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Conserved domains on  [gi|1360496189|gb|PSC04819|]
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UDP-glucose 4-epimerase [Alsobacter soli]

Protein Classification

NAD-dependent epimerase/dehydratase family protein( domain architecture ID 11418686)

NAD-dependent epimerase/dehydratase belonging to the extended (e) short-chain dehydrogenase/reductases (SDR) family uses nucleotide-sugar substrates for a variety of chemical reactions

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
2-237 5.62e-40

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


:

Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 140.11  E-value: 5.62e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   2 KILITGGAGHVGRTLRRELAGRFELVRIFDMVAAE----PIGPNEESVVGDIADIAAVENATRGMDAVIHLAAEPN--EA 75
Cdd:COG0451     1 RILVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGaanlAALPGVEFVRGDLRDPEALAAALAGVDAVVHLAAPAGvgEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  76 PFGIILQANVVGTWNVYEAARRCGAKRVIFGSSNHAVGFYPRsqRINETVPVKPDSRYGLSKCWGEAVAQLYADKYGVKS 155
Cdd:COG0451    81 DPDETLEVNVEGTLNLLEAARAAGVKRFVYASSSSVYGDGEG--PIDEDTPLRPVSPYGASKLAAELLARAYARRYGLPV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189 156 LLLRIGN---------------------AAATPGSARALAIWVSGRDLAQLVTIGLEHPDIHCNVVYGVSNNA------- 207
Cdd:COG0451   159 TILRPGNvygpgdrgvlprlirralagePVPVFGDGDQRRDFIHVDDVARAIVLALEAPAAPGGVYNVGGGEPvtlrela 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1360496189 208 -----------------------ACWYDNSAAYR-LGYKPQDRAEDYTDAAMAA 237
Cdd:COG0451   239 eaiaealgrppeivyparpgdvrPRRADNSKARReLGWRPRTSLEEGLRETVAW 292
 
Name Accession Description Interval E-value
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
2-237 5.62e-40

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 140.11  E-value: 5.62e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   2 KILITGGAGHVGRTLRRELAGRFELVRIFDMVAAE----PIGPNEESVVGDIADIAAVENATRGMDAVIHLAAEPN--EA 75
Cdd:COG0451     1 RILVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGaanlAALPGVEFVRGDLRDPEALAAALAGVDAVVHLAAPAGvgEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  76 PFGIILQANVVGTWNVYEAARRCGAKRVIFGSSNHAVGFYPRsqRINETVPVKPDSRYGLSKCWGEAVAQLYADKYGVKS 155
Cdd:COG0451    81 DPDETLEVNVEGTLNLLEAARAAGVKRFVYASSSSVYGDGEG--PIDEDTPLRPVSPYGASKLAAELLARAYARRYGLPV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189 156 LLLRIGN---------------------AAATPGSARALAIWVSGRDLAQLVTIGLEHPDIHCNVVYGVSNNA------- 207
Cdd:COG0451   159 TILRPGNvygpgdrgvlprlirralagePVPVFGDGDQRRDFIHVDDVARAIVLALEAPAAPGGVYNVGGGEPvtlrela 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1360496189 208 -----------------------ACWYDNSAAYR-LGYKPQDRAEDYTDAAMAA 237
Cdd:COG0451   239 eaiaealgrppeivyparpgdvrPRRADNSKARReLGWRPRTSLEEGLRETVAW 292
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
3-150 2.74e-26

uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, extended (e) SDRs; This subgroup contains proteins of unknown function related to aldehyde reductase and flavonoid reductase of the extended SDR-type. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187539 [Multi-domain]  Cd Length: 318  Bit Score: 104.67  E-value: 2.74e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   3 ILITGGAGHVGRTLRRELAGRFELVRIF---DMVAAEPIGPNEESVVGDIADIAAVENATRGMDAVIHLAAEPNEAP--F 77
Cdd:cd05228     1 ILVTGATGFLGSNLVRALLAQGYRVRALvrsGSDAVLLDGLPVEVVEGDLTDAASLAAAMKGCDRVFHLAAFTSLWAkdR 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1360496189  78 GIILQANVVGTWNVYEAARRCGAKRVIFGSSNHAVGFyPRSQRINETVPVKPDSR---YGLSKCWGEAVAQLYADK 150
Cdd:cd05228    81 KELYRTNVEGTRNVLDAALEAGVRRVVHTSSIAALGG-PPDGRIDETTPWNERPFpndYYRSKLLAELEVLEAAAE 155
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
3-162 4.75e-23

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


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 94.29  E-value: 4.75e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   3 ILITGGAGHVGRTLRRELAGRFELVRIFDM---VAAEPIGPNEESVVGDIADIAAVENATRGM--DAVIHLAAEP----- 72
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIGLDRltsASNTARLADLRFVEGDLTDRDALEKLLADVrpDAVIHLAAVGgvgas 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  73 NEAPfGIILQANVVGTWNVYEAARRCGAKRVIFGSSNHAVGFYPRSQRI--NETVPVKPDSRYGLSKCWGEAVAQLYADK 150
Cdd:pfam01370  81 IEDP-EDFIEANVLGTLNLLEAARKAGVKRFLFASSSEVYGDGAEIPQEetTLTGPLAPNSPYAAAKLAGEWLVLAYAAA 159
                         170
                  ....*....|..
gi 1360496189 151 YGVKSLLLRIGN 162
Cdd:pfam01370 160 YGLRAVILRLFN 171
yfcH TIGR01777
TIGR01777 family protein; This model represents a clade of proteins of unknown function ...
3-208 9.16e-12

TIGR01777 family protein; This model represents a clade of proteins of unknown function including the E. coli yfcH protein. [Hypothetical proteins, Conserved]


Pssm-ID: 273800 [Multi-domain]  Cd Length: 291  Bit Score: 63.81  E-value: 9.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   3 ILITGGAGHVGRTLRRELAGRFELVRIFdmvAAEPIGPNEESVVGDIADIAAVENATRGMDAVIHLAAEP------NEAP 76
Cdd:TIGR01777   1 ILITGGTGFIGRALTQRLTKRGHEVTIL---TRSPPPGANTKWEGYKPWAGEDADSLEGADAVINLAGEPiadkrwTEER 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  77 FGIILQANVVGTWNVYEAARRCGAKRVIFGSSNhAVGFYPRS-QRINETVPVKPDSRY--GLSKCWgEAVAQLyADKYGV 153
Cdd:TIGR01777  78 KQEIRDSRIDTTRLLVEAIAAAEQKPKVFISAS-AVGYYGPSeDREYTEEDSPAGDDFlaELCRDW-EEAAQA-AEDLGT 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1360496189 154 KSLLLRIGNAAATPGSARALAI-------------------WVSGRDLAQLVTIGLEHPDIHcnvvyGVSNNAA 208
Cdd:TIGR01777 155 RVVLLRTGIVLGPKGGALAKMLlpfrlglggplgsgrqwfsWIHIEDLVQLILFALENASVS-----GPVNATA 223
PLN02695 PLN02695
GDP-D-mannose-3',5'-epimerase
1-183 2.20e-11

GDP-D-mannose-3',5'-epimerase


Pssm-ID: 178298 [Multi-domain]  Cd Length: 370  Bit Score: 63.29  E-value: 2.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   1 MKILITGGAGHVGRTLRRELAGRFELVRIFDMVAAEPIgpnEESVVGD---IADIAAVEN---ATRGMDAVIHLAAEPNE 74
Cdd:PLN02695   22 LRICITGAGGFIASHIARRLKAEGHYIIASDWKKNEHM---SEDMFCHefhLVDLRVMENclkVTKGVDHVFNLAADMGG 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  75 APF-----GIILQANVVGTWNVYEAARRCGAKRVIFGSSnhaVGFYPRSQRINETV--------PVKPDSRYGLSKCWGE 141
Cdd:PLN02695   99 MGFiqsnhSVIMYNNTMISFNMLEAARINGVKRFFYASS---ACIYPEFKQLETNVslkesdawPAEPQDAYGLEKLATE 175
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1360496189 142 AVAQLYADKYGVKSLLLRIGNAAATPGSaralaiWVSGRDLA 183
Cdd:PLN02695  176 ELCKHYTKDFGIECRIGRFHNIYGPFGT------WKGGREKA 211
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
4-108 3.28e-04

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: 40.54  E-value: 3.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189    4 LITGGAGHVGRTL----------------RRELAGRFELVRIFDMVAAepiGPNEESVVGDIADIAAVENATRGM----- 62
Cdd:smart00822   4 LITGGLGGLGRALarwlaergarrlvllsRSGPDAPGAAALLAELEAA---GARVTVVACDVADRDALAAVLAAIpaveg 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1360496189   63 --DAVIHLAAEPNEAPFGII--------LQANVVGTWNVYEAARRCGAKRVIFGSS 108
Cdd:smart00822  81 plTGVIHAAGVLDDGVLASLtperfaavLAPKAAGAWNLHELTADLPLDFFVLFSS 136
 
Name Accession Description Interval E-value
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
2-237 5.62e-40

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 140.11  E-value: 5.62e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   2 KILITGGAGHVGRTLRRELAGRFELVRIFDMVAAE----PIGPNEESVVGDIADIAAVENATRGMDAVIHLAAEPN--EA 75
Cdd:COG0451     1 RILVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGaanlAALPGVEFVRGDLRDPEALAAALAGVDAVVHLAAPAGvgEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  76 PFGIILQANVVGTWNVYEAARRCGAKRVIFGSSNHAVGFYPRsqRINETVPVKPDSRYGLSKCWGEAVAQLYADKYGVKS 155
Cdd:COG0451    81 DPDETLEVNVEGTLNLLEAARAAGVKRFVYASSSSVYGDGEG--PIDEDTPLRPVSPYGASKLAAELLARAYARRYGLPV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189 156 LLLRIGN---------------------AAATPGSARALAIWVSGRDLAQLVTIGLEHPDIHCNVVYGVSNNA------- 207
Cdd:COG0451   159 TILRPGNvygpgdrgvlprlirralagePVPVFGDGDQRRDFIHVDDVARAIVLALEAPAAPGGVYNVGGGEPvtlrela 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1360496189 208 -----------------------ACWYDNSAAYR-LGYKPQDRAEDYTDAAMAA 237
Cdd:COG0451   239 eaiaealgrppeivyparpgdvrPRRADNSKARReLGWRPRTSLEEGLRETVAW 292
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
3-150 2.74e-26

uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, extended (e) SDRs; This subgroup contains proteins of unknown function related to aldehyde reductase and flavonoid reductase of the extended SDR-type. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187539 [Multi-domain]  Cd Length: 318  Bit Score: 104.67  E-value: 2.74e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   3 ILITGGAGHVGRTLRRELAGRFELVRIF---DMVAAEPIGPNEESVVGDIADIAAVENATRGMDAVIHLAAEPNEAP--F 77
Cdd:cd05228     1 ILVTGATGFLGSNLVRALLAQGYRVRALvrsGSDAVLLDGLPVEVVEGDLTDAASLAAAMKGCDRVFHLAAFTSLWAkdR 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1360496189  78 GIILQANVVGTWNVYEAARRCGAKRVIFGSSNHAVGFyPRSQRINETVPVKPDSR---YGLSKCWGEAVAQLYADK 150
Cdd:cd05228    81 KELYRTNVEGTRNVLDAALEAGVRRVVHTSSIAALGG-PPDGRIDETTPWNERPFpndYYRSKLLAELEVLEAAAE 155
UDP_G4E_5_SDR_e cd05264
UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially ...
2-163 1.03e-25

UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially conserves the characteristic active site tetrad and NAD-binding motif of the extended SDRs, and has been identified as possible UDP-glucose 4-epimerase (aka UDP-galactose 4-epimerase), a homodimeric member of the extended SDR family. UDP-glucose 4-epimerase catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187574 [Multi-domain]  Cd Length: 300  Bit Score: 102.78  E-value: 1.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   2 KILITGGAGHVGRTLRRELAGRFELVRIFDMVAAEPIGPNE--ESVVGDIADIAAVENATRGMDAVIHLAAE--PNEAPF 77
Cdd:cd05264     1 RVLIVGGNGFIGSHLVDALLEEGPQVRVFDRSIPPYELPLGgvDYIKGDYENRADLESALVGIDTVIHLASTtnPATSNK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  78 GIIL--QANVVGTWNVYEAARRCGAKRVIFGSSNHAVGFYPRSQRINETVPVKPDSRYGLSKCWGEAVAQLYADKYGVKS 155
Cdd:cd05264    81 NPILdiQTNVAPTVQLLEACAAAGIGKIIFASSGGTVYGVPEQLPISESDPTLPISSYGISKLAIEKYLRLYQYLYGLDY 160

                  ....*...
gi 1360496189 156 LLLRIGNA 163
Cdd:cd05264   161 TVLRISNP 168
UDP_AE_SDR_e cd05256
UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains ...
2-162 5.48e-24

UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains UDP-N-acetylglucosamine 4-epimerase of Pseudomonas aeruginosa, WbpP, an extended SDR, that catalyzes the NAD+ dependent conversion of UDP-GlcNAc and UDPGalNA to UDP-Glc and UDP-Gal. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187566 [Multi-domain]  Cd Length: 304  Bit Score: 98.06  E-value: 5.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   2 KILITGGAGHVGRTLRRELAGRFELVRIFDMVAA------EPIGPNEESVVGDIADIAAVENATRGMDAVIHLAAEPN-- 73
Cdd:cd05256     1 RVLVTGGAGFIGSHLVERLLERGHEVIVLDNLSTgkkenlPEVKPNVKFIEGDIRDDELVEFAFEGVDYVFHQAAQASvp 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  74 ---EAPFGIiLQANVVGTWNVYEAARRCGAKRVIFGSSNHAVG---FYPrsqrINETVPVKPDSRYGLSKCWGEAVAQLY 147
Cdd:cd05256    81 rsiEDPIKD-HEVNVLGTLNLLEAARKAGVKRFVYASSSSVYGdppYLP----KDEDHPPNPLSPYAVSKYAGELYCQVF 155
                         170
                  ....*....|....*
gi 1360496189 148 ADKYGVKSLLLRIGN 162
Cdd:cd05256   156 ARLYGLPTVSLRYFN 170
UDP_G4E_2_SDR_e cd05234
UDP-glucose 4 epimerase, subgroup 2, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
3-162 6.33e-24

UDP-glucose 4 epimerase, subgroup 2, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup is comprised of archaeal and bacterial proteins, and has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187545 [Multi-domain]  Cd Length: 305  Bit Score: 97.76  E-value: 6.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   3 ILITGGAGHVGRTLRRELAGRFELVRIFDMVAA--------EPIGPNEESVVGDIADIAAvENATRGMDAVIHLAAEPN- 73
Cdd:cd05234     2 ILVTGGAGFIGSHLVDRLLEEGNEVVVVDNLSSgrreniepEFENKAFRFVKRDLLDTAD-KVAKKDGDTVFHLAANPDv 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  74 ---EAPFGIILQANVVGTWNVYEAARRCGAKRVIFGSSNhAVGFYPRSQRINETVPVKPDSRYGLSKCWGEAVAQLYADK 150
Cdd:cd05234    81 rlgATDPDIDLEENVLATYNVLEAMRANGVKRIVFASSS-TVYGEAKVIPTPEDYPPLPISVYGASKLAAEALISAYAHL 159
                         170
                  ....*....|..
gi 1360496189 151 YGVKSLLLRIGN 162
Cdd:cd05234   160 FGFQAWIFRFAN 171
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
3-162 4.75e-23

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


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 94.29  E-value: 4.75e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   3 ILITGGAGHVGRTLRRELAGRFELVRIFDM---VAAEPIGPNEESVVGDIADIAAVENATRGM--DAVIHLAAEP----- 72
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIGLDRltsASNTARLADLRFVEGDLTDRDALEKLLADVrpDAVIHLAAVGgvgas 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  73 NEAPfGIILQANVVGTWNVYEAARRCGAKRVIFGSSNHAVGFYPRSQRI--NETVPVKPDSRYGLSKCWGEAVAQLYADK 150
Cdd:pfam01370  81 IEDP-EDFIEANVLGTLNLLEAARKAGVKRFLFASSSEVYGDGAEIPQEetTLTGPLAPNSPYAAAKLAGEWLVLAYAAA 159
                         170
                  ....*....|..
gi 1360496189 151 YGVKSLLLRIGN 162
Cdd:pfam01370 160 YGLRAVILRLFN 171
SDR_e cd08946
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ...
3-163 6.04e-22

extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 212494 [Multi-domain]  Cd Length: 200  Bit Score: 90.44  E-value: 6.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   3 ILITGGAGHVGRTLRRELAGRFELVRIFDMvaaepigpneesvvgdiadiaavenatrgMDAVIHLAAEPNEAPFG---- 78
Cdd:cd08946     1 ILVTGGAGFIGSHLVRRLLERGHEVVVIDR-----------------------------LDVVVHLAALVGVPASWdnpd 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  79 IILQANVVGTWNVYEAARRCGAKRVIFGSSNHAvgfYPR--SQRINETVPVKPDSRYGLSKCWGEAVAQLYADKYGVKSL 156
Cdd:cd08946    52 EDFETNVVGTLNLLEAARKAGVKRFVYASSASV---YGSpeGLPEEEETPPRPLSPYGVSKLAAEHLLRSYGESYGLPVV 128

                  ....*..
gi 1360496189 157 LLRIGNA 163
Cdd:cd08946   129 ILRLANV 135
dTDP_GD_SDR_e cd05246
dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4, ...
1-163 4.22e-20

dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4,6-dehydratase and related proteins, members of the extended-SDR family, with the characteristic Rossmann fold core region, active site tetrad and NAD(P)-binding motif. dTDP-D-glucose 4,6-dehydratase is closely related to other sugar epimerases of the SDR family. dTDP-D-dlucose 4,6,-dehydratase catalyzes the second of four steps in the dTDP-L-rhamnose pathway (the dehydration of dTDP-D-glucose to dTDP-4-keto-6-deoxy-D-glucose) in the synthesis of L-rhamnose, a cell wall component of some pathogenic bacteria. In many gram negative bacteria, L-rhamnose is an important constituent of lipopoylsaccharide O-antigen. The larger N-terminal portion of dTDP-D-Glucose 4,6-dehydratase forms a Rossmann fold NAD-binding domain, while the C-terminus binds the sugar substrate. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187557 [Multi-domain]  Cd Length: 315  Bit Score: 87.60  E-value: 4.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   1 MKILITGGAGHVGRTLRRELAGRFELVRI-----------FDMVAAEPIGPNEESVVGDIADIAAVEN--ATRGMDAVIH 67
Cdd:cd05246     1 MKILVTGGAGFIGSNFVRYLLNKYPDYKIinldkltyagnLENLEDVSSSPRYRFVKGDICDAELVDRlfEEEKIDAVIH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  68 LAAEPN-----EAPFGIIlQANVVGTWNVYEAARRCGAKRVIFGSSNHAVGFYPRSQRINETVPVKPDSRYGLSKCWGEA 142
Cdd:cd05246    81 FAAESHvdrsiSDPEPFI-RTNVLGTYTLLEAARKYGVKRFVHISTDEVYGDLLDDGEFTETSPLAPTSPYSASKAAADL 159
                         170       180
                  ....*....|....*....|.
gi 1360496189 143 VAQLYADKYGVKSLLLRIGNA 163
Cdd:cd05246   160 LVRAYHRTYGLPVVITRCSNN 180
Gne_like_SDR_e cd05238
Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; ...
1-174 9.14e-20

Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; Nucleoside-diphosphate-sugar 4-epimerase has the characteristic active site tetrad and NAD-binding motif of the extended SDR, and is related to more specifically defined epimerases such as UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), which catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup includes Escherichia coli 055:H7 Gne, a UDP-GlcNAc 4-epimerase, essential for O55 antigen synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187549 [Multi-domain]  Cd Length: 305  Bit Score: 86.67  E-value: 9.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   1 MKILITGGAGHVGRTLRRELAGRFELVRIFDMVAAEPIGPNEES----VVGDIADIAAVENATRG-MDAVIHLAA---EP 72
Cdd:cd05238     1 MKVLITGASGFVGQRLAERLLSDVPNERLILIDVVSPKAPSGAPrvtqIAGDLAVPALIEALANGrPDVVFHLAAivsGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  73 NEAPFGIILQANVVGTWNVYEAARRCGAK-RVIFGSSNHAVGFYPRSQRINETvPVKPDSRYGLSKCWGEAVAQLYADKY 151
Cdd:cd05238    81 AEADFDLGYRVNVDGTRNLLEALRKNGPKpRFVFTSSLAVYGLPLPNPVTDHT-ALDPASSYGAQKAMCELLLNDYSRRG 159
                         170       180
                  ....*....|....*....|...
gi 1360496189 152 GVKSLLLRIGNAAATPGSARALA 174
Cdd:cd05238   160 FVDGRTLRLPTVCVRPGRPNKAA 182
GalE COG1087
UDP-glucose 4-epimerase [Cell wall/membrane/envelope biogenesis];
1-164 1.27e-19

UDP-glucose 4-epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440704 [Multi-domain]  Cd Length: 328  Bit Score: 86.61  E-value: 1.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   1 MKILITGGAGHVGRTLRRELAGRFELVRIFDMVA---AEPIGPNEESVVGDIADIAAVEN--ATRGMDAVIHLAA----- 70
Cdd:COG1087     1 MKILVTGGAGYIGSHTVVALLEAGHEVVVLDNLSnghREAVPKGVPFVEGDLRDRAALDRvfAEHDIDAVIHFAAlkavg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  71 EPNEAPfgiiL---QANVVGTWNVYEAARRCGAKRVIFgSSNHAVgfY--PRSQRINETVPVKPDSRYGLSKCWGEAVAQ 145
Cdd:COG1087    81 ESVEKP----LkyyRNNVVGTLNLLEAMREAGVKRFVF-SSSAAV--YgePESVPITEDAPTNPTNPYGRSKLMVEQILR 153
                         170
                  ....*....|....*....
gi 1360496189 146 LYADKYGVKSLLLRIGNAA 164
Cdd:COG1087   154 DLARAYGLRYVALRYFNPA 172
RfbB COG1088
dTDP-D-glucose 4,6-dehydratase [Cell wall/membrane/envelope biogenesis];
1-162 1.69e-19

dTDP-D-glucose 4,6-dehydratase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440705 [Multi-domain]  Cd Length: 333  Bit Score: 86.29  E-value: 1.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   1 MKILITGGAGHVGRTLRRELAGRFELVRI--FD--MVAAepigpNEES------------VVGDIADIAAVEN--ATRGM 62
Cdd:COG1088     2 MRILVTGGAGFIGSNFVRYLLAKYPGAEVvvLDklTYAG-----NLENladleddpryrfVKGDIRDRELVDElfAEHGP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  63 DAVIHLAAEP-------NEAPFgiiLQANVVGTWNVYEAARRCG--AKRVIFGSSNHAVGFYPRSQRINETVPVKPDSRY 133
Cdd:COG1088    77 DAVVHFAAEShvdrsidDPAAF---VETNVVGTFNLLEAARKYWveGFRFHHVSTDEVYGSLGEDGPFTETTPLDPSSPY 153
                         170       180
                  ....*....|....*....|....*....
gi 1360496189 134 GLSKCWGEAVAQLYADKYGVKSLLLRIGN 162
Cdd:COG1088   154 SASKAASDHLVRAYHRTYGLPVVITRCSN 182
CDP_TE_SDR_e cd05258
CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that ...
1-161 7.38e-19

CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that catalyzes the conversion of CDP-D-paratose to CDP-D-tyvelose, the last step in tyvelose biosynthesis. This subgroup is a member of the extended SDR subfamily, with a characteristic active site tetrad and NAD-binding motif. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187568 [Multi-domain]  Cd Length: 337  Bit Score: 84.65  E-value: 7.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   1 MKILITGGAGHVGRTLRRELAGRFELVRIFD------------MVAAEPIGPNEESVVGDIADIAAVENATRGMDAVIHL 68
Cdd:cd05258     1 MRVLITGGAGFIGSNLARFFLKQGWEVIGFDnlmrrgsfgnlaWLKANREDGGVRFVHGDIRNRNDLEDLFEDIDLIIHT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  69 AAEPN-----EAPFgIILQANVVGTWNVYEAARR-CGAKRVIFGSSNHAVGFYP-------RSQR------------INE 123
Cdd:cd05258    81 AAQPSvttsaSSPR-LDFETNALGTLNVLEAARQhAPNAPFIFTSTNKVYGDLPnylpleeLETRyelapegwspagISE 159
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1360496189 124 TVPVKPD-SRYGLSKCWGEAVAQLYADKYGVKSLLLRIG 161
Cdd:cd05258   160 SFPLDFShSLYGASKGAADQYVQEYGRIFGLKTVVFRCG 198
UDP_G4E_4_SDR_e cd05232
UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
2-159 2.61e-18

UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup is comprised of bacterial proteins, and includes the Staphylococcus aureus capsular polysaccharide Cap5N, which may have a role in the synthesis of UDP-N-acetyl-d-fucosamine. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187543 [Multi-domain]  Cd Length: 303  Bit Score: 82.40  E-value: 2.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   2 KILITGGAGHVGRTLRRELAGRFELVRIfdMV-AAEPIGPNEesVVGDIADIAAVENATRGMDAVIHLAA------EPNE 74
Cdd:cd05232     1 KVLVTGANGFIGRALVDKLLSRGEEVRI--AVrNAENAEPSV--VLAELPDIDSFTDLFLGVDAVVHLAArvhvmnDQGA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  75 APFGIILQANVVGTWNVYEAARRCGAKRVIFGSSNHAVGFYPRSQRINETVPVKPDSRYGLSKCWGE-AVAQLYADkYGV 153
Cdd:cd05232    77 DPLSDYRKVNTELTRRLARAAARQGVKRFVFLSSVKVNGEGTVGAPFDETDPPAPQDAYGRSKLEAErALLELGAS-DGM 155

                  ....*.
gi 1360496189 154 KSLLLR 159
Cdd:cd05232   156 EVVILR 161
3Beta_HSD pfam01073
3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid ...
4-142 6.61e-18

3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid dehydrogenase/5-ene-4-ene isomerase (3 beta-HSD) catalyzes the oxidation and isomerization of 5-ene-3 beta-hydroxypregnene and 5-ene-hydroxyandrostene steroid precursors into the corresponding 4-ene-ketosteroids necessary for the formation of all classes of steroid hormones.


Pssm-ID: 366449 [Multi-domain]  Cd Length: 279  Bit Score: 80.87  E-value: 6.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   4 LITGGAGHVGRTLRREL--AGRFELVRIFDMVAAEPIGPNEESV------VGDIADIAAVENATRGMDAVIHLAAEPN-- 73
Cdd:pfam01073   1 VVTGGGGFLGRHIIKLLvrEGELKEVRVFDLRESPELLEDFSKSnvikyiQGDVTDKDDLDNALEGVDVVIHTASAVDvf 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1360496189  74 -EAPFGIILQANVVGTWNVYEAARRCGAKRVIFGSSNHAVGFYPRSQRI---NETVPV--KPDSRYGLSKCWGEA 142
Cdd:pfam01073  81 gKYTFDEIMKVNVKGTQNVLEACVKAGVRVLVYTSSAEVVGPNSYGQPIlngDEETPYesTHQDAYPRSKAIAEK 155
UDP_G4E_3_SDR_e cd05240
UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs; Members of this bacterial ...
3-134 8.17e-17

UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs; Members of this bacterial subgroup are identified as possible sugar epimerases, such as UDP-glucose 4 epimerase. However, while the NAD(P)-binding motif is fairly well conserved, not all members retain the canonical active site tetrad of the extended SDRs. UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187551 [Multi-domain]  Cd Length: 306  Bit Score: 78.56  E-value: 8.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   3 ILITGGAGHVGRTLRRELAG--RFELVRIFDMVAAEPIGPNEESVVGDIADIAAVENAT-RGMDAVIHLAA--EPNEAPf 77
Cdd:cd05240     1 ILVTGAAGGLGRLLARRLAAspRVIGVDGLDRRRPPGSPPKVEYVRLDIRDPAAADVFReREADAVVHLAFilDPPRDG- 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  78 GIILQANVVGTWNVYEAARRCGAKRVIFGSSNHAVGFYPRSQ-RINETVPVK--PDSRYG 134
Cdd:cd05240    80 AERHRINVDGTQNVLDACAAAGVPRVVVTSSVAVYGAHPDNPaPLTEDAPLRgsPEFAYS 139
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
3-169 1.18e-16

UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; UDP-Glcnac inverting 4,6-dehydratase was identified in Helicobacter pylori as the hexameric flaA1 gene product (FlaA1). FlaA1 is hexameric, possesses UDP-GlcNAc-inverting 4,6-dehydratase activity, and catalyzes the first step in the creation of a pseudaminic acid derivative in protein glycosylation. Although this subgroup has the NADP-binding motif characteristic of extended SDRs, its members tend to have a Met substituted for the active site Tyr found in most SDR families. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187548 [Multi-domain]  Cd Length: 287  Bit Score: 77.66  E-value: 1.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   3 ILITGGAGHVGRTLRRELAgRF--ELVRIFDM-----------VAAEPIGPNEESVVGDIADIAAVENA--TRGMDAVIH 67
Cdd:cd05237     5 ILVTGGAGSIGSELVRQIL-KFgpKKLIVFDRdenklhelvreLRSRFPHDKLRFIIGDVRDKERLRRAfkERGPDIVFH 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  68 LAA---------EPNEApfgiiLQANVVGTWNVYEAARRCGAKRVIFGSSNHAvgfyprsqrinetvpVKPDSRYGLSKC 138
Cdd:cd05237    84 AAAlkhvpsmedNPEEA-----IKTNVLGTKNVIDAAIENGVEKFVCISTDKA---------------VNPVNVMGATKR 143
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1360496189 139 WGEAVAQLYADKYG-VKSLLLRIGNAAATPGS 169
Cdd:cd05237   144 VAEKLLLAKNEYSSsTKFSTVRFGNVLGSRGS 175
GME-like_SDR_e cd05273
Arabidopsis thaliana GDP-mannose-3',5'-epimerase (GME)-like, extended (e) SDRs; This subgroup ...
2-163 8.93e-16

Arabidopsis thaliana GDP-mannose-3',5'-epimerase (GME)-like, extended (e) SDRs; This subgroup of NDP-sugar epimerase/dehydratases are extended SDRs; they have the characteristic active site tetrad, and an NAD-binding motif: TGXXGXX[AG], which is a close match to the canonical NAD-binding motif. Members include Arabidopsis thaliana GDP-mannose-3',5'-epimerase (GME) which catalyzes the epimerization of two positions of GDP-alpha-D-mannose to form GDP-beta-L-galactose. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187581 [Multi-domain]  Cd Length: 328  Bit Score: 75.59  E-value: 8.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   2 KILITGGAGHVGRTLRRELAGRFELVRIFDMVAAE---PIGPNEESVVGDIADIAAVENATRGMDAVIHLAAEPNEAPF- 77
Cdd:cd05273     2 RALVTGAGGFIGSHLAERLKAEGHYVRGADWKSPEhmtQPTDDDEFHLVDLREMENCLKATEGVDHVFHLAADMGGMGYi 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  78 ----GIILQANVVGTWNVYEAARRCGAKRVIFGSSnhaVGFYPRSQRINETV---------PVKPDSRYGLSKCWGEAVA 144
Cdd:cd05273    82 qsnhAVIMYNNTLINFNMLEAARINGVERFLFASS---ACVYPEFKQLETTVvrlreedawPAEPQDAYGWEKLATERLC 158
                         170
                  ....*....|....*....
gi 1360496189 145 QLYADKYGVKSLLLRIGNA 163
Cdd:cd05273   159 QHYNEDYGIETRIVRFHNI 177
3b-HSD-like_SDR_e cd05241
3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family ...
3-141 1.06e-15

3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family domains belonging to this subgroup have the characteristic active site tetrad and a fairly well-conserved NAD(P)-binding motif. 3b-HSD catalyzes the NAD-dependent conversion of various steroids, such as pregnenolone to progesterone, or androstenediol to testosterone. This subgroup includes an unusual bifunctional 3b-HSD/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. It also includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7]. C(27) 3beta-HSD/HSD3B7 is a membrane-bound enzyme of the endoplasmic reticulum, that catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human NSDHL (NAD(P)H steroid dehydrogenase-like protein) cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187552 [Multi-domain]  Cd Length: 331  Bit Score: 75.55  E-value: 1.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   3 ILITGGAGHVGRTLRRELAGRF-ELVRIFDMV-AAEPIG----PNEESVVGDIADIAAVENATRGMDAVIHLAAE-PNEA 75
Cdd:cd05241     2 VLVTGGSGFFGERLVKQLLERGgTYVRSFDIApPGEALSawqhPNIEFLKGDITDRNDVEQALSGADCVFHTAAIvPLAG 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1360496189  76 PFGIILQANVVGTWNVYEAARRCGAKRVIFGSSNHAVGfypRSQRI---NETVPVKPDSR--YGLSKCWGE 141
Cdd:cd05241    82 PRDLYWEVNVGGTQNVLDACQRCGVQKFVYTSSSSVIF---GGQNIhngDETLPYPPLDSdmYAETKAIAE 149
Arna_like_SDR_e cd05257
Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme ...
2-174 1.49e-15

Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme involved in the modification of outer membrane protein lipid A of gram-negative bacteria. It is a bifunctional enzyme that catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid and N-10-formyltetrahydrofolate-dependent formylation of UDP-4-amino-4-deoxy-l-arabinose; its NAD-dependent decaboxylating activity is in the C-terminal 360 residues. This subgroup belongs to the extended SDR family, however the NAD binding motif is not a perfect match and the upstream Asn of the canonical active site tetrad is not conserved. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187567 [Multi-domain]  Cd Length: 316  Bit Score: 75.03  E-value: 1.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   2 KILITGGAGHVGRTLRRELAGRFELVRIFDMVA--------AEPIGPNEESVVGDIADIAAVENATRGMDAVIHLAA--- 70
Cdd:cd05257     1 NVLVTGADGFIGSHLTERLLREGHEVRALDIYNsfnswgllDNAVHDRFHFISGDVRDASEVEYLVKKCDVVFHLAAlia 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  71 --EPNEAPFGIILqANVVGTWNVYEAARRCGAKRVIFGSSN----HAVGFYprsqrINETVPV----KPDSRYGLSKCWG 140
Cdd:cd05257    81 ipYSYTAPLSYVE-TNVFGTLNVLEAACVLYRKRVVHTSTSevygTAQDVP-----IDEDHPLlyinKPRSPYSASKQGA 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1360496189 141 EAVAQLYADKYGVKSLLLR----IG------NAAATPGSARALA 174
Cdd:cd05257   155 DRLAYSYGRSFGLPVTIIRpfntYGprqsarAVIPTIISQRAIG 198
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
3-175 2.45e-14

Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases (SDRs, aka tyrosine-dependent oxidoreductases) are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187537 [Multi-domain]  Cd Length: 176  Bit Score: 69.35  E-value: 2.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   3 ILITGGAGHVGRTLRRELAGRFELVRIFD---MVAAEPIGPNEESVVGDIADIAAVENATRGMDAVIHLAAEPNEAPFGI 79
Cdd:cd05226     1 ILILGATGFIGRALARELLEQGHEVTLLVrntKRLSKEDQEPVAVVEGDLRDLDSLSDAVQGVDVVIHLAGAPRDTRDFC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  80 ilQANVVGTWNVYEAARRCGAKRVIFGSSnhaVGFYPRSqriNETVPVKPDSRYGLSKCWGEAVAQlyadKYGVKSLLLR 159
Cdd:cd05226    81 --EVDVEGTRNVLEAAKEAGVKHFIFISS---LGAYGDL---HEETEPSPSSPYLAVKAKTEAVLR----EASLPYTIVR 148
                         170
                  ....*....|....*.
gi 1360496189 160 IGNAAATPGSARALAI 175
Cdd:cd05226   149 PGVIYGDLARAIANAV 164
Polysacc_synt_2 pfam02719
Polysaccharide biosynthesis protein; This is a family of diverse bacterial polysaccharide ...
3-169 8.63e-14

Polysaccharide biosynthesis protein; This is a family of diverse bacterial polysaccharide biosynthesis proteins including the CapD protein, WalL protein mannosyl-transferase and several putative epimerases (e.g. WbiI).


Pssm-ID: 426938 [Multi-domain]  Cd Length: 284  Bit Score: 69.47  E-value: 8.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   3 ILITGGAGHVGRTL-RRELAGRFELVRIFD---------------MVAAEPIGPNEESVVGDIADIAAVENA--TRGMDA 64
Cdd:pfam02719   1 VLVTGGGGSIGSELcRQILKFNPKKIILFSrdelklyeirqelreKFNDPKLRFFIVPVIGDVRDRERLERAmeQYGVDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  65 VIHLAA-------E--PNEApfgiiLQANVVGTWNVYEAARRCGAKRVIFGSSNHAvgfyprsqrinetvpVKPDSRYGL 135
Cdd:pfam02719  81 VFHAAAykhvplvEynPMEA-----IKTNVLGTENVADAAIEAGVKKFVLISTDKA---------------VNPTNVMGA 140
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1360496189 136 SKCWGEAVAQLYADKYGVKSLLL---RIGNAAATPGS 169
Cdd:pfam02719 141 TKRLAEKLFQAANRESGSGGTRFsvvRFGNVLGSRGS 177
UDP_GE_SDE_e cd05253
UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid ...
1-159 8.87e-14

UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid 4-epimerase, an extended SDR, which catalyzes the conversion of UDP-alpha-D-glucuronic acid to UDP-alpha-D-galacturonic acid. This group has the SDR's canonical catalytic tetrad and the TGxxGxxG NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187563 [Multi-domain]  Cd Length: 332  Bit Score: 70.06  E-value: 8.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   1 MKILITGGAGHVGRTLRRELAGRFELVRIFDMV-------------AAEPIGPNEESVVGDIADIAAVEN--ATRGMDAV 65
Cdd:cd05253     1 MKILVTGAAGFIGFHVAKRLLERGDEVVGIDNLndyydvrlkearlELLGKSGGFKFVKGDLEDREALRRlfKDHEFDAV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  66 IHLAAEPN-----EAPFgIILQANVVGTWNVYEAARRCGAKRVIFGSSNHAVGfyprsqrINETVPVK-------PDSRY 133
Cdd:cd05253    81 IHLAAQAGvryslENPH-AYVDSNIVGFLNLLELCRHFGVKHLVYASSSSVYG-------LNTKMPFSeddrvdhPISLY 152
                         170       180
                  ....*....|....*....|....*.
gi 1360496189 134 GLSKCWGEAVAQLYADKYGVKSLLLR 159
Cdd:cd05253   153 AATKKANELMAHTYSHLYGIPTTGLR 178
UDP_G4E_1_SDR_e cd05247
UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
2-164 1.34e-13

UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187558 [Multi-domain]  Cd Length: 323  Bit Score: 69.49  E-value: 1.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   2 KILITGGAGHVGRTLRRELAGRFELVRIFD---------MVAAEPIGPneESVVGDIADIAAVEN--ATRGMDAVIHLAA 70
Cdd:cd05247     1 KVLVTGGAGYIGSHTVVELLEAGYDVVVLDnlsnghreaLPRIEKIRI--EFYEGDIRDRAALDKvfAEHKIDAVIHFAA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  71 -----EPNEAPfgiiL---QANVVGTWNVYEAARRCGAKRVIFgSSNHAVGFYPRSQRINETVPVKPDSRYGLSKCWGEA 142
Cdd:cd05247    79 lkavgESVQKP----LkyyDNNVVGTLNLLEAMRAHGVKNFVF-SSSAAVYGEPETVPITEEAPLNPTNPYGRTKLMVEQ 153
                         170       180
                  ....*....|....*....|..
gi 1360496189 143 VAQLYADKYGVKSLLLRIGNAA 164
Cdd:cd05247   154 ILRDLAKAPGLNYVILRYFNPA 175
MupV_like_SDR_e cd05263
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family ...
3-151 2.50e-13

Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family domains have the characteristic active site tetrad and a well-conserved NAD(P)-binding motif. This subgroup is not well characterized, its members are annotated as having a variety of putative functions. One characterized member is Pseudomonas fluorescens MupV a protein involved in the biosynthesis of Mupirocin, a polyketide-derived antibiotic. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187573 [Multi-domain]  Cd Length: 293  Bit Score: 68.16  E-value: 2.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   3 ILITGGAGHVGRTLRRELA-----------GRFELVRIFDMVAAEPIGPNEESVVGDIA------DIAAVENATRGMDAV 65
Cdd:cd05263     1 VFVTGGTGFLGRHLVKRLLengfkvlvlvrSESLGEAHERIEEAGLEADRVRVLEGDLTqpnlglSAAASRELAGKVDHV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  66 IHLAAEPN-EAPFGIILQANVVGTWNVYEAARRCGAKRVIFGSSNHAVGfyPRSQRINETVPVKPDSR---YGLSKCWGE 141
Cdd:cd05263    81 IHCAASYDfQAPNEDAWRTNIDGTEHVLELAARLDIQRFHYVSTAYVAG--NREGNIRETELNPGQNFknpYEQSKAEAE 158
                         170
                  ....*....|
gi 1360496189 142 AVAQLYADKY 151
Cdd:cd05263   159 QLVRAAATQI 168
WbmH_like_SDR_e cd08957
Bordetella bronchiseptica enzymes WbmH and WbmG-like, extended (e) SDRs; Bordetella ...
1-163 2.65e-13

