   160 AWKTITDIVLNGTAfVTLEIGKQLIKAQKGAAFLSITTIYAETGsgfvVPSASA----KAGVEAMSKSLAAEWGKYGMRF 235
Cdd:PRK07024 102 VFREVMDTNYFGMV-ATFQPFIAPMRAARRGTLVGIASVAGVRG----LPGAGAysasKAAAIKYLESLRVELRPAGVRV 176

                        170
                 ....*....|
gi 4503301   236 NVIQPGPIKT 245
Cdd:PRK07024 177 VTIAPGYIRT 186
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 83-241 2.12e-04

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 42.05  E-value: 2.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    83 GAQCVIASRKMDVLKAtaeqISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNF-ISPTERLSPNAW 161
Cdd:PRK10538  24 GHKVIATGRRQERLQE----LKDELGDNLYIAQLDVRNRAAIEEMLASLPAEWRNIDVLVNNAGLALgLEPAHKASVEDW 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   162 KTITDIVLNGTAFVTLEIGKQLIKAQKGaaflSITTIYAETGS----GFVVPSASaKAGVEAMSKSLAAEWGKYGMRFNV 237
Cdd:PRK10538 100 ETMIDTNNKGLVYMTRAVLPGMVERNHG----HIINIGSTAGSwpyaGGNVYGAT-KAFVRQFSLNLRTDLHGTAVRVTD 174


                 ....
gi 4503301   238 IQPG 241
Cdd:PRK10538 175 IEPG 178
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 83-240 2.25e-04

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: 42.05  E-value: 2.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   83 GAQCVIASRKMDV---LKAT----AEQISsQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTER 155
Cdd:cd09762  27 GANVVIAAKTAEPhpkLPGTiytaAEEIE-AAGGKALPCIVDIRDEDQVRAAVEKAVEKFGGIDILVNNASAISLTGTLD 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  156 LSPNAWKTITDIVLNGTaFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSAS--AKAGVEAMSKSLAAEWGKYGM 233
Cdd:cd09762 106 TPMKRYDLMMGVNTRGT-YLCSKACLPYLKKSKNPHILNLSPPLNLNPKWFKNHTAYtmAKYGMSMCVLGMAEEFKPGGI 184


                ....*..
gi 4503301  234 RFNVIQP 240
Cdd:cd09762 185 AVNALWP 191
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 56-254 4.41e-04

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 41.46  E-value: 4.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    56 SFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISsqtgnKVHAIQCDVRDPDMVQNTVSELIKVA 135
Cdd:PRK07825   2 DLRGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAELG-----LVVGGPLDVTDPASFAAFLDAVEADL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   136 GHPNIVINNA----AGNFISPTERLSpnawKTITDI----VLNGTAFVTLEIgkqlikaqkgaaflsittiyAETGSGFV 207
Cdd:PRK07825  77 GPIDVLVNNAgvmpVGPFLDEPDAVT----RRILDVnvygVILGSKLAAPRM--------------------VPRGRGHV 132

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   208 VPSASA---------------KAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTK--------GAFSRLDP 254
Cdd:PRK07825 133 VNVASLagkipvpgmatycasKHAVVGFTDAARLELRGTGVHVSVVLPSFVNTEliagtggaKGFKNVEP 202
PRK06182 PRK06182
short chain dehydrogenase; Validated
 58-245 5.65e-04

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 41.10  E-value: 5.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301    58 QGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEqissqTGnkVHAIQCDVRDPDMVQNTVSELIKVAGH 137
Cdd:PRK06182   2 QKKVALVTGASSGIGKATARRLAAQGYTVYGAARRVDKMEDLAS-----LG--VHPLSLDVTDEASIKAAVDTIIAEEGR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   138 PNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTleigkQLI----KAQKGAAFLSITTIyaetGSGFVVPSAS- 212
Cdd:PRK06182  75 IDVLVNNAGYGSYGAIEDVPIDEARRQFEVNLFGAARLT-----QLVlphmRAQRSGRIINISSM----GGKIYTPLGAw 145

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 4503301   213 ---AKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKT 245
Cdd:PRK06182 146 yhaTKFALEGFSDALRLEVAPFGIDVVVIEPGGIKT 181
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 145-245 1.29e-03

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


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 39.43  E-value: 1.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  145 AAGNFI-SPTERLSPNAWKTITDIVLNGTAFVtLEIGKQLIKAQKGAAFLSIttiYAE--TGSGFVVpSASAKAGVEAMS 221
Cdd:cd11730  73 AAGAILgKPLARTKPAAWRRILDANLTGAALV-LKHALALLAAGARLVFLGA---YPElvMLPGLSA-YAAAKAALEAYV 147

                        90       100
                ....*....|....*....|....
gi 4503301  222 KSLAAEWgkYGMRFNVIQPGPIKT 245
Cdd:cd11730 148 EVARKEV--RGLRLTLVRPPAVDT 169
PRK05693 PRK05693
SDR family oxidoreductase;
113-245 4.93e-03

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 38.23  E-value: 4.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301   113 AIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISP-----TERLSPNAWKTITDIV-LNGTAFVTLEIGKQLIka 186
Cdd:PRK05693  48 AVQLDVNDGAALARLAEELEAEHGGLDVLINNAGYGAMGPlldggVEAMRRQFETNVFAVVgVTRALFPLLRRSRGLV-- 125

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 4503301   187 qkgaafLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKT 245
Cdd:PRK05693 126 ------VNIGSVSGVLVTPFAGAYCASKAAVHALSDALRLELAPFGVQVMEVQPGAIAS 178
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 141-301 4.95e-03

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


Pssm-ID: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 37.69  E-value: 4.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  141 VINNAAGNFI--SPTERLSPNAWKTITDIVLNgTAFVTLEIGKQLIKaqKGAAFLSITTIYAETGSGFVVPSASAKAGVE 218
Cdd:cd05334  71 ALICVAGGWAggSAKSKSFVKNWDLMWKQNLW-TSFIASHLATKHLL--SGGLLVLTGAKAALEPTPGMIGYGAAKAAVH 147

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503301  219 AMSKSLAAEWG--KYGMRFNVIQPGPIKTKGafSRLD-PTGTFekemigripcGRLGTVEELANLAAFLCSDYASWINGA 295
Cdd:cd05334 148 QLTQSLAAENSglPAGSTANAILPVTLDTPA--NRKAmPDADF----------SSWTPLEFIAELILFWASGAARPKSGS 215


                ....*.
gi 4503301  296 VIKFDG 301
Cdd:cd05334 216 LIPVVT 221
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH