NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|4504505|ref|NP_000405|]
View 

peroxisomal multifunctional enzyme type 2 isoform 2 [Homo sapiens]

Protein Classification

peroxisomal multifunctional enzyme type 2( domain architecture ID 11563767)

peroxisomal multifunctional enzyme type 2 (MFE-2) is a bifunctional enzyme that catalyzes the formation of 3-ketoacyl-CoA intermediates from straight-chain, 2-methyl-branched-chain fatty acids bile acid intermediates

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
5-254 3.80e-174

(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: 498.39  E-value: 3.80e-174
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    5 LRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDFKGVGKGSLAADKVVEEIRRRGGKAVANYDSVEEGEKVVK 84
Cdd:cd05353   1 LRFDGRVVLVTGAGGGLGRAYALAFAERGAKVVVNDLGGDRKGSGKSSSAADKVVDEIKAAGGKAVANYDSVEDGEKIVK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   85 TALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANY 164
Cdd:cd05353  81 TAIDAFGRVDILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLYGNFGQANY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  165 SAAKLGLLGLANSLAIEGRKSNIHCNTIAPNAGSRMTQTVMPEDLVEALKPEYVAPLVLWLCHESCEENGGLFEVGAGWI 244
Cdd:cd05353 161 SAAKLGLLGLSNTLAIEGAKYNITCNTIAPAAGSRMTETVMPEDLFDALKPEYVAPLVLYLCHESCEVTGGLFEVGAGWI 240
                       250
                ....*....|
gi 4504505  245 GKLRWERTLG 254
Cdd:cd05353 241 GKLRWERSGG 250
PLN02864 super family cl28571
enoyl-CoA hydratase
328-605 4.44e-88

enoyl-CoA hydratase


The actual alignment was detected with superfamily member PLN02864:

Pssm-ID: 178455 [Multi-domain]  Cd Length: 310  Bit Score: 279.36  E-value: 4.44e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   328 IGQKLPPFSYAYTELEAIMYALGVGASIK---DPKDLKFIY--EGSSDFSCLPTFGVIIGQKSMMGGGLaEIPGLSINFA 402
Cdd:PLN02864  14 LAHKFPEVTYSYTERDVALYALGVGACGRdavDEDELKYVYhrDGQQFIKVLPTFASLFNLGSLDGFGL-DLPGLNYDPS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   403 KVLHGEQYLELYKPLPRAGKLKCEAVVADVLDKGSGVVIIMDVYSYSEK--ELICHNQFSLFLVGSGGFG--------GK 472
Cdd:PLN02864  93 LLLHGQQYIEIYKPIPSSASVRNKVSIAGLHDKGKAAILELETLSYEKDsgELLCMNRSTIFLRGAGGFSnssqpfsySN 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   473 RTSDKVKvAVAIPNRPPDAVLTDTTSLNQAALYRLSGDWNPLHIDPNFASLAGFDKPILHGLCTFGFSARRVLQQFADND 552
Cdd:PLN02864 173 YPTNQVS-AVKIPKSQPDAVFEDQTQPSQALLYRLSGDYNPLHSDPMFAKVAGFTRPILHGLCTLGFAVRAVIKCFCNGD 251
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 4504505   553 VSRFKAIKARFAKPVYPGQTLQTEMWKEGNRIHFQTKVQETGDIVISnAYVDL 605
Cdd:PLN02864 252 PTAVKTISGRFLLHVYPGETLVTEMWLEGLRVIYQTKVKERNKAVLS-GYVDL 303
SCP2 pfam02036
SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the ...
628-731 4.05e-25

SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the SCP2 protein as well as the C terminus of the enzyme estradiol 17 beta-dehydrogenase EC:1.1.1.62. The UNC-24 protein contains an SPFH domain pfam01145.


:

Pssm-ID: 460423 [Multi-domain]  Cd Length: 100  Bit Score: 100.02  E-value: 4.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    628 FEEIGRRLKDiGPEVVKKVNA-VFEWHITKGGNigaKWTIDLKSGSGKVyQGPAKGAADTTIILSDEDFMEVVLGKLDPQ 706
Cdd:pfam02036   1 LNQLLARDPA-ARELLKKLNGkVIRFDLTDLGL---SLTLDLKDGGGRV-LAGDEGKADVTLSASDSDLLALATGKLNPQ 75
                          90       100
                  ....*....|....*....|....*
gi 4504505    707 KAFFSGRLKARGNIMLSQKLQMILK 731
Cdd:pfam02036  76 KAFMQGKLKIEGDMELAQKLEGLLK 100
 
Name Accession Description Interval E-value
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
5-254 3.80e-174

(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: 498.39  E-value: 3.80e-174
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    5 LRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDFKGVGKGSLAADKVVEEIRRRGGKAVANYDSVEEGEKVVK 84
Cdd:cd05353   1 LRFDGRVVLVTGAGGGLGRAYALAFAERGAKVVVNDLGGDRKGSGKSSSAADKVVDEIKAAGGKAVANYDSVEDGEKIVK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   85 TALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANY 164
Cdd:cd05353  81 TAIDAFGRVDILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLYGNFGQANY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  165 SAAKLGLLGLANSLAIEGRKSNIHCNTIAPNAGSRMTQTVMPEDLVEALKPEYVAPLVLWLCHESCEENGGLFEVGAGWI 244
Cdd:cd05353 161 SAAKLGLLGLSNTLAIEGAKYNITCNTIAPAAGSRMTETVMPEDLFDALKPEYVAPLVLYLCHESCEVTGGLFEVGAGWI 240
                       250
                ....*....|
gi 4504505  245 GKLRWERTLG 254
Cdd:cd05353 241 GKLRWERSGG 250
PLN02864 PLN02864
enoyl-CoA hydratase
328-605 4.44e-88

enoyl-CoA hydratase


Pssm-ID: 178455 [Multi-domain]  Cd Length: 310  Bit Score: 279.36  E-value: 4.44e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   328 IGQKLPPFSYAYTELEAIMYALGVGASIK---DPKDLKFIY--EGSSDFSCLPTFGVIIGQKSMMGGGLaEIPGLSINFA 402
Cdd:PLN02864  14 LAHKFPEVTYSYTERDVALYALGVGACGRdavDEDELKYVYhrDGQQFIKVLPTFASLFNLGSLDGFGL-DLPGLNYDPS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   403 KVLHGEQYLELYKPLPRAGKLKCEAVVADVLDKGSGVVIIMDVYSYSEK--ELICHNQFSLFLVGSGGFG--------GK 472
Cdd:PLN02864  93 LLLHGQQYIEIYKPIPSSASVRNKVSIAGLHDKGKAAILELETLSYEKDsgELLCMNRSTIFLRGAGGFSnssqpfsySN 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   473 RTSDKVKvAVAIPNRPPDAVLTDTTSLNQAALYRLSGDWNPLHIDPNFASLAGFDKPILHGLCTFGFSARRVLQQFADND 552
Cdd:PLN02864 173 YPTNQVS-AVKIPKSQPDAVFEDQTQPSQALLYRLSGDYNPLHSDPMFAKVAGFTRPILHGLCTLGFAVRAVIKCFCNGD 251
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 4504505   553 VSRFKAIKARFAKPVYPGQTLQTEMWKEGNRIHFQTKVQETGDIVISnAYVDL 605
Cdd:PLN02864 252 PTAVKTISGRFLLHVYPGETLVTEMWLEGLRVIYQTKVKERNKAVLS-GYVDL 303
PRK07791 PRK07791
short chain dehydrogenase; Provisional
8-244 2.13e-81

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 260.76  E-value: 2.13e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     8 DGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDFKGVGKGSLAADKVVEEIRRRGGKAVANYDSV---EEGEKVVK 84
Cdd:PRK07791   5 DGRVVIVTGAGGGIGRAHALAFAAEGARVVVNDIGVGLDGSASGGSAAQAVVDEIVAAGGEAVANGDDIadwDGAANLVD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    85 TALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQ-KYG-----RIIMTSSASGIYGN 158
Cdd:PRK07791  85 AAVETFGGLDVLVNNAGILRDRMIANMSEEEWDAVIAVHLKGHFATLRHAAAYWRAEsKAGravdaRIINTSSGAGLQGS 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   159 FGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNAGSRMTQTVMP-------EDLVEALKPEYVAPLVLWLCHESCE 231
Cdd:PRK07791 165 VGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAPAARTRMTETVFAemmakpeEGEFDAMAPENVSPLVVWLGSAESR 244
                        250
                 ....*....|....
gi 4504505   232 E-NGGLFEVGAGWI 244
Cdd:PRK07791 245 DvTGKVFEVEGGKI 258
HDE_HSD cd03448
HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), ...
485-606 4.44e-75

HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), and Hydratase-Dehydrogenase-Epimerase (HDE) proteins. Other enzymes with this fold include MaoC dehydratase, and the fatty acid synthase beta subunit.


Pssm-ID: 239532 [Multi-domain]  Cd Length: 122  Bit Score: 237.89  E-value: 4.44e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  485 PNRPPDAVLTDTTSLNQAALYRLSGDWNPLHIDPNFASLAGFDKPILHGLCTFGFSARRVLQQFADNDVSRFKAIKARFA 564
Cdd:cd03448   1 PDRAPDAVVEIPTSPDQALLYRLSGDYNPLHIDPAFAKAAGFPRPILHGLCTYGFAARAVLEAFADGDPARFKAIKVRFS 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 4504505  565 KPVYPGQTLQTEMWKEGNRIHFQTKVQETGDIVISNAYVDLA 606
Cdd:cd03448  81 SPVFPGETLRTEMWKEGNRVIFQTKVVERDVVVLSNGAALLA 122
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
6-226 8.34e-71

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: 231.60  E-value: 8.34e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKA------VANYDSVEEg 79
Cdd:COG1028   3 RLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAE---------ALEAAAAELRAAGGRAlavaadVTDEAAVEA- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   80 ekVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNF 159
Cdd:COG1028  73 --LVAAAVAAFGRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSP 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  160 GQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPnaG---SRMTQTVMP-EDLVEAL----------KPEYVAPLVLWL 225
Cdd:COG1028 151 GQAAYAASKAAVVGLTRSLALELAPRGIRVNAVAP--GpidTPMTRALLGaEEVREALaariplgrlgTPEEVAAAVLFL 228

                .
gi 4504505  226 C 226
Cdd:COG1028 229 A 229
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
12-226 1.88e-57

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


Pssm-ID: 273824 [Multi-domain]  Cd Length: 239  Bit Score: 195.51  E-value: 1.88e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     12 VLVTGAGAGLGRAYALAFAERGALVVVNDLGGDFKgvgkgslaADKVVEEIRRRGGKA---VANYDSVEEGEKVVKTALD 88
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYRSSEEG--------AEEVVEELKALGVKAlgvVLDVSDREDVKAVVEEIEE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     89 AFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSAAK 168
Cdd:TIGR01830  73 ELGTIDILVNNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRSGRIINISSVVGLMGNAGQANYAASK 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4504505    169 LGLLGLANSLAIEGRKSNIHCNTIAPnaG---SRMTQtVMPEDLVEAL----------KPEYVAPLVLWLC 226
Cdd:TIGR01830 153 AGVIGFTKSLAKELASRNITVNAVAP--GfidTDMTD-KLSEKVKKKIlsqiplgrfgQPEEVANAVAFLA 220
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
10-194 2.49e-48

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 168.95  E-value: 2.49e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     10 RVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKA------VANYDSVEegeKVV 83
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEE---------KLEAVAKELGALGGKAlfiqgdVTDRAQVK---ALV 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     84 KTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQAN 163
Cdd:pfam00106  69 EQAVERLGRLDILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSA 148
                         170       180       190
                  ....*....|....*....|....*....|.
gi 4504505    164 YSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:pfam00106 149 YSASKAAVIGFTRSLALELAPHGIRVNAVAP 179
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
480-601 3.34e-47

MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the synthesis of monoamine oxidase. The MaoC protein is found to share similarity with a wide variety of enzymes; estradiol 17 beta-dehydrogenase 4, peroxisomal hydratase-dehydrogenase-epimerase, fatty acid synthase beta subunit. Several bacterial proteins that are composed solely of this domain have (R)-specific enoyl-CoA hydratase activity. This domain is also present in the NodN nodulation protein N.


Pssm-ID: 396243 [Multi-domain]  Cd Length: 123  Bit Score: 163.28  E-value: 3.34e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    480 VAVAIPNRPPDAVLTDTTSLNQAALYRL-SGDWNPLHIDPNFASLAGFDKPILHGLCTFGFSARRVLQQFADNDVSRFKA 558
Cdd:pfam01575   1 DFQNAPGEPPDTEKPRTVTEADIALFALvSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGGDNVIARFGE 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 4504505    559 IKARFAKPVYPGQTLQTEMWKEGNRIHFQTKVQETGDIVISNA 601
Cdd:pfam01575  81 IKVRFTKPVFPGDTLRTEAEVVGKRDGRQTKVVEVTVEVTEVA 123
SCP2 pfam02036
SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the ...
628-731 4.05e-25

SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the SCP2 protein as well as the C terminus of the enzyme estradiol 17 beta-dehydrogenase EC:1.1.1.62. The UNC-24 protein contains an SPFH domain pfam01145.


Pssm-ID: 460423 [Multi-domain]  Cd Length: 100  Bit Score: 100.02  E-value: 4.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    628 FEEIGRRLKDiGPEVVKKVNA-VFEWHITKGGNigaKWTIDLKSGSGKVyQGPAKGAADTTIILSDEDFMEVVLGKLDPQ 706
Cdd:pfam02036   1 LNQLLARDPA-ARELLKKLNGkVIRFDLTDLGL---SLTLDLKDGGGRV-LAGDEGKADVTLSASDSDLLALATGKLNPQ 75
                          90       100
                  ....*....|....*....|....*
gi 4504505    707 KAFFSGRLKARGNIMLSQKLQMILK 731
Cdd:pfam02036  76 KAFMQGKLKIEGDMELAQKLEGLLK 100
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
10-167 2.87e-19

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 86.00  E-value: 2.87e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505      10 RVVLVTGAGAGLGRAYALAFAERGA--LVVVNDLGGDfkgvgkgSLAADKVVEEIRRRGGKA------VANYDSVEEgek 81
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGArrLVLLSRSGPD-------APGAAALLAELEAAGARVtvvacdVADRDALAA--- 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505      82 VVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDiihrvhlrgsfQVTRA----AW---EHMKKQKYGRIIMTSSASG 154
Cdd:smart00822  71 VLAAIPAVEGPLTGVIHAAGVLDDGVLASLTPERFA-----------AVLAPkaagAWnlhELTADLPLDFFVLFSSIAG 139
                          170
                   ....*....|...
gi 4504505     155 IYGNFGQANYSAA 167
Cdd:smart00822 140 VLGSPGQANYAAA 152
SCP2 COG3255
Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];
627-733 5.50e-19

Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];


Pssm-ID: 442486 [Multi-domain]  Cd Length: 104  Bit Score: 82.65  E-value: 5.50e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  627 VFEEIGRRLKdiGPEVVKKVNAVFEWHITKGGniGAKWTIDLKSGSGKVYQGPAkGAADTTIILSDEDFMEVVLGKLDPQ 706
Cdd:COG3255   3 WAEALCEKLN--AADAAAGWDGVVQFVITGEG--GGAYYLVIDDGKCTVSEGDD-DDADVTLTASYEDWKKLLTGELDPM 77
                        90       100
                ....*....|....*....|....*..
gi 4504505  707 KAFFSGRLKARGNIMLSQKLQMILKDY 733
Cdd:COG3255  78 TAFMTGKLKVEGDMGLAMKLMSLFKAL 104
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
506-578 1.27e-14

Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 71.46  E-value: 1.27e-14
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4504505  506 RLSGDWNPLHIDPNFASLAGFDKPILHGLCTFGFSARRVLQQFADNDVSRFKAIKARFAKPVYPGQTLQTEMW 578
Cdd:COG2030  28 GATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPGTAVANLGLQEVRFLRPVRVGDTLRARVE 100
 
Name Accession Description Interval E-value
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
5-254 3.80e-174

(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: 498.39  E-value: 3.80e-174
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    5 LRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDFKGVGKGSLAADKVVEEIRRRGGKAVANYDSVEEGEKVVK 84
Cdd:cd05353   1 LRFDGRVVLVTGAGGGLGRAYALAFAERGAKVVVNDLGGDRKGSGKSSSAADKVVDEIKAAGGKAVANYDSVEDGEKIVK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   85 TALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANY 164
Cdd:cd05353  81 TAIDAFGRVDILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLYGNFGQANY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  165 SAAKLGLLGLANSLAIEGRKSNIHCNTIAPNAGSRMTQTVMPEDLVEALKPEYVAPLVLWLCHESCEENGGLFEVGAGWI 244
Cdd:cd05353 161 SAAKLGLLGLSNTLAIEGAKYNITCNTIAPAAGSRMTETVMPEDLFDALKPEYVAPLVLYLCHESCEVTGGLFEVGAGWI 240
                       250
                ....*....|
gi 4504505  245 GKLRWERTLG 254
Cdd:cd05353 241 GKLRWERSGG 250
PLN02864 PLN02864
enoyl-CoA hydratase
328-605 4.44e-88

enoyl-CoA hydratase


Pssm-ID: 178455 [Multi-domain]  Cd Length: 310  Bit Score: 279.36  E-value: 4.44e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   328 IGQKLPPFSYAYTELEAIMYALGVGASIK---DPKDLKFIY--EGSSDFSCLPTFGVIIGQKSMMGGGLaEIPGLSINFA 402
Cdd:PLN02864  14 LAHKFPEVTYSYTERDVALYALGVGACGRdavDEDELKYVYhrDGQQFIKVLPTFASLFNLGSLDGFGL-DLPGLNYDPS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   403 KVLHGEQYLELYKPLPRAGKLKCEAVVADVLDKGSGVVIIMDVYSYSEK--ELICHNQFSLFLVGSGGFG--------GK 472
Cdd:PLN02864  93 LLLHGQQYIEIYKPIPSSASVRNKVSIAGLHDKGKAAILELETLSYEKDsgELLCMNRSTIFLRGAGGFSnssqpfsySN 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   473 RTSDKVKvAVAIPNRPPDAVLTDTTSLNQAALYRLSGDWNPLHIDPNFASLAGFDKPILHGLCTFGFSARRVLQQFADND 552
Cdd:PLN02864 173 YPTNQVS-AVKIPKSQPDAVFEDQTQPSQALLYRLSGDYNPLHSDPMFAKVAGFTRPILHGLCTLGFAVRAVIKCFCNGD 251
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 4504505   553 VSRFKAIKARFAKPVYPGQTLQTEMWKEGNRIHFQTKVQETGDIVISnAYVDL 605
Cdd:PLN02864 252 PTAVKTISGRFLLHVYPGETLVTEMWLEGLRVIYQTKVKERNKAVLS-GYVDL 303
PRK07791 PRK07791
short chain dehydrogenase; Provisional
8-244 2.13e-81

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 260.76  E-value: 2.13e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     8 DGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDFKGVGKGSLAADKVVEEIRRRGGKAVANYDSV---EEGEKVVK 84
Cdd:PRK07791   5 DGRVVIVTGAGGGIGRAHALAFAAEGARVVVNDIGVGLDGSASGGSAAQAVVDEIVAAGGEAVANGDDIadwDGAANLVD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    85 TALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQ-KYG-----RIIMTSSASGIYGN 158
Cdd:PRK07791  85 AAVETFGGLDVLVNNAGILRDRMIANMSEEEWDAVIAVHLKGHFATLRHAAAYWRAEsKAGravdaRIINTSSGAGLQGS 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   159 FGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNAGSRMTQTVMP-------EDLVEALKPEYVAPLVLWLCHESCE 231
Cdd:PRK07791 165 VGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAPAARTRMTETVFAemmakpeEGEFDAMAPENVSPLVVWLGSAESR 244
                        250
                 ....*....|....
gi 4504505   232 E-NGGLFEVGAGWI 244
Cdd:PRK07791 245 DvTGKVFEVEGGKI 258
HDE_HSD cd03448
HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), ...
485-606 4.44e-75

HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), and Hydratase-Dehydrogenase-Epimerase (HDE) proteins. Other enzymes with this fold include MaoC dehydratase, and the fatty acid synthase beta subunit.


Pssm-ID: 239532 [Multi-domain]  Cd Length: 122  Bit Score: 237.89  E-value: 4.44e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  485 PNRPPDAVLTDTTSLNQAALYRLSGDWNPLHIDPNFASLAGFDKPILHGLCTFGFSARRVLQQFADNDVSRFKAIKARFA 564
Cdd:cd03448   1 PDRAPDAVVEIPTSPDQALLYRLSGDYNPLHIDPAFAKAAGFPRPILHGLCTYGFAARAVLEAFADGDPARFKAIKVRFS 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 4504505  565 KPVYPGQTLQTEMWKEGNRIHFQTKVQETGDIVISNAYVDLA 606
Cdd:cd03448  81 SPVFPGETLRTEMWKEGNRVIFQTKVVERDVVVLSNGAALLA 122
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
6-226 8.34e-71

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: 231.60  E-value: 8.34e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKA------VANYDSVEEg 79
Cdd:COG1028   3 RLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAE---------ALEAAAAELRAAGGRAlavaadVTDEAAVEA- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   80 ekVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNF 159
Cdd:COG1028  73 --LVAAAVAAFGRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSP 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  160 GQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPnaG---SRMTQTVMP-EDLVEAL----------KPEYVAPLVLWL 225
Cdd:COG1028 151 GQAAYAASKAAVVGLTRSLALELAPRGIRVNAVAP--GpidTPMTRALLGaEEVREALaariplgrlgTPEEVAAAVLFL 228

                .
gi 4504505  226 C 226
Cdd:COG1028 229 A 229
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
10-237 1.65e-64

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: 214.33  E-value: 1.65e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   10 RVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKA------VANYDSVEegeKVV 83
Cdd:cd05333   1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEE---------AAAETVEEIKALGGNAaaleadVSDREAVE---ALV 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   84 KTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQAN 163
Cdd:cd05333  69 EKVEAEFGPVDILVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQAN 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  164 YSAAKLGLLGLANSLAIEGRKSNIHCNTIAPN-AGSRMTQtVMPEDLVEAL----------KPEYVAPLVLWLCHE---- 228
Cdd:cd05333 149 YAASKAGVIGFTKSLAKELASRGITVNAVAPGfIDTDMTD-ALPEKVKEKIlkqiplgrlgTPEEVANAVAFLASDdasy 227
                       250
                ....*....|...
gi 4504505  229 ----SCEENGGLF 237
Cdd:cd05333 228 itgqVLHVNGGMY 240
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
6-226 1.49e-63

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 211.94  E-value: 1.49e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKA------VANYDSVEEg 79
Cdd:PRK05653   2 SLQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEE---------AAEALAAELRAAGGEArvlvfdVSDEAAVRA- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    80 ekVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNF 159
Cdd:PRK05653  72 --LIEAAVEAFGALDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNP 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4504505   160 GQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNA-GSRMTQTVMPEDLVEAL---------KPEYVAPLVLWLC 226
Cdd:PRK05653 150 GQTNYSAAKAGVIGFTKALALELASRGITVNAVAPGFiDTDMTEGLPEEVKAEILkeiplgrlgQPEEVANAVAFLA 226
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
7-225 6.95e-63

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 210.44  E-value: 6.95e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     7 FDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgsLAADKVVEEIRRRGGKA------VANYDSVEege 80
Cdd:PRK05557   3 LEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSE--------AGAEALVAEIGALGGKAlavqgdVSDAESVE--- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    81 KVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFG 160
Cdd:PRK05557  72 RAVDEAKAEFGGVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPG 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4504505   161 QANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPN-AGSRMTQTVmPEDLVEAL----------KPEYVAPLVLWL 225
Cdd:PRK05557 152 QANYAASKAGVIGFTKSLARELASRGITVNAVAPGfIETDMTDAL-PEDVKEAIlaqiplgrlgQPEEIASAVAFL 226
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-239 1.92e-62

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 211.18  E-value: 1.92e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     1 MGSPLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGdfkgvgkgSLAADKVVEEIRRRGGKAVANYDSVEE-- 78
Cdd:PRK07792   4 TTNTTDLSGKVAVVTGAAAGLGRAEALGLARLGATVVVNDVAS--------ALDASDVLDEIRAAGAKAVAVAGDISQra 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    79 -GEKVVKTAlDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAA---WEHMKKQK----YGRIIMTS 150
Cdd:PRK07792  76 tADELVATA-VGLGGLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAaayWRAKAKAAggpvYGRIVNTS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   151 SASGIYGNFGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNAGSRMTQTV------MPEDLVEALKPEYVAPLVLW 224
Cdd:PRK07792 155 SEAGLVGPVGQANYGAAKAGITALTLSAARALGRYGVRANAICPRARTAMTADVfgdapdVEAGGIDPLSPEHVVPLVQF 234
                        250
                 ....*....|....*.
gi 4504505   225 LCHESCEE-NGGLFEV 239
Cdd:PRK07792 235 LASPAAAEvNGQVFIV 250
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
12-231 1.24e-60

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: 203.67  E-value: 1.24e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   12 VLVTGAGAGLGRAYALAFAERGALVVVNDLggdfkgvgkgSLAADKVVEEIRRRGGKAVANYDSV---EEGEKVVKTALD 88
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAREGAKVVLADR----------NEEALAELAAIEALGGNAVAVQADVsdeEDVEALVEEALE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   89 AFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSAAK 168
Cdd:cd05233  71 EFGRLDILVNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASK 150
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4504505  169 LGLLGLANSLAIEGRKSNIHCNTIAPNAG-SRMTQTVMPEDLVE----------ALKPEYVAPLVLWLCHESCE 231
Cdd:cd05233 151 AALEGLTRSLALELAPYGIRVNAVAPGLVdTPMLAKLGPEEAEKelaaaiplgrLGTPEEVAEAVVFLASDEAS 224
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
12-226 1.88e-57

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


Pssm-ID: 273824 [Multi-domain]  Cd Length: 239  Bit Score: 195.51  E-value: 1.88e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     12 VLVTGAGAGLGRAYALAFAERGALVVVNDLGGDFKgvgkgslaADKVVEEIRRRGGKA---VANYDSVEEGEKVVKTALD 88
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYRSSEEG--------AEEVVEELKALGVKAlgvVLDVSDREDVKAVVEEIEE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     89 AFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSAAK 168
Cdd:TIGR01830  73 ELGTIDILVNNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRSGRIINISSVVGLMGNAGQANYAASK 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4504505    169 LGLLGLANSLAIEGRKSNIHCNTIAPnaG---SRMTQtVMPEDLVEAL----------KPEYVAPLVLWLC 226
Cdd:TIGR01830 153 AGVIGFTKSLAKELASRNITVNAVAP--GfidTDMTD-KLSEKVKKKIlsqiplgrfgQPEEVANAVAFLA 220
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
6-228 2.15e-56

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 192.78  E-value: 2.15e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgsLAADKVVEEIRRRGGKA------VANYDSVEEg 79
Cdd:PRK12825   3 SLMGRVALVTGAARGLGRAIALRLARAGADVVVHYRSDE--------EAAEELVEAVEALGRRAqavqadVTDKAALEA- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    80 ekVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNF 159
Cdd:PRK12825  74 --AVAAAVERFGRIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGLPGWP 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4504505   160 GQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP-NAGSRMTQTVMPEDLVEALK---------PEYVAPLVLWLCHE 228
Cdd:PRK12825 152 GRSNYAAAKAGLVGLTKALARELAEYGITVNMVAPgDIDTDMKEATIEEAREAKDAetplgrsgtPEDIARAVAFLCSD 230
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
6-249 1.09e-53

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 185.46  E-value: 1.09e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKA------VANYDSVEEg 79
Cdd:COG0300   2 SLTGKTVLITGASSGIGRALARALAARGARVVLVARDAE---------RLEALAAELRAAGARVevvaldVTDPDAVAA- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   80 ekVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNF 159
Cdd:COG0300  72 --LAEAVLARFGPIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLP 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  160 GQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNA-GSRMTQTVMPEDLVEALKPEYVAPLVLWLCHEsceengGLFE 238
Cdd:COG0300 150 GMAAYAASKAALEGFSESLRAELAPTGVRVTAVCPGPvDTPFTARAGAPAGRPLLSPEEVARAILRALER------GRAE 223
                       250
                ....*....|.
gi 4504505  239 VGAGWIGKLRW 249
Cdd:COG0300 224 VYVGWDARLLA 234
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
8-227 3.56e-52

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: 181.15  E-value: 3.56e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    8 DGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIrrrGGKA------VANYDSVEEgek 81
Cdd:COG4221   4 KGKVALITGASSGIGAATARALAAAGARVVLAARRAE---------RLEALAAEL---GGRAlavpldVTDEAAVEA--- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   82 VVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQ 161
Cdd:COG4221  69 AVAAAVAEFGRLDVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGG 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4504505  162 ANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP-NAGSRMTQTVMPEDL---------VEALKPEYVAPLVLWLCH 227
Cdd:COG4221 149 AVYAATKAAVRGLSESLRAELRPTGIRVTVIEPgAVDTEFLDSVFDGDAeaaaavyegLEPLTPEDVAEAVLFALT 224
PRK12826 PRK12826
SDR family oxidoreductase;
6-225 7.87e-50

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 175.10  E-value: 7.87e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKAVA---NYDSVEEGEKV 82
Cdd:PRK12826   3 DLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGD---------DAAATAELVEAAGGKARArqvDVRDRAALKAA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    83 VKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIY-GNFGQ 161
Cdd:PRK12826  74 VAAGVEDFGRLDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGPRvGYPGL 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4504505   162 ANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNA-GSRMTQTVMPEDLVEALK----------PEYVAPLVLWL 225
Cdd:PRK12826 154 AHYAASKAGLVGFTRALALELAARNITVNSVHPGGvDTPMAGNLGDAQWAEAIAaaiplgrlgePEDIAAAVLFL 228
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
10-194 2.49e-48

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 168.95  E-value: 2.49e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     10 RVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKA------VANYDSVEegeKVV 83
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEE---------KLEAVAKELGALGGKAlfiqgdVTDRAQVK---ALV 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     84 KTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQAN 163
Cdd:pfam00106  69 EQAVERLGRLDILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSA 148
                         170       180       190
                  ....*....|....*....|....*....|.
gi 4504505    164 YSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:pfam00106 149 YSASKAAVIGFTRSLALELAPHGIRVNAVAP 179
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
480-601 3.34e-47

MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the synthesis of monoamine oxidase. The MaoC protein is found to share similarity with a wide variety of enzymes; estradiol 17 beta-dehydrogenase 4, peroxisomal hydratase-dehydrogenase-epimerase, fatty acid synthase beta subunit. Several bacterial proteins that are composed solely of this domain have (R)-specific enoyl-CoA hydratase activity. This domain is also present in the NodN nodulation protein N.


Pssm-ID: 396243 [Multi-domain]  Cd Length: 123  Bit Score: 163.28  E-value: 3.34e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    480 VAVAIPNRPPDAVLTDTTSLNQAALYRL-SGDWNPLHIDPNFASLAGFDKPILHGLCTFGFSARRVLQQFADNDVSRFKA 558
Cdd:pfam01575   1 DFQNAPGEPPDTEKPRTVTEADIALFALvSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGGDNVIARFGE 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 4504505    559 IKARFAKPVYPGQTLQTEMWKEGNRIHFQTKVQETGDIVISNA 601
Cdd:pfam01575  81 IKVRFTKPVFPGDTLRTEAEVVGKRDGRQTKVVEVTVEVTEVA 123
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
6-244 1.68e-46

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 165.79  E-value: 1.68e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVN-DLGGDfkgvgkgslAADKVVEEIRRRGGKA------VANYDSVEe 78
Cdd:PRK05565   2 KLMGKVAIVTGASGGIGRAIAELLAKEGAKVVIAyDINEE---------AAQELLEEIKEEGGDAiavkadVSSEEDVE- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    79 geKVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGN 158
Cdd:PRK05565  72 --NLVEQIVEKFGKIDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   159 FGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPnaGSRMTQ--TVMPEDLVEAL----------KPEYVAPLVLWLC 226
Cdd:PRK05565 150 SCEVLYSASKGAVNAFTKALAKELAPSGIRVNAVAP--GAIDTEmwSSFSEEDKEGLaeeiplgrlgKPEEIAKVVLFLA 227
                        250
                 ....*....|....*....
gi 4504505   227 -HESCEENGGLFEVGAGWI 244
Cdd:PRK05565 228 sDDASYITGQIITVDGGWT 246
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
6-194 1.53e-44

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 160.44  E-value: 1.53e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKAV---ANYDSVEEGEKV 82
Cdd:PRK12429   1 MLKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDE---------AAAAAAEALQKAGGKAIgvaMDVTDEEAINAG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    83 VKTALDAFGRIDVVVNNAGIlrdRSFARISD---EDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNF 159
Cdd:PRK12429  72 IDYAVETFGGVDILVNNAGI---QHVAPIEDfptEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVGSA 148
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 4504505   160 GQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK12429 149 GKAAYVSAKHGLIGLTKVVALEGATHGVTVNAICP 183
PRK12827 PRK12827
short chain dehydrogenase; Provisional
8-244 1.42e-43

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 157.57  E-value: 1.42e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     8 DGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgKGSLAADKVVEEIRRRGGKAVANYDSVEEGEkVVKTAL 87
Cdd:PRK12827   5 DSRRVLITGGSGGLGRAIAVRLAADGADVIVLDIHPM-----RGRAEADAVAAGIEAAGGKALGLAFDVRDFA-ATRAAL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    88 DA----FGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHM-KKQKYGRIIMTSSASGIYGNFGQA 162
Cdd:PRK12827  79 DAgveeFGRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMiRARRGGRIVNIASVAGVRGNRGQV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   163 NYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNA-GSRMTQTVMPEDLVE-------ALKPEYVAPLVLWLCHESCEE-N 233
Cdd:PRK12827 159 NYAASKAGLIGLTKTLANELAPRGITVNAVAPGAiNTPMADNAAPTEHLLnpvpvqrLGEPDEVAALVAFLVSDAASYvT 238
                        250
                 ....*....|.
gi 4504505   234 GGLFEVGAGWI 244
Cdd:PRK12827 239 GQVIPVDGGFC 249
AcAcCoA_reduct TIGR01829
acetoacetyl-CoA reductase; This model represent acetoacetyl-CoA reductase, a member of the ...
10-237 9.05e-43

acetoacetyl-CoA reductase; This model represent acetoacetyl-CoA reductase, a member of the family short-chain-alcohol dehydrogenases. Note that, despite the precision implied by the enzyme name, the reaction of EC 1.1.1.36 is defined more generally as (R)-3-hydroxyacyl-CoA + NADP+ = 3-oxoacyl-CoA + NADPH. Members of this family may act in the biosynthesis of poly-beta-hydroxybutyrate (e.g. Rhizobium meliloti) and related poly-beta-hydroxyalkanoates. Note that the member of this family from Azospirillum brasilense, designated NodG, appears to lack acetoacetyl-CoA reductase activity and to act instead in the production of nodulation factor. This family is downgraded to subfamily for this NodG. Other proteins designated NodG, as from Rhizobium, belong to related but distinct protein families.


Pssm-ID: 273823 [Multi-domain]  Cd Length: 242  Bit Score: 155.28  E-value: 9.05e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     10 RVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDFKGvgKGSLAADKVVEEIRRRGGKAVANYDSVEEGekvVKTALDA 89
Cdd:TIGR01829   1 RIALVTGGMGGIGTAICQRLAKDGYRVAANCGPNEERA--EAWLQEQGALGFDFRVVEGDVSSFESCKAA---VAKVEAE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     90 FGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSAAKL 169
Cdd:TIGR01829  76 LGPVDVLVNNAGITRDATFKKMTYEQWDAVIDTNLNSVFNVTQPVIDGMRERGWGRIINISSVNGQKGQFGQTNYSAAKA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    170 GLLGLANSLAIEGRKSNIHCNTIAPN-AGSRMTqTVMPEDLVEAL----------KPEYVAPLVLWLCHE--------SC 230
Cdd:TIGR01829 156 GMIGFTKALAQEGATKGVTVNTISPGyIATDMV-MAMREDVLNSIvaqipvkrlgRPEEIAAAVAFLASEeagyitgaTL 234

                  ....*..
gi 4504505    231 EENGGLF 237
Cdd:TIGR01829 235 SINGGLY 241
FabG-like PRK07231
SDR family oxidoreductase;
5-226 5.33e-42

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 153.45  E-value: 5.33e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     5 LRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIrRRGGKAV---ANYDSVEEGEK 81
Cdd:PRK07231   1 MRLEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEE---------AAERVAAEI-LAGGRAIavaADVSDEADVEA 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    82 VVKTALDAFGRIDVVVNNAGI-LRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFG 160
Cdd:PRK07231  71 AVAAALERFGSVDILVNNAGTtHRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   161 QANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNAG-SRMTQTVMPEDLVEAL-------------KPEYVAPLVLWLC 226
Cdd:PRK07231 151 LGWYNASKGAVITLTKALAAELGPDKIRVNAVAPVVVeTGLLEAFMGEPTPENRakflatiplgrlgTPEDIANAALFLA 230
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
10-237 1.44e-41

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 151.84  E-value: 1.44e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    10 RVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGdfkgvGKGSLAADKVVEEIRRRGGKAVANYDSVEEGEKVVKTALDA 89
Cdd:PRK12824   3 KIALVTGAKRGIGSAIARELLNDGYRVIATYFSG-----NDCAKDWFEEYGFTEDQVRLKELDVTDTEECAEALAEIEEE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    90 FGRIDVVVNNAGILRDRSFARISDEDW-DIIHrVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSAAK 168
Cdd:PRK12824  78 EGPVDILVNNAGITRDSVFKRMSHQEWnDVIN-TNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQFGQTNYSAAK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   169 LGLLGLANSLAIEGRKSNIHCNTIAPN-AGSRMTQtVMPEDLVEALK----------PEYVAPLVLWLCHESC------- 230
Cdd:PRK12824 157 AGMIGFTKALASEGARYGITVNCIAPGyIATPMVE-QMGPEVLQSIVnqipmkrlgtPEEIAAAVAFLVSEAAgfitget 235

                 ....*...
gi 4504505   231 -EENGGLF 237
Cdd:PRK12824 236 iSINGGLY 243
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
6-237 1.74e-41

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 151.70  E-value: 1.74e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNdlggdfkgVGKGSLAADKVVEEIRRRGGKAVA---NYDSVEEGEKV 82
Cdd:PRK12935   3 QLNGKVAIVTGGAKGIGKAITVALAQEGAKVVIN--------YNSSKEAAENLVNELGKEGHDVYAvqaDVSKVEDANRL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    83 VKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQA 162
Cdd:PRK12935  75 VEEAVNHFGKVDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFGQT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   163 NYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPnaGSRMTQTVM--PEDLVEAL----------KPEYVAPLVLWLCHESC 230
Cdd:PRK12935 155 NYSAAKAGMLGFTKSLALELAKTNVTVNAICP--GFIDTEMVAevPEEVRQKIvakipkkrfgQADEIAKGVVYLCRDGA 232
                        250
                 ....*....|....
gi 4504505   231 -------EENGGLF 237
Cdd:PRK12935 233 yitgqqlNINGGLY 246
PRK12829 PRK12829
short chain dehydrogenase; Provisional
7-242 2.34e-41

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 151.75  E-value: 2.34e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     7 FDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEI-RRRGGKAVANYDSVEEGEKVVKT 85
Cdd:PRK12829   9 LDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEA---------ALAATAARLpGAKVTATVADVADPAQVERVFDT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    86 ALDAFGRIDVVVNNAGI-LRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGR-IIMTSSASGIYGNFGQAN 163
Cdd:PRK12829  80 AVERFGGLDVLVNNAGIaGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGHGGvIIALSSVAGRLGYPGRTP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   164 YSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNA--GSRMTQTVMPE-------------------DLVEALKPEYVAPLV 222
Cdd:PRK12829 160 YAASKWAVVGLVKSLAIELGPLGIRVNAILPGIvrGPRMRRVIEARaqqlgigldemeqeylekiSLGRMVEPEDIAATA 239
                        250       260
                 ....*....|....*....|.
gi 4504505   223 LWLCH-ESCEENGGLFEVGAG 242
Cdd:PRK12829 240 LFLASpAARYITGQAISVDGN 260
PHB_DH TIGR01963
3-hydroxybutyrate dehydrogenase; This model represents a subfamily of the short chain ...
9-243 1.26e-40

3-hydroxybutyrate dehydrogenase; This model represents a subfamily of the short chain dehydrogenases. Characterized members so far as 3-hydroxybutyrate dehydrogenases and are found in species that accumulate ester polmers called polyhydroxyalkanoic acids (PHAs) under certain conditions. Several members of the family are from species not known to accumulate PHAs, including Oceanobacillus iheyensis and Bacillus subtilis. However, polymer formation is not required for there be a role for 3-hydroxybutyrate dehydrogenase; it may be members of this family have the same function in those species.


Pssm-ID: 211705 [Multi-domain]  Cd Length: 255  Bit Score: 149.44  E-value: 1.26e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505      9 GRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkGSLAADKVVEEIRRRGGKAVANYDSVEEGEKVVKTALD 88
Cdd:TIGR01963   1 GKTALVTGAASGIGLAIARALAAAGANVVVNDFGEE------GAEAAAKVAGDAGGSVIYLPADVTKEDEIADMIAAAAA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     89 AFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSAAK 168
Cdd:TIGR01963  75 EFGGLDILVNNAGIQHVAPIEEFPPEDWDRIIAVMLTSAFHTIRAALPHMKKQGWGRIINIASAHGLVASPFKSAYVAAK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    169 LGLLGLANSLAIEGRKSNIHCNTIAPnaGSRMTQTV------------MPEDLV------------EALKPEYVAPLVLW 224
Cdd:TIGR01963 155 HGLIGLTKVLALEVAEHGITVNAICP--GYVRTPLVekqiadqaktrgIPEEQVirevmlkgqptkRFVTVDEVAETALY 232
                         250       260
                  ....*....|....*....|
gi 4504505    225 LC-HESCEENGGLFEVGAGW 243
Cdd:TIGR01963 233 LAsDAAAQITGQAIVLDGGW 252
PRK07774 PRK07774
SDR family oxidoreductase;
6-244 2.57e-40

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 148.35  E-value: 2.57e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKAVANYDSVEEGEKV--- 82
Cdd:PRK07774   3 RFDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAE---------GAERVAKQIVADGGTAIAVQVDVSDPDSAkam 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    83 VKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHR---VHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASG-IYGN 158
Cdd:PRK07774  74 ADATVSAFGGIDYLVNNAAIYGGMKLDLLITVPWDYYKKfmsVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTAAwLYSN 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   159 FgqanYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPN-AGSRMTQTVMPEDLVEAL----------KPEYVAPLVLWLCH 227
Cdd:PRK07774 154 F----YGLAKVGLNGLTQQLARELGGMNIRVNAIAPGpIDTEATRTVTPKEFVADMvkgiplsrmgTPEDLVGMCLFLLS 229
                        250
                 ....*....|....*...
gi 4504505   228 ESCEE-NGGLFEVGAGWI 244
Cdd:PRK07774 230 DEASWiTGQIFNVDGGQI 247
PRK12939 PRK12939
short chain dehydrogenase; Provisional
8-225 1.00e-39

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 147.04  E-value: 1.00e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     8 DGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKAV---ANYDSVEEGEKVVK 84
Cdd:PRK12939   6 AGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAA---------EARELAAALEAAGGRAHaiaADLADPASVQRFFD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    85 TALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANY 164
Cdd:PRK12939  77 AAAAALGGLDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPKLGAY 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4504505   165 SAAKLGLLGLANSLAIEGRKSNIHCNTIAPN-AGSRMTQTVMPEDLVEALK----------PEYVAPLVLWL 225
Cdd:PRK12939 157 VASKGAVIGMTRSLARELGGRGITVNAIAPGlTATEATAYVPADERHAYYLkgralerlqvPDDVAGAVLFL 228
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
8-225 3.55e-39

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: 145.60  E-value: 3.55e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    8 DGRVVLVTGAGAGLGRAYALAFAERGALVVVNdlggdfkGVGKGSlAADKVVEEIRRRGGKAVANYDSVEEGEKVVK--- 84
Cdd:cd05358   2 KGKVALVTGASSGIGKAIAIRLATAGANVVVN-------YRSKED-AAEEVVEEIKAVGGKAIAVQADVSKEEDVVAlfq 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   85 TALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQK-YGRIIMTSSASGIYGNFGQAN 163
Cdd:cd05358  74 SAIKEFGTLDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKiKGKIINMSSVHEKIPWPGHVN 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4504505  164 YSAAKLGLLGLANSLAIEGRKSNIHCNTIAP-------NAGSRMTqtvmPEDLVEALK---------PEYVAPLVLWL 225
Cdd:cd05358 154 YAASKGGVKMMTKTLAQEYAPKGIRVNAIAPgaintpiNAEAWDD----PEQRADLLSlipmgrigePEEIAAAAAWL 227
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
9-244 2.98e-38

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: 142.41  E-value: 2.98e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    9 GRVVLVTGAGAGLGRAYALAFAERGALVVVNdlggdfkgVGKGSLAADKVVEEIRRRGGKAV---ANYDSVEEGEKVVKT 85
Cdd:cd05362   3 GKVALVTGASRGIGRAIAKRLARDGASVVVN--------YASSKAAAEEVVAEIEAAGGKAIavqADVSDPSQVARLFDA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   86 ALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQkyGRII-MTSSASGIY-GNFGQan 163
Cdd:cd05362  75 AEKAFGGVDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLRDG--GRIInISSSLTAAYtPNYGA-- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  164 YSAAKLGLLGLANSLAIEGRKSNIHCNTIAPN-AGSRMTQTVMPEDLVEAL----------KPEYVAPLVLWLCHEscee 232
Cdd:cd05362 151 YAGSKAAVEAFTRVLAKELGGRGITVNAVAPGpVDTDMFYAGKTEEAVEGYakmsplgrlgEPEDIAPVVAFLASP---- 226
                       250
                ....*....|..
gi 4504505  233 ngglfevGAGWI 244
Cdd:cd05362 227 -------DGRWV 231
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
9-237 2.43e-37

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: 139.84  E-value: 2.43e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    9 GRVVLVTGAGAGLGRAYALAFAERGALVVV---NDLGGDFKGVGKGSLAADKVVEEIRRRGGKAVA---NYDSVEEGEKV 82
Cdd:cd05338   3 GKVAFVTGASRGIGRAIALRLAKAGATVVVaakTASEGDNGSAKSLPGTIEETAEEIEAAGGQALPivvDVRDEDQVRAL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   83 VKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQA 162
Cdd:cd05338  83 VEATVDQFGRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLSLRPARGDV 162
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4504505  163 NYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPN---AGSRMTQTVMPEDLVEALKPEYVAPLVLWLCHESCEENGGLF 237
Cdd:cd05338 163 AYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPStaiETPAATELSGGSDPARARSPEILSDAVLAILSRPAAERTGLV 240
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
8-243 4.69e-37

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 139.65  E-value: 4.69e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     8 DGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKA------VANYDSVEEGek 81
Cdd:PRK13394   6 NGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQD---------GANAVADEINKAGGKAigvamdVTNEDAVNAG-- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    82 vVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKK-QKYGRIIMTSSASGIYGNFG 160
Cdd:PRK13394  75 -IDKVAERFGSVDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKdDRGGVVIYMGSVHSHEASPL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   161 QANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPN--------------------AGSRMTQTVMPEDLVEAL--KPEYV 218
Cdd:PRK13394 154 KSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGfvrtplvdkqipeqakelgiSEEEVVKKVMLGKTVDGVftTVEDV 233
                        250       260
                 ....*....|....*....|....*.
gi 4504505   219 APLVLWLCH-ESCEENGGLFEVGAGW 243
Cdd:PRK13394 234 AQTVLFLSSfPSAALTGQSFVVSHGW 259
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
9-243 5.14e-37

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: 139.50  E-value: 5.14e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    9 GRVVLVTGAGAGLGRAYALAFAERGALVVVNdlggdfkgvGKGSLAADKVVEE--IRRRGGKAVA-NYD--SVEEGEKVV 83
Cdd:cd08940   2 GKVALVTGSTSGIGLGIARALAAAGANIVLN---------GFGDAAEIEAVRAglAAKHGVKVLYhGADlsKPAAIEDMV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   84 KTALDAFGRIDVVVNNAGIlrdRSFARISD---EDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFG 160
Cdd:cd08940  73 AYAQRQFGGVDILVNNAGI---QHVAPIEDfptEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVASAN 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  161 QANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPnaGSRMTQTVmpEDLVEAL--------------------------K 214
Cdd:cd08940 150 KSAYVAAKHGVVGLTKVVALETAGTGVTCNAICP--GWVLTPLV--EKQISALaqkngvpqeqaarelllekqpskqfvT 225
                       250       260       270
                ....*....|....*....|....*....|
gi 4504505  215 PEYVAPLVLWLCHESCEE-NGGLFEVGAGW 243
Cdd:cd08940 226 PEQLGDTAVFLASDAASQiTGTAVSVDGGW 255
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
1-226 5.99e-37

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 147.68  E-value: 5.99e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     1 MGSPLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKA-----VANYDS 75
Cdd:PRK08324 414 MPKPKPLAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEE---------AAEAAAAELGGPDRALgvacdVTDEAA 484
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    76 VEEGekvVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQK-YGRIIMTSSASG 154
Cdd:PRK08324 485 VQAA---FEEAALAFGGVDIVVSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGlGGSIVFIASKNA 561
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   155 IYGNFGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNA---GS----------RMTQTVMPEDLVEA-------LK 214
Cdd:PRK08324 562 VNPGPNFGAYGAAKAAELHLVRQLALELGPDGIRVNGVNPDAvvrGSgiwtgewieaRAAAYGLSEEELEEfyrarnlLK 641
                        250
                 ....*....|....*.
gi 4504505   215 ----PEYVAPLVLWLC 226
Cdd:PRK08324 642 revtPEDVAEAVVFLA 657
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
20-226 1.68e-36

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: 137.18  E-value: 1.68e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     20 GLGRAYALAFAERGALVVVNDLGGDFKgvgkgslaadKVVEEIRRRGGKA-----VANYDSVEegeKVVKTALDAFGRID 94
Cdd:pfam13561   7 GIGWAIARALAEEGAEVVLTDLNEALA----------KRVEELAEELGAAvlpcdVTDEEQVE---ALVAAAVEKFGRLD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     95 VVVNNAGILR--DRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQkyGRIIMTSSASGIYGNFGQANYSAAKLGLL 172
Cdd:pfam13561  74 ILVNNAGFAPklKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKEG--GSIVNLSSIGAERVVPNYNAYGAAKAALE 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    173 GLANSLAIEGRKSNIHCNTIAPnaGsrMTQTVM------PEDLVEAL----------KPEYVAPLVLWLC 226
Cdd:pfam13561 152 ALTRYLAVELGPRGIRVNAISP--G--PIKTLAasgipgFDELLAAAearaplgrlgTPEEVANAAAFLA 217
PRK06138 PRK06138
SDR family oxidoreductase;
5-243 1.39e-34

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 132.20  E-value: 1.39e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     5 LRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRrGGKAVANYDSVEEGEKVvK 84
Cdd:PRK06138   1 MRLAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAE---------AAERVAAAIAA-GGRAFARQGDVGSAEAV-E 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    85 TALD----AFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFG 160
Cdd:PRK06138  70 ALVDfvaaRWGRLDVLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGRG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   161 QANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNA-GSRM-----TQTVMPEDLVEALK----------PEYVAPLVLW 224
Cdd:PRK06138 150 RAAYVASKGAIASLTRAMALDHATDGIRVNAVAPGTiDTPYfrrifARHADPEALREALRarhpmnrfgtAEEVAQAALF 229
                        250       260
                 ....*....|....*....|
gi 4504505   225 LC-HESCEENGGLFEVGAGW 243
Cdd:PRK06138 230 LAsDESSFATGTTLVVDGGW 249
PRK06841 PRK06841
short chain dehydrogenase; Provisional
5-194 2.45e-34

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 131.70  E-value: 2.45e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     5 LRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDFKGVGKGSLAADkvveeirrRGGKA--VANYDSVEegeKV 82
Cdd:PRK06841  11 FDLSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGGN--------AKGLVcdVSDSQSVE---AA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    83 VKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQA 162
Cdd:PRK06841  80 VAAVISAFGRIDILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVVALERHV 159
                        170       180       190
                 ....*....|....*....|....*....|..
gi 4504505   163 NYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK06841 160 AYCASKAGVVGMTKVLALEWGPYGITVNAISP 191
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
6-194 2.62e-34

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 131.85  E-value: 2.62e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslaADKVVEEIRRRGGKA------VANYDSVEEg 79
Cdd:PRK08226   3 KLTGKTALITGALQGIGEGIARVFARHGANLILLDISPE----------IEKLADELCGRGHRCtavvadVRDPASVAA- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    80 ekVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASG-IYGN 158
Cdd:PRK08226  72 --AIKRAKEKEGRIDILVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSVTGdMVAD 149
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 4504505   159 FGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK08226 150 PGETAYALTKAAIVGLTKSLAVEYAQSGIRVNAICP 185
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
9-228 4.48e-34

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: 130.86  E-value: 4.48e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    9 GRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKA---VANYDSVEEGEKVVKT 85
Cdd:cd05344   1 GKVALVTAASSGIGLAIARALAREGARVAICARNRE---------NLERAASELRAGGAGVlavVADLTDPEDIDRLVEK 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   86 ALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYS 165
Cdd:cd05344  72 AGDAFGRVDILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEPEPNLVLSN 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  166 AAKLGLLGLANSLAIEGRKSNIHCNTIAP----------NAGSRMTQTVMPEDLVEAL-----------KPEYVAPLVLW 224
Cdd:cd05344 152 VARAGLIGLVKTLSRELAPDGVTVNSVLPgyidtervrrLLEARAEKEGISVEEAEKEvasqiplgrvgKPEELAALIAF 231

                ....
gi 4504505  225 LCHE 228
Cdd:cd05344 232 LASE 235
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
9-194 5.23e-34

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 130.19  E-value: 5.23e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     9 GRVVLVTGAGAGLGRAYALAFAERGalVVVNDLGGDFKGVgkgslaaDKVVEEIRRRGGKA------VANYDSVEEGEKV 82
Cdd:PRK07666   7 GKNALITGAGRGIGRAVAIALAKEG--VNVGLLARTEENL-------KAVAEEVEAYGVKVviatadVSDYEEVTAAIEQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    83 VKTALdafGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQA 162
Cdd:PRK07666  78 LKNEL---GSIDILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKGAAVTS 154
                        170       180       190
                 ....*....|....*....|....*....|..
gi 4504505   163 NYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK07666 155 AYSASKFGVLGLTESLMQEVRKHNIRVTALTP 186
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
10-194 2.90e-33

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: 128.50  E-value: 2.90e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   10 RVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgvgkGSLAADKVVEEIRRRGGKA------VANYDSVEegeKVV 83
Cdd:cd05374   1 KVVLITGCSSGIGLALALALAAQGYRVIA------------TARNPDKLESLGELLNDNLevleldVTDEESIK---AAV 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   84 KTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQAN 163
Cdd:cd05374  66 KEVIERFGRIDVLVNNAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGP 145
                       170       180       190
                ....*....|....*....|....*....|.
gi 4504505  164 YSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:cd05374 146 YCASKAALEALSESLRLELAPFGIKVTIIEP 176
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
6-245 3.14e-33

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: 128.27  E-value: 3.14e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgVGKgslaadKVVEEIRRRggkavANY---DSVEEGE-- 80
Cdd:cd05341   2 RLKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDE---EGQ------AAAAELGDA-----ARFfhlDVTDEDGwt 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   81 KVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFG 160
Cdd:cd05341  68 AVVDTAREAFGRLDVLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPA 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  161 QANYSAAKLGLLGLANSLAIEGRK--SNIHCNTIAPNagsrMTQTVMPEDLVEAL---------------KPEYVAPLVL 223
Cdd:cd05341 148 LAAYNASKGAVRGLTKSAALECATqgYGIRVNSVHPG----YIYTPMTDELLIAQgemgnypntpmgragEPDEIAYAVV 223
                       250       260
                ....*....|....*....|...
gi 4504505  224 WLC-HESCEENGGLFEVGAGWIG 245
Cdd:cd05341 224 YLAsDESSFVTGSELVVDGGYTA 246
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
6-194 6.27e-33

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 127.93  E-value: 6.27e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDFkgvgkgslaaDKVVEEIRRRGGKAV---ANYDSVEEGEKV 82
Cdd:PRK06935  12 SLDGKVAIVTGGNTGLGQGYAVALAKAGADIIITTHGTNW----------DETRRLIEKEGRKVTfvqVDLTKPESAEKV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    83 VKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQA 162
Cdd:PRK06935  82 VKEALEEFGKIDILVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASMLSFQGGKFVP 161
                        170       180       190
                 ....*....|....*....|....*....|..
gi 4504505   163 NYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK06935 162 AYTASKHGVAGLTKAFANELAAYNIQVNAIAP 193
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
7-194 3.03e-32

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: 125.30  E-value: 3.03e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    7 FDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIrrrGGKAVANYDSVEEGEKV---V 83
Cdd:cd08944   1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGG---------AAQAVVAQI---AGGALALRVDVTDEQQVaalF 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   84 KTALDAFGRIDVVVNNAGILRDRS-FARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQA 162
Cdd:cd08944  69 ERAVEEFGGLDLLVNNAGAMHLTPaIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGDPGYG 148
                       170       180       190
                ....*....|....*....|....*....|..
gi 4504505  163 NYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:cd08944 149 AYGASKAAIRNLTRTLAAELRHAGIRCNALAP 180
PRK06172 PRK06172
SDR family oxidoreductase;
6-228 3.42e-32

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 125.63  E-value: 3.42e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLggDFKGvgkgslaADKVVEEIRRRGGKAVANYDSV---EEGEKV 82
Cdd:PRK06172   4 TFSGKVALVTGGAAGIGRATALAFAREGAKVVVADR--DAAG-------GEETVALIREAGGEALFVACDVtrdAEVKAL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    83 VKTALDAFGRIDVVVNNAGILRDRS-FARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQ 161
Cdd:PRK06172  75 VEQTIAAYGRLDYAFNNAGIEIEQGrLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPKM 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   162 ANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNAgsrmTQTVMPEDLVEAL-----------------KPEYVAPLVLW 224
Cdd:PRK06172 155 SIYAASKHAVIGLTKSAAIEYAKKGIRVNAVCPAV----IDTDMFRRAYEADprkaefaaamhpvgrigKVEEVASAVLY 230

                 ....
gi 4504505   225 LCHE 228
Cdd:PRK06172 231 LCSD 234
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
5-194 5.74e-32

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: 124.75  E-value: 5.74e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    5 LRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGG---KA----VANYDSVE 77
Cdd:cd05352   4 FSLKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAP---------RAEEKAEELAKKYGvktKAykcdVSSQESVE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   78 egeKVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYG 157
Cdd:cd05352  75 ---KTFKQIQKDFGKIDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSGTIV 151
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 4504505  158 NFGQ--ANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:cd05352 152 NRPQpqAAYNASKAAVIHLAKSLAVEWAKYFIRVNSISP 190
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
12-226 1.89e-31

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: 122.85  E-value: 1.89e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   12 VLVTGAGAGLGRAYALAFAERGALVVVNdlggdFKgvgKGSLAADKVVEEIRRRGGKAVANYDSVEEGEKV---VKTALD 88
Cdd:cd05359   1 ALVTGGSRGIGKAIALRLAERGADVVIN-----YR---KSKDAAAEVAAEIEELGGKAVVVRADVSQPQDVeemFAAVKE 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   89 AFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSAAK 168
Cdd:cd05359  73 RFGRLDVLVSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALPNYLAVGTAK 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  169 LGLLGLANSLAIEGRKSNIHCNTIAPNA-GSRMTQTVM-PEDLVEALK----------PEYVAPLVLWLC 226
Cdd:cd05359 153 AALEALVRYLAVELGPRGIRVNAVSPGViDTDALAHFPnREDLLEAAAantpagrvgtPQDVADAVGFLC 222
PRK06124 PRK06124
SDR family oxidoreductase;
3-225 1.95e-31

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 123.28  E-value: 1.95e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     3 SPLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNdlggdfkgvGKGSLAADKVVEEIRRRGGKAVANYDSVEEGE-- 80
Cdd:PRK06124   5 QRFSLAGQVALVTGSARGLGFEIARALAGAGAHVLVN---------GRNAATLEAAVAALRAAGGAAEALAFDIADEEav 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    81 -KVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNF 159
Cdd:PRK06124  76 aAAFARIDAEHGRLDILVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQVARA 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4504505   160 GQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNAGSRMTQTVMPED--LVEALK----------PEYVAPLVLWL 225
Cdd:PRK06124 156 GDAVYPAAKQGLTGLMRALAAEFGPHGITSNAIAPGYFATETNAAMAADpaVGPWLAqrtplgrwgrPEEIAGAAVFL 233
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
9-194 2.17e-31

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 123.10  E-value: 2.17e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     9 GRVVLVTGAGAGLGRAYALAFAERGALVVVNdlggdfkgvGKGSLAADKVVEEIRRRGGKAVANYDSVEEGEKVVKTALD 88
Cdd:PRK12936   6 GRKALVTGASGGIGEEIARLLHAQGAIVGLH---------GTRVEKLEALAAELGERVKIFPANLSDRDEVKALGQKAEA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    89 AFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSAAK 168
Cdd:PRK12936  77 DLEGVDILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVGVTGNPGQANYCASK 156
                        170       180
                 ....*....|....*....|....*.
gi 4504505   169 LGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK12936 157 AGMIGFSKSLAQEIATRNVTVNCVAP 182
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
9-194 2.41e-31

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: 122.85  E-value: 2.41e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    9 GRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKAVA---NYDSVEEGEKVVKT 85
Cdd:cd05347   5 GKVALVTGASRGIGFGIASGLAEAGANIVINSRNEE---------KAEEAQQLIEKEGVEATAftcDVSDEEAIKAAVEA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   86 ALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYS 165
Cdd:cd05347  76 IEEDFGKIDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPAYA 155
                       170       180
                ....*....|....*....|....*....
gi 4504505  166 AAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:cd05347 156 ASKGGVAGLTKALATEWARHGIQVNAIAP 184
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
6-225 3.45e-31

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: 122.56  E-value: 3.45e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKAVANYDSVEEG-EKVVK 84
Cdd:cd05326   1 RLDGKVAIITGGASGIGEATARLFAKHGARVVIADIDDD---------AGQAVAAELGDPDISFVHCDVTVEADvRAAVD 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   85 TALDAFGRIDVVVNNAGIL--RDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQA 162
Cdd:cd05326  72 TAVARFGRLDIMFNNAGVLgaPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPH 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4504505  163 NYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPN--AGSRMTQTVMPED-------------LVEALKPEYVAPLVLWL 225
Cdd:cd05326 152 AYTASKHAVLGLTRSAATELGEHGIRVNCVSPYgvATPLLTAGFGVEDeaieeavrgaanlKGTALRPEDIAAAVLYL 229
PRK12937 PRK12937
short chain dehydrogenase; Provisional
9-194 3.85e-31

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 122.16  E-value: 3.85e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     9 GRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgsLAADKVVEEIRRRGGKAVANYDSVEEGEKVVK---T 85
Cdd:PRK12937   5 NKVAIVTGASRGIGAAIARRLAADGFAVAVNYAGSA--------AAADELVAEIEAAGGRAIAVQADVADAAAVTRlfdA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    86 ALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQkyGRII-MTSSASGIYGNfGQANY 164
Cdd:PRK12937  77 AETAFGRIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHLGQG--GRIInLSTSVIALPLP-GYGPY 153
                        170       180       190
                 ....*....|....*....|....*....|
gi 4504505   165 SAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK12937 154 AASKAAVEGLVHVLANELRGRGITVNAVAP 183
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
5-216 3.94e-31

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 122.38  E-value: 3.94e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     5 LRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKA---VANYDSVEEGEK 81
Cdd:PRK08217   1 MDLKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQE---------KLEEAVAECGALGTEVrgyAANVTDEEDVEA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    82 VVKTALDAFGRIDVVVNNAGILRDRSFARISD---------EDWDIIHRVHLRGSFQVTRAAWEHM-KKQKYGRIIMTSS 151
Cdd:PRK08217  72 TFAQIAEDFGQLNGLINNAGILRDGLLVKAKDgkvtskmslEQFQSVIDVNLTGVFLCGREAAAKMiESGSKGVIINISS 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4504505   152 ASgIYGNFGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNagsrmtqtVMPEDLVEALKPE 216
Cdd:PRK08217 152 IA-RAGNMGQTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPG--------VIETEMTAAMKPE 207
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
6-226 4.57e-31

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: 122.11  E-value: 4.57e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIrrrGGKA------VANYDSVEEg 79
Cdd:cd05345   2 RLEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINAD---------GAERVAADI---GEAAiaiqadVTKRADVEA- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   80 ekVVKTALDAFGRIDVVVNNAGIL-RDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGN 158
Cdd:cd05345  69 --MVEAALSKFGRLDILVNNAGIThRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGLRPR 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  159 FGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNAG-SRMTQTVMPEDLVEAL-------------KPEYVAPLVLW 224
Cdd:cd05345 147 PGLTWYNASKGWVVTATKAMAVELAPRNIRVNCLCPVAGeTPLLSMFMGEDTPENRakfratiplgrlsTPDDIANAALY 226

                ..
gi 4504505  225 LC 226
Cdd:cd05345 227 LA 228
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
10-241 5.83e-31

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 121.66  E-value: 5.83e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    10 RVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkGVGKGSLAADKVVEEIRRRGGKAVANYDSVEEGEKVvKTALDA 89
Cdd:PRK12938   4 RIAYVTGGMGGIGTSICQRLHKDGFKVVA--------GCGPNSPRRVKWLEDQKALGFDFIASEGNVGDWDST-KAAFDK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    90 F----GRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYS 165
Cdd:PRK12938  75 VkaevGEIDVLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFGQTNYS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   166 AAKLGLLGLANSLAIEGRKSNIHCNTIAPN-AGSRMTQTVMPeDLVEAL----------KPEYVAPLVLWLcheSCEENG 234
Cdd:PRK12938 155 TAKAGIHGFTMSLAQEVATKGVTVNTVSPGyIGTDMVKAIRP-DVLEKIvatipvrrlgSPDEIGSIVAWL---ASEESG 230

                 ....*..
gi 4504505   235 glFEVGA 241
Cdd:PRK12938 231 --FSTGA 235
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
3-226 1.73e-30

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 120.72  E-value: 1.73e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     3 SPLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKAVA---NYDSVEEG 79
Cdd:PRK06113   5 DNLRLDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINAD---------AANHVVDEIQQLGGQAFAcrcDITSEQEL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    80 EKVVKTALDAFGRIDVVVNNAGILRDRSFaRISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNF 159
Cdd:PRK06113  76 SALADFALSKLGKVDILVNNAGGGGPKPF-DMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNI 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4504505   160 GQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNA-GSRMTQTVMPEDLVEAL----------KPEYVAPLVLWLC 226
Cdd:PRK06113 155 NMTSYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAiLTDALKSVITPEIEQKMlqhtpirrlgQPQDIANAALFLC 232
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
11-226 1.86e-30

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: 120.37  E-value: 1.86e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   11 VVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKAVA---NYDSVEEGEKVVKTAL 87
Cdd:cd05365   1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKSE---------GAEAVAAAIQQAGGQAIGlecNVTSEQDLEAVVKATV 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   88 DAFGRIDVVVNNAGILRDRSFAR-ISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSA 166
Cdd:cd05365  72 SQFGGITILVNNAGGGGPKPFDMpMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRIAAYGS 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4504505  167 AKLGLLGLANSLAIEGRKSNIHCNTIAPNA------GSRMT----QTVMPEDLVEAL-KPEYVAPLVLWLC 226
Cdd:cd05365 152 SKAAVNHMTRNLAFDLGPKGIRVNAVAPGAvktdalASVLTpeieRAMLKHTPLGRLgEPEDIANAALFLC 222
PRK07063 PRK07063
SDR family oxidoreductase;
6-194 1.87e-30

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 120.54  E-value: 1.87e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRR--RGGKAVANYDSVEEGEKV- 82
Cdd:PRK07063   4 RLAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAA---------LAERAAAAIARdvAGARVLAVPADVTDAASVa 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    83 --VKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASG---IYG 157
Cdd:PRK07063  75 aaVAAAEEAFGPLDVLVNNAGINVFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASTHAfkiIPG 154
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 4504505   158 NFgqaNYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK07063 155 CF---PYPVAKHGLLGLTRALGIEYAARNVRVNAIAP 188
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
4-194 3.49e-30

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 124.56  E-value: 3.49e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     4 PLrfDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDlggdfkgVGKGSLAADKVVEEIrrrGGKAVAnYD--SVEEGEK 81
Cdd:PRK08261 207 PL--AGKVALVTGAARGIGAAIAEVLARDGAHVVCLD-------VPAAGEALAAVANRV---GGTALA-LDitAPDAPAR 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    82 VVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQ 161
Cdd:PRK08261 274 IAEHLAERHGGLDIVVHNAGITRDKTLANMDEARWDSVLAVNLLAPLRITEALLAAGALGDGGRIVGVSSISGIAGNRGQ 353
                        170       180       190
                 ....*....|....*....|....*....|...
gi 4504505   162 ANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK08261 354 TNYAASKAGVIGLVQALAPLLAERGITINAVAP 386
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
9-223 4.34e-30

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: 119.42  E-value: 4.34e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    9 GRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKA-----VANYDSVEEGekvV 83
Cdd:cd08943   1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPE---------IAEKVAEAAQGGPRALgvqcdVTSEAQVQSA---F 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   84 KTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKY-GRIIMTSSASGIYGNFGQA 162
Cdd:cd08943  69 EQAVLEFGGLDIVVSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGIgGNIVFNASKNAVAPGPNAA 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  163 NYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNA----------GSRMTQTVMPEDLVE------ALK----PEYVAPLV 222
Cdd:cd08943 149 AYSAAKAAEAHLARCLALEGGEDGIRVNTVNPDAvfrgskiwegVWRAARAKAYGLLEEeyrtrnLLKrevlPEDVAEAV 228

                .
gi 4504505  223 L 223
Cdd:cd08943 229 V 229
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
11-237 4.77e-30

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: 118.88  E-value: 4.77e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   11 VVLVTGAGAGLGRAYALAFAERGALVVVNDlggdfkgVGKGSLAAdkVVEEIRRRGGKA------VANYDSVEEgekVVK 84
Cdd:cd05339   1 IVLITGGGSGIGRLLALEFAKRGAKVVILD-------INEKGAEE--TANNVRKAGGKVhyykcdVSKREEVYE---AAK 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   85 TALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANY 164
Cdd:cd05339  69 KIKKEVGDVTILINNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADY 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  165 SAAKLGLLGLANSLAIE---GRKSNIHCNTIAP---NAGsrMTQTVMP--EDLVEALKPEYVAPLVLWlcheSCEENGGL 236
Cdd:cd05339 149 CASKAAAVGFHESLRLElkaYGKPGIKTTLVCPyfiNTG--MFQGVKTprPLLAPILEPEYVAEKIVR----AILTNQQM 222

                .
gi 4504505  237 F 237
Cdd:cd05339 223 L 223
PRK12828 PRK12828
short chain dehydrogenase; Provisional
6-225 7.14e-30

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 118.36  E-value: 7.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgVGKGSLAADKVVEEIRRRGGKAVA-NYDSVEEGEKVVK 84
Cdd:PRK12828   4 SLQGKVVAITGGFGGLGRATAAWLAARGARVAL---------IGRGAAPLSQTLPGVPADALRIGGiDLVDPQAARRAVD 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    85 TALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANY 164
Cdd:PRK12828  75 EVNRQFGRLDALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAGPGMGAY 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4504505   165 SAAKLGLLGLANSLAIEGRKSNIHCNTIAPnaGSRMTQTV---MP-EDLVEALKPEYVAPLVLWL 225
Cdd:PRK12828 155 AAAKAGVARLTEALAAELLDRGITVNAVLP--SIIDTPPNradMPdADFSRWVTPEQIAAVIAFL 217
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
10-196 9.72e-30

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: 117.87  E-value: 9.72e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   10 RVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgVGKGSLAADKVVEEIRRRGGKA------VANYDSVEEgekVV 83
Cdd:cd05360   1 QVVVITGASSGIGRATALAFAERGAKVVL---------AARSAEALHELAREVRELGGEAiavvadVADAAQVER---AA 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   84 KTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQAN 163
Cdd:cd05360  69 DTAVERFGRIDTWVNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRSAPLQAA 148
                       170       180       190
                ....*....|....*....|....*....|....*
gi 4504505  164 YSAAKLGLLGLANSLAIEGRKS--NIHCNTIAPNA 196
Cdd:cd05360 149 YSASKHAVRGFTESLRAELAHDgaPISVTLVQPTA 183
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
8-243 1.05e-29

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


Pssm-ID: 187626 [Multi-domain]  Cd Length: 241  Bit Score: 117.96  E-value: 1.05e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    8 DGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGgdfkgvgkgslaaDKVVEEIRRRGGKAVANYDsVEEGEKVVKTAL 87
Cdd:cd05368   1 DGKVALITAAAQGIGRAIALAFAREGANVIATDIN-------------EEKLKELERGPGITTRVLD-VTDKEQVAALAK 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   88 DaFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSS-ASGIYGNFGQANYSA 166
Cdd:cd05368  67 E-EGRIDVLFNCAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSvASSIKGVPNRFVYST 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  167 AKLGLLGLANSLAIEGRKSNIHCNTI------APNAGSRMTQTVMPEDLVEAL----------KPEYVAPLVLWLCH-ES 229
Cdd:cd05368 146 TKAAVIGLTKSVAADFAQQGIRCNAIcpgtvdTPSLEERIQAQPDPEEALKAFaarqplgrlaTPEEVAALAVYLASdES 225
                       250
                ....*....|....
gi 4504505  230 CEENGGLFEVGAGW 243
Cdd:cd05368 226 AYVTGTAVVIDGGW 239
PRK06181 PRK06181
SDR family oxidoreductase;
9-224 1.78e-29

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 117.77  E-value: 1.78e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     9 GRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKA---VANYDSVEEGEKVVKT 85
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNET---------RLASLAQELADHGGEAlvvPTDVSDAEACERLIEA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    86 ALDAFGRIDVVVNNAGILRDRSFARISDEDW-DIIHRVHLRGSFQVTRAAWEHMKKQKyGRIIMTSSASGIYGNFGQANY 164
Cdd:PRK06181  72 AVARFGGIDILVNNAGITMWSRFDELTDLSVfERVMRVNYLGAVYCTHAALPHLKASR-GQIVVVSSLAGLTGVPTRSGY 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4504505   165 SAAKLGLLGLANSLAIEGRKSNIHCNTIAPN-------------AGSRMTQTVMPEDlvEALKPEYVAPLVLW 224
Cdd:PRK06181 151 AASKHALHGFFDSLRIELADDGVAVTVVCPGfvatdirkraldgDGKPLGKSPMQES--KIMSAEECAEAILP 221
kduD TIGR01832
2-deoxy-D-gluconate 3-dehydrogenase; This model describes 2-deoxy-D-gluconate 3-dehydrogenase ...
9-194 2.15e-29

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: 117.17  E-value: 2.15e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505      9 GRVVLVTGAGAGLGRAYALAFAERGALVVvndlggdfkGVGKGSLA-ADKVVEEIRRRGGKAVANYDSVEEGEKVVKTAL 87
Cdd:TIGR01832   5 GKVALVTGANTGLGQGIAVGLAEAGADIV---------GAGRSEPSeTQQQVEALGRRFLSLTADLSDIEAIKALVDSAV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     88 DAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQ-KYGRIIMTSSASGIYGNFGQANYSA 166
Cdd:TIGR01832  76 EEFGHIDILVNNAGIIRRADAEEFSEKDWDDVMNVNLKSVFFLTQAAAKHFLKQgRGGKIINIASMLSFQGGIRVPSYTA 155
                         170       180
                  ....*....|....*....|....*...
gi 4504505    167 AKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:TIGR01832 156 SKHAVAGLTKLLANEWAAKGINVNAIAP 183
PRK08589 PRK08589
SDR family oxidoreductase;
6-194 8.33e-29

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 116.42  E-value: 8.33e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLggdfkgvgkgSLAADKVVEEIRRRGGKAVANYDSVEEGEKVVKT 85
Cdd:PRK08589   3 RLENKVAVITGASTGIGQASAIALAQEGAYVLAVDI----------AEAVSETVDKIKSNGGKAKAYHVDISDEQQVKDF 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    86 A---LDAFGRIDVVVNNAGIlrDRSFARISD---EDWDIIHRVHLRGSFQVTRAAWEHMKKQKyGRIIMTSSASGIYGNF 159
Cdd:PRK08589  73 AseiKEQFGRVDVLFNNAGV--DNAAGRIHEypvDVFDKIMAVDMRGTFLMTKMLLPLMMEQG-GSIINTSSFSGQAADL 149
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 4504505   160 GQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK08589 150 YRSGYNAAKGAVINFTKSIAIEYGRDGIRANAIAP 184
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
10-226 9.81e-29

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: 114.77  E-value: 9.81e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   10 RVVLVTGAGAGLGRAYALAFAERGALVVvndLGGDFKGVGKGSLAADKVVEEIrrrggkavaNYD--SVEEGEKVVKTAL 87
Cdd:cd08932   1 KVALVTGASRGIGIEIARALARDGYRVS---LGLRNPEDLAALSASGGDVEAV---------PYDarDPEDARALVDALR 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   88 DAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSAA 167
Cdd:cd08932  69 DRFGRIDVLVHNAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSAS 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4504505  168 KLGLLGLANSLAIEGRKSNIHCNTIAPNA-GSRMTQTVM---PEDLVEALKPEYVAPLVLWLC 226
Cdd:cd08932 149 KFALRALAHALRQEGWDHGVRVSAVCPGFvDTPMAQGLTlvgAFPPEEMIQPKDIANLVRMVI 211
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
487-599 1.11e-28

(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl CoA to (R)-3-hydroxyacyl-CoA as part of the PHA (polyhydroxyalkanoate) biosynthetic pathway. The structure of the monomer includes a five-strand antiparallel beta-sheet wrapped around a central alpha helix, referred to as a hot dog fold. The active site lies within a substrate-binding tunnel formed by the homodimer. Other enzymes with this fold include MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and the fatty acid synthase beta subunit.


Pssm-ID: 239525 [Multi-domain]  Cd Length: 127  Bit Score: 111.20  E-value: 1.11e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  487 RPPDAVLTDTTSLNQAALYRLSGDWNPLHIDPNFASLAGFDKPILHGLCTFGFSARRVLQQFADNDVSRFKAIKARFAKP 566
Cdd:cd03441   1 GELDSSGRTVTEADIALFARLSGDPNPIHVDPEYAKAAGFGGRIAHGMLTLSLASGLLVQWLPGTDGANLGSQSVRFLAP 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 4504505  567 VYPGQTLQTEMWKEGNR---------IHFQTKVQEtGDIVIS 599
Cdd:cd03441  81 VFPGDTLRVEVEVLGKRpskgrgvvtVRTEARNQG-GEVVLS 121
PRK07478 PRK07478
short chain dehydrogenase; Provisional
6-225 1.83e-28

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 114.64  E-value: 1.83e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNdlggdfkgvGKGSLAADKVVEEIRRRGGKAVANYDSVEE---GEKV 82
Cdd:PRK07478   3 RLNGKVAIITGASSGIGRAAAKLFAREGAKVVVG---------ARRQAELDQLVAEIRAEGGEAVALAGDVRDeayAKAL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    83 VKTALDAFGRIDVVVNNAGILRD-RSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNF-G 160
Cdd:PRK07478  74 VALAVERFGGLDIAFNNAGTLGEmGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARGGGSLIFTSTFVGHTAGFpG 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4504505   161 QANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNA-----GSRMTQTVMPEDLVE---ALK----PEYVAPLVLWL 225
Cdd:PRK07478 154 MAAYAASKAGLIGLTQVLAAEYGAQGIRVNALLPGGtdtpmGRAMGDTPEALAFVAglhALKrmaqPEEIAQAALFL 230
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
9-224 3.93e-28

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: 113.50  E-value: 3.93e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    9 GRVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgVGKGSLAADKVVEEIRRRGGKA----------VANYDSVEe 78
Cdd:cd08939   1 GKHVLITGGSSGIGKALAKELVKEGANVII---------VARSESKLEEAVEEIEAEANASgqkvsyisadLSDYEEVE- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   79 geKVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGN 158
Cdd:cd08939  71 --QAFAQAVEKGGPPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGI 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4504505  159 FGQANYSAAKLGLLGLANSLAIEGRKSNIH------CNTIAP-----NAgSRMTQTVMPEDLVEALKPEYVAPLVLW 224
Cdd:cd08939 149 YGYSAYCPSKFALRGLAESLRQELKPYNIRvsvvypPDTDTPgfeeeNK-TKPEETKAIEGSSGPITPEEAARIIVK 224
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
9-225 3.96e-28

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: 114.01  E-value: 3.96e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    9 GRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgsLAADKVVEEIRRRGGKAVA---NYDSVEEGEKVVKT 85
Cdd:cd05366   2 SKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLE--------EAAKSTIQEISEAGYNAVAvgaDVTDKDDVEALIDQ 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   86 ALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKY-GRIIMTSSASGIYGNFGQANY 164
Cdd:cd05366  74 AVEKFGSFDVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGHgGKIINASSIAGVQGFPNLGAY 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  165 SAAKLGLLGLANSLAIEGRKSNIHCNTIAP---------------------NAGSRMTQTVMPEDLVEALKPEYVAPLVL 223
Cdd:cd05366 154 SASKFAVRGLTQTAAQELAPKGITVNAYAPgivktemwdyideevgeiagkPEGEGFAEFSSSIPLGRLSEPEDVAGLVS 233

                ..
gi 4504505  224 WL 225
Cdd:cd05366 234 FL 235
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
9-221 4.37e-28

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 113.98  E-value: 4.37e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     9 GRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGK-----AVANYDSVEEGEKVV 83
Cdd:PRK12384   2 NQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSE---------KAANVAQEINAEYGEgmaygFGADATSEQSVLALS 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    84 KTALDAFGRIDVVVNNAGILRDrsfARISD---EDWDIIHRVHLRGSFQVTRAAWEHMKKQKY-GRIIMTSSASGIYGNF 159
Cdd:PRK12384  73 RGVDEIFGRVDLLVYNAGIAKA---AFITDfqlGDFDRSLQVNLVGYFLCAREFSRLMIRDGIqGRIIQINSKSGKVGSK 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4504505   160 GQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIapnagsrMTQTVMPEDLVEALKPEYVAPL 221
Cdd:PRK12384 150 HNSGYSAAKFGGVGLTQSLALDLAEYGITVHSL-------MLGNLLKSPMFQSLLPQYAKKL 204
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
7-216 6.30e-28

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: 113.38  E-value: 6.30e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    7 FDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkGSLAADKVVEEIR--RRGGKAVANYDSVEEGEKVVK 84
Cdd:cd05330   1 FKDKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEE------GLEAAKAALLEIApdAEVLLIKADVSDEAQVEAYVD 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   85 TALDAFGRIDVVVNNAGIlrDRSFARISDEDWDIIHRV---HLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQ 161
Cdd:cd05330  75 ATVEQFGRIDGFFNNAGI--EGKQNLTEDFGADEFDKVvsiNLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQ 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 4504505  162 ANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNAgsrmTQTVMPEDLVEALKPE 216
Cdd:cd05330 153 SGYAAAKHGVVGLTRNSAVEYGQYGIRINAIAPGA----ILTPMVEGSLKQLGPE 203
PRK06198 PRK06198
short chain dehydrogenase; Provisional
4-225 7.36e-28

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 113.18  E-value: 7.36e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     4 PLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkGVGKGSLAADKVVEEIRRRGGKAV---ANYDSVEEGE 80
Cdd:PRK06198   1 MGRLDGKVALVTGGTQGLGAAIARAFAERGAAGLV--------ICGRNAEKGEAQAAELEALGAKAVfvqADLSDVEDCR 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    81 KVVKTALDAFGRIDVVVNNAGiLRDR-SFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKY-GRI--IMTSSASGiy 156
Cdd:PRK06198  73 RVVAAADEAFGRLDALVNAAG-LTDRgTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKAeGTIvnIGSMSAHG-- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   157 gnfGQ---ANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP----NAGSRMTQTVM---PEDLVEA----------LKPE 216
Cdd:PRK06198 150 ---GQpflAAYCASKGALATLTRNAAYALLRNRIRVNGLNIgwmaTEGEDRIQREFhgaPDDWLEKaaatqpfgrlLDPD 226

                 ....*....
gi 4504505   217 YVAPLVLWL 225
Cdd:PRK06198 227 EVARAVAFL 235
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
10-242 2.29e-27

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


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 111.24  E-value: 2.29e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   10 RVVLVTGAGAGLGRAYALAFAERGALVVVNDLggDFKGVGKGSLAADKvveeirrRGGKAV---ANYDSVEEGEKVVKTA 86
Cdd:cd05323   1 KVAIITGGASGIGLATAKLLLKKGAKVAILDR--NENPGAAAELQAIN-------PKVKATfvqCDVTSWEQLAAAFKKA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   87 LDAFGRIDVVVNNAGILRDRS--FARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKY---GRIIMTSSASGIYGNFGQ 161
Cdd:cd05323  72 IEKFGRVDILINNAGILDEKSylFAGKLPPPWEKTIDVNLTGVINTTYLALHYMDKNKGgkgGVIVNIGSVAGLYPAPQF 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  162 ANYSAAKLGLLGLANSLAIEG-RKSNIHCNTIAPNAGSrmTQTVMPEDLVEA--------LKPEYVAPLVLWLChESCEE 232
Cdd:cd05323 152 PVYSASKHGVVGFTRSLADLLeYKTGVRVNAICPGFTN--TPLLPDLVAKEAemlpsaptQSPEVVAKAIVYLI-EDDEK 228
                       250
                ....*....|
gi 4504505  233 NGGLFEVGAG 242
Cdd:cd05323 229 NGAIWIVDGG 238
PRK07890 PRK07890
short chain dehydrogenase; Provisional
7-194 3.45e-27

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 111.20  E-value: 3.45e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     7 FDGRVVLVTGAGAGLGRAYALAFAERGALVVvndlggdfkgvgkgsLAA------DKVVEEIRRRGGKAVA---NYDSVE 77
Cdd:PRK07890   3 LKGKVVVVSGVGPGLGRTLAVRAARAGADVV---------------LAArtaerlDEVAAEIDDLGRRALAvptDITDED 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    78 EGEKVVKTALDAFGRIDVVVNNAgiLRDRSFARISDEDWDIIHRV---HLRGSFQVTRAAWEHMKKQKyGRIIMTSSASG 154
Cdd:PRK07890  68 QCANLVALALERFGRVDALVNNA--FRVPSMKPLADADFAHWRAVielNVLGTLRLTQAFTPALAESG-GSIVMINSMVL 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 4504505   155 IYGNFGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK07890 145 RHSQPKYGAYKMAKGALLAASQSLATELGPQGIRVNSVAP 184
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
9-225 4.09e-27

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: 110.84  E-value: 4.09e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    9 GRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfKGVGkgslaadkvVEEIRRRGGKAVANYDSVEEGEKVVKTALD 88
Cdd:cd05371   2 GLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNS-PGET---------VAKLGDNCRFVPVDVTSEKDVKAALALAKA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   89 AFGRIDVVVNNAGIL-------RDRSFArISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQ------KYGRIIMTSSASGI 155
Cdd:cd05371  72 KFGRLDIVVNCAGIAvaaktynKKGQQP-HSLELFQRVINVNLIGTFNVIRLAAGAMGKNepdqggERGVIINTASVAAF 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  156 YGNFGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNA-GSRMTQTvMPEDLVEAL-----------KPEYVAPLVL 223
Cdd:cd05371 151 EGQIGQAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLfDTPLLAG-LPEKVRDFLakqvpfpsrlgDPAEYAHLVQ 229

                ..
gi 4504505  224 WL 225
Cdd:cd05371 230 HI 231
PRK07109 PRK07109
short chain dehydrogenase; Provisional
6-196 4.26e-27

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 112.71  E-value: 4.26e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgVGKGSLAADKVVEEIRRRGGKA------VANYDSVEEg 79
Cdd:PRK07109   5 PIGRQVVVITGASAGVGRATARAFARRGAKVVL---------LARGEEGLEALAAEIRAAGGEAlavvadVADAEAVQA- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    80 ekVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNF 159
Cdd:PRK07109  75 --AADRAEEELGPIDTWVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALAYRSIP 152
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 4504505   160 GQANYSAAKLGLLGLANSLAIE--GRKSNIHCNTIAPNA 196
Cdd:PRK07109 153 LQSAYCAAKHAIRGFTDSLRCEllHDGSPVSVTMVQPPA 191
PRK06114 PRK06114
SDR family oxidoreductase;
6-194 5.12e-27

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 110.64  E-value: 5.12e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkGSLAadKVVEEIRRRGGKAV---ANYDSVEEGEKV 82
Cdd:PRK06114   5 DLDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTD------DGLA--ETAEHIEAAGRRAIqiaADVTSKADLRAA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    83 VKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFG-- 160
Cdd:PRK06114  77 VARTEAELGALTLAVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASMSGIIVNRGll 156
                        170       180       190
                 ....*....|....*....|....*....|....
gi 4504505   161 QANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK06114 157 QAHYNASKAGVIHLSKSLAMEWVGRGIRVNSISP 190
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
7-208 5.47e-27

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: 110.75  E-value: 5.47e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    7 FDGRVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgVGKGSLAADKVVEEIRRRGGKAV----ANYDSVEEGEKV 82
Cdd:cd05332   1 LQGKVVIITGASSGIGEELAYHLARLGARLVL---------SARREERLEEVKSECLELGAPSPhvvpLDMSDLEDAEQV 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   83 VKTALDAFGRIDVVVNNAGIlrdRSFARISDEDWDI---IHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNF 159
Cdd:cd05332  72 VEEALKLFGGLDILINNAGI---SMRSLFHDTSIDVdrkIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVP 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 4504505  160 GQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPnaGSRMTQTVMPED 208
Cdd:cd05332 149 FRTAYAASKHALQGFFDSLRAELSEPNISVTVVCP--GLIDTNIAMNAL 195
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
9-225 5.67e-27

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 110.59  E-value: 5.67e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     9 GRVVLVTGAGAGLGRAYALAFAERGALVVVNDLgGDFKGvgkgslaADKVVEEIRRRGGKAVANYD--SVEEG-EKVVKT 85
Cdd:PRK08936   7 GKVVVITGGSTGLGRAMAVRFGKEKAKVVINYR-SDEEE-------ANDVAEEIKKAGGEAIAVKGdvTVESDvVNLIQT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    86 ALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQ-KYGRII-MTSSASGI-YGNFgqA 162
Cdd:PRK08936  79 AVKEFGTLDVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHdIKGNIInMSSVHEQIpWPLF--V 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4504505   163 NYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNA------GSRMTQTVMPEDLVEAL------KPEYVAPLVLWL 225
Cdd:PRK08936 157 HYAASKGGVKLMTETLAMEYAPKGIRVNNIGPGAintpinAEKFADPKQRADVESMIpmgyigKPEEIAAVAAWL 231
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
3-205 6.42e-27

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 110.36  E-value: 6.42e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     3 SPLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLggDFKGVGKGSLAADKVveeirrrggkAVANYDSVEEgekV 82
Cdd:PRK08220   2 NAMDFSGKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQ--AFLTQEDYPFATFVL----------DVSDAAAVAQ---V 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    83 VKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQA 162
Cdd:PRK08220  67 CQRLLAETGPLDVLVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAAHVPRIGMA 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 4504505   163 NYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPnaGSrmTQTVM 205
Cdd:PRK08220 147 AYGASKAALTSLAKCVGLELAPYGVRCNVVSP--GS--TDTDM 185
PRK07825 PRK07825
short chain dehydrogenase; Provisional
6-212 8.33e-27

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 110.42  E-value: 8.33e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKA--VANYDSVEEgekVV 83
Cdd:PRK07825   2 DLRGKVVAITGGARGIGLATARALAALGARVAIGDLDEA---------LAKETAAELGLVVGGPldVTDPASFAA---FL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    84 KTALDAFGRIDVVVNNAGILRDRSFArisDEDWDIIHR---VHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFG 160
Cdd:PRK07825  70 DAVEADLGPIDVLVNNAGVMPVGPFL---DEPDAVTRRildVNVYGVILGSKLAAPRMVPRGRGHVVNVASLAGKIPVPG 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4504505   161 QANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPN-------AGSRMT---QTVMPEDLVEA 212
Cdd:PRK07825 147 MATYCASKHAVVGFTDAARLELRGTGVHVSVVLPSfvnteliAGTGGAkgfKNVEPEDVAAA 208
PRK07831 PRK07831
SDR family oxidoreductase;
8-213 1.02e-26

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 110.12  E-value: 1.02e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     8 DGRVVLVTGA-GAGLGRAYALAFAERGALVVVND-----LGGdfkgvgkgslAADKVVEEI-RRRGGKAVANYDSVEEGE 80
Cdd:PRK07831  16 AGKVVLVTAAaGTGIGSATARRALEEGARVVISDiherrLGE----------TADELAAELgLGRVEAVVCDVTSEAQVD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    81 KVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMT-SSASGIYGNF 159
Cdd:PRK07831  86 ALIDAAVERLGRLDVLVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGHGGVIVNnASVLGWRAQH 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 4504505   160 GQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPN-AGSRMTQTVMPEDLVEAL 213
Cdd:PRK07831 166 GQAHYAAAKAGVMALTRCSALEAAEYGVRINAVAPSiAMHPFLAKVTSAELLDEL 220
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
9-225 1.75e-26

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: 108.43  E-value: 1.75e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    9 GRVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgVGKGSLAADKVVEEIRRRGGKA----VANYD--SVEEGEKV 82
Cdd:cd05340   4 DRIILVTGASDGIGREAALTYARYGATVIL---------LGRNEEKLRQVADHINEEGGRQpqwfILDLLtcTSENCQQL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   83 VKTALDAFGRIDVVVNNAGILRDRS-FARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQ 161
Cdd:cd05340  75 AQRIAVNYPRLDGVLHNAGLLGDVCpLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANW 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4504505  162 ANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNA--GSRMTQTVMPEDLVEALKPEYVAPLVLWL 225
Cdd:cd05340 155 GAYAVSKFATEGL*QVLADEYQQRNLRVNCINPGGtrTAMRASAFPTEDPQKLKTPADIMPLYLWL 220
PRK12743 PRK12743
SDR family oxidoreductase;
10-244 2.18e-26

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 108.97  E-value: 2.18e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    10 RVVLVTGAGAGLGRAYALAFAERGAlvvvnDLGGDFKGVGKGslaADKVVEEIRRRGGKAVA---NYDSVEEGEKVVKTA 86
Cdd:PRK12743   3 QVAIVTASDSGIGKACALLLAQQGF-----DIGITWHSDEEG---AKETAEEVRSHGVRAEIrqlDLSDLPEGAQALDKL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    87 LDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQ-KYGRIIMTSSASGIYGNFGQANYS 165
Cdd:PRK12743  75 IQRLGRIDVLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQgQGGRIINITSVHEHTPLPGASAYT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   166 AAKLGLLGLANSLAIEGRKSNIHCNTIAPNA-GSRMTQtVMPEDLVEALKPEY----------VAPLVLWLCHEsceenG 234
Cdd:PRK12743 155 AAKHALGGLTKAMALELVEHGILVNAVAPGAiATPMNG-MDDSDVKPDSRPGIplgrpgdtheIASLVAWLCSE-----G 228
                        250
                 ....*....|
gi 4504505   235 GLFEVGAGWI 244
Cdd:PRK12743 229 ASYTTGQSLI 238
PRK05650 PRK05650
SDR family oxidoreductase;
12-194 2.24e-26

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 109.36  E-value: 2.24e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    12 VLVTGAGAGLGRAYALAFAERG---ALVVVNDLGGDfkgvgkgslaadKVVEEIRRRGGKA------VANYDSVEegeKV 82
Cdd:PRK05650   3 VMITGAASGLGRAIALRWAREGwrlALADVNEEGGE------------ETLKLLREAGGDGfyqrcdVRDYSQLT---AL 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    83 VKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQA 162
Cdd:PRK05650  68 AQACEEKWGGIDVIVNNAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAMS 147
                        170       180       190
                 ....*....|....*....|....*....|..
gi 4504505   163 NYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK05650 148 SYNVAKAGVVALSETLLVELADDEIGVHVVCP 179
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
6-226 2.29e-26

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: 108.69  E-value: 2.29e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgVGKGSLAADKVVEEIRRRGGKA---VANYDSVEEGEKV 82
Cdd:cd05329   3 NLEGKTALVTGGTKGIGYAIVEELAGLGAEVYT---------CARNQKELDECLTEWREKGFKVegsVCDVSSRSERQEL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   83 VKTALDAF-GRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQ 161
Cdd:cd05329  74 MDTVASHFgGKLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSG 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4504505  162 ANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPN-AGSRMTQTVMPED-----------LVEALKPEYVAPLVLWLC 226
Cdd:cd05329 154 APYGATKGALNQLTRSLACEWAKDNIRVNAVAPWvIATPLVEPVIQQKenldkviertpLKRFGEPEEVAALVAFLC 230
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
6-230 3.28e-26

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: 108.53  E-value: 3.28e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgSLAADKVVEEIRRRGGKAVA-NYDSVEEG--EKV 82
Cdd:cd05355  23 KLKGKKALITGGDSGIGRAVAIAFAREGADVAINYLPEE-------EDDAEETKKLIEEEGRKCLLiPGDLGDESfcRDL 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   83 VKTALDAFGRIDVVVNNAGILRD-RSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQkyGRIIMTSSASGIYGNFGQ 161
Cdd:cd05355  96 VKEVVKEFGKLDILVNNAAYQHPqESIEDITTEQLEKTFRTNIFSMFYLTKAALPHLKKG--SSIINTTSVTAYKGSPHL 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  162 ANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPnaGSRMTQTV---MPEDLVE----------ALKPEYVAPLVLWLCHE 228
Cdd:cd05355 174 LDYAATKGAIVAFTRGLSLQLAEKGIRVNAVAP--GPIWTPLIpssFPEEKVSefgsqvpmgrAGQPAEVAPAYVFLASQ 251

                ..
gi 4504505  229 SC 230
Cdd:cd05355 252 DS 253
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
10-194 1.28e-25

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: 106.39  E-value: 1.28e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   10 RVVLVTGAGAGLGRAYALAFAERGALVVVNDLggdfkgvgKGSLAADKVVEEIrrrGGKAVANYDSVEEGEKV---VKTA 86
Cdd:cd05349   1 QVVLVTGASRGLGAAIARSFAREGARVVVNYY--------RSTESAEAVAAEA---GERAIAIQADVRDRDQVqamIEEA 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   87 LDAFGRIDVVVNNAgiLRDRSF-----ARISDEDW-DIIHRVH--LRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGN 158
Cdd:cd05349  70 KNHFGPVDTIVNNA--LIDFPFdpdqrKTFDTIDWeDYQQQLEgaVKGALNLLQAVLPDFKERGSGRVINIGTNLFQNPV 147
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 4504505  159 FGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:cd05349 148 VPYHDYTTAKAALLGFTRNMAKELGPYGITVNMVSG 183
PRK07326 PRK07326
SDR family oxidoreductase;
7-225 1.32e-25

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 105.86  E-value: 1.32e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     7 FDGRVVLVTGAGAGLGRAYALAFAERGALVVVNdlGGDFKGVGKgslAADKVVEEIRRRGGKA-VANYDSVEegeKVVKT 85
Cdd:PRK07326   4 LKGKVALITGGSKGIGFAIAEALLAEGYKVAIT--ARDQKELEE---AAAELNNKGNVLGLAAdVRDEADVQ---RAVDA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    86 ALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKyGRIIMTSSASGIygNF--GQAN 163
Cdd:PRK07326  76 IVAAFGGLDVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGG-GYIINISSLAGT--NFfaGGAA 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4504505   164 YSAAKLGLLGLANSLAIEGRKSNIHCNTIAPnaGSRMTQ---TVMPEDLVEALKPEYVAPLVLWL 225
Cdd:PRK07326 153 YNASKFGLVGFSEAAMLDLRQYGIKVSTIMP--GSVATHfngHTPSEKDAWKIQPEDIAQLVLDL 215
PRK08267 PRK08267
SDR family oxidoreductase;
12-187 1.53e-25

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 106.56  E-value: 1.53e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    12 VLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKA----VANYDSVEEgekvvktAL 87
Cdd:PRK08267   4 IFITGAASGIGRATALLFAAEGWRVGAYDINEA---------GLAALAAELGAGNAWTgaldVTDRAAWDA-------AL 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    88 DAF-----GRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQA 162
Cdd:PRK08267  68 ADFaaatgGRLDVLFNNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSSASAIYGQPGLA 147
                        170       180
                 ....*....|....*....|....*
gi 4504505   163 NYSAAKLGLLGLANSLAIEGRKSNI 187
Cdd:PRK08267 148 VYSATKFAVRGLTEALDLEWRRHGI 172
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
9-225 1.58e-25

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 106.11  E-value: 1.58e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     9 GRVVLVTGAGAGLGRAYALAFAERGALVVVndLGgdfKGVGKgsLAAdkVVEEIRRRGGK--AVANYD----SVEEGEKV 82
Cdd:PRK08945  12 DRIILVTGAGDGIGREAALTYARHGATVIL--LG---RTEEK--LEA--VYDEIEAAGGPqpAIIPLDlltaTPQNYQQL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    83 VKTALDAFGRIDVVVNNAGILRDRS-FARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQ 161
Cdd:PRK08945  83 ADTIEEQFGRLDGVLHNAGLLGELGpMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSSSVGRQGRANW 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   162 ANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNAgsrmTQTVM-----PEDLVEALK-PEYVAPLVLWL 225
Cdd:PRK08945 163 GAYAVSKFATEGMMQVLADEYQGTNLRVNCINPGG----TRTAMrasafPGEDPQKLKtPEDIMPLYLYL 228
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
7-206 2.69e-25

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 105.80  E-value: 2.69e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     7 FD--GRVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgVGKGSLAADKVVEEIRRRGGKAV---ANYDSVEEGEK 81
Cdd:PRK08213   8 FDlsGKTALVTGGSRGLGLQIAEALGEAGARVVL---------SARKAEELEEAAAHLEALGIDALwiaADVADEADIER 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    82 VVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEH-MKKQKYGRIIMTSSASGIYGN-- 158
Cdd:PRK08213  79 LAEETLERFGHVDILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAVAKRsMIPRGYGRIINVASVAGLGGNpp 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 4504505   159 --FGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPnaG---SRMTQTVMP 206
Cdd:PRK08213 159 evMDTIAYNTSKGAVINFTRALAAEWGPHGIRVNAIAP--GffpTKMTRGTLE 209
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
6-194 3.11e-25

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 105.41  E-value: 3.11e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDlggdfkgvgKGSLAADkVVEEIRRRGGKA---VANYDSVEEGEKV 82
Cdd:PRK12823   5 RFAGKVVVVTGAAQGIGRGVALRAAAEGARVVLVD---------RSELVHE-VAAELRAAGGEAlalTADLETYAGAQAA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    83 VKTALDAFGRIDVVVNN-AGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSAS--GIYgnf 159
Cdd:PRK12823  75 MAAAVEAFGRIDVLINNvGGTIWAKPFEEYEEEQIEAEIRRSLFPTLWCCRAVLPHMLAQGGGAIVNVSSIAtrGIN--- 151
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 4504505   160 gQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK12823 152 -RVPYSAAKGGVNALTASLAFEYAEHGIRVNAVAP 185
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
7-194 3.91e-25

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: 104.98  E-value: 3.91e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    7 FDGRVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgVGKGSLAADKVVEEIRR-RGGKA------VANYDSVEEg 79
Cdd:cd05369   1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAI---------AGRKPEVLEAAAEEISSaTGGRAhpiqcdVRDPEAVEA- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   80 ekVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEH-MKKQKYGRIIMTSSASGIYGN 158
Cdd:cd05369  71 --AVDETLKEFGKIDILINNAAGNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKRlIEAKHGGSILNISATYAYTGS 148
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 4504505  159 FGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:cd05369 149 PFQVHSAAAKAGVDALTRSLAVEWGPYGIRVNAIAP 184
SCP2 pfam02036
SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the ...
628-731 4.05e-25

SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the SCP2 protein as well as the C terminus of the enzyme estradiol 17 beta-dehydrogenase EC:1.1.1.62. The UNC-24 protein contains an SPFH domain pfam01145.


Pssm-ID: 460423 [Multi-domain]  Cd Length: 100  Bit Score: 100.02  E-value: 4.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    628 FEEIGRRLKDiGPEVVKKVNA-VFEWHITKGGNigaKWTIDLKSGSGKVyQGPAKGAADTTIILSDEDFMEVVLGKLDPQ 706
Cdd:pfam02036   1 LNQLLARDPA-ARELLKKLNGkVIRFDLTDLGL---SLTLDLKDGGGRV-LAGDEGKADVTLSASDSDLLALATGKLNPQ 75
                          90       100
                  ....*....|....*....|....*
gi 4504505    707 KAFFSGRLKARGNIMLSQKLQMILK 731
Cdd:pfam02036  76 KAFMQGKLKIEGDMELAQKLEGLLK 100
PRK05855 PRK05855
SDR family oxidoreductase;
6-194 6.68e-25

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 109.69  E-value: 6.68e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLggdfkgvgkGSLAADKVVEEIRRRGGKA------VANYDSVEE- 78
Cdd:PRK05855 312 PFSGKLVVVTGAGSGIGRETALAFAREGAEVVASDI---------DEAAAERTAELIRAAGAVAhayrvdVSDADAMEAf 382
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    79 GEKVVKTAldafGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQ-KYGRIIMTSSASGIYG 157
Cdd:PRK05855 383 AEWVRAEH----GVPDIVVNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVERgTGGHIVNVASAAAYAP 458
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 4504505   158 NFGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK05855 459 SRSLPAYATSKAAVLMLSECLRAELAAAGIGVTAICP 495
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
8-194 7.53e-25

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 104.76  E-value: 7.53e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     8 DGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKA------VANYDSVEEGek 81
Cdd:PRK07097   9 KGKIALITGASYGIGFAIAKAYAKAGATIVFNDINQE---------LVDKGLAAYRELGIEAhgyvcdVTDEDGVQAM-- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    82 vVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQ 161
Cdd:PRK07097  78 -VSQIEKEVGVIDILVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMMSELGRETV 156
                        170       180       190
                 ....*....|....*....|....*....|...
gi 4504505   162 ANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK07097 157 SAYAAAKGGLKMLTKNIASEYGEANIQCNGIGP 189
PRK07856 PRK07856
SDR family oxidoreductase;
4-181 1.22e-24

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 103.47  E-value: 1.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     4 PLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVV---------NDLGGDFkgvgkgsLAADkvveeirrrggkaVANYD 74
Cdd:PRK07856   1 NLDLTGRVVLVTGGTRGIGAGIARAFLAAGATVVVcgrrapetvDGRPAEF-------HAAD-------------VRDPD 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    75 SVeegEKVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKY-GRIIMTSSAS 153
Cdd:PRK07856  61 QV---AALVDAIVERHGRLDVLVNNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQQPGgGSIVNIGSVS 137
                        170       180
                 ....*....|....*....|....*...
gi 4504505   154 GIYGNFGQANYSAAKLGLLGLANSLAIE 181
Cdd:PRK07856 138 GRRPSPGTAAYGAAKAGLLNLTRSLAVE 165
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
1-194 1.25e-24

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 103.94  E-value: 1.25e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     1 MGSPLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDL-GGDFKGVGKGSLAADkvveeirrrggkaVANYDSVEEG 79
Cdd:PRK06171   1 MQDWLNLQGKIIIVTGGSSGIGLAIVKELLANGANVVNADIhGGDGQHENYQFVPTD-------------VSSAEEVNHT 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    80 ekvVKTALDAFGRIDVVVNNAGI-----LRD----RSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTS 150
Cdd:PRK06171  68 ---VAEIIEKFGRIDGLVNNAGIniprlLVDekdpAGKYELNEAAFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMS 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 4504505   151 SASGIYGNFGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK06171 145 SEAGLEGSEGQSCYAATKAALNSFTRSWAKELGKHNIRVVGVAP 188
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
6-225 1.59e-24

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 103.32  E-value: 1.59e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGgdfkgvgkgslaADKVVEEIRRRGG---KA-VANYDSVEEGEK 81
Cdd:PRK06463   4 RFKGKVALITGGTRGIGRAIAEAFLREGAKVAVLYNS------------AENEAKELREKGVftiKCdVGNRDQVKKSKE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    82 VVKtalDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGI-YGNFG 160
Cdd:PRK06463  72 VVE---KEFGRVDVLVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIgTAAEG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   161 QANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPN-AGSRMTQTVMPEDLVEAL--------------KPEYVAPLVLWL 225
Cdd:PRK06463 149 TTFYAITKAGIIILTRRLAFELGKYGIRVNAVAPGwVETDMTLSGKSQEEAEKLrelfrnktvlkttgKPEDIANIVLFL 228
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
9-194 1.81e-24

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: 103.18  E-value: 1.81e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    9 GRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKAV----ANYDSVEEGEKVVK 84
Cdd:cd08930   2 DKIILITGAAGLIGKAFCKALLSAGARLILADINAP---------ALEQLKEELTNLYKNRVialeLDITSKESIKELIE 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   85 TALDAFGRIDVVVNNAGI---LRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASG------- 154
Cdd:cd08930  73 SYLEKFGRIDILINNAYPspkVWGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGviapdfr 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 4504505  155 IYGNFGQ---ANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:cd08930 153 IYENTQMyspVEYSVIKAGIIHLTKYLAKYYADTGIRVNAISP 195
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
9-216 2.78e-24

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 102.88  E-value: 2.78e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     9 GRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKAVANYDSVEEGEKV---VKT 85
Cdd:PRK08643   2 SKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEE---------TAQAAADKLSKDGGKAIAVKADVSDRDQVfaaVRQ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    86 ALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKY-GRIIMTSSASGIYGNFGQANY 164
Cdd:PRK08643  73 VVDTFGDLNVVVNNAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGHgGKIINATSQAGVVGNPELAVY 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 4504505   165 SAAKLGLLGLANSLAIEGRKSNIHCNTIAPNagsrMTQTVMPEDLV-----EALKPE 216
Cdd:PRK08643 153 SSTKFAVRGLTQTAARDLASEGITVNAYAPG----IVKTPMMFDIAhqvgeNAGKPD 205
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
6-196 2.89e-24

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: 102.61  E-value: 2.89e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLggdfkgvgkgSLAADKVVEEIRRRGGKAV---ANYDSVEEGEKV 82
Cdd:cd08937   1 RFEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDR----------SELVHEVLAEILAAGDAAHvhtADLETYAGAQGV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   83 VKTALDAFGRIDVVVNNAG--ILRdRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSAS--GIYgn 158
Cdd:cd08937  71 VRAAVERFGRVDVLINNVGgtIWA-KPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSIAtrGIY-- 147
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 4504505  159 fgQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNA 196
Cdd:cd08937 148 --RIPYSAAKGGVNALTASLAFEHARDGIRVNAVAPGG 183
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
8-223 3.99e-24

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 102.34  E-value: 3.99e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     8 DGRVVLVTGAGAGLGRAYALAFAERGALVVVNDlggdfkgvgkgsLAADKvVEEIRRRGGKAVA----NYDSVEEGEKVV 83
Cdd:PRK06200   5 HGQVALITGGGSGIGRALVERFLAEGARVAVLE------------RSAEK-LASLRQRFGDHVLvvegDVTSYADNQRAV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    84 KTALDAFGRIDVVVNNAGI------LRDRSFARIsDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKyGRIIMTSSASGIYG 157
Cdd:PRK06200  72 DQTVDAFGKLDCFVGNAGIwdyntsLVDIPAETL-DTAFDEIFNVNVKGYLLGAKAALPALKASG-GSMIFTLSNSSFYP 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   158 NFGQANYSAAKLGLLGLANSLAIEgRKSNIHCNTIAPNA--------------GSRMTQTVMPEDLVEALKP-------- 215
Cdd:PRK06200 150 GGGGPLYTASKHAVVGLVRQLAYE-LAPKIRVNGVAPGGtvtdlrgpaslgqgETSISDSPGLADMIAAITPlqfapqpe 228

                 ....*...
gi 4504505   216 EYVAPLVL 223
Cdd:PRK06200 229 DHTGPYVL 236
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
8-194 7.26e-24

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: 101.46  E-value: 7.26e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    8 DGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgSLAAdkVVEEIRRRGGKA---VANYDSVEEGEKVVK 84
Cdd:cd08945   2 DSEVALVTGATSGIGLAIARRLGKEGLRVFVCARGEE-------GLAT--TVKELREAGVEAdgrTCDVRSVPEIEALVA 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   85 TALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEH--MKKQKYGRIIMTSSASGIYGNFGQA 162
Cdd:cd08945  73 AAVARYGPIDVLVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKAggMLERGTGRIINIASTGGKQGVVHAA 152
                       170       180       190
                ....*....|....*....|....*....|..
gi 4504505  163 NYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:cd08945 153 PYSASKHGVVGFTKALGLELARTGITVNAVCP 184
PRK06057 PRK06057
short chain dehydrogenase; Provisional
6-194 8.11e-24

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 101.35  E-value: 8.11e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgKGSLAADKVveeirrrGGKAV-ANYDSVEEGEKVVK 84
Cdd:PRK06057   4 RLAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPE-----AGKAAADEV-------GGLFVpTDVTDEDAVNALFD 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    85 TALDAFGRIDVVVNNAGIL--RDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGN-FGQ 161
Cdd:PRK06057  72 TAAETYGSVDIAFNNAGISppEDDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASFVAVMGSaTSQ 151
                        170       180       190
                 ....*....|....*....|....*....|...
gi 4504505   162 ANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK06057 152 ISYTASKGGVLAMSRELGVQFARQGIRVNALCP 184
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
4-194 9.26e-24

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 101.26  E-value: 9.26e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     4 PLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIrrrGGKA------VANYDSVE 77
Cdd:PRK07067   1 MMRLQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPA---------RARLAALEI---GPAAiavsldVTRQDSID 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    78 EGekvVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQ-KYGRIIMTSSASGIY 156
Cdd:PRK07067  69 RI---VAAAVERFGGIDILFNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQgRGGKIINMASQAGRR 145
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 4504505   157 GNFGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK07067 146 GEALVSHYCATKAAVISYTQSAALALIRHGINVNAIAP 183
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
7-205 1.26e-23

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 100.04  E-value: 1.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     7 FDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGdfKGVGKGSLAADKVveeirrrggkavanyDSVEEgekvVKTA 86
Cdd:PRK06550   3 FMTKTVLITGAASGIGLAQARAFLAQGAQVYGVDKQD--KPDLSGNFHFLQL---------------DLSDD----LEPL 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    87 LDAFGRIDVVVNNAGILRD-RSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRII-MTSSASGIYGNFGQAnY 164
Cdd:PRK06550  62 FDWVPSVDILCNTAGILDDyKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIInMCSIASFVAGGGGAA-Y 140
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 4504505   165 SAAKLGLLGLANSLAIEGRKSNIHCNTIAPNAgsrmTQTVM 205
Cdd:PRK06550 141 TASKHALAGFTKQLALDYAKDGIQVFGIAPGA----VKTPM 177
PRK07074 PRK07074
SDR family oxidoreductase;
10-202 1.94e-23

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 100.23  E-value: 1.94e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    10 RVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRrrGGKAVANYDSVEEGEKV---VKTA 86
Cdd:PRK07074   3 RTALVTGAAGGIGQALARRFLAAGDRVLALDIDAA---------ALAAFADALG--DARFVPVACDLTDAASLaaaLANA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    87 LDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGnFGQANYSA 166
Cdd:PRK07074  72 AAERGPVDVLVANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVNGMAA-LGHPAYSA 150
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 4504505   167 AKLGLLGLANSLAIEGRKSNIHCNTIAPnaGSRMTQ 202
Cdd:PRK07074 151 AKAGLIHYTKLLAVEYGRFGIRANAVAP--GTVKTQ 184
PRK07060 PRK07060
short chain dehydrogenase; Provisional
1-206 2.89e-23

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 99.40  E-value: 2.89e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     1 MGSPLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVvndlggdfkgvgkgslAADKVVEEIRRRGGKAVANYDSVEEG- 79
Cdd:PRK07060   1 MNMAFDFSGKSVLVTGASSGIGRACAVALAQRGARVV----------------AAARNAAALDRLAGETGCEPLRLDVGd 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    80 EKVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHM-KKQKYGRIIMTSSASGIYGN 158
Cdd:PRK07060  65 DAAIRAALAAAGAFDGLVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMiAAGRGGSIVNVSSQAALVGL 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 4504505   159 FGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPnagsrmTQTVMP 206
Cdd:PRK07060 145 PDHLAYCASKAALDAITRVLCVELGPHGIRVNSVNP------TVTLTP 186
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
8-196 2.94e-23

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: 99.53  E-value: 2.94e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    8 DGRVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgVGKGSLAADKVVEEIRRRGGKA-VANYDSVEEGE--KVVK 84
Cdd:cd08934   2 QGKVALVTGASSGIGEATARALAAEGAAVAI---------AARRVDRLEALADELEAEGGKAlVLELDVTDEQQvdAAVE 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   85 TALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANY 164
Cdd:cd08934  73 RTVEALGRLDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVY 152
                       170       180       190
                ....*....|....*....|....*....|..
gi 4504505  165 SAAKLGLLGLANSLAIEGRKSNIHCNTIAPNA 196
Cdd:cd08934 153 NATKFGVNAFSEGLRQEVTERGVRVVVIEPGT 184
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
1-226 3.02e-23

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 99.83  E-value: 3.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     1 MGSPLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKA------VANYD 74
Cdd:PRK08085   1 MNDLFSLAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAE---------RAELAVAKLRQEGIKAhaapfnVTHKQ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    75 SVEEG-EKVVKTaldaFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSAS 153
Cdd:PRK08085  72 EVEAAiEHIEKD----IGPIDVLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMQ 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4504505   154 GIYGNFGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNagsrMTQTVMPEDLVEalKPEYVAplvlWLC 226
Cdd:PRK08085 148 SELGRDTITPYAASKGAVKMLTRGMCVELARHNIQVNGIAPG----YFKTEMTKALVE--DEAFTA----WLC 210
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
9-213 3.04e-23

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 99.41  E-value: 3.04e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     9 GRVVLVTGAGAGLGRAYALAFAERGALVVVNdlggdfkgVGKGSLAADKVVEEIRRRGGKAV---ANYDSVEEGEKVVKT 85
Cdd:PRK06077   6 DKVVVVTGSGRGIGRAIAVRLAKEGSLVVVN--------AKKRAEEMNETLKMVKENGGEGIgvlADVSTREGCETLAKA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    86 ALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQkyGRIIMTSSASGIYGNFGQANYS 165
Cdd:PRK06077  78 TIDRYGVADILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEMREG--GAIVNIASVAGIRPAYGLSIYG 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 4504505   166 AAKLGLLGLANSLAIEgRKSNIHCNTIAPNagsrMTQTVMPEDLVEAL 213
Cdd:PRK06077 156 AMKAAVINLTKYLALE-LAPKIRVNAIAPG----FVKTKLGESLFKVL 198
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
12-205 5.13e-23

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: 98.70  E-value: 5.13e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   12 VLVTGAGAGLGRAYALAFAERGALVVvndlggdfkgvgkgslAADKVVEEIRRRGGKA------VANYDSVEEgekVVKT 85
Cdd:cd05331   1 VIVTGAAQGIGRAVARHLLQAGATVI----------------ALDLPFVLLLEYGDPLrltpldVADAAAVRE---VCSR 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   86 ALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYS 165
Cdd:cd05331  62 LLAEHGPIDALVNCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRISMAAYG 141
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 4504505  166 AAKLGLLGLANSLAIEGRKSNIHCNTIAPnaGSrmTQTVM 205
Cdd:cd05331 142 ASKAALASLSKCLGLELAPYGVRCNVVSP--GS--TDTAM 177
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
1-199 5.15e-23

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 104.23  E-value: 5.15e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    1 MGSPLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKAVANYDSVEEG- 79
Cdd:COG3347 417 MPKPKPLAGRVALVTGGAGGIGRATAARLAAEGAAVVVADLDGE---------AAEAAAAELGGGYGADAVDATDVDVTa 487
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   80 EKVVKTALD----AFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQK-YGRIIMTSSASG 154
Cdd:COG3347 488 EAAVAAAFGfaglDIGGSDIGVANAGIASSSPEEETRLSFWLNNFAHLSTGQFLVARAAFQGTGGQGlGGSSVFAVSKNA 567
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 4504505  155 IYGNFGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNAGSR 199
Cdd:COG3347 568 AAAAYGAAAAATAKAAAQHLLRALAAEGGANGINANRVNPDAVLD 612
PRK08278 PRK08278
SDR family oxidoreductase;
7-194 5.26e-23

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 99.59  E-value: 5.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     7 FDGRVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgVGKGSLAADK-------VVEEIRRRGGKAVANYDSVEEG 79
Cdd:PRK08278   4 LSGKTLFITGASRGIGLAIALRAARDGANIVI---------AAKTAEPHPKlpgtihtAAEEIEAAGGQALPLVGDVRDE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    80 EKV---VKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIY 156
Cdd:PRK08278  75 DQVaaaVAKAVERFGGIDICVNNASAINLTGTEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKSENPHILTLSPPLNLD 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 4504505   157 GN-FGQ-ANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK08278 155 PKwFAPhTAYTMAKYGMSLCTLGLAEEFRDDGIAVNALWP 194
PRK06701 PRK06701
short chain dehydrogenase; Provisional
9-218 5.49e-23

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 99.72  E-value: 5.49e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     9 GRVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgvgkGSLAADKVVEEIRRR----GGKAVANYDSVEEG---EK 81
Cdd:PRK06701  46 GKVALITGGDSGIGRAVAVLFAKEGADIAI------------VYLDEHEDANETKQRvekeGVKCLLIPGDVSDEafcKD 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    82 VVKTALDAFGRIDVVVNNAGI-LRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQkyGRIIMTSSASGIYGNFG 160
Cdd:PRK06701 114 AVEETVRELGRLDILVNNAAFqYPQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHLKQG--SAIINTGSITGYEGNET 191
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4504505   161 QANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP-------NAGSRM--------TQTVM-----PEDLVealkPEYV 218
Cdd:PRK06701 192 LIDYSATKGAIHAFTRSLAQSLVQKGIRVNAVAPgpiwtplIPSDFDeekvsqfgSNTPMqrpgqPEELA----PAYV 265
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
4-194 6.36e-23

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 98.82  E-value: 6.36e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     4 PLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVvndlggdfkGVG-KGSLAADKVVEEIRRRGGKAVANYDSVEEGEKV 82
Cdd:PRK12481   3 LFDLNGKVAIITGCNTGLGQGMAIGLAKAGADIV---------GVGvAEAPETQAQVEALGRKFHFITADLIQQKDIDSI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    83 VKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRA-AWEHMKKQKYGRIIMTSSASGIYGNFGQ 161
Cdd:PRK12481  74 VSQAVEVMGHIDILINNAGIIRRQDLLEFGNKDWDDVININQKTVFFLSQAvAKQFVKQGNGGKIINIASMLSFQGGIRV 153
                        170       180       190
                 ....*....|....*....|....*....|...
gi 4504505   162 ANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK12481 154 PSYTASKSAVMGLTRALATELSQYNINVNAIAP 186
PRK06484 PRK06484
short chain dehydrogenase; Validated
9-214 7.99e-23

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 103.01  E-value: 7.99e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     9 GRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDFKGVGKGSLAADKVVEEIRrrggkaVANYDSVEEGekvVKTALD 88
Cdd:PRK06484   5 SRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDHHALAMD------VSDEAQIREG---FEQLHR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    89 AFGRIDVVVNNAGILrDRSFARISD---EDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGR-IIMTSSASGIYGNFGQANY 164
Cdd:PRK06484  76 EFGRIDVLVNNAGVT-DPTMTATLDttlEEFARLQAINLTGAYLVAREALRLMIEQGHGAaIVNVASGAGLVALPKRTAY 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 4504505   165 SAAKLGLLGLANSLAIEGRKSNIHCNTIAPNagsrMTQTVMPEDLVEALK 214
Cdd:PRK06484 155 SASKAAVISLTRSLACEWAAKGIRVNAVLPG----YVRTQMVAELERAGK 200
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
9-221 1.28e-22

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: 97.92  E-value: 1.28e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    9 GRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRR-GGKAV---ANYDSVEEGEKVVK 84
Cdd:cd05322   2 NQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSE---------NAEKVADEINAEyGEKAYgfgADATNEQSVIALSK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   85 TALDAFGRIDVVVNNAGILRDrsfARISD---EDWDIIHRVHLRGSFQVTRAAWEHMKKQKY-GRIIMTSSASGIYGNFG 160
Cdd:cd05322  73 GVDEIFKRVDLLVYSAGIAKS---AKITDfelGDFDRSLQVNLVGYFLCAREFSKLMIRDGIqGRIIQINSKSGKVGSKH 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4504505  161 QANYSAAKLGLLGLANSLAIEGRKSNIHCNTIapnagsrMTQTVMPEDLVEALKPEYVAPL 221
Cdd:cd05322 150 NSGYSAAKFGGVGLTQSLALDLAEHGITVNSL-------MLGNLLKSPMFQSLLPQYAKKL 203
FAS_MaoC cd03447
FAS_MaoC, the MaoC-like hot dog fold of the fatty acid synthase, beta subunit. Other enzymes ...
487-599 2.78e-22

FAS_MaoC, the MaoC-like hot dog fold of the fatty acid synthase, beta subunit. Other enzymes with this fold include MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and 17-beta-hydroxysteriod dehydrogenase (HSD).