Bordetella bronchiseptica enzymes WbmH and WbmG-like, extended (e) SDRs; Bordetella bronchiseptica enzymes WbmH and WbmG, and related proteins. This subgroup exhibits the active site tetrad and NAD-binding motif of the extended SDR family. It has been proposed that the active site in Bordetella WbmG and WbmH cannot function as an epimerase, and that it plays a role in O-antigen synthesis pathway from UDP-2,3-diacetamido-2,3-dideoxy-l-galacturonic acid. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187660 [Multi-domain]  Cd Length: 307  Bit Score: 68.30  E-value: 2.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   1 MKILITGGAGHVGRTLRRELAGRFELVRIFDMVAAE-----PIGPNEESVVGDIADIAAVENATRGM--DAVIHLAA--- 70
Cdd:cd08957     1 MKVLITGGAGQIGSHLIEHLLERGHQVVVIDNFATGrrehlPDHPNLTVVEGSIADKALVDKLFGDFkpDAVVHTAAayk 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  71 EP----NEApfgiilQANVVGTWNVYEAARRCGAKRVIFGSSNHAVGFYPRSQRINETVPV-KPDSRYGLSKCWGEAvaq 145
Cdd:cd08957    81 DPddwyEDT------LTNVVGGANVVQAAKKAGVKRLIYFQTALCYGLKPMQQPIRLDHPRaPPGSSYAISKTAGEY--- 151
                         170
                  ....*....|....*...
gi 1360496189 146 lYADKYGVKSLLLRIGNA 163
Cdd:cd08957   152 -YLELSGVDFVTFRLANV 168
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
2-111 5.98e-13

Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 66.02  E-value: 5.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   2 KILITGGAGHVGRTLRRELAGRFELVRIfdMV-----AAEPIGPNEESVVGDIADIAAVENATRGMDAVIHLAAEPNEAP 76
Cdd:COG0702     1 KILVTGATGFIGRRVVRALLARGHPVRA--LVrdpekAAALAAAGVEVVQGDLDDPESLAAALAGVDAVFLLVPSGPGGD 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1360496189  77 FGIILQANVvgtwNVYEAARRCGAKRVIFGSSNHA 111
Cdd:COG0702    79 FAVDVEGAR----NLADAAKAAGVKRIVYLSALGA 109
3b-HSD-NSDHL-like_SDR_e cd09813
human NSDHL (NAD(P)H steroid dehydrogenase-like protein)-like, extended (e) SDRs; This ...
4-142 1.06e-12

human NSDHL (NAD(P)H steroid dehydrogenase-like protein)-like, extended (e) SDRs; This subgroup includes human NSDHL and related proteins. These proteins have the characteristic active site tetrad of extended SDRs, and also have a close match to their NAD(P)-binding motif. Human NSDHL is a 3beta-hydroxysteroid dehydrogenase (3 beta-HSD) which functions in the cholesterol biosynthetic pathway. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. Mutations in the gene encoding NSDHL cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. This subgroup also includes an unusual bifunctional [3beta-hydroxysteroid dehydrogenase (3b-HSD)/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187673 [Multi-domain]  Cd Length: 335  Bit Score: 67.00  E-value: 1.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   4 LITGGAGHVGRTLRRELAGRFEL-VRIFDMVAAEPIGPNEESVV----GDIADIAAVENA--TRGMDAVIHLAAEPNEAP 76
Cdd:cd09813     3 LVVGGSGFLGRHLVEQLLRRGNPtVHVFDIRPTFELDPSSSGRVqfhtGDLTDPQDLEKAfnEKGPNVVFHTASPDHGSN 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  77 FGIILQANVVGTWNVYEAARRCGAKRVIFGSSNHAVgfYPRSQRIN--ETVPV--KPDSRYGLSKCWGEA 142
Cdd:cd09813    83 DDLYYKVNVQGTRNVIEACRKCGVKKLVYTSSASVV--FNGQDIINgdESLPYpdKHQDAYNETKALAEK 150
RfbD COG1091
dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];
2-160 6.46e-12

dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440708 [Multi-domain]  Cd Length: 279  Bit Score: 64.00  E-value: 6.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   2 KILITGGAGHVGRTLRRELAGRfelvrifdmvAAEPIGPNEESVvgDIADIAAVENATRGM--DAVIHLAA--------- 70
Cdd:COG1091     1 RILVTGANGQLGRALVRLLAER----------GYEVVALDRSEL--DITDPEAVAALLEEVrpDVVINAAAytavdkaes 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  71 EPNEApfgiiLQANVVGTWNVYEAARRCGAkRVIF--------GSSNHAvgfYprsqriNETVPVKPDSRYGLSKCWGEA 142
Cdd:COG1091    69 EPELA-----YAVNATGPANLAEACAELGA-RLIHistdyvfdGTKGTP---Y------TEDDPPNPLNVYGRSKLAGEQ 133
                         170
                  ....*....|....*...
gi 1360496189 143 VAQLYADKYgvksLLLRI 160
Cdd:COG1091   134 AVRAAGPRH----LILRT 147
GDP_MD_SDR_e cd05260
GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, ...
2-162 6.65e-12

GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, catalyzes the NADP(H)-dependent conversion of GDP-(D)-mannose to GDP-4-keto, 6-deoxy-(D)-mannose in the fucose biosynthesis pathway. These proteins have the canonical active site triad and NAD-binding pattern, however the active site Asn is often missing and may be substituted with Asp. A Glu residue has been identified as an important active site base. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187570 [Multi-domain]  Cd Length: 316  Bit Score: 64.54  E-value: 6.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   2 KILITGGAGHVGRTLRRELAGR----FELVR---IFDMVAAEPIGPNEESVV---GDIADIAAVENATRGM--DAVIHLA 69
Cdd:cd05260     1 RALITGITGQDGSYLAEFLLEKgyevHGIVRrssSFNTDRIDHLYINKDRITlhyGDLTDSSSLRRAIEKVrpDEIYHLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  70 AE---------PNEApfgiiLQANVVGTWNVYEAARRCGAK-RVIFGSSNHAVGFYPRSqRINETVPVKPDSRYGLSKCW 139
Cdd:cd05260    81 AQshvkvsfddPEYT-----AEVNAVGTLNLLEAIRILGLDaRFYQASSSEEYGKVQEL-PQSETTPFRPRSPYAVSKLY 154
                         170       180
                  ....*....|....*....|...
gi 1360496189 140 GEAVAQLYADKYGVKSLLLRIGN 162
Cdd:cd05260   155 ADWITRNYREAYGLFAVNGRLFN 177
yfcH TIGR01777
TIGR01777 family protein; This model represents a clade of proteins of unknown function ...
3-208 9.16e-12

TIGR01777 family protein; This model represents a clade of proteins of unknown function including the E. coli yfcH protein. [Hypothetical proteins, Conserved]