Pssm-ID: 239531 [Multi-domain]  Cd Length: 126  Bit Score: 92.73  E-value: 2.78e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  487 RPPDAVLTDTTSLNQAALYRLSGDWNPLHIDPNFASLAGFDKPILHGLCTFGfSARRVLQQ-FADNDVSRFKAIKARFAK 565
Cdd:cd03447   1 RSGGASLTITAPASNEPYARVSGDFNPIHVSRVFASYAGLPGTITHGMYTSA-AVRALVETwAADNDRSRVRSFTASFVG 79
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 4504505  566 PVYPGQTLQTEMWKEG-----NRIHFQTKVQETGDIVIS 599
Cdd:cd03447  80 MVLPNDELEVRLEHVGmvdgrKVIKVEARNEETGELVLR 118
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
7-194 3.00e-22

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: 96.71  E-value: 3.00e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    7 FDGRVVLVTGAGAGLGRAYALAFAERGALVVVNdlggdfkgvGKGSLAADKVVEEIRRRGGKA------VANYDSVEEGE 80
Cdd:cd05364   1 LSGKVAIITGSSSGIGAGTAILFARLGARLALT---------GRDAERLEETRQSCLQAGVSEkkillvVADLTEEEGQD 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   81 KVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKyGRIIMTSSASGIYGNFG 160
Cdd:cd05364  72 RIISTTLAKFGRLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTK-GEIVNVSSVAGGRSFPG 150
                       170       180       190
                ....*....|....*....|....*....|....
gi 4504505  161 QANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:cd05364 151 VLYYCISKAALDQFTRCTALELAPKGVRVNSVSP 184
PRK07832 PRK07832
SDR family oxidoreductase;
12-196 3.59e-22

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 97.04  E-value: 3.59e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    12 VLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgSLAAdkVVEEIRRRGGKA-------VANYDSVEE-GEKVV 83
Cdd:PRK07832   3 CFVTGAASGIGRATALRLAAQGAELFLTDRDAD-------GLAQ--TVADARALGGTVpehraldISDYDAVAAfAADIH 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    84 KtaldAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRA-AWEHMKKQKYGRIIMTSSASGIYGNFGQA 162
Cdd:PRK07832  74 A----AHGSMDVVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETfVPPMVAAGRGGHLVNVSSAAGLVALPWHA 149
                        170       180       190
                 ....*....|....*....|....*....|....
gi 4504505   163 NYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNA 196
Cdd:PRK07832 150 AYSASKFGLRGLSEVLRFDLARHGIGVSVVVPGA 183
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
9-208 5.02e-22

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: 96.36  E-value: 5.02e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    9 GRVVLVTGAGAGLGRAYALAFAERGALVVVNdlggdfkgvGKGSL-AADKVVEEIRRRGGKAVANY-DSVEEGEkvVKTA 86
Cdd:cd09763   3 GKIALVTGASRGIGRGIALQLGEAGATVYIT---------GRTILpQLPGTAEEIEARGGKCIPVRcDHSDDDE--VEAL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   87 LDAF-----GRIDVVVNNA-------GILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASG 154
Cdd:cd09763  72 FERVareqqGRLDILVNNAyaavqliLVGVAKPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAGKGLIVIISSTGG 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4504505  155 IYGNFGQAnYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPnaGSRMTQTV--MPED 208
Cdd:cd09763 152 LEYLFNVA-YGVGKAAIDRMAADMAHELKPHGVAVVSLWP--GFVRTELVleMPED 204
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
12-231 5.89e-22

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: 95.21  E-value: 5.89e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   12 VLVTGAGAGLGRAYALAFAERGALVVVNDLGGDFKGVGKGSLAADKVVE---EIRRRGGKAVANYD-SVEEGekvvktal 87
Cdd:cd08931   3 IFITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELGAENVVAgalDVTDRAAWAAALADfAAATG-------- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   88 dafGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSAA 167
Cdd:cd08931  75 ---GRLDALFNNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAIYGQPDLAVYSAT 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4504505  168 KLGLLGLANSLAIEGRKSNIHCNTIAP--------NAGSrmTQTVMPEDLVEALKPEYVAPlVLWLCHESCE 231
Cdd:cd08931 152 KFAVRGLTEALDVEWARHGIRVADVWPwfvdtpilTKGE--TGAAPKKGLGRVLPVSDVAK-VVWAAAHGVP 220
PRK07454 PRK07454
SDR family oxidoreductase;
10-225 1.19e-21

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 94.64  E-value: 1.19e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    10 RVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgVGKGSLAADKVVEEIRRRGGKAVA---NYDSVEEGEKVVKTA 86
Cdd:PRK07454   7 PRALITGASSGIGKATALAFAKAGWDLAL---------VARSQDALEALAAELRSTGVKAAAysiDLSNPEAIAPGIAEL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    87 LDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGiYGNFGQ-ANYS 165
Cdd:PRK07454  78 LEQFGCPDVLINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAA-RNAFPQwGAYC 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4504505   166 AAKLGLLGLANSLAIEGRKSNIHCNTIAPNA-----------GSRMTQTVMpedlveaLKPEYVAPLVLWL 225
Cdd:PRK07454 157 VSKAALAAFTKCLAEEERSHGIRVCTITLGAvntplwdtetvQADFDRSAM-------LSPEQVAQTILHL 220
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
5-226 1.35e-21

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 94.77  E-value: 1.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     5 LRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLggdfkgvgKGSLAADKVVEEIrrrGGKAVANYDSVEEGEKV-- 82
Cdd:PRK08642   1 MQISEQTVLVTGGSRGLGAAIARAFAREGARVVVNYH--------QSEDAAEALADEL---GDRAIALQADVTDREQVqa 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    83 -VKTALDAFGR-IDVVVNNAgiLRDRSF---AR-----ISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIImtssa 152
Cdd:PRK08642  70 mFATATEHFGKpITTVVNNA--LADFSFdgdARkkaddITWEDFQQQLEGSVKGALNTIQAALPGMREQGFGRII----- 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   153 sGIYGNFGQA------NYSAAKLGLLGLANSLAIEGRKSNIHCNTIA------PNAGSRMTQTVMpeDLVEA---LK--- 214
Cdd:PRK08642 143 -NIGTNLFQNpvvpyhDYTTAKAALLGLTRNLAAELGPYGITVNMVSggllrtTDASAATPDEVF--DLIAAttpLRkvt 219
                        250
                 ....*....|...
gi 4504505   215 -PEYVAPLVLWLC 226
Cdd:PRK08642 220 tPQEFADAVLFFA 232
PRK07035 PRK07035
SDR family oxidoreductase;
8-194 1.37e-21

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 94.70  E-value: 1.37e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     8 DGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKAVA---NYDSVEEGEKVVK 84
Cdd:PRK07035   7 TGKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLD---------GCQAVADAIVAAGGKAEAlacHIGEMEQIDALFA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    85 TALDAFGRIDVVVNNAGIlrDRSFARISDED---WDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQ 161
Cdd:PRK07035  78 HIRERHGRLDILVNNAAA--NPYFGHILDTDlgaFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVSPGDFQ 155
                        170       180       190
                 ....*....|....*....|....*....|...
gi 4504505   162 ANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK07035 156 GIYSITKAAVISMTKAFAKECAPFGIRVNALLP 188
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
9-194 1.50e-21

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 94.56  E-value: 1.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     9 GRVVLVTGAGAGLGRAYALAFAERGALVVvndlggdfkgvGKGSLAADKVVEEIRRRGGKAV---ANYDSVEEGEKVVKT 85
Cdd:PRK08993  10 GKVAVVTGCDTGLGQGMALGLAEAGCDIV-----------GINIVEPTETIEQVTALGRRFLsltADLRKIDGIPALLER 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    86 ALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQ-KYGRIIMTSSASGIYGNFGQANY 164
Cdd:PRK08993  79 AVAEFGHIDILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQgNGGKIINIASMLSFQGGIRVPSY 158
                        170       180       190
                 ....*....|....*....|....*....|
gi 4504505   165 SAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK08993 159 TASKSGVMGVTRLMANEWAKHNINVNAIAP 188
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
6-231 3.81e-21

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 93.25  E-value: 3.81e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLggdfkgvgKGSLAADKVVEEIRRRGGKAV---ANYDSVEEGEKV 82
Cdd:PRK08063   1 VFSGKVALVTGSSRGIGKAIALRLAEEGYDIAVNYA--------RSRKAAEETAEEIEALGRKALavkANVGDVEKIKEM 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    83 VKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGI-----YG 157
Cdd:PRK08063  73 FAQIDEEFGRLDVFVNNAASGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLSSLGSIrylenYT 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   158 NFGqanysAAKLGLLGLANSLAIEGRKSNIHCNTIApnAGSRMTQTV--MP--EDLVE----------ALKPEYVAPLVL 223
Cdd:PRK08063 153 TVG-----VSKAALEALTRYLAVELAPKGIAVNAVS--GGAVDTDALkhFPnrEELLEdaraktpagrMVEPEDVANAVL 225

                 ....*...
gi 4504505   224 WLCHESCE 231
Cdd:PRK08063 226 FLCSPEAD 233
PRK07814 PRK07814
SDR family oxidoreductase;
6-201 4.16e-21

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 93.69  E-value: 4.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgVGKGSLAADKVVEEIRRRGGKA---VANYDSVEEGEKV 82
Cdd:PRK07814   7 RLDDQVAVVTGAGRGLGAAIALAFAEAGADVLI---------AARTESQLDEVAEQIRAAGRRAhvvAADLAHPEATAGL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    83 VKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHM-KKQKYGRIIMTSSASGIYGNFGQ 161
Cdd:PRK07814  78 AGQAVEAFGRLDIVVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLMlEHSGGGSVINISSTMGRLAGRGF 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 4504505   162 ANYSAAKlGLLGLANSLAIEGRKSNIHCNTIAPnaGSRMT 201
Cdd:PRK07814 158 AAYGTAK-AALAHYTRLAALDLCPRIRVNAIAP--GSILT 194
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
7-229 5.59e-21

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: 93.29  E-value: 5.59e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    7 FDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKAVANYDSVEEGEKVVKTA 86
Cdd:cd08935   3 LKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQE---------KGDKVAKEITALGGRAIALAADVLDRASLERAR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   87 ---LDAFGRIDVVVNNAG--------------ILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMT 149
Cdd:cd08935  74 eeiVAQFGTVDILINGAGgnhpdattdpehyePETEQNFFDLDEEGWEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINI 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  150 SSASGIYGNFGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP---------------------NAGSRMTQTVM--- 205
Cdd:cd08935 154 SSMNAFSPLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPgffvtpqnrkllinpdgsytdRSNKILGRTPMgrf 233
                       250       260
                ....*....|....*....|....*.
gi 4504505  206 --PEDLVEALkpeyvaplvLWLCHES 229
Cdd:cd08935 234 gkPEELLGAL---------LFLASEK 250
PRK05872 PRK05872
short chain dehydrogenase; Provisional
1-181 6.91e-21

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 93.88  E-value: 6.91e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     1 MGSPLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGgdfkgvgKGSLAADKVVEEIRRRGGKAVANYDSVEEGE 80
Cdd:PRK05872   1 GPPMTSLAGKVVVVTGAARGIGAELARRLHARGAKLALVDLE-------EAELAALAAELGGDDRVLTVVADVTDLAAMQ 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    81 KVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKyGRIIMTSSASGIYGNFG 160
Cdd:PRK05872  74 AAAEEAVERFGGIDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERR-GYVLQVSSLAAFAAAPG 152
                        170       180
                 ....*....|....*....|.
gi 4504505   161 QANYSAAKLGLLGLANSLAIE 181
Cdd:PRK05872 153 MAAYCASKAGVEAFANALRLE 173
PRK09242 PRK09242
SDR family oxidoreductase;
6-226 1.13e-20

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 92.12  E-value: 1.13e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgVGKGSLAADKVVEEIR--RRGGKA---VANYDSVEEGE 80
Cdd:PRK09242   6 RLDGQTALITGASKGIGLAIAREFLGLGADVLI---------VARDADALAQARDELAeeFPEREVhglAADVSDDEDRR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    81 KVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFG 160
Cdd:PRK09242  77 AILDWVEDHWDGLHILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRS 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4504505   161 QANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNA-GSRMTQTVM--PEDLVEALK---------PEYVAPLVLWLC 226
Cdd:PRK09242 157 GAPYGMTKAALLQMTRNLAVEWAEDGIRVNAVAPWYiRTPLTSGPLsdPDYYEQVIErtpmrrvgePEEVAAAVAFLC 234
PRK06398 PRK06398
aldose dehydrogenase; Validated
7-204 1.19e-20

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 92.20  E-value: 1.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     7 FDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLggdfkgvgkgSLAADKVVEEIRrrggKAVANYDSVEEG-EKVVKT 85
Cdd:PRK06398   4 LKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDI----------KEPSYNDVDYFK----VDVSNKEQVIKGiDYVISK 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    86 aldaFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYS 165
Cdd:PRK06398  70 ----YGRIDILVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRNAAAYV 145
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 4504505   166 AAKLGLLGLANSLAIEgRKSNIHCNTIAPnaGSRMTQTV 204
Cdd:PRK06398 146 TSKHAVLGLTRSIAVD-YAPTIRCVAVCP--GSIRTPLL 181
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
7-230 1.39e-20

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 92.27  E-value: 1.39e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     7 FDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKA---VANYDSVEEGEKVV 83
Cdd:PRK08277   8 LKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQE---------KAEAVVAEIKAAGGEAlavKADVLDKESLEQAR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    84 KTALDAFGRIDVVVNNAG---------------ILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIM 148
Cdd:PRK08277  79 QQILEDFGPCDILINGAGgnhpkattdnefhelIEPTKTFFDLDEEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIIN 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   149 TSSASGIYGNFGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPN---------------------AGSRMTQTVM-- 205
Cdd:PRK08277 159 ISSMNAFTPLTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGfflteqnrallfnedgslterANKILAHTPMgr 238
                        250       260
                 ....*....|....*....|....*...
gi 4504505   206 ---PEDLVEALkpeyvaplvLWLCHESC 230
Cdd:PRK08277 239 fgkPEELLGTL---------LWLADEKA 257
PRK05876 PRK05876
short chain dehydrogenase; Provisional
7-194 1.80e-20

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 91.94  E-value: 1.80e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     7 FDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDlggdfkgVGKGSLaaDKVVEEIRRRGGKAVANYDSVEEGEKVVKTA 86
Cdd:PRK05876   4 FPGRGAVITGGASGIGLATGTEFARRGARVVLGD-------VDKPGL--RQAVNHLRAEGFDVHGVMCDVRHREEVTHLA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    87 LDAF---GRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKY-GRIIMTSSASGIYGNFGQA 162
Cdd:PRK05876  75 DEAFrllGHVDVVFSNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEQGTgGHVVFTASFAGLVPNAGLG 154
                        170       180       190
                 ....*....|....*....|....*....|..
gi 4504505   163 NYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK05876 155 AYGVAKYGVVGLAETLAREVTADGIGVSVLCP 186
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
9-228 2.23e-20

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: 91.45  E-value: 2.23e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    9 GRVVLVTGAGAGLGRAYALAFAERGALVVVNDlggdfkgvgKGSLAADKVVEEIRRRGGK---AVANYDSVEEGEKVVKT 85
Cdd:cd08936  10 NKVALVTASTDGIGLAIARRLAQDGAHVVVSS---------RKQQNVDRAVATLQGEGLSvtgTVCHVGKAEDRERLVAT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   86 ALDAFGRIDVVVNNAGIlrDRSFARISD---EDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQA 162
Cdd:cd08936  81 AVNLHGGVDILVSNAAV--NPFFGNILDsteEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAAFHPFPGLG 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4504505  163 NYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP----NAGSRM--TQTVMPEDLVEAL------KPEYVAPLVLWLCHE 228
Cdd:cd08936 159 PYNVSKTALLGLTKNLAPELAPRNIRVNCLAPglikTSFSSAlwMDKAVEESMKETLrirrlgQPEDCAGIVSFLCSE 236
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
9-228 3.19e-20

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: 90.72  E-value: 3.19e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    9 GRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslaADKVVEEIRRRGGKAVANyDSVEEGEK--VVKTA 86
Cdd:cd09761   1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEE----------RGADFAEAEGPNLFFVHG-DVADETLVkfVVYAM 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   87 LDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKyGRIIMTSSASGIYGNFGQANYSA 166
Cdd:cd09761  70 LEKLGRIDVLVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNK-GRIINIASTRAFQSEPDSEAYAA 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4504505  167 AKLGLLGLANSLAIE-GRksNIHCNTIAP------NAGSRMTQTVMPEDLVEAL-----KPEYVAPLVLWLCHE 228
Cdd:cd09761 149 SKGGLVALTHALAMSlGP--DIRVNCISPgwinttEQQEFTAAPLTQEDHAQHPagrvgTPKDIANLVLFLCQQ 220
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
12-225 4.28e-20

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: 88.73  E-value: 4.28e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   12 VLVTGAGAGLGRAYALAFAERGAlvvvndlggdfkgvgkgslaaDKVVEEIRRrggkavanydsveegekvvktaldafg 91
Cdd:cd02266   1 VLVTGGSGGIGGAIARWLASRGS---------------------PKVLVVSRR--------------------------- 32
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   92 riDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSAAKLGL 171
Cdd:cd02266  33 --DVVVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAAL 110
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4504505  172 LGLANSLAIEGRKSNIHCNTIA--PNAGSRMTQT-VMPED-------LVEALKPEYVAPLVLWL 225
Cdd:cd02266 111 DGLAQQWASEGWGNGLPATAVAcgTWAGSGMAKGpVAPEEilgnrrhGVRTMPPEEVARALLNA 174
PRK06123 PRK06123
SDR family oxidoreductase;
10-242 9.56e-20

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 89.45  E-value: 9.56e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    10 RVVLVTGAGAGLGRAYALAFAERGALVVVNDLggdfkgvgKGSLAADKVVEEIRRRGGKAVANYDSVEEGEKVVK--TAL 87
Cdd:PRK06123   3 KVMIITGASRGIGAATALLAAERGYAVCLNYL--------RNRDAAEAVVQAIRRQGGEALAVAADVADEADVLRlfEAV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    88 DA-FGRIDVVVNNAGILRDRsfARISDEDWDIIHRV---HLRGSFQVTRAAWEHMKKQKYGR---IIMTSSASGIYGNFG 160
Cdd:PRK06123  75 DReLGRLDALVNNAGILEAQ--MRLEQMDAARLTRIfatNVVGSFLCAREAVKRMSTRHGGRggaIVNVSSMAARLGSPG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   161 Q-ANYSAAKLGL----LGLANSLAIEGRKSN----------IHCNTIAPNAGSRMTQTVmpeDLVEALKPEYVAPLVLWL 225
Cdd:PRK06123 153 EyIDYAASKGAIdtmtIGLAKEVAAEGIRVNavrpgviyteIHASGGEPGRVDRVKAGI---PMGRGGTAEEVARAILWL 229
                        250
                 ....*....|....*...
gi 4504505   226 CH-ESCEENGGLFEVGAG 242
Cdd:PRK06123 230 LSdEASYTTGTFIDVSGG 247
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
12-225 1.16e-19

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: 88.33  E-value: 1.16e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   12 VLVTGAGAGLGRAYALAFAERGALVVVndLGGDFKGVGKgslAADKVVEEIRrrggKAVANYDSVEEGEKVVKTALDAFG 91
Cdd:cd08929   3 ALVTGASRGIGEATARLLHAEGYRVGI--CARDEARLAA---AAAQELEGVL----GLAGDVRDEADVRRAVDAMEEAFG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   92 RIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSAAKLGL 171
Cdd:cd08929  74 GLDALVNNAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGL 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 4504505  172 LGLANSLAIEGRKSNIHCNTIAPnaGSRMTQ-TVMPEDLVEALKPEYVAPLVLWL 225
Cdd:cd08929 154 LGLSEAAMLDLREANIRVVNVMP--GSVDTGfAGSPEGQAWKLAPEDVAQAVLFA 206
PRK08628 PRK08628
SDR family oxidoreductase;
5-194 1.94e-19

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 88.48  E-value: 1.94e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     5 LRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgVGKgSLAADKVVEEIRRRGGKA------VANYDSVee 78
Cdd:PRK08628   3 LNLKDKVVIVTGGASGIGAAISLRLAEEGAIPVI---------FGR-SAPDDEFAEELRALQPRAefvqvdLTDDAQC-- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    79 gEKVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHR--VHLrgsFQVTRAAWEHMKKQKyGRIIMTSSASGIY 156
Cdd:PRK08628  71 -RDAVEQTVAKFGRIDGLVNNAGVNDGVGLEAGREAFVASLERnlIHY---YVMAHYCLPHLKASR-GAIVNISSKTALT 145
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 4504505   157 GNFGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK08628 146 GQGGTSGYAAAKGAQLALTREWAVALAKDGVRVNAVIP 183
PRK07069 PRK07069
short chain dehydrogenase; Validated
13-194 2.23e-19

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 88.23  E-value: 2.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    13 LVTGAGAGLGRAYALAFAERGALVVVNDLGgDFKGvgkgslaADKVVEEIRRRGGKAVA---NYDSVEEGE--KVVKTAL 87
Cdd:PRK07069   3 FITGAAGGLGRAIARRMAEQGAKVFLTDIN-DAAG-------LDAFAAEINAAHGEGVAfaaVQDVTDEAQwqALLAQAA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    88 DAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSAA 167
Cdd:PRK07069  75 DAMGGLSVLVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKAEPDYTAYNAS 154
                        170       180
                 ....*....|....*....|....*....
gi 4504505   168 KLGLLGLANSLAIE--GRKSNIHCNTIAP 194
Cdd:PRK07069 155 KAAVASLTKSIALDcaRRGLDVRCNSIHP 183
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
6-194 2.47e-19

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: 88.18  E-value: 2.47e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDlggdfkgvgkgsLAADKVVEEIRRRGGKAVA---NYDSVEEGEKV 82
Cdd:cd05348   1 WLKGEVALITGGGSGLGRALVERFVAEGAKVAVLD------------RSAEKVAELRADFGDAVVGvegDVRSLADNERA 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   83 VKTALDAFGRIDVVVNNAGI------LRDRSFARIsDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKyGRIIMTSSASGIY 156
Cdd:cd05348  69 VARCVERFGKLDCFIGNAGIwdystsLVDIPEEKL-DEAFDELFHINVKGYILGAKAALPALYATE-GSVIFTVSNAGFY 146
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 4504505  157 GNFGQANYSAAKLGLLGLANSLAIEgRKSNIHCNTIAP 194
Cdd:cd05348 147 PGGGGPLYTASKHAVVGLVKQLAYE-LAPHIRVNGVAP 183
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
10-194 2.48e-19

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: 87.72  E-value: 2.48e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   10 RVVLVTGAGAGLGRAYALAFAERGALVVVNdlggdfkgVGKGSLAADKVVEEIRRRGGKAV---ANYDSVEEGEKVVKTA 86
Cdd:cd05357   1 AVALVTGAAKRIGRAIAEALAAEGYRVVVH--------YNRSEAEAQRLKDELNALRNSAVlvqADLSDFAACADLVAAA 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   87 LDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSA 166
Cdd:cd05357  73 FRAFGRCDVLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIIDAMTDRPLTGYFAYCM 152
                       170       180
                ....*....|....*....|....*...
gi 4504505  167 AKLGLLGLANSLAIEgRKSNIHCNTIAP 194
Cdd:cd05357 153 SKAALEGLTRSAALE-LAPNIRVNGIAP 179
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
10-167 2.87e-19

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 86.00  E-value: 2.87e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505      10 RVVLVTGAGAGLGRAYALAFAERGA--LVVVNDLGGDfkgvgkgSLAADKVVEEIRRRGGKA------VANYDSVEEgek 81
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGArrLVLLSRSGPD-------APGAAALLAELEAAGARVtvvacdVADRDALAA--- 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505      82 VVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDiihrvhlrgsfQVTRA----AW---EHMKKQKYGRIIMTSSASG 154
Cdd:smart00822  71 VLAAIPAVEGPLTGVIHAAGVLDDGVLASLTPERFA-----------AVLAPkaagAWnlhELTADLPLDFFVLFSSIAG 139
                          170
                   ....*....|...
gi 4504505     155 IYGNFGQANYSAA 167
Cdd:smart00822 140 VLGSPGQANYAAA 152
PRK09072 PRK09072
SDR family oxidoreductase;
5-223 3.15e-19

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 88.07  E-value: 3.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     5 LRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgVGK--GSLAAdkvveeiRRRGGKAVANYDSV------ 76
Cdd:PRK09072   1 MDLKDKRVLLTGASGGIGQALAEALAAAGARLLL---------VGRnaEKLEA-------LAARLPYPGRHRWVvadlts 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    77 EEGEKVVKTALDAFGRIDVVVNNAGILRdrsFARISDEDWDIIHR---VHLRGSFQVTRAAWEHMKKQKYGRIIMTSSAS 153
Cdd:PRK09072  65 EAGREAVLARAREMGGINVLINNAGVNH---FALLEDQDPEAIERllaLNLTAPMQLTRALLPLLRAQPSAMVVNVGSTF 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4504505   154 GIYGNFGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPnagsRMTQTVMPEDLVEAL---------KPEYVAPLVL 223
Cdd:PRK09072 142 GSIGYPGYASYCASKFALRGFSEALRRELADTGVRVLYLAP----RATRTAMNSEAVQALnralgnamdDPEDVAAAVL 216
PRK07201 PRK07201
SDR family oxidoreductase;
9-222 3.79e-19

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 91.94  E-value: 3.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     9 GRVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgVGKGSLAADKVVEEIRRRGGKA------VANYDSVeegEKV 82
Cdd:PRK07201 371 GKVVLITGASSGIGRATAIKVAEAGATVFL---------VARNGEALDELVAEIRAKGGTAhaytcdLTDSAAV---DHT 438
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    83 VKTALDAFGRIDVVVNNAGilrdRSFARISDEDWDIIH------RVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSAsGIY 156
Cdd:PRK07201 439 VKDILAEHGHVDYLVNNAG----RSIRRSVENSTDRFHdyertmAVNYFGAVRLILGLLPHMRERRFGHVVNVSSI-GVQ 513
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4504505   157 GN---FgqANYSAAKLGLLGLANSLAIEGRKSNIHCNTIapnagsRM--TQTVM--PEDL---VEALKPEYVAPLV 222
Cdd:PRK07201 514 TNaprF--SAYVASKAALDAFSDVAASETLSDGITFTTI------HMplVRTPMiaPTKRynnVPTISPEEAADMV 581
PRK06947 PRK06947
SDR family oxidoreductase;
8-242 4.01e-19

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 87.55  E-value: 4.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     8 DGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGgdfkgvgkGSLAADKVVEEIRRRGGKAVANYDSVEEGEKVV---K 84
Cdd:PRK06947   1 MRKVVLITGASRGIGRATAVLAAARGWSVGINYAR--------DAAAAEETADAVRAAGGRACVVAGDVANEADVIamfD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    85 TALDAFGRIDVVVNNAGI------LRDRSFARISDedwdiIHRVHLRGSFQVTRAAWEHMKKQKYGR---IIMTSSASGI 155
Cdd:PRK06947  73 AVQSAFGRLDALVNNAGIvapsmpLADMDAARLRR-----MFDTNVLGAYLCAREAARRLSTDRGGRggaIVNVSSIASR 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   156 YGN-FGQANYSAAKLGL----LGLANSLAIEGRKSN----------IHCNTIAPNAGSRMTQTVmpeDLVEALKPEYVAP 220
Cdd:PRK06947 148 LGSpNEYVDYAGSKGAVdtltLGLAKELGPHGVRVNavrpglieteIHASGGQPGRAARLGAQT---PLGRAGEADEVAE 224
                        250       260
                 ....*....|....*....|...
gi 4504505   221 LVLWLCHE-SCEENGGLFEVGAG 242
Cdd:PRK06947 225 TIVWLLSDaASYVTGALLDVGGG 247
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
9-196 4.52e-19

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


Pssm-ID: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 87.67  E-value: 4.52e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    9 GRVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgVGKGSLAADKVVEEIRRRGGKA--------VANYDSVeegE 80
Cdd:cd05327   1 GKVVVITGANSGIGKETARELAKRGAHVII---------ACRNEEKGEEAAAEIKKETGNAkveviqldLSSLASV---R 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   81 KVVKTALDAFGRIDVVVNNAGILrdRSFARISDEDWDIIHRV-HLrGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNF 159
Cdd:cd05327  69 QFAEEFLARFPRLDILINNAGIM--APPRRLTKDGFELQFAVnYL-GHFLLTNLLLPVLKASAPSRIVNVSSIAHRAGPI 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 4504505  160 GQAN--------------YSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNA 196
Cdd:cd05327 146 DFNDldlennkeyspykaYGQSKLANILFTRELARRLEGTGVTVNALHPGV 196
SCP2 COG3255
Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];
627-733 5.50e-19

Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];


Pssm-ID: 442486 [Multi-domain]  Cd Length: 104  Bit Score: 82.65  E-value: 5.50e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  627 VFEEIGRRLKdiGPEVVKKVNAVFEWHITKGGniGAKWTIDLKSGSGKVYQGPAkGAADTTIILSDEDFMEVVLGKLDPQ 706
Cdd:COG3255   3 WAEALCEKLN--AADAAAGWDGVVQFVITGEG--GGAYYLVIDDGKCTVSEGDD-DDADVTLTASYEDWKKLLTGELDPM 77
                        90       100
                ....*....|....*....|....*..
gi 4504505  707 KAFFSGRLKARGNIMLSQKLQMILKDY 733
Cdd:COG3255  78 TAFMTGKLKVEGDMGLAMKLMSLFKAL 104
PRK08263 PRK08263
short chain dehydrogenase; Provisional
9-203 6.75e-19

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 87.40  E-value: 6.75e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     9 GRVVLVTGAGAGLGRAYALAFAERGALVVvndlggdfkGVGKGSLAADKVVEeirRRGGKAVANYDSVEEGEKV---VKT 85
Cdd:PRK08263   3 EKVWFITGASRGFGRAWTEAALERGDRVV---------ATARDTATLADLAE---KYGDRLLPLALDVTDRAAVfaaVET 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    86 ALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYS 165
Cdd:PRK08263  71 AVEHFGRLDIVVNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGGISAFPMSGIYH 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 4504505   166 AAKLGLLGLANSLAIEGRKSNIHCNTIAPN------AGSRMTQT 203
Cdd:PRK08263 151 ASKWALEGMSEALAQEVAEFGIKVTLVEPGgystdwAGTSAKRA 194
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
10-217 7.26e-19

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: 86.75  E-value: 7.26e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   10 RVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgsLAADKVVEEIRRRGGKAV---ANYDSVEEGEKVVKTA 86
Cdd:cd05337   2 PVAIVTGASRGIGRAIATELAARGFDIAINDLPDD--------DQATEVVAEVLAAGRRAIyfqADIGELSDHEALLDQA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   87 LDAFGRIDVVVNNAGI--LRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQK------YGRIIMTSSASGIYGN 158
Cdd:cd05337  74 WEDFGRLDCLVNNAGIavRPRGDLLDLTEDSFDRLIAINLRGPFFLTQAVARRMVEQPdrfdgpHRSIIFVTSINAYLVS 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4504505  159 FGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNagsrmtqtVMPEDLVEALKPEY 217
Cdd:cd05337 154 PNRGEYCISKAGLSMATRLLAYRLADEGIAVHEIRPG--------LIHTDMTAPVKEKY 204
PRK05867 PRK05867
SDR family oxidoreductase;
7-225 8.18e-19

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 86.63  E-value: 8.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     7 FD--GRVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgVGKGSLAADKVVEEIRRRGGKAVANYDSVEEGEKV-- 82
Cdd:PRK05867   5 FDlhGKRALITGASTGIGKRVALAYVEAGAQVAI---------AARHLDALEKLADEIGTSGGKVVPVCCDVSQHQQVts 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    83 -VKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQ-KYGRIIMTSSASGIYGNFG 160
Cdd:PRK05867  76 mLDQVTAELGGIDIAVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQgQGGVIINTASMSGHIINVP 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4504505   161 Q--ANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPnaGSRMTQTVMPEDLVEAL-----------KPEYVAPLVLWL 225
Cdd:PRK05867 156 QqvSHYCASKAAVIHLTKAMAVELAPHKIRVNSVSP--GYILTELVEPYTEYQPLwepkiplgrlgRPEELAGLYLYL 231
PRK06139 PRK06139
SDR family oxidoreductase;
1-194 1.04e-18

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 87.85  E-value: 1.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     1 MGSPLRfdGRVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgVGKGSLAADKVVEEIRRRGGKAVANYDSVEEGE 80
Cdd:PRK06139   1 MMGPLH--GAVVVITGASSGIGQATAEAFARRGARLVL---------AARDEEALQAVAEECRALGAEVLVVPTDVTDAD 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    81 KV---VKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYG 157
Cdd:PRK06139  70 QVkalATQAASFGGRIDVWVNNVGVGAVGRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFINMISLGGFAA 149
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 4504505   158 NFGQANYSAAKLGLLGLANSLAIE-GRKSNIHCNTIAP 194
Cdd:PRK06139 150 QPYAAAYSASKFGLRGFSEALRGElADHPDIHVCDVYP 187
PRK08265 PRK08265
short chain dehydrogenase; Provisional
6-226 1.51e-18

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 86.22  E-value: 1.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKAVANYDSVEEGEKVVKT 85
Cdd:PRK08265   3 GLAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDAD---------NGAAVAASLGERARFIATDITDDAAIERAVAT 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    86 ALDAFGRIDVVVNNAGILRDRSFARiSDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKyGRIIMTSSASGIYGNFGQANYS 165
Cdd:PRK08265  74 VVARFGRVDILVNLACTYLDDGLAS-SRADWLAALDVNLVSAAMLAQAAHPHLARGG-GAIVNFTSISAKFAQTGRWLYP 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4504505   166 AAKLGLLGLANSLAIEGRKSNIHCNTIAP-----NAGSRMTQ-TVMPEDLVEAL--------KPEYVAPLVLWLC 226
Cdd:PRK08265 152 ASKAAIRQLTRSMAMDLAPDGIRVNSVSPgwtwsRVMDELSGgDRAKADRVAAPfhllgrvgDPEEVAQVVAFLC 226
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
11-188 1.52e-18

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: 85.51  E-value: 1.52e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   11 VVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgVGKGSLAADKV-VEEIRRRGGKAVA-NYDSVEEGE--KVVKTA 86
Cdd:cd05373   1 VAAVVGAGDGLGAAIARRFAAEGFSVAL---------AARREAKLEALlVDIIRDAGGSAKAvPTDARDEDEviALFDLI 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   87 LDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSA 166
Cdd:cd05373  72 EEEIGPLEVLVYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASLRGRAGFAAFAG 151
                       170       180
                ....*....|....*....|..
gi 4504505  167 AKLGLLGLANSLAIEGRKSNIH 188
Cdd:cd05373 152 AKFALRALAQSMARELGPKGIH 173
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
2-167 1.54e-18

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


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 88.96  E-value: 1.54e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    2 GSPLRfDGRVVLVTGAGAGLGRAYALAFAERGALVVVndLggdfkgVGKGSLAADK-----VVEEIRRRGGKA------V 70
Cdd:cd08953 199 SAPLK-PGGVYLVTGGAGGIGRALARALARRYGARLV--L------LGRSPLPPEEewkaqTLAALEALGARVlyisadV 269
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   71 ANYDSVEEgekVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAwehmKKQKYGRIIMTS 150
Cdd:cd08953 270 TDAAAVRR---LLEKVRERYGAIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGLLNLAQAL----ADEPLDFFVLFS 342
                       170
                ....*....|....*..
gi 4504505  151 SASGIYGNFGQANYSAA 167
Cdd:cd08953 343 SVSAFFGGAGQADYAAA 359
PRK06179 PRK06179
short chain dehydrogenase; Provisional
10-187 1.55e-18

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 86.11  E-value: 1.55e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    10 RVVLVTGAGAGLGRAYALAFAERGALVVvndlGGDFKGVGKGSLAADKVVEeirrrggKAVANYDSVEEGekvVKTALDA 89
Cdd:PRK06179   5 KVALVTGASSGIGRATAEKLARAGYRVF----GTSRNPARAAPIPGVELLE-------LDVTDDASVQAA---VDEVIAR 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    90 FGRIDVVVNNAGI-----LRDRSFA---RISDedwdiihrVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGI----YG 157
Cdd:PRK06179  71 AGRIDVLVNNAGVglagaAEESSIAqaqALFD--------TNVFGILRMTRAVLPHMRAQGSGRIINISSVLGFlpapYM 142
                        170       180       190
                 ....*....|....*....|....*....|
gi 4504505   158 nfgqANYSAAKLGLLGLANSLAIEGRKSNI 187
Cdd:PRK06179 143 ----ALYAASKHAVEGYSESLDHEVRQFGI 168
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
9-202 2.16e-18

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


Pssm-ID: 187614 [Multi-domain]  Cd Length: 239  Bit Score: 84.96  E-value: 2.16e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    9 GRVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgVGKGSLAADKVVEEIRRRGG---KAVANYDSVEEG-----E 80
Cdd:cd05356   1 GTWAVVTGATDGIGKAYAEELAKRGFNVIL---------ISRTQEKLDAVAKEIEEKYGvetKTIAADFSAGDDiyeriE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   81 KVVKTaLDafgrIDVVVNNAGILRDRS--FARIS-DEDWDIIHrVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYG 157
Cdd:cd05356  72 KELEG-LD----IGILVNNVGISHSIPeyFLETPeDELQDIIN-VNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIP 145
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 4504505  158 NFGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNA-GSRMTQ 202
Cdd:cd05356 146 TPLLATYSASKAFLDFFSRALYEEYKSQGIDVQSLLPYLvATKMSK 191
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
10-194 3.01e-18

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: 84.21  E-value: 3.01e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   10 RVVLVTGAGAGLGRAYALAFAERGALVVVndLGGdfKGVGKGSLAadkvVEEIRRRGGKA------VANYDSVEEGEKVV 83
Cdd:cd05324   1 KVALVTGANRGIGFEIVRQLAKSGPGTVI--LTA--RDVERGQAA----VEKLRAEGLSVrfhqldVTDDASIEAAADFV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   84 KTAldaFGRIDVVVNNAGILRD-RSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIygnfGQA 162
Cdd:cd05324  73 EEK---YGGLDILVNNAGIAFKgFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLGS----LTS 145
                       170       180       190
                ....*....|....*....|....*....|..
gi 4504505  163 NYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:cd05324 146 AYGVSKAALNALTRILAKELKETGIKVNACCP 177
PRK07677 PRK07677
short chain dehydrogenase; Provisional
9-194 3.05e-18

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 85.12  E-value: 3.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     9 GRVVLVTGAGAGLGRAYALAFAERGALVVVNdlggdfkgvGKGSLAADKVVEEIRRRGGKA------VANYDSVeegEKV 82
Cdd:PRK07677   1 EKVVIITGGSSGMGKAMAKRFAEEGANVVIT---------GRTKEKLEEAKLEIEQFPGQVltvqmdVRNPEDV---QKM 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    83 VKTALDAFGRIDVVVNNAGilrdRSF----ARISDEDWDIIHRVHLRGSFQVTRAAWEH-MKKQKYGRIIMTSSASGIYG 157
Cdd:PRK07677  69 VEQIDEKFGRIDALINNAA----GNFicpaEDLSVNGWNSVIDIVLNGTFYCSQAVGKYwIEKGIKGNIINMVATYAWDA 144
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 4504505   158 NFGQANYSAAKLGLLGLANSLAIE-GRKSNIHCNTIAP 194
Cdd:PRK07677 145 GPGVIHSAAAKAGVLAMTRTLAVEwGRKYGIRVNAIAP 182
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
9-239 3.06e-18

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: 84.30  E-value: 3.06e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    9 GRVVLVTGAGAGLGRAYALAFAERGALVVVNDLggdfkgvgKGSLAADKVVEeirrrggkAVANYDSVEEGEKVVKTALD 88
Cdd:cd05334   1 ARVVLVYGGRGALGSAVVQAFKSRGWWVASIDL--------AENEEADASII--------VLDSDSFTEQAKQVVASVAR 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   89 AFGRIDVVVNNAG-----ILRDRSFArisdEDWDIIHRVHLRGSFQVTRAAWEHMKkqKYGRIIMTSSASGIYGNFGQAN 163
Cdd:cd05334  65 LSGKVDALICVAGgwaggSAKSKSFV----KNWDLMWKQNLWTSFIASHLATKHLL--SGGLLVLTGAKAALEPTPGMIG 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  164 YSAAKLGLLGLANSLAIE--GRKSNIHCNTIAPNA-GSRMTQTVMP-EDLVEALKPEYVAPLVL-WLCHESCEENGGLFE 238
Cdd:cd05334 139 YGAAKAAVHQLTQSLAAEnsGLPAGSTANAILPVTlDTPANRKAMPdADFSSWTPLEFIAELILfWASGAARPKSGSLIP 218

                .
gi 4504505  239 V 239
Cdd:cd05334 219 V 219
PRK09134 PRK09134
SDR family oxidoreductase;
10-133 3.75e-18

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 84.98  E-value: 3.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    10 RVVLVTGAGAGLGRAYALAFAERGALVVVNdlggdfkgvGKGSLA-ADKVVEEIRRRGGKAV---ANYDSVEEGEKVVKT 85
Cdd:PRK09134  10 RAALVTGAARRIGRAIALDLAAHGFDVAVH---------YNRSRDeAEALAAEIRALGRRAValqADLADEAEVRALVAR 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 4504505    86 ALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRA 133
Cdd:PRK09134  81 ASAALGPITLLVNNASLFEYDSAASFTRASWDRHMATNLRAPFVLAQA 128
PRK06180 PRK06180
short chain dehydrogenase; Provisional
8-203 4.67e-18

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 84.97  E-value: 4.67e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     8 DGRVVLVTGAGAGLGRAYALAFAERGALVVVNdlggdfkgVGKGSLAADKVVEEIRRRGGKA--VANYDSVEEgekVVKT 85
Cdd:PRK06180   3 SMKTWLITGVSSGFGRALAQAALAAGHRVVGT--------VRSEAARADFEALHPDRALARLldVTDFDAIDA---VVAD 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    86 ALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYS 165
Cdd:PRK06180  72 AEATFGPIDVLVNNAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGLITMPGIGYYC 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 4504505   166 AAKLGLLGLANSLAIEGRKSNIHCNTIAPN------AGSRMTQT 203
Cdd:PRK06180 152 GSKFALEGISESLAKEVAPFGIHVTAVEPGsfrtdwAGRSMVRT 195
PRK07576 PRK07576
short chain dehydrogenase; Provisional
1-194 1.06e-17

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 83.47  E-value: 1.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     1 MGSPLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNdlggdfkgvgkgSLAADKV---VEEIRRRGGKA------VA 71
Cdd:PRK07576   1 MTTMFDFAGKNVVVVGGTSGINLGIAQAFARAGANVAVA------------SRSQEKVdaaVAQLQQAGPEGlgvsadVR 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    72 NYDSVEEGekvVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKyGRIIMTSS 151
Cdd:PRK07576  69 DYAAVEAA---FAQIADEFGPIDVLVSGAAGNFPAPAAGMSANGFKTVVDIDLLGTFNVLKAAYPLLRRPG-ASIIQISA 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 4504505   152 ASGIYGNFGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK07576 145 PQAFVPMPMQAHVCAAKAGVDMLTRTLALEWGPEGIRVNSIVP 187
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
1-201 1.30e-17

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


Pssm-ID: 187638 [Multi-domain]  Cd Length: 261  Bit Score: 83.35  E-value: 1.30e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    1 MGSPLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDlggdfkgvgKGSLAADKVVEEIRRRG-GKAVANYDSVEEg 79
Cdd:cd08933   1 MASGLRYADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCA---------RGEAAGQALESELNRAGpGSCKFVPCDVTK- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   80 EKVVKTALDA----FGRIDVVVNNAGIL-RDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKyGRIIMTSSASG 154
Cdd:cd08933  71 EEDIKTLISVtverFGRIDCLVNNAGWHpPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQ-GNIINLSSLVG 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 4504505  155 IYGNFGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPnaGSRMT 201
Cdd:cd08933 150 SIGQKQAAPYVATKGAITAMTKALAVDESRYGVRVNCISP--GNIWT 194
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
7-194 1.36e-17

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: 82.35  E-value: 1.36e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    7 FDGRVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgVGKGSLAADKVVEEIRRRGGKaVANYDSVEEGEKVVKTA 86
Cdd:cd05370   3 LTGNTVLITGGTSGIGLALARKFLEAGNTVII---------TGRREERLAEAKKELPNIHTI-VLDVGDAESVEALAEAL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   87 LDAFGRIDVVVNNAGILRDRSFARISD--EDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANY 164
Cdd:cd05370  73 LSEYPNLDILINNAGIQRPIDLRDPASdlDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANPVY 152
                       170       180       190
                ....*....|....*....|....*....|
gi 4504505  165 SAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:cd05370 153 CATKAALHSYTLALRHQLKDTGVEVVEIVP 182
PRK05866 PRK05866
SDR family oxidoreductase;
2-192 1.71e-17

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 83.64  E-value: 1.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     2 GSPLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgVGKGSLAADKVVEEIRRRGGKAVA------NYDS 75
Cdd:PRK05866  33 RQPVDLTGKRILLTGASSGIGEAAAEQFARRGATVVA---------VARREDLLDAVADRITRAGGDAMAvpcdlsDLDA 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    76 VEEgekVVKTALDAFGRIDVVVNNAGilrdRSFARISDEDWDIIHRV------HLRGSFQVTRAAWEHMKKQKYGRIIMT 149
Cdd:PRK05866 104 VDA---LVADVEKRIGGVDILINNAG----RSIRRPLAESLDRWHDVertmvlNYYAPLRLIRGLAPGMLERGDGHIINV 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 4504505   150 SS---ASGIYGNFGQanYSAAKLGLLGLANSLAIEGRKSNIHCNTI 192
Cdd:PRK05866 177 ATwgvLSEASPLFSV--YNASKAALSAVSRVIETEWGDRGVHSTTL 220
PLN02253 PLN02253
xanthoxin dehydrogenase
3-208 5.91e-17

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 81.79  E-value: 5.91e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     3 SPLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDFKGVGKGSLAADKVVEEIRrrggkavANYDSVEEGEKV 82
Cdd:PLN02253  12 PSQRLLGKVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNVCDSLGGEPNVCFFH-------CDVTVEDDVSRA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    83 VKTALDAFGRIDVVVNNAGI-------LRDRSFArisdeDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGI 155
Cdd:PLN02253  85 VDFTVDKFGTLDIMVNNAGLtgppcpdIRNVELS-----EFEKVFDVNVKGVFLGMKHAARIMIPLKKGSIVSLCSVASA 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 4504505   156 YGNFGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNA-GSRMTQTVMPED 208
Cdd:PLN02253 160 IGGLGPHAYTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAvPTALALAHLPED 213
PRK09730 PRK09730
SDR family oxidoreductase;
11-242 6.03e-17

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 81.05  E-value: 6.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    11 VVLVTGAGAGLGRAYALAFAERGALVVVNDLggdfkgvgKGSLAADKVVEEIRRRGGKAVANYDSVEEGEKVVK--TALD 88
Cdd:PRK09730   3 IALVTGGSRGIGRATALLLAQEGYTVAVNYQ--------QNLHAAQEVVNLITQAGGKAFVLQADISDENQVVAmfTAID 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    89 AF-GRIDVVVNNAGILRDRS-FARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQ---KYGRIIMTSSASGIYGNFGQ-A 162
Cdd:PRK09730  75 QHdEPLAALVNNAGILFTQCtVENLTAERINRVLSTNVTGYFLCCREAVKRMALKhggSGGAIVNVSSAASRLGAPGEyV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   163 NYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP-------NAGSRMTQTVmpeDLVEAL-------KPEYVAPLVLWLCHE 228
Cdd:PRK09730 155 DYAASKGAIDTLTTGLSLEVAAQGIRVNCVRPgfiytemHASGGEPGRV---DRVKSNipmqrggQPEEVAQAIVWLLSD 231
                        250
                 ....*....|....
gi 4504505   229 SCEENGGLFEVGAG 242
Cdd:PRK09730 232 KASYVTGSFIDLAG 245
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
1-194 8.34e-17

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 80.97  E-value: 8.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     1 MGSPLrFD--GRVVLVTGAGAGLGRAYALAFAERGALVVVNdlggdfkgvGKGSLAADKVVEEIRRRGGKAVANYDSVEE 78
Cdd:PRK07523   1 MSLNL-FDltGRRALVTGSSQGIGYALAEGLAQAGAEVILN---------GRDPAKLAAAAESLKGQGLSAHALAFDVTD 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    79 GEkVVKTALDAF----GRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASG 154
Cdd:PRK07523  71 HD-AVRAAIDAFeaeiGPIDILVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVQS 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 4504505   155 IYGNFGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK07523 150 ALARPGIAPYTATKGAVGNLTKGMATDWAKHGLQCNAIAP 189
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
10-182 1.33e-16

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 80.39  E-value: 1.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    10 RVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkGSLAAdkVVEEIRRRGGKAVANYDSVEEG---EKVVKTA 86
Cdd:PRK12745   3 PVALVTGGRRGIGLGIARALAAAGFDLAINDRPDD------EELAA--TQQELRALGVEVIFFPADVADLsahEAMLDAA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    87 LDAFGRIDVVVNNAGI--LRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQK------YGRIIMTSSASGIYGN 158
Cdd:PRK12745  75 QAAWGRIDCLVNNAGVgvKVRGDLLDLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPepeelpHRSIVFVSSVNAIMVS 154
                        170       180
                 ....*....|....*....|....*...
gi 4504505   159 FGQANYSAAKLGL----LGLANSLAIEG 182
Cdd:PRK12745 155 PNRGEYCISKAGLsmaaQLFAARLAEEG 182
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
7-194 1.80e-16

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: 79.97  E-value: 1.80e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    7 FDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKAVANYDSVEEGEKVVKTA 86
Cdd:cd05363   1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLE---------AARATAAEIGPAACAISLDVTDQASIDRCVAAL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   87 LDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQ-KYGRIIMTSSASGIYGNFGQANYS 165
Cdd:cd05363  72 VDRWGSIDILVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQgRGGKIINMASQAGRRGEALVGVYC 151
                       170       180
                ....*....|....*....|....*....
gi 4504505  166 AAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:cd05363 152 ATKAAVISLTQSAGLNLIRHGINVNAIAP 180
PRK07577 PRK07577
SDR family oxidoreductase;
10-194 2.11e-16

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 79.00  E-value: 2.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    10 RVVLVTGAGAGLGRAYALAFAERGALVVV--NDLGGDFKGVgkgSLAADkvveeirrrggkaVANYDSVEEgekvVKTAL 87
Cdd:PRK07577   4 RTVLVTGATKGIGLALSLRLANLGHQVIGiaRSAIDDFPGE---LFACD-------------LADIEQTAA----TLAQI 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    88 DAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASgIYGNFGQANYSAA 167
Cdd:PRK07577  64 NEIHPVDAIVNNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNICSRA-IFGALDRTSYSAA 142
                        170       180
                 ....*....|....*....|....*..
gi 4504505   168 KLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK07577 143 KSALVGCTRTWALELAEYGITVNAVAP 169
PRK06128 PRK06128
SDR family oxidoreductase;
6-242 2.25e-16

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 80.29  E-value: 2.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDFKGvgkgslaADKVVEEIRRRGGKAVA-NYDSVEEG--EKV 82
Cdd:PRK06128  52 RLQGRKALITGADSGIGRATAIAFAREGADIALNYLPEEEQD-------AAEVVQLIQAEGRKAVAlPGDLKDEAfcRQL 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    83 VKTALDAFGRIDVVVNNAGILRDRS-FARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQkyGRIIMTSSASGIYGNFGQ 161
Cdd:PRK06128 125 VERAVKELGGLDILVNIAGKQTAVKdIADITTEQFDATFKTNVYAMFWLCKAAIPHLPPG--ASIINTGSIQSYQPSPTL 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   162 ANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPN--------AGSRMTQTVmPE-----DLVEALKPEYVAPL-VLWLCH 227
Cdd:PRK06128 203 LDYASTKAAIVAFTKALAKQVAEKGIRVNAVAPGpvwtplqpSGGQPPEKI-PDfgsetPMKRPGQPVEMAPLyVLLASQ 281
                        250
                 ....*....|....*
gi 4504505   228 ESCEENGGLFEVGAG 242
Cdd:PRK06128 282 ESSYVTGEVFGVTGG 296
PRK06484 PRK06484
short chain dehydrogenase; Validated
1-194 2.53e-16

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 82.59  E-value: 2.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     1 MGSPLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDFKGVGKGSLAAdkvvEEIRRRggkavANYDSVEEGE 80
Cdd:PRK06484 261 APSPLAESPRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGD----EHLSVQ-----ADITDEAAVE 331
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    81 KVVKTALDAFGRIDVVVNNAGIlrDRSFARISDEDWDIIHR---VHLRGSFQVTRAAWEHMKKqkyGRIIMTSSASGIYG 157
Cdd:PRK06484 332 SAFAQIQARWGRLDVLVNNAGI--AEVFKPSLEQSAEDFTRvydVNLSGAFACARAAARLMSQ---GGVIVNLGSIASLL 406
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 4504505   158 NFGQAN-YSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK06484 407 ALPPRNaYCASKAAVTMLSRSLACEWAPAGIRVNTVAP 444
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
5-194 3.51e-16

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: 78.67  E-value: 3.51e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    5 LRFDGRVVLVTGAGAGLGRAYALAFAERGALVV-VNDLGGDFKGVGKGSLAADKVVEEirrrggkaVANYDSVEEgekvv 83
Cdd:cd05351   3 LDFAGKRALVTGAGKGIGRATVKALAKAGARVVaVSRTQADLDSLVRECPGIEPVCVD--------LSDWDATEE----- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   84 ktALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKY-GRIIMTSSASGIYGNFGQA 162
Cdd:cd05351  70 --ALGSVGPVDLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGVpGSIVNVSSQASQRALTNHT 147
                       170       180       190
                ....*....|....*....|....*....|..
gi 4504505  163 NYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:cd05351 148 VYCSTKAALDMLTKVMALELGPHKIRVNSVNP 179
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
11-167 3.64e-16

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


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 76.83  E-value: 3.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     11 VVLVTGAGAGLGRAYALAFAERGA--LVVVNDLGGdfkgvgkGSLAADKVVEEIRRRGGKA------VANYDSVEegeKV 82
Cdd:pfam08659   2 TYLITGGLGGLGRELARWLAERGArhLVLLSRSAA-------PRPDAQALIAELEARGVEVvvvacdVSDPDAVA---AL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     83 VKTALDAFGRIDVVVNNAGILRDRSFARISDEDWdiiHRVhLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQA 162
Cdd:pfam08659  72 LAEIKAEGPPIRGVIHAAGVLRDALLENMTDEDW---RRV-LAPKVTGTWNLHEATPDEPLDFFVLFSSIAGLLGSPGQA 147

                  ....*
gi 4504505    163 NYSAA 167
Cdd:pfam08659 148 NYAAA 152
PRK12746 PRK12746
SDR family oxidoreductase;
7-194 1.04e-15

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 77.77  E-value: 1.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     7 FDGRVVLVTGAGAGLGRAYALAFAERGALVVVNdlggdfkgVGKGSLAADKVVEEIRRRGGKAV---ANYDSVEEGEKVV 83
Cdd:PRK12746   4 LDGKVALVTGASRGIGRAIAMRLANDGALVAIH--------YGRNKQAADETIREIESNGGKAFlieADLNSIDGVKKLV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    84 KTALDAF------GRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQkyGRIIMTSSASGIYG 157
Cdd:PRK12746  76 EQLKNELqirvgtSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLRAE--GRVINISSAEVRLG 153
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 4504505   158 NFGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK12746 154 FTGSIAYGLSKGALNTMTLPLAKHLGERGITVNTIMP 190
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
12-194 1.22e-15

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: 76.98  E-value: 1.22e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   12 VLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgsLAADKVVEEIRRRGGKAVANYDSVEEG--EKVVKTALDA 89
Cdd:cd05350   1 VLITGASSGIGRALAREFAKAGYNVALAARRTD--------RLDELKAELLNPNPSVEVEILDVTDEErnQLVIAELEAE 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   90 FGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSAAKL 169
Cdd:cd05350  73 LGGLDLVIINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKA 152
                       170       180
                ....*....|....*....|....*
gi 4504505  170 GLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:cd05350 153 ALSSLAESLRYDVKKRGIRVTVINP 177
PRK08219 PRK08219
SDR family oxidoreductase;
10-223 1.27e-15

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 76.51  E-value: 1.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    10 RVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgvGKGSLAADKVVEEIRRRGGKAV--ANYDSVEEgekvvktAL 87
Cdd:PRK08219   4 PTALITGASRGIGAAIARELAPTHTLLLG----------GRPAERLDELAAELPGATPFPVdlTDPEAIAA-------AV 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    88 DAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKyGRIIMTSSASGIYGNFGQANYSAA 167
Cdd:PRK08219  67 EQLGRLDVLVHNAGVADLGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAH-GHVVFINSGAGLRANPGWGSYAAS 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4504505   168 KLGLLGLANSLAIEGRkSNIHCNTIAPNAgsrmTQTVMPEDLVEA----------LKPEYVAPLVL 223
Cdd:PRK08219 146 KFALRALADALREEEP-GNVRVTSVHPGR----TDTDMQRGLVAQeggeydperyLRPETVAKAVR 206
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
7-194 1.58e-15

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: 76.72  E-value: 1.58e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    7 FDGRVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgVGKGSLAADK-------VVEEIRRRGGKAVANYDSVEEG 79
Cdd:cd09762   1 LAGKTLFITGASRGIGKAIALKAARDGANVVI---------AAKTAEPHPKlpgtiytAAEEIEAAGGKALPCIVDIRDE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   80 EKV---VKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGI- 155
Cdd:cd09762  72 DQVraaVEKAVEKFGGIDILVNNASAISLTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILNLSPPLNLn 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 4504505  156 ---YGNfgQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:cd09762 152 pkwFKN--HTAYTMAKYGMSMCVLGMAEEFKPGGIAVNALWP 191
PRK06523 PRK06523
short chain dehydrogenase; Provisional
1-194 1.97e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 76.87  E-value: 1.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     1 MGSPLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgvgkgslAADKVVEEIRRRGGKAVANYDSVEEGE 80
Cdd:PRK06523   1 MSFFLELAGKRALVTGGTKGIGAATVARLLEAGARVVT---------------TARSRPDDLPEGVEFVAADLTTAEGCA 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    81 KVVKTALDAFGRIDVVVNNAGILRDRS--FARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASG---I 155
Cdd:PRK06523  66 AVARAVLERLGGVDILVHVLGGSSAPAggFAALTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSIQRrlpL 145
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 4504505   156 YGNFgqANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK06523 146 PEST--TAYAAAKAALSTYSKSLSKEVAPKGVRVNTVSP 182
PRK07775 PRK07775
SDR family oxidoreductase;
8-215 2.15e-15

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 77.10  E-value: 2.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     8 DGRVVLVTGAGAGLGRAYALAFAERGALVvvndlggdfkgvgkgSLAADKV------VEEIRRRGGKAVANYDSVEEGEK 81
Cdd:PRK07775   9 DRRPALVAGASSGIGAATAIELAAAGFPV---------------ALGARRVekceelVDKIRADGGEAVAFPLDVTDPDS 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    82 V---VKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGN 158
Cdd:PRK07775  74 VksfVAQAEEALGEIEVLVSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALRQR 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 4504505   159 FGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNAgsrmTQTVMPEDL-VEALKP 215
Cdd:PRK07775 154 PHMGAYGAAKAGLEAMVTNLQMELEGTGVRASIVHPGP----TLTGMGWSLpAEVIGP 207
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
10-243 3.28e-15

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: 75.69  E-value: 3.28e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   10 RVVLVTGAGAGLGRAYALAFAERGALVVVNDlgGDFKGvgkgslAADKVVEEIRRRGGKAVanydSVEEGEKVVKTALDA 89
Cdd:cd05361   2 SIALVTHARHFAGPASAEALTEDGYTVVCHD--ASFAD------AAERQAFESENPGTKAL----SEQKPEELVDAVLQA 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   90 FGRIDVVVNNAGILRDRS-FARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSAAK 168
Cdd:cd05361  70 GGAIDVLVSNDYIPRPMNpIDGTSEADIRQAFEALSIFPFALLQAAIAQMKKAGGGSIIFITSAVPKKPLAYNSLYGPAR 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  169 LGLLGLANSLAIEGRKSNIHCNTIAPNAGSrmTQTVMPEDLVE-------------AL----KPEYVAPLVLWLCHESCE 231
Cdd:cd05361 150 AAAVALAESLAKELSRDNILVYAIGPNFFN--SPTYFPTSDWEnnpelrervkrdvPLgrlgRPDEMGALVAFLASRRAD 227
                       250
                ....*....|...
gi 4504505  232 E-NGGLFEVGAGW 243
Cdd:cd05361 228 PiTGQFFAFAGGY 240
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
9-171 4.85e-15

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: 75.58  E-value: 4.85e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    9 GRVVLVTGAGAGLGRAYALAFAERGALVVV--------NDLGGDFKGVGkgSLAADkvveeirrrggkaVANYDSVEege 80
Cdd:COG3967   5 GNTILITGGTSGIGLALAKRLHARGNTVIItgrreeklEEAAAANPGLH--TIVLD-------------VADPASIA--- 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   81 KVVKTALDAFGRIDVVVNNAGILRDRSFARiSDEDWDIIHR---VHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYG 157
Cdd:COG3967  67 ALAEQVTAEFPDLNVLINNAGIMRAEDLLD-EAEDLADAEReitTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGLAFVP 145
                       170
                ....*....|....
gi 4504505  158 NFGQANYSAAKLGL 171
Cdd:COG3967 146 LAVTPTYSATKAAL 159
PRK08264 PRK08264
SDR family oxidoreductase;
9-223 6.02e-15

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 74.93  E-value: 6.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     9 GRVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgvgkgslAADKVVEEIRRRGGKA------VANYDSVEEgekv 82
Cdd:PRK08264   6 GKVVLVTGANRGIGRAFVEQLLARGAAKVY---------------AAARDPESVTDLGPRVvplqldVTDPASVAA---- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    83 vktALDAFGRIDVVVNNAGILRDRSFarISDEDWDIIHR---VHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNF 159
Cdd:PRK08264  67 ---AAEAASDVTILVNNAGIFRTGSL--LLEGDEDALRAemeTNYFGPLAMARAFAPVLAANGGGAIVNVLSVLSWVNFP 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4504505   160 GQANYSAAKLGLLGLANSLAIEGRKSNIHcnTIAPNAGS---RMTQTVMpedlVEALKPEYVAPLVL 223
Cdd:PRK08264 142 NLGTYSASKAAAWSLTQALRAELAPQGTR--VLGVHPGPidtDMAAGLD----APKASPADVARQIL 202
PRK06949 PRK06949
SDR family oxidoreductase;
1-194 1.07e-14

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 74.80  E-value: 1.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     1 MGSPLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgvgkGSLAADKVVE---EIRRRGGKA------VA 71
Cdd:PRK06949   1 MGRSINLEGKVALVTGASSGLGARFAQVLAQAGAKVVL------------ASRRVERLKElraEIEAEGGAAhvvsldVT 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    72 NYDSVEEGekvVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHM--------KKQKY 143
Cdd:PRK06949  69 DYQSIKAA---VAHAETEAGTIDILVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMiarakgagNTKPG 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 4504505   144 GRIIMTSSASG--IYGNFGQanYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK06949 146 GRIINIASVAGlrVLPQIGL--YCMSKAAVVHMTRAMALEWGRHGINVNAICP 196
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
506-578 1.27e-14

Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 71.46  E-value: 1.27e-14
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4504505  506 RLSGDWNPLHIDPNFASLAGFDKPILHGLCTFGFSARRVLQQFADNDVSRFKAIKARFAKPVYPGQTLQTEMW 578
Cdd:COG2030  28 GATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPGTAVANLGLQEVRFLRPVRVGDTLRARVE 100
PRK06482 PRK06482
SDR family oxidoreductase;
13-181 1.80e-14

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 74.38  E-value: 1.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    13 LVTGAGAGLGRAYALAFAERGALVVvndlggdfkgvgkGSLAADKVVEEIRRRGGKA--VANYDSVEEG--EKVVKTALD 88
Cdd:PRK06482   6 FITGASSGFGRGMTERLLARGDRVA-------------ATVRRPDALDDLKARYGDRlwVLQLDVTDSAavRAVVDRAFA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    89 AFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSAAK 168
Cdd:PRK06482  73 ALGRIDVVVSNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQIAYPGFSLYHATK 152
                        170
                 ....*....|...
gi 4504505   169 LGLLGLANSLAIE 181
Cdd:PRK06482 153 WGIEGFVEAVAQE 165
PRK06194 PRK06194
hypothetical protein; Provisional
6-178 4.94e-14

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 73.13  E-value: 4.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKA------VANYDSVeeg 79
Cdd:PRK06194   3 DFAGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQD---------ALDRAVAELRAQGAEVlgvrtdVSDAAQV--- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    80 EKVVKTALDAFGRIDVVVNNAGIlrdRSFARI---SDEDWDIIHRVHLRGSFQVTRAAWEHM-----KKQKY-GRIIMTS 150
Cdd:PRK06194  71 EALADAALERFGAVHLLFNNAGV---GAGGLVwenSLADWEWVLGVNLWGVIHGVRAFTPLMlaaaeKDPAYeGHIVNTA 147
                        170       180
                 ....*....|....*....|....*...
gi 4504505   151 SASGIYGNFGQANYSAAKLGLLGLANSL 178
Cdd:PRK06194 148 SMAGLLAPPAMGIYNVSKHAVVSLTETL 175
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
12-194 7.26e-14

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


Pssm-ID: 187604 [Multi-domain]  Cd Length: 249  Bit Score: 71.93  E-value: 7.26e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   12 VLVTGAGAGLGRAYALAFAERGALVVvndlggdfkGVGKGSLAADKVVEEIRR--RGGKAVANYD--SVEEGEKVVKTAL 87
Cdd:cd05346   3 VLITGASSGIGEATARRFAKAGAKLI---------LTGRRAERLQELADELGAkfPVKVLPLQLDvsDRESIEAALENLP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   88 DAFGRIDVVVNNAGILRD-RSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSA 166
Cdd:cd05346  74 EEFRDIDILVNNAGLALGlDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYAGGNVYCA 153
                       170       180
                ....*....|....*....|....*...
gi 4504505  167 AKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:cd05346 154 TKAAVRQFSLNLRKDLIGTGIRVTNIEP 181
PRK06182 PRK06182
short chain dehydrogenase; Validated
10-181 9.37e-14

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 72.30  E-value: 9.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    10 RVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgvgkgslAADKV--VEEIRRRGGKA----VANYDSVEEGekvV 83
Cdd:PRK06182   4 KVALVTGASSGIGKATARRLAAQGYTVYG---------------AARRVdkMEDLASLGVHPlsldVTDEASIKAA---V 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    84 KTALDAFGRIDVVVNNAGIlrdRSFARISDEDWDIIHR---VHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASG-IYGNF 159
Cdd:PRK06182  66 DTIIAEEGRIDVLVNNAGY---GSYGAIEDVPIDEARRqfeVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGkIYTPL 142
                        170       180
                 ....*....|....*....|..
gi 4504505   160 GqANYSAAKLGLLGLANSLAIE 181
Cdd:PRK06182 143 G-AWYHATKFALEGFSDALRLE 163
PRK06500 PRK06500
SDR family oxidoreductase;
6-194 9.82e-14

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 71.53  E-value: 9.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNdlggdfkGVGKGSLAADKvveeiRRRGGKAV---ANYDSVEEGEKV 82
Cdd:PRK06500   3 RLQGKTALITGGTSGIGLETARQFLAEGARVAIT-------GRDPASLEAAR-----AELGESALvirADAGDVAAQKAL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    83 VKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQkyGRIIMTSSASGIYGNFGQA 162
Cdd:PRK06500  71 AQALAEAFGRLDAVFINAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLLANP--ASIVLNGSINAHIGMPNSS 148
                        170       180       190
                 ....*....|....*....|....*....|..
gi 4504505   163 NYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK06500 149 VYAASKAALLSLAKTLSGELLPRGIRVNAVSP 180
PRK09135 PRK09135
pteridine reductase; Provisional
8-196 1.99e-13

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 70.73  E-value: 1.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     8 DGRVVLVTGAGAGLGRAYALAFAERGALVVVNdlggdfkgvGKGSLA-ADKVVEEI-RRRGGKAV---ANYDSVEEGEKV 82
Cdd:PRK09135   5 SAKVALITGGARRIGAAIARTLHAAGYRVAIH---------YHRSAAeADALAAELnALRPGSAAalqADLLDPDALPEL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    83 VKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKyGRIImtsSASGIYGNFGQA 162
Cdd:PRK09135  76 VAACVAAFGRLDALVNNASSFYPTPLGSITEAQWDDLFASNLKAPFFLSQAAAPQLRKQR-GAIV---NITDIHAERPLK 151
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 4504505   163 N---YSAAKLGLLGLANSLAIEgRKSNIHCNTIAPNA 196
Cdd:PRK09135 152 GypvYCAAKAALEMLTRSLALE-LAPEVRVNAVAPGA 187
PRK06914 PRK06914
SDR family oxidoreductase;
9-201 2.38e-13

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 71.21  E-value: 2.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     9 GRVVLVTGAGAGLGRAYALAFAERGALVV--VNDLGgdfkgvgkgslAADKVVEEIRRRGGKA--------VANYDSVEE 78
Cdd:PRK06914   3 KKIAIVTGASSGFGLLTTLELAKKGYLVIatMRNPE-----------KQENLLSQATQLNLQQnikvqqldVTDQNSIHN 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    79 GEKVVKTaldaFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGN 158
Cdd:PRK06914  72 FQLVLKE----IGRIDLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRVGF 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 4504505   159 FGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPnaGSRMT 201
Cdd:PRK06914 148 PGLSPYVSSKYALEGFSESLRLELKPFGIDVALIEP--GSYNT 188
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
12-249 3.52e-13

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


Pssm-ID: 187586 [Multi-domain]  Cd Length: 233  Bit Score: 69.63  E-value: 3.52e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   12 VLVTGAGAGLGRAYALAFAERGALVVV-----NDLGGDFKGVGKGSLAADKVVEEIRRRGGKAVANydsveegekvVKTA 86
Cdd:cd05325   1 VLITGASRGIGLELVRQLLARGNNTVIatcrdPSAATELAALGASHSRLHILELDVTDEIAESAEA----------VAER 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   87 LDaFGRIDVVVNNAGILRDRSFAR-ISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRII-MTSSASGIYGN--FGQA 162
Cdd:cd05325  71 LG-DAGLDVLINNAGILHSYGPASeVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIInISSRVGSIGDNtsGGWY 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  163 NYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPnaGsrMTQTVMPEDLVEALKPEYVAPLVLWLCH---ESCEENGGLFEv 239
Cdd:cd05325 150 SYRASKAALNMLTKSLAVELKRDGITVVSLHP--G--WVRTDMGGPFAKNKGPITPEESVAGLLKvidNLNEEDSGKFL- 224
                       250
                ....*....|.
gi 4504505  240 gaGWIGK-LRW 249
Cdd:cd05325 225 --DYDGTeIPW 233
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
8-175 3.71e-13

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 71.65  E-value: 3.71e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    8 DGRVVLVTGAGAGLGRAYALAFAERGA--LVVVndlggdfkgvGKGSLAADKVVEEIRRRGGKAVANYDSV----EEGEK 81
Cdd:cd05274 149 LDGTYLITGGLGGLGLLVARWLAARGArhLVLL----------SRRGPAPRAAARAALLRAGGARVSVVRCdvtdPAALA 218
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   82 VVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKqkygRIIMTSSASGIYGNFGQ 161
Cdd:cd05274 219 ALLAELAAGGPLAGVIHAAGVLRDALLAELTPAAFAAVLAAKVAGALNLHELTPDLPLD----FFVLFSSVAALLGGAGQ 294
                       170
                ....*....|....
gi 4504505  162 ANYSAAKLGLLGLA 175
Cdd:cd05274 295 AAYAAANAFLDALA 308
PRK07024 PRK07024
SDR family oxidoreductase;
12-194 4.11e-13

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 69.96  E-value: 4.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    12 VLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgVGKGSLAADKVVEEIRRRGGKAVANYDsVEEGEKVVKTA---LD 88
Cdd:PRK07024   5 VFITGASSGIGQALAREYARQGATLGL---------VARRTDALQAFAARLPKAARVSVYAAD-VRDADALAAAAadfIA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    89 AFGRIDVVVNNAGILR--DRSFArisdEDWDIIHRVH------LRGSFQVTRAAwehMKKQKYGRIIMTSSASGIYGNFG 160
Cdd:PRK07024  75 AHGLPDVVIANAGISVgtLTEER----EDLAVFREVMdtnyfgMVATFQPFIAP---MRAARRGTLVGIASVAGVRGLPG 147
                        170       180       190
                 ....*....|....*....|....*....|....
gi 4504505   161 QANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK07024 148 AGAYSASKAAAIKYLESLRVELRPAGVRVVTIAP 181
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
6-224 4.93e-13

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


Pssm-ID: 187601 [Multi-domain]  Cd Length: 250  Bit Score: 69.46  E-value: 4.93e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVV--------VNDLGGDFKGVGKGSLAADKVveEIRRRggkavanydsvE 77
Cdd:cd05343   3 RWRGRVALVTGASVGIGAAVARALVQHGMKVVgcarrvdkIEALAAECQSAGYPTLFPYQC--DLSNE-----------E 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   78 EGEKVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKY--GRIIMTSSASG- 154
Cdd:cd05343  70 QILSMFSAIRTQHQGVDVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNVddGHIININSMSGh 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  155 --IYGNFGQAnYSAAKLGLLGLANSLAIEGR--KSNIHCNTIAPNA-----GSRMTQTVmpEDLVEA-------LKPEYV 218
Cdd:cd05343 150 rvPPVSVFHF-YAATKHAVTALTEGLRQELReaKTHIRATSISPGLvetefAFKLHDND--PEKAAAtyesipcLKPEDV 226

                ....*.
gi 4504505  219 APLVLW 224
Cdd:cd05343 227 ANAVLY 232
PRK06720 PRK06720
hypothetical protein; Provisional
5-170 5.79e-13

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 67.69  E-value: 5.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     5 LRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgslAADKVVEEIRRRGGKAV-ANYDSVEEG--EK 81
Cdd:PRK06720  12 MKLAGKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDIDQE---------SGQATVEEITNLGGEALfVSYDMEKQGdwQR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    82 VVKTALDAFGRIDVVVNNAGILR-DRSFARISDEDWDI--IHRVhlrgSFQVTRAAWEHMKKQKygRIIMTS-SASGIYG 157
Cdd:PRK06720  83 VISITLNAFSRIDMLFQNAGLYKiDSIFSRQQENDSNVlcINDV----WIEIKQLTSSFMKQQE--EVVLSDlPIFGIIG 156
                        170
                 ....*....|...
gi 4504505   158 NFGQANYSAAKLG 170
Cdd:PRK06720 157 TKGQSFHTVEALV 169
PRK09186 PRK09186
flagellin modification protein A; Provisional
8-194 7.27e-13

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 69.25  E-value: 7.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     8 DGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLggdfkGVGKGSLAADKVVEEIRRRGGKAVANYDSVEEG-EKVVKTA 86
Cdd:PRK09186   3 KGKTILITGAGGLIGSALVKAILEAGGIVIAADI-----DKEALNELLESLGKEFKSKKLSLVELDITDQESlEEFLSKS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    87 LDAFGRIDVVVNNA-------GilrdRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYG-N 158
Cdd:PRK09186  78 AEKYGKIDGAVNCAyprnkdyG----KKFFDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGGGNLVNISSIYGVVApK 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 4504505   159 FGQAN---------YSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK09186 154 FEIYEgtsmtspveYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSP 198
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
9-226 1.27e-12

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: 68.28  E-value: 1.27e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    9 GRVVLVTGAGAGLGRAYALAFAERGALVVVNdlggdfkgvGKGSLAADKVVEEIRRRGG-KAV-ANYDSVEEGEKVVKTA 86
Cdd:cd08942   6 GKIVLVTGGSRGIGRMIAQGFLEAGARVIIS---------ARKAEACADAAEELSAYGEcIAIpADLSSEEGIEALVARV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   87 LDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKY----GRIIMTSSASGIYGNFGQA 162
Cdd:cd08942  77 AERSDRLDVLVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAATaenpARVINIGSIAGIVVSGLEN 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4504505  163 -NYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNA-GSRMTQTVM--PEDLVEALK---------PEYVAPLVLWLC 226
Cdd:cd08942 157 ySYGASKAAVHQLTRKLAKELAGEHITVNAIAPGRfPSKMTAFLLndPAALEAEEKsiplgrwgrPEDMAGLAIMLA 233
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
5-225 1.34e-12

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 68.25  E-value: 1.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     5 LRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDFKGVGKGSLAADKVVEEIrrrggkaVANYDSVEEGEKVVK 84
Cdd:PRK05786   1 MRLKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTLSKYGNIHYV-------VGDVSSTESARNVIE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    85 TALDAFGRIDVVVNNAGILRDRSFARISDEDwDIIHRvHLRGSFQVTRAAWEHMKKQKygRIIMTSSASGIYGNF-GQAN 163
Cdd:PRK05786  74 KAAKVLNAIDGLVVTVGGYVEDTVEEFSGLE-EMLTN-HIKIPLYAVNASLRFLKEGS--SIVLVSSMSGIYKASpDQLS 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   164 YSAAKLGLLGLANSLAIEGRKSNIHCNTIAPnagSRMTQTVMPEDLVEALK--------PEYVAPLVLWL 225
Cdd:PRK05786 150 YAVAKAGLAKAVEILASELLGRGIRVNGIAP---TTISGDFEPERNWKKLRklgddmapPEDFAKVIIWL 216
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
10-194 1.61e-12

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


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 68.26  E-value: 1.61e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   10 RVVLVTG--AGAGLGRAYALAFAERGALVVVNDLggdfKGVGKGslaaDKVVEEIRRRGGKA-------VANYDSVEEGE 80
Cdd:cd09806   1 TVVLITGcsSGIGLHLAVRLASDPSKRFKVYATM----RDLKKK----GRLWEAAGALAGGTletlqldVCDSKSVAAAV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   81 KVVKTaldafGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFG 160
Cdd:cd09806  73 ERVTE-----RHVDVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPF 147
                       170       180       190
                ....*....|....*....|....*....|....
gi 4504505  161 QANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:cd09806 148 NDVYCASKFALEGLCESLAVQLLPFNVHLSLIEC 181
PRK07985 PRK07985
SDR family oxidoreductase;
6-225 2.18e-12

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 68.48  E-value: 2.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     6 RFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDFKGvgkgslaADKVVEEIRRRGGKAV---ANYDSVEEGEKV 82
Cdd:PRK07985  46 RLKDRKALVTGGDSGIGRAAAIAYAREGADVAISYLPVEEED-------AQDVKKIIEECGRKAVllpGDLSDEKFARSL 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    83 VKTALDAFGRIDVVVNNAGI-LRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQkyGRIIMTSSASGIYGNFGQ 161
Cdd:PRK07985 119 VHEAHKALGGLDIMALVAGKqVAIPDIADLTSEQFQKTFAINVFALFWLTQEAIPLLPKG--ASIITTSSIQAYQPSPHL 196
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4504505   162 ANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPN--------AGSRmTQTVMPE-----DLVEALKPEYVAPLVLWL 225
Cdd:PRK07985 197 LDYAATKAAILNYSRGLAKQVAEKGIRVNIVAPGpiwtalqiSGGQ-TQDKIPQfgqqtPMKRAGQPAELAPVYVYL 272
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
7-223 2.31e-11

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: 64.35  E-value: 2.31e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    7 FDGRVVLVTGAGAGLGRAYALAFAERGALVV---VNDLGGDFKGVGKgslAADKVVeEIRRRggkaVANYDSVEEgekvv 83
Cdd:cd05354   1 IKDKTVLVTGANRGIGKAFVESLLAHGAKKVyaaVRDPGSAAHLVAK---YGDKVV-PLRLD----VTDPESIKA----- 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   84 ktALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIH-RVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQA 162
Cdd:cd05354  68 --AAAQAKDVDVVINNAGVLKPATLLEEGALEALKQEmDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKNFPAMG 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4504505  163 NYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNA-GSRMTQTV-MPEDlvealKPEYVAPLVL 223
Cdd:cd05354 146 TYSASKSAAYSLTQGLRAELAAQGTLVLSVHPGPiDTRMAAGAgGPKE-----SPETVAEAVL 203
PRK12742 PRK12742
SDR family oxidoreductase;
7-225 3.11e-11

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 64.01  E-value: 3.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     7 FDGRVVLVTGAGAGLGRAYALAFAERGALVVvndlggdFKGVGKGSlAADKVVEEIrrrGGKAVANyDSVEEGEkvVKTA 86
Cdd:PRK12742   4 FTGKKVLVLGGSRGIGAAIVRRFVTDGANVR-------FTYAGSKD-AAERLAQET---GATAVQT-DSADRDA--VIDV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    87 LDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQkyGRIIMTSSASGIYGNF-GQANYS 165
Cdd:PRK12742  70 VRKSGALDILVVNAGIAVFGDALELDADDIDRLFKINIHAPYHASVEAARQMPEG--GRIIIIGSVNGDRMPVaGMAAYA 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4504505   166 AAKLGLLGLANSLAIEGRKSNIHCNTIAPNAgsrmTQTVM-PED--------LVEALK----PEYVAPLVLWL 225
Cdd:PRK12742 148 ASKSALQGMARGLARDFGPRGITINVVQPGP----IDTDAnPANgpmkdmmhSFMAIKrhgrPEEVAGMVAWL 216
PRK07806 PRK07806
SDR family oxidoreductase;
8-100 3.34e-11

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 63.97  E-value: 3.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     8 DGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGgdfkgvgkGSLAADKVVEEIRRRGGKAV---ANYDSVEEGEKVVK 84
Cdd:PRK07806   5 PGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQ--------KAPRANKVVAEIEAAGGRASavgADLTDEESVAALMD 76
                         90
                 ....*....|....*.
gi 4504505    85 TALDAFGRIDVVVNNA 100
Cdd:PRK07806  77 TAREEFGGLDALVLNA 92
PRK12744 PRK12744
SDR family oxidoreductase;
9-194 9.13e-11

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 62.83  E-value: 9.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     9 GRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgKGSLAADKVVEEIRRRGGKAV---ANYDSVEEGEKVVKT 85
Cdd:PRK12744   8 GKVVLIAGGAKNLGGLIARDLAAQGAKAVAIHYNSA-----ASKADAEETVAAVKAAGAKAVafqADLTTAAAVEKLFDD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    86 ALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQkyGRII-MTSSASGIYGNFgQANY 164
Cdd:PRK12744  83 AKAAFGRPDIAINTVGKVLKKPIVEISEAEYDEMFAVNSKSAFFFIKEAGRHLNDN--GKIVtLVTSLLGAFTPF-YSAY 159
                        170       180       190
                 ....*....|....*....|....*....|
gi 4504505   165 SAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK12744 160 AGSKAPVEHFTRAASKEFGARGISVTAVGP 189
SAV4209_like cd03453
SAV4209_like. Similar in sequence to the Streptomyces avermitilis SAV4209 protein, with a hot ...
508-574 1.02e-10

SAV4209_like. Similar in sequence to the Streptomyces avermitilis SAV4209 protein, with a hot dog fold that is similar to those of (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit.


Pssm-ID: 239537 [Multi-domain]  Cd Length: 127  Bit Score: 59.64  E-value: 1.02e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4504505  508 SGDWNPLHIDPNFASLAGFDKPILHGLCTFGFSArRVLQQFADnDVSRFKAIKARFAKPVYPGQTLQ 574
Cdd:cd03453  24 SGDFNPIHYDEDFAKKVGLPGVIAHGMLTMGLLG-RLVTDWVG-DPGRVVSFGVRFTKPVPVPDTLT 88
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
3-244 1.38e-10

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 62.40  E-value: 1.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     3 SPLRfdGRVVLVTGA--GAGLGRAYALAFAERGALVVVNDLGGDFKGVGKGSLAADKVV--EEIRRRGGK---AVANYDS 75
Cdd:PRK12748   1 LPLM--KKIALVTGAsrLNGIGAAVCRRLAAKGIDIFFTYWSPYDKTMPWGMHDKEPVLlkEEIESYGVRcehMEIDLSQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    76 VEEGEKVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRII-MTSsasg 154
Cdd:PRK12748  79 PYAPNRVFYAVSERLGDPSILINNAAYSTHTRLEELTAEQLDKHYAVNVRATMLLSSAFAKQYDGKAGGRIInLTS---- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   155 iyGNF-----GQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNAgsrmTQT-VMPEDLVEALKPEY----------V 218
Cdd:PRK12748 155 --GQSlgpmpDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGP----TDTgWITEELKHHLVPKFpqgrvgepvdA 228
                        250       260
                 ....*....|....*....|....*.
gi 4504505   219 APLVLWLCHESceengglfevgAGWI 244
Cdd:PRK12748 229 ARLIAFLVSEE-----------AKWI 243
PRK07062 PRK07062
SDR family oxidoreductase;
8-192 1.43e-10

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 62.37  E-value: 1.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     8 DGRVVLVTGAGAGLGRAYALAFAERGALVVvndlggdFKGVGKGSLAAdkVVEEIRRRGGKA--------VANYDSVEEG 79
Cdd:PRK07062   7 EGRVAVVTGGSSGIGLATVELLLEAGASVA-------ICGRDEERLAS--AEARLREKFPGArllaarcdVLDEADVAAF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    80 EKVVKTAldaFGRIDVVVNNAGILRDRSFARISDEDWdiIHRVHLRgSFQV---TRAAWEHMKKQKYGRIIMTSSASGIY 156
Cdd:PRK07062  78 AAAVEAR---FGGVDMLVNNAGQGRVSTFADTTDDAW--RDELELK-YFSVinpTRAFLPLLRASAAASIVCVNSLLALQ 151
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 4504505   157 GNFGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTI 192
Cdd:PRK07062 152 PEPHMVATSAARAGLLNLVKSLATELAPKGVRVNSI 187
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
12-158 4.00e-10

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 61.53  E-value: 4.00e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   12 VLVTGAgAG-LGRAYALAFAERGALVVVNDLGGDfkgvGKGSLAADKVVEEIRrrggkA-VANYDSVEEgekvvktaldA 89
Cdd:COG0451   2 ILVTGG-AGfIGSHLARRLLARGHEVVGLDRSPP----GAANLAALPGVEFVR-----GdLRDPEALAA----------A 61
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4504505   90 FGRIDVVVNNAGILRDRSfarisdEDWDIIHRVHLRGsfqvTRAAWEHMKKQKYGRIIMTSSASgIYGN 158
Cdd:COG0451  62 LAGVDAVVHLAAPAGVGE------EDPDETLEVNVEG----TLNLLEAARAAGVKRFVYASSSS-VYGD 119
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
507-599 4.38e-10

(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA to (R)-3-hydroxyacyl-CoA as part of the PHA (polyhydroxyalkanoate) biosynthetic pathway. (R)-hydratase contains a hot-dog fold similar to those of thioesterase II, and beta-hydroxydecanoyl-ACP dehydratase, MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and the fatty acid synthase beta subunit. The active site lies within a substrate-binding tunnel formed by the (R)-hydratase homodimer. A subset of the bacterial (R)-hydratases contain a C-terminal phosphotransacetylase (PTA) domain.


Pssm-ID: 239533 [Multi-domain]  Cd Length: 128  Bit Score: 57.94  E-value: 4.38e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  507 LSGDWNPLHIDPNFASLAGFDKPILHGLCTFG-FSArrVL-------------QQFadndvsrfkaikaRFAKPVYPGQT 572
Cdd:cd03449  24 LSGDFNPIHLDEEYAKKTRFGGRIAHGMLTASlISA--VLgtllpgpgtiylsQSL-------------RFLRPVFIGDT 88
                        90       100       110
                ....*....|....*....|....*....|...
gi 4504505  573 LQ-----TEMWKEGNRIHFQTKVQ-ETGDIVIS 599
Cdd:cd03449  89 VTatvtvTEKREDKKRVTLETVCTnQNGEVVIE 121
PRK06125 PRK06125
short chain dehydrogenase; Provisional
5-154 4.47e-10

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 60.83  E-value: 4.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     5 LRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgkgSLAADKvvEEIRRRGGKAVA----NYDSVEEGE 80
Cdd:PRK06125   3 LHLAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDAD-------ALEALA--ADLRAAHGVDVAvhalDLSSPEARE 73
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4504505    81 KVVKTAldafGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASG 154
Cdd:PRK06125  74 QLAAEA----GDIDILVNNAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIVNVIGAAG 143
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
9-194 4.83e-10

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


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 60.94  E-value: 4.83e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    9 GRVVLVTGAGAGLGRAYALAFAERGALVVVNdlggdFKGVGKGSLAAdkvvEEIRRRGGKA--------VANYDSVEEge 80
Cdd:cd09807   1 GKTVIITGANTGIGKETARELARRGARVIMA-----CRDMAKCEEAA----AEIRRDTLNHevivrhldLASLKSIRA-- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   81 kVVKTALDAFGRIDVVVNNAGILRdrsFARISDED-WDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYG-- 157
Cdd:cd09807  70 -FAAEFLAEEDRLDVLINNAGVMR---CPYSKTEDgFEMQFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSSLAHKAGki 145
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 4504505  158 NFGQAN----------YSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:cd09807 146 NFDDLNseksyntgfaYCQSKLANVLFTRELARRLQGTGVTVNALHP 192
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
11-184 6.65e-10

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: 59.99  E-value: 6.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   11 VVLVTGAGAGLGRAYALAFAERGALVVV----NDLGGDFKgvGKGSLAADKVVEEIrrrggkaVANYDSVEEGEKVVKTA 86
Cdd:cd05367   1 VIILTGASRGIGRALAEELLKRGSPSVVvllaRSEEPLQE--LKEELRPGLRVTTV-------KADLSDAAGVEQLLEAI 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   87 LDAFGRIDVVVNNAGILRD-RSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKY-GRIIMTSSASGIYGNFGQANY 164
Cdd:cd05367  72 RKLDGERDLLINNAGSLGPvSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGLkKTVVNVSSGAAVNPFKGWGLY 151
                       170       180
                ....*....|....*....|
gi 4504505  165 SAAKLGLLGLANSLAIEGRK 184
Cdd:cd05367 152 CSSKAARDMFFRVLAAEEPD 171
PRK06197 PRK06197
short chain dehydrogenase; Provisional
8-103 9.81e-10

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 60.42  E-value: 9.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     8 DGRVVLVTGAGAGLGRAYALAFAERGALVV--VNDLggdfkgvGKGSLAADKvveeIRRRGGKA--------VANYDSVE 77
Cdd:PRK06197  15 SGRVAVVTGANTGLGYETAAALAAKGAHVVlaVRNL-------DKGKAAAAR----ITAATPGAdvtlqeldLTSLASVR 83
                         90       100
                 ....*....|....*....|....*.
gi 4504505    78 EGEKVVKTaldAFGRIDVVVNNAGIL 103
Cdd:PRK06197  84 AAADALRA---AYPRIDLLINNAGVM 106
PRK08703 PRK08703
SDR family oxidoreductase;
9-239 1.52e-09

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 59.17  E-value: 1.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     9 GRVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgVGKGSLAADKVVEEIRRRGG--KAVANYDSVEEGEK----- 81
Cdd:PRK08703   6 DKTILVTGASQGLGEQVAKAYAAAGATVIL---------VARHQKKLEKVYDAIVEAGHpePFAIRFDLMSAEEKefeqf 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    82 VVKTALDAFGRIDVVVNNAGILRDRS---FARIsdEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGN 158
Cdd:PRK08703  77 AATIAEATQGKLDGIVHCAGYFYALSpldFQTV--AEWVNQYRINTVAPMGLTRALFPLLKQSPDASVIFVGESHGETPK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   159 FGQANYSAAKLGLLGLANSLAIE-GRKSNIHCNTIAP---NAGSRmTQTVMPEDLVEALKPEYVAP-LVLWLCHESCEEN 233
Cdd:PRK08703 155 AYWGGFGASKAALNYLCKVAADEwERFGNLRANVLVPgpiNSPQR-IKSHPGEAKSERKSYGDVLPaFVWWASAESKGRS 233

                 ....*.
gi 4504505   234 GGLFEV 239
Cdd:PRK08703 234 GEIVYL 239
PRK09291 PRK09291
SDR family oxidoreductase;
9-196 1.75e-09

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 59.24  E-value: 1.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     9 GRVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkGVGKGSLAADkVVEEIRRRGGK-AVANYDSVEEGEKVVKTAL 87
Cdd:PRK09291   2 SKTILITGAGSGFGREVALRLARKGHNVIA--------GVQIAPQVTA-LRAEAARRGLAlRVEKLDLTDAIDRAQAAEW 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    88 DafgrIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSAA 167
Cdd:PRK09291  73 D----VDVLLNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLITGPFTGAYCAS 148
                        170       180
                 ....*....|....*....|....*....
gi 4504505   168 KLGLLGLANSLAIEGRKSNIHCNTIAPNA 196
Cdd:PRK09291 149 KHALEAIAEAMHAELKPFGIQVATVNPGP 177
MaoC_like cd03446
MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but ...
507-577 3.44e-09

MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but without the N-terminal PutA domain. This protein family has a hot-dog fold similar to that of (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit.


Pssm-ID: 239530 [Multi-domain]  Cd Length: 140  Bit Score: 55.77  E-value: 3.44e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4504505  507 LSGDWNPLHIDPNFASLAGFDKPILHGLctFGFSARRVLQQFA---DNDVSRFKAI-KARFAKPVYPGQTLQTEM 577
Cdd:cd03446  29 LSGDWNPIHTDAEYAKKTRFGERIAHGL--LTLSIATGLLQRLgvfERTVVAFYGIdNLRFLNPVFIGDTIRAEA 101
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
12-223 4.75e-09

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: 57.15  E-value: 4.75e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   12 VLVTGAGAGLGRAYALAFAERG-ALVVVNDLGGDFKGVGKGSLAADKVVEEIrrrggkavanydsveeGEKVVKTALDAF 90
Cdd:cd11730   1 ALILGATGGIGRALARALAGRGwRLLLSGRDAGALAGLAAEVGALARPADVA----------------AELEVWALAQEL 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   91 GRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQkyGRIIMTSSASGIYGNFGQANYSAAKLG 170
Cdd:cd11730  65 GPLDLLVYAAGAILGKPLARTKPAAWRRILDANLTGAALVLKHALALLAAG--ARLVFLGAYPELVMLPGLSAYAAAKAA 142
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 4504505  171 LLGLANSLAIEGRKSNIhCNTIAPNAGSRMTQTV--MPEDlveALKPEYVAPLVL 223
Cdd:cd11730 143 LEAYVEVARKEVRGLRL-TLVRPPAVDTGLWAPPgrLPKG---ALSPEDVAAAIL 193
PRK12747 PRK12747
short chain dehydrogenase; Provisional
9-194 2.00e-08

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 55.85  E-value: 2.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     9 GRVVLVTGAGAGLGRAYALAFAERGALVVVNdlggdfkgVGKGSLAADKVVEEIRRRGGKAV---ANYDSVeEGEKVVKT 85
Cdd:PRK12747   4 GKVALVTGASRGIGRAIAKRLANDGALVAIH--------YGNRKEEAEETVYEIQSNGGSAFsigANLESL-HGVEALYS 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    86 ALD-------AFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKygRIIMTSSASGIYGN 158
Cdd:PRK12747  75 SLDnelqnrtGSTKFDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRLRDNS--RIINISSAATRISL 152
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 4504505   159 FGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK12747 153 PDFIAYSMTKGAINTMTFTLAKQLGARGITVNAILP 188
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
5-217 3.58e-08

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 55.18  E-value: 3.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     5 LRFDGRVVLVTGAG--AGLGRAYALAFAERGALVVVNDLGGDFKGVGKGSLAAD--KVVEEIRRRGGKaVANYD---SVE 77
Cdd:PRK12859   2 NQLKNKVAVVTGVSrlDGIGAAICKELAEAGADIFFTYWTAYDKEMPWGVDQDEqiQLQEELLKNGVK-VSSMEldlTQN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    78 EGEK-VVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIY 156
Cdd:PRK12859  81 DAPKeLLNKVTEQLGYPHILVNNAAYSTNNDFSNLTAEELDKHYMVNVRATTLLSSQFARGFDKKSGGRIINMTSGQFQG 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4504505   157 GNFGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNAgsrmTQT-VMPEDLVEALKPEY 217
Cdd:PRK12859 161 PMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGP----TDTgWMTEEIKQGLLPMF 218
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
10-211 1.32e-07

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: 53.82  E-value: 1.32e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   10 RVVLVTGAGAGLGRAYALAFAERGALVvvndLGGDFKGVGKGSLAADKVVEEIRRRGGKAVANYDSVEEGEKVVKTALDA 89
Cdd:cd09805   1 KAVLITGCDSGFGNLLAKKLDSLGFTV----LAGCLTKNGPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   90 FGrIDVVVNNAGILrdrsfARISDEDW---DIIHR---VHLRGSFQVTRAAWEHMKKQKyGRIIMTSSASGIYGNFGQAN 163
Cdd:cd09805  77 KG-LWGLVNNAGIL-----GFGGDEELlpmDDYRKcmeVNLFGTVEVTKAFLPLLRRAK-GRVVNVSSMGGRVPFPAGGA 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 4504505  164 YSAAKLGLLGLANSLAIEGRKSNIHCNTIAPnaGSRMTQTVMPEDLVE 211
Cdd:cd09805 150 YCASKAAVEAFSDSLRRELQPWGVKVSIIEP--GNFKTGITGNSELWE 195
PRK08017 PRK08017
SDR family oxidoreductase;
12-204 1.53e-07

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 53.17  E-value: 1.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    12 VLVTGAGAGLGRAYALAFAERGALVvvndLGGDFKgvgkgslAADkvVEEIRRRGGKAVA----NYDSVEEGEKVVKTAL 87
Cdd:PRK08017   5 VLITGCSSGIGLEAALELKRRGYRV----LAACRK-------PDD--VARMNSLGFTGILldldDPESVERAADEVIALT 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    88 DafGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSAA 167
Cdd:PRK08017  72 D--NRLYGLFNNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGEGRIVMTSSVMGLISTPGRGAYAAS 149
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 4504505   168 KLGLLGLANSLAIEGRKSNIHCNTIAPNA-GSRMTQTV 204
Cdd:PRK08017 150 KYALEAWSDALRMELRHSGIKVSLIEPGPiRTRFTDNV 187
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
12-209 2.63e-07

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


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 52.49  E-value: 2.63e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   12 VLVTGAGAGLGRAYALAFAERGALVVVNdlggdfkgVGKGSLAADkVVEEIRRRGGKAVANYDSVEEGEKVVKTAlDAFG 91
Cdd:cd08951  10 IFITGSSDGLGLAAARTLLHQGHEVVLH--------ARSQKRAAD-AKAACPGAAGVLIGDLSSLAETRKLADQV-NAIG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   92 RIDVVVNNAGILRDRsFARISDEDWDIIHRVHLRGSFQVTraAWEHMKKqkygRIIMTSS--------------ASGIYG 157
Cdd:cd08951  80 RFDAVIHNAGILSGP-NRKTPDTGIPAMVAVNVLAPYVLT--ALIRRPK----RLIYLSSgmhrggnaslddidWFNRGE 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 4504505  158 NFGQAnYSAAKLGLLGLANSLAIegRKSNIHCNTIAPN-AGSRMTQTVMPEDL 209
Cdd:cd08951 153 NDSPA-YSDSKLHVLTLAAAVAR--RWKDVSSNAVHPGwVPTKMGGAGAPDDL 202
KR_2_FAS_SDR_x cd08955
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...
3-176 3.29e-07

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); Ketoreductase, a module of the multidomain polyketide synthase, has 2 subdomains, each corresponding to a short-chain dehydrogenases/reductase (SDR) family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerizes but is composed of 2 subdomains, each resembling an SDR monomer. In some instances, as in porcine FAS, an enoyl reductase (a Rossman fold NAD binding domain of the MDR family) module is inserted between the sub-domains. The active site resembles that of typical SDRs, except that the usual positions of the catalytic asparagine and tyrosine are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular polyketide synthases are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) fatty acid synthase. In some instances, such as porcine FAS , an enoyl reductase module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER). Polyketide syntheses also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes the KR domain of the Lyngbya majuscule Jam J, -K, and #L which are encoded on the jam gene cluster and are involved in the synthesis of the Jamaicamides (neurotoxins); Lyngbya majuscule Jam P belongs to a different KR_FAS_SDR_x subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187658 [Multi-domain]  Cd Length: 376  Bit Score: 53.06  E-value: 3.29e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    3 SPLRFDGrVVLVTGAGAGLGRAYALAFAERGA--LVVVndlggdfkgvGKGSLAADK--VVEEIRRRGGKAVanydsVEE 78
Cdd:cd08955 144 RPLRPDA-TYLITGGLGGLGLLVAEWLVERGArhLVLT----------GRRAPSAAArqAIAALEEAGAEVV-----VLA 207
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   79 GEKVVKTAL-DAFGRIDV-------VVNNAGILRDrsfARISDEDWDIIHRV---HLRGSFQVTRAAwehmKKQKYGRII 147
Cdd:cd08955 208 ADVSDRDALaAALAQIRAslpplrgVIHAAGVLDD---GVLANQDWERFRKVlapKVQGAWNLHQLT----QDLPLDFFV 280
                       170       180
                ....*....|....*....|....*....
gi 4504505  148 MTSSASGIYGNFGQANYSAAKLGLLGLAN 176
Cdd:cd08955 281 LFSSVASLLGSPGQANYAAANAFLDALAH 309
PRK05717 PRK05717
SDR family oxidoreductase;
1-225 3.57e-07

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 52.20  E-value: 3.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     1 MGSPLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgvgKGSLAAdKVVEEIRRRGGKAVANYDSVEEGe 80
Cdd:PRK05717   2 SEPNPGHNGRVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRE-----RGSKVA-KALGENAWFIAMDVADEAQVAAG- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    81 kvVKTALDAFGRIDVVVNNAGIL--RDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKyGRIIMTSSASGIYGN 158
Cdd:PRK05717  75 --VAEVLGQFGRLDALVCNAAIAdpHNTTLESLSLAHWNRVLAVNLTGPMLLAKHCAPYLRAHN-GAIVNLASTRARQSE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   159 FGQANYSAAKLGLLGLANSLAIEgRKSNIHCNTIAP------NAGSRMTQTVMPEDlvEALKP-------EYVAPLVLWL 225
Cdd:PRK05717 152 PDTEAYAASKGGLLALTHALAIS-LGPEIRVNAVSPgwidarDPSQRRAEPLSEAD--HAQHPagrvgtvEDVAAMVAWL 228
PRK05993 PRK05993
SDR family oxidoreductase;
10-194 5.45e-07

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 51.95  E-value: 5.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    10 RVVLVTGAGAGLGRAYALAFAERGALVvvndlggdFKGVGKgslaaDKVVEEIRRRGGKAVA-NYDSVEEGEKVVKTALD 88
Cdd:PRK05993   5 RSILITGCSSGIGAYCARALQSDGWRV--------FATCRK-----EEDVAALEAEGLEAFQlDYAEPESIAALVAQVLE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    89 -AFGRIDVVVNN-----AGILRDRSfarisdedwdiihRVHLRGSF--------QVTRAAWEHMKKQKYGRIIMTSSASG 154
Cdd:PRK05993  72 lSGGRLDALFNNgaygqPGAVEDLP-------------TEALRAQFeanffgwhDLTRRVIPVMRKQGQGRIVQCSSILG 138
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 4504505   155 IYGNFGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK05993 139 LVPMKYRGAYNASKFAIEGLSLTLRMELQGSGIHVSLIEP 178
SAV4209 cd03455
SAV4209 is a Streptomyces avermitilis protein with a hot dog fold that is similar to those of ...
493-573 6.98e-07

SAV4209 is a Streptomyces avermitilis protein with a hot dog fold that is similar to those of (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. The alpha- and gamma-proteobacterial members of this CD have, in addition to a hot dog fold, an N-terminal extension.


Pssm-ID: 239539 [Multi-domain]  Cd Length: 123  Bit Score: 48.85  E-value: 6.98e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  493 LTDTTSLNQAALYRlsgDWNPLHIDPNFASLAGFDKPILHGLCTFGFSARRVLQQFadNDVSRFKAIKARFAKPVYPGQT 572
Cdd:cd03455  11 PDPTLLFRYSAATR---DFHRIHHDRDYARAVGYPDLYVNGPTLAGLVIRYVTDWA--GPDARVKSFAFRLGAPLYAGDT 85

                .
gi 4504505  573 L 573
Cdd:cd03455  86 L 86
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
11-168 1.83e-06

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 49.76  E-value: 1.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    11 VVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDFKGVGKGSLAADKVVEEIRRRGGKAVanydsveegEKVVKTALDAF 90
Cdd:PRK10538   2 IVLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNLYIAQLDVRNRAAI---------EEMLASLPAEW 72
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4504505    91 GRIDVVVNNAGILRDRSFA-RISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSAAK 168
Cdd:PRK10538  73 RNIDVLVNNAGLALGLEPAhKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATK 151
PRK08339 PRK08339
short chain dehydrogenase; Provisional
9-194 2.28e-06

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 49.85  E-value: 2.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     9 GRVVLVTGAGAGLGRAYALAFAERGALVVVndLGGDFKGVGKgslAADKVVEEIRRRGGKAVANYDSVEEGEKVVKTALD 88
Cdd:PRK08339   8 GKLAFTTASSKGIGFGVARVLARAGADVIL--LSRNEENLKK---AREKIKSESNVDVSYIVADLTKREDLERTVKELKN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    89 aFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSAAK 168
Cdd:PRK08339  83 -IGEPDIFFFSTGGPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSVAIKEPIPNIALSNVVR 161
                        170       180
                 ....*....|....*....|....*.
gi 4504505   169 LGLLGLANSLAIEGRKSNIHCNTIAP 194
Cdd:PRK08339 162 ISMAGLVRTLAKELGPKGITVNGIMP 187
PRK07102 PRK07102
SDR family oxidoreductase;
12-219 2.61e-06

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 49.54  E-value: 2.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    12 VLVTGAGAGLGRAYALAFAERGAlvvvndlggDFKGVGKGSLAADKVVEEIRRRGGKAVANY----DSVEEGEKVVKTAL 87
Cdd:PRK07102   4 ILIIGATSDIARACARRYAAAGA---------RLYLAARDVERLERLADDLRARGAVAVSTHeldiLDTASHAAFLDSLP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    88 DAFgriDVVVNNAGILRDRSfarISDEDWDIIHRVhLRGSFQ-----VTRAAwEHMKKQKYGRIIMTSSASGIYGNfgQA 162
Cdd:PRK07102  75 ALP---DIVLIAVGTLGDQA---ACEADPALALRE-FRTNFEgpialLTLLA-NRFEARGSGTIVGISSVAGDRGR--AS 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4504505   163 N--YSAAKLG----LLGLANSLAiegrKSNIHCNTIAPN-AGSRMTQTV-MPEDLVEalKPEYVA 219
Cdd:PRK07102 145 NyvYGSAKAAltafLSGLRNRLF----KSGVHVLTVKPGfVRTPMTAGLkLPGPLTA--QPEEVA 203
PRK05875 PRK05875
short chain dehydrogenase; Provisional
5-219 4.15e-06

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 49.03  E-value: 4.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     5 LRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgVGKGSLAADKVVEEIRRRGGKAVANY---DSVEEGE- 80
Cdd:PRK05875   3 LSFQDRTYLVTGGGSGIGKGVAAGLVAAGAAVMI---------VGRNPDKLAAAAEEIEALKGAGAVRYepaDVTDEDQv 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    81 -KVVKTALDAFGRIDVVVNNAGilRDRSFARISDEDWDIIHR---VHLRGSFQVTRAAWEHMKKQKYGRIIMTSS--ASG 154
Cdd:PRK05875  74 aRAVDAATAWHGRLHGVVHCAG--GSETIGPITQIDSDAWRRtvdLNVNGTMYVLKHAARELVRGGGGSFVGISSiaASN 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4504505   155 IYGNFGQanYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPnaGSRMTQTVMPEDLVEALKPEYVA 219
Cdd:PRK05875 152 THRWFGA--YGVTKSAVDHLMKLAADELGPSWVRVNSIRP--GLIRTDLVAPITESPELSADYRA 212
PLN02780 PLN02780
ketoreductase/ oxidoreductase
5-187 4.93e-06

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 49.09  E-value: 4.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     5 LRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgVGKGSLAADKVVEEIRRRGGKA-----VANYD-SVEE 78
Cdd:PLN02780  49 LKKYGSWALVTGPTDGIGKGFAFQLARKGLNLVL---------VARNPDKLKDVSDSIQSKYSKTqiktvVVDFSgDIDE 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    79 GEKVVKTALDAFGrIDVVVNNAGILRD--RSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIY 156
Cdd:PLN02780 120 GVKRIKETIEGLD-VGVLINNVGVSYPyaRFFHEVDEELLKNLIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAIV 198
                        170       180       190
                 ....*....|....*....|....*....|...
gi 4504505   157 --GNFGQANYSAAKLGLLGLANSLAIEGRKSNI 187
Cdd:PLN02780 199 ipSDPLYAVYAATKAYIDQFSRCLYVEYKKSGI 231
PRK07904 PRK07904
decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;
12-222 6.64e-06

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


Pssm-ID: 181162 [Multi-domain]  Cd Length: 253  Bit Score: 48.16  E-value: 6.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    12 VLVTGAGAGLGRAYALAFAERG-ALVVVNDLggdfkgvgKGSLAADKVVEEIRRRGGKAVA--NYDSV--EEGEKVVKTA 86
Cdd:PRK07904  11 ILLLGGTSEIGLAICERYLKNApARVVLAAL--------PDDPRRDAAVAQMKAAGASSVEviDFDALdtDSHPKVIDAA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    87 LdAFGRIDVVVNNAGILRDrsfariSDEDWD------IIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIY---G 157
Cdd:PRK07904  83 F-AGGDVDVAIVAFGLLGD------AEELWQnqrkavQIAEINYTAAVSVGVLLGEKMRAQGFGQIIAMSSVAGERvrrS 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4504505   158 NFgqaNYSAAKLGL----LGLANSLaiegRKSNIHCNTIAPNagsrMTQTVMPEDLVEA---LKPEYVAPLV 222
Cdd:PRK07904 156 NF---VYGSTKAGLdgfyLGLGEAL----REYGVRVLVVRPG----QVRTRMSAHAKEApltVDKEDVAKLA 216
PRK05693 PRK05693
SDR family oxidoreductase;
11-208 1.15e-05

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 47.86  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    11 VVLVTGAGAGLGRAYALAFAERGALVVVNdlggdfkgvgkGSLAADkvVEEIRRRGGKAVA-NYDSVEEGEKVVKTALDA 89
Cdd:PRK05693   3 VVLITGCSSGIGRALADAFKAAGYEVWAT-----------ARKAED--VEALAAAGFTAVQlDVNDGAALARLAEELEAE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    90 FGRIDVVVNNAGIlrdRSFARISDEDWDIIHRVHLRGSF---QVTRAAWEHMKKQKyGRIIMTSSASGIYGNFGQANYSA 166
Cdd:PRK05693  70 HGGLDVLINNAGY---GAMGPLLDGGVEAMRRQFETNVFavvGVTRALFPLLRRSR-GLVVNIGSVSGVLVTPFAGAYCA 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 4504505   167 AKLGLLGLANSLAIEGRKSNIHCNTIAP---------NAGSRMTQtVMPED 208
Cdd:PRK05693 146 SKAAVHALSDALRLELAPFGVQVMEVQPgaiasqfasNASREAEQ-LLAEQ 195
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
12-195 1.76e-05

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


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 46.42  E-value: 1.76e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   12 VLVTGAGAGLGRAYALAFAERGALVVVndlggdfKGVGKGSLAADkvveeirrrggkaVANYDSVeegekvvKTALDAFG 91
Cdd:cd11731   1 IIVIGATGTIGLAVAQLLSAHGHEVIT-------AGRSSGDYQVD-------------ITDEASI-------KALFEKVG 53
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   92 RIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQkyGRIIMTSSASGIYGNFGQANYSAAKLGL 171
Cdd:cd11731  54 HFDAIVSTAGDAEFAPLAELTDADFQRGLNSKLLGQINLVRHGLPYLNDG--GSITLTSGILAQRPIPGGAAAATVNGAL 131
                       170       180
                ....*....|....*....|....
gi 4504505  172 LGLANSLAIEGRKSnIHCNTIAPN 195
Cdd:cd11731 132 EGFVRAAAIELPRG-IRINAVSPG 154
PRK06196 PRK06196
oxidoreductase; Provisional
8-212 2.09e-05

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 47.37  E-value: 2.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     8 DGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDfkgVGKGSLAADKVVEeirrRGGKAVANYDSVEEGEKVVktaL 87
Cdd:PRK06196  25 SGKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPD---VAREALAGIDGVE----VVMLDLADLESVRAFAERF---L 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    88 DAFGRIDVVVNNAGILRDrSFARISDeDWDIIHRV-HLrGSFQVTRAAWEHMKKQKYGRIIMTSSA----SGIygNFGQA 162
Cdd:PRK06196  95 DSGRRIDILINNAGVMAC-PETRVGD-GWEAQFATnHL-GHFALVNLLWPALAAGAGARVVALSSAghrrSPI--RWDDP 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4504505   163 N----------YSAAKlgllgLANSL-AIE----GRKSNIHCNTIAPnaGSRMT--QTVMP-EDLVEA 212
Cdd:PRK06196 170 HftrgydkwlaYGQSK-----TANALfAVHldklGKDQGVRAFSVHP--GGILTplQRHLPrEEQVAL 230
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
507-608 6.79e-05

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 46.03  E-value: 6.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   507 LSGDWNPLHIDPNFASLAGFDKPILHGLCTFG-FSArrVL--------QQFADNDVsrfkaikaRFAKPVYPGQTLQ--- 574
Cdd:PRK08190  37 MSGDVNPAHLDAAYAASDGFHHVVAHGMWGGAlISA--VLgtrlpgpgTIYLGQSL--------RFRRPVRIGDTLTvtv 106
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 4504505   575 --TEMWKEGNRIHFQTK-VQETGDIVISNAYVDLAPT 608
Cdd:PRK08190 107 tvREKDPEKRIVVLDCRcTNQDGEVVITGTAEVIAPT 143
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
11-232 8.68e-05

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: 44.92  E-value: 8.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     11 VVLVTGAGAGLGRAYALAFAERGALVVVNdlggdfkgVGKGSLAADKVVEEI-RRRGGKAV------ANYDSV-EEGEKV 82
Cdd:TIGR02685   3 AAVVTGAAKRIGSSIAVALHQEGYRVVLH--------YHRSAAAASTLAAELnARRPNSAVtcqadlSNSATLfSRCEAI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     83 VKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDI------IHRVHLRGS-----FQVTRAaweHMKKQKYGRIIMTSS 151
Cdd:TIGR02685  75 IDACFRAFGRCDVLVNNASAFYPTPLLRGDAGEGVGdkksleVQVAELFGSnaiapYFLIKA---FAQRQAGTRAEQRST 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    152 ASGIYGN---------FGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNAgsrmtqTVMPEDLVEALKPEYVAPLV 222
Cdd:TIGR02685 152 NLSIVNLcdamtdqplLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGL------SLLPDAMPFEVQEDYRRKVP 225
                         250
                  ....*....|
gi 4504505    223 LWLCHESCEE 232
Cdd:TIGR02685 226 LGQREASAEQ 235
Alkyl_sulf_C pfam14864
Alkyl sulfatase C-terminal; This domain is found at the C-terminus of alkyl sulfatases. ...
649-726 1.41e-04

Alkyl sulfatase C-terminal; This domain is found at the C-terminus of alkyl sulfatases. Together with the N-terminal catalytic domain, this domain forms a hydrophobic chute and may recruit hydrophobic substrates.


Pssm-ID: 405542 [Multi-domain]  Cd Length: 124  Bit Score: 42.18  E-value: 1.41e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4504505    649 VFEWHITkggNIGAKWTIDLKSGSGKVYQGPAKGAADTTIILSDEDFMEVVLGKLDPQKAFFSGRLKARGNIMLSQKL 726
Cdd:pfam14864  34 TINLVFP---DVDEQYRLTLSNGVLTYRKGRQADDADATLTLTRADLLALLLGKATLGKLIAAGKIKVEGDPSALAEL 108
PRK13693 PRK13693
(3R)-hydroxyacyl-ACP dehydratase subunit HadB; Provisional
473-621 2.49e-04

(3R)-hydroxyacyl-ACP dehydratase subunit HadB; Provisional


Pssm-ID: 184249 [Multi-domain]  Cd Length: 142  Bit Score: 41.74  E-value: 2.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   473 RTSDKVKVAVAIPNRPpdAVLTDTTSLNQAALyrlSGDWNPLHIDPNFASLAGFDKPILHGLCTFGFSARRVLQQFADNd 552
Cdd:PRK13693   4 REFSSVKVGDQLPEKT--YPLTRQDLVNYAGV---SGDLNPIHWDDEIAKVVGLDTAIAHGMLTMGLGGGYVTSWVGDP- 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4504505   553 vSRFKAIKARFAKPVYPGQTLQtemwkeGNRIHFQTKVQEtgdivisnayVDLAPTSGTSAKTPSEGGK 621
Cdd:PRK13693  78 -GAVTEYNVRFTAVVPVPNDGK------GAELVFNGRVKS----------VDPESKSVTIALTATTGGK 129
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
9-138 5.04e-04

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 42.69  E-value: 5.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    9 GRVVLVTGAGaGLGRAYALAFAERGALVVVNDLGGDfkgvgKGSLAadkvveeiRRRGGKAVANYDSVEEGEKVVKTald 88
Cdd:cd05188 135 GDTVLVLGAG-GVGLLAAQLAKAAGARVIVTDRSDE-----KLELA--------KELGADHVIDYKEEDLEEELRLT--- 197
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   89 AFGRIDVVVNNAGILRD--------RSFARI-----------SDEDWDIIHR-VHLRGSFQVTRAAWEHM 138
Cdd:cd05188 198 GGGGADVVIDAVGGPETlaqalrllRPGGRIvvvggtsggppLDDLRRLLFKeLTIIGSTGGTREDFEEA 267
KR_3_FAS_SDR_x cd08956
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); ...
12-167 9.08e-04

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta- ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the second KR domains of SpiE,-G, I, and -J, both KR domains of SpiD, and the third KR domain of SpiH. The single KR domain of SpiF, the first and second KR domains of SpiH, the first KR domains of SpiE,-G,- I, and -J, and the third KR domain of SpiG, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187659 [Multi-domain]  Cd Length: 448  Bit Score: 42.25  E-value: 9.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   12 VLVTGAGAGLGRAYA--LAfAERGA--LVVVNDLGGDFKGvgkgslaADKVVEEIRRRGGKA------VANYDSVEEgek 81
Cdd:cd08956 196 VLITGGTGTLGALLArhLV-TEHGVrhLLLVSRRGPDAPG-------AAELVAELAALGAEVtvaacdVADRAALAA--- 264
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   82 vVKTALDAFGRIDVVVNNAGILRDrsfARISDEDWDIIHRVhLRGsfQVTrAAW---EHMKKQKYGRIIMTSSASGIYGN 158
Cdd:cd08956 265 -LLAAVPADHPLTAVVHAAGVLDD---GVLTSLTPERLDAV-LRP--KVD-AAWhlhELTRDLDLAAFVLFSSAAGVLGS 336

                ....*....
gi 4504505  159 FGQANYSAA 167
Cdd:cd08956 337 PGQANYAAA 345
PRK08340 PRK08340
SDR family oxidoreductase;
12-153 1.07e-03

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 41.33  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    12 VLVTGAGAGLGRAYALAFAERGALVVVNDlggdfkgvgKGSLAADKVVEEIRRRGG-KAV-ANYDSVEEGEKVVKTALDA 89
Cdd:PRK08340   3 VLVTASSRGIGFNVARELLKKGARVVISS---------RNEENLEKALKELKEYGEvYAVkADLSDKDDLKNLVKEAWEL 73
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4504505    90 FGRIDVVVNNAGILR-DRSFARISD-EDWDIIHRVHLRGSFQVTR---AAWehMKKQKYGRIIMTSSAS 153
Cdd:PRK08340  74 LGGIDALVWNAGNVRcEPCMLHEAGySDWLEAALLHLVAPGYLTTlliQAW--LEKKMKGVLVYLSSVS 140
KR_1_FAS_SDR_x cd08954
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; ...
70-198 1.28e-03

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; NADP-dependent KR domain of the multidomain type I FAS, a complex SDR family. This subfamily also includes proteins identified as polyketide synthase (PKS), a protein with related modular protein architecture and similar function. It includes the KR domains of mammalian and chicken FAS, and Dictyostelium discoideum putative polyketide synthases (PKSs). These KR domains contain two subdomains, each of which is related to SDR Rossmann fold domains. However, while the C-terminal subdomain has an active site similar to the other SDRs and a NADP-binding capability, the N-terminal SDR-like subdomain is truncated and lacks these functions, serving a supportive structural role. In some instances, such as porcine FAS, an enoyl reductase (a Rossman fold NAD-binding domain of the medium-chain dehydrogenase/reductase, MDR family) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER); this KR and ER are members of the SDR family. This KR subfamily has an active site tetrad with a similar 3D orientation compared to archetypical SDRs, but the active site Lys and Asn residue positions are swapped. The characteristic NADP-binding is typical of the multidomain complex SDRs, with a GGXGXXG NADP 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 prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187657 [Multi-domain]  Cd Length: 452  Bit Score: 42.05  E-value: 1.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   70 VANYDSVEEGEKVVKTALDaFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYgrIIMT 149
Cdd:cd08954 280 VSDVSSLEKAINLILNAPK-IGPIGGIFHLAFVLIDKVLEIDTESLFISVNKAKVMGAINLHNQSIKRCWKLDY--FVLF 356
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 4504505  150 SSASGIYGNFGQANYSAAKLGLLGLANSLAIEGRKSnihcntIAPNAGS 198
Cdd:cd08954 357 SSVSSIRGSAGQCNYVCANSVLDSLSRYRKSIGLPS------IAINWGA 399
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
9-238 1.51e-03

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


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 41.04  E-value: 1.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    9 GRVVLVTGAGAGLGRAYALAFAERGALVVVndlggdfkgVGKGSLAADKVVEEIRRRGG--KAVANYDSVEEGEKV---V 83
Cdd:cd09808   1 GRSFLITGANSGIGKAAALAIAKRGGTVHM---------VCRNQTRAEEARKEIETESGnqNIFLHIVDMSDPKQVwefV 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505   84 KTALDAFGRIDVVVNNAGILRDRSfaRISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIImTSSASGIY------- 156
Cdd:cd09808  72 EEFKEEGKKLHVLINNAGCMVNKR--ELTEDGLEKNFATNTLGTYILTTHLIPVLEKEEDPRVI-TVSSGGMLvqklntn 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505  157 ------GNF-GQANYSAAKLGLLGLANSLAieGRKSNIHCNTIAPN-AGSRMTQTVMPeDLVEALK-----PEYVAPLVL 223
Cdd:cd09808 149 nlqserTAFdGTMVYAQNKRQQVIMTEQWA--KKHPEIHFSVMHPGwADTPAVRNSMP-DFHARFKdrlrsEEQGADTVV 225
                       250
                ....*....|....*...
gi 4504505  224 WLCHESC---EENGGLFE 238
Cdd:cd09808 226 WLALSSAaakAPSGRFYQ 243
PRK08303 PRK08303
short chain dehydrogenase; Provisional
1-99 1.55e-03

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 41.14  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505     1 MGSPLRfdGRVVLVTGAGAGLGRAYALAFAERGALVVVNdlgGDFKGVGKGSLAADKVVEE----IRRRGGKAVA---NY 73
Cdd:PRK08303   2 MMKPLR--GKVALVAGATRGAGRGIAVELGAAGATVYVT---GRSTRARRSEYDRPETIEEtaelVTAAGGRGIAvqvDH 76
                         90       100
                 ....*....|....*....|....*.
gi 4504505    74 DSVEEGEKVVKTALDAFGRIDVVVNN 99
Cdd:PRK08303  77 LVPEQVRALVERIDREQGRLDILVND 102
PRK08862 PRK08862
SDR family oxidoreductase;
11-99 1.94e-03

SDR family oxidoreductase;


Pssm-ID: 236342 [Multi-domain]  Cd Length: 227  Bit Score: 40.48  E-value: 1.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504505    11 VVLVTGAGAGLGRAYALAFAERGALVVVNDlggdfkgvgKGSLAADKVVEEIRRRGGKaVANYDSVEEGEKVVKTALDA- 89
Cdd:PRK08862   7 IILITSAGSVLGRTISCHFARLGATLILCD---------QDQSALKDTYEQCSALTDN-VYSFQLKDFSQESIRHLFDAi 76
                         90
                 ....*....|....
gi 4504505    90 ---FGR-IDVVVNN 99
Cdd:PRK08862  77 eqqFNRaPDVLVNN 90
FkbR2 cd03451
FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved ...
506-576 3.60e-03

FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved family of proteins found in prokaryotes and archaea but not in eukaryotes. FkbR2 has sequence similarity to (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. The function of FkbR2 is unknown.


Pssm-ID: 239535 [Multi-domain]  Cd Length: 146  Bit Score: 38.34  E-value: 3.60e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4504505  506 RLSGDWNPLHIDPNFASLAGFDKPILHGLCTFGfsarrVLQQFADNDVSRfKAI------KARFAKPVYPGQTLQTE 576
Cdd:cd03451  31 LLTMNTAPLHFDAAYAAKTEFGRRLVNSLFTLS-----LALGLSVNDTSL-TAVanlgydEVRFPAPVFHGDTLYAE 101
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
529-599 4.78e-03

The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.


Pssm-ID: 239524 [Multi-domain]  Cd Length: 100  Bit Score: 37.07  E-value: 4.78e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4504505  529 PILHGLCTFGFS----ARRVLQQFADNDVSRFKAIKARFAKPVYPGQTLQTEMW---KEGNRIHFQTKV-QETGDIVIS 599
Cdd:cd03440  16 GIVHGGLLLALAdeaaGAAAARLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEvvrVGRSSVTVEVEVrNEDGKLVAT 94
MaoC_dehydrat_N pfam13452
N-terminal half of MaoC dehydratase; It is clear from the structures of bacterial members of ...
375-445 6.38e-03

N-terminal half of MaoC dehydratase; It is clear from the structures of bacterial members of MaoC dehydratase, pfam01575, that the full-length functional dehydratase enzyme is made up of two structures that dimerize to form a whole. Divergence of the N- and C- monomers in higher eukaryotes has led to two distinct domains, this one and MaoC_dehydratas. However, in order to function as an enzyme both are required together.


Pssm-ID: 433220 [Multi-domain]  Cd Length: 132  Bit Score: 37.67  E-value: 6.38e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4504505    375 PTFGVIIGqksMMGGGLAEIPGlsINFAKVLHGEQYLELYKPLpRAG-KLKCEAVVADVLDK-GSGVVIIMDV 445
Cdd:pfam13452  51 PTFLFVLG---WDAPGFMEQLG--IDLSRLLHGEQRFTYHRPL-RAGdELTCRSQIADVYDKkGNGALCFVVV 117
 
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