Pssm-ID: 273800 [Multi-domain]  Cd Length: 291  Bit Score: 63.81  E-value: 9.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   3 ILITGGAGHVGRTLRRELAGRFELVRIFdmvAAEPIGPNEESVVGDIADIAAVENATRGMDAVIHLAAEP------NEAP 76
Cdd:TIGR01777   1 ILITGGTGFIGRALTQRLTKRGHEVTIL---TRSPPPGANTKWEGYKPWAGEDADSLEGADAVINLAGEPiadkrwTEER 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  77 FGIILQANVVGTWNVYEAARRCGAKRVIFGSSNhAVGFYPRS-QRINETVPVKPDSRY--GLSKCWgEAVAQLyADKYGV 153
Cdd:TIGR01777  78 KQEIRDSRIDTTRLLVEAIAAAEQKPKVFISAS-AVGYYGPSeDREYTEEDSPAGDDFlaELCRDW-EEAAQA-AEDLGT 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1360496189 154 KSLLLRIGNAAATPGSARALAI-------------------WVSGRDLAQLVTIGLEHPDIHcnvvyGVSNNAA 208
Cdd:TIGR01777 155 RVVLLRTGIVLGPKGGALAKMLlpfrlglggplgsgrqwfsWIHIEDLVQLILFALENASVS-----GPVNATA 223
SDR_a3 cd05229
atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a ...
2-192 1.46e-11

atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a glycine-rich NAD(P)-binding motif consensus that is very similar to the extended SDRs, GXXGXXG. Generally, this group has poor conservation of the active site tetrad, However, individual sequences do contain matches to the YXXXK active site motif, and generally Tyr or Asn in place of the upstream Ser found in most SDRs. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187540 [Multi-domain]  Cd Length: 302  Bit Score: 63.50  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   2 KILITGGAGHVGRTLRRELAGRFELVRIFDMVAAEPIG-PNEESVVGDIADIAAVENATRGMDAVIHLA--AEPNEAPFG 78
Cdd:cd05229     1 TAHVLGASGPIGREVARELRRRGWDVRLVSRSGSKLAWlPGVEIVAADAMDASSVIAAARGADVIYHCAnpAYTRWEELF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  79 IILQANVVgtwnvyEAARRCGAKRVIFGSsnhaVGFY--PRSQRINETVPVKPDSRYGLSKCWGEAVAQLYADKYGVKSL 156
Cdd:cd05229    81 PPLMENVV------AAAEANGAKLVLPGN----VYMYgpQAGSPITEDTPFQPTTRKGRIRAEMEERLLAAHAKGDIRAL 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1360496189 157 LLR----IGNAAATPGSARALAIWVSGRDLAQLVTIGLEH 192
Cdd:cd05229   151 IVRapdfYGPGAINSWLGAALFAILQGKTAVFPGNLDTPH 190
PLN02695 PLN02695
GDP-D-mannose-3',5'-epimerase
1-183 2.20e-11

GDP-D-mannose-3',5'-epimerase


Pssm-ID: 178298 [Multi-domain]  Cd Length: 370  Bit Score: 63.29  E-value: 2.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   1 MKILITGGAGHVGRTLRRELAGRFELVRIFDMVAAEPIgpnEESVVGD---IADIAAVEN---ATRGMDAVIHLAAEPNE 74
Cdd:PLN02695   22 LRICITGAGGFIASHIARRLKAEGHYIIASDWKKNEHM---SEDMFCHefhLVDLRVMENclkVTKGVDHVFNLAADMGG 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  75 APF-----GIILQANVVGTWNVYEAARRCGAKRVIFGSSnhaVGFYPRSQRINETV--------PVKPDSRYGLSKCWGE 141
Cdd:PLN02695   99 MGFiqsnhSVIMYNNTMISFNMLEAARINGVKRFFYASS---ACIYPEFKQLETNVslkesdawPAEPQDAYGLEKLATE 175
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1360496189 142 AVAQLYADKYGVKSLLLRIGNAAATPGSaralaiWVSGRDLA 183
Cdd:PLN02695  176 ELCKHYTKDFGIECRIGRFHNIYGPFGT------WKGGREKA 211
GDP_Man_Dehyd pfam16363
GDP-mannose 4,6 dehydratase;
4-162 1.09e-10

GDP-mannose 4,6 dehydratase;


Pssm-ID: 465104 [Multi-domain]  Cd Length: 327  Bit Score: 61.02  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   4 LITGGAGHVGRTLRRELAGR-------------FELVRIfDMVAAEPIGPNEESVVGDIADIAAVENATRGM--DAVIHL 68
Cdd:pfam16363   1 LITGITGQDGSYLAELLLEKgyevhgivrrsssFNTGRL-EHLYDDHLNGNLVLHYGDLTDSSNLVRLLAEVqpDEIYNL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  69 AAE---------PNEApfgiiLQANVVGTWNVYEAARRCG---AKRVIFGSSNHavgFYPRSQR--INETVPVKPDSRYG 134
Cdd:pfam16363  80 AAQshvdvsfeqPEYT-----ADTNVLGTLRLLEAIRSLGlekKVRFYQASTSE---VYGKVQEvpQTETTPFYPRSPYA 151
                         170       180
                  ....*....|....*....|....*...
gi 1360496189 135 LSKCWGEAVAQLYADKYGVKSLLLRIGN 162
Cdd:pfam16363 152 AAKLYADWIVVNYRESYGLFACNGILFN 179
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
2-160 1.16e-10

dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; dTDP-6-deoxy-L-lyxo-4-hexulose reductase, an extended SDR, synthesizes dTDP-L-rhamnose from alpha-D-glucose-1-phosphate, providing the precursor of L-rhamnose, an essential cell wall component of many pathogenic bacteria. This subgroup has the characteristic active site tetrad and NADP-binding motif. This subgroup also contains human MAT2B, the regulatory subunit of methionine adenosyltransferase (MAT); MAT catalyzes S-adenosylmethionine synthesis. The human gene encoding MAT2B encodes two major splicing variants which are induced in human cell liver cancer and regulate HuR, an mRNA-binding protein which stabilizes the mRNA of several cyclins, to affect cell proliferation. Both MAT2B variants include this extended SDR domain. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187564 [Multi-domain]  Cd Length: 280  Bit Score: 60.33  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   2 KILITGGAGHVGRTLRRELAGR-FELVRIfdmvaaepIGPNEESVVGDIADIAAVENATRGM--DAVIHLAA-------- 70
Cdd:cd05254     1 KILITGATGMLGRALVRLLKERgYEVIGT--------GRSRASLFKLDLTDPDAVEEAIRDYkpDVIINCAAytrvdkce 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  71 -EPNEApfgiiLQANVVGTWNVYEAARRCGAkRVIFGSSNHaV-----GFYprsqriNETVPVKPDSRYGLSKCWGEava 144
Cdd:cd05254    73 sDPELA-----YRVNVLAPENLARAAKEVGA-RLIHISTDY-VfdgkkGPY------KEEDAPNPLNVYGKSKLLGE--- 136
                         170
                  ....*....|....*.
gi 1360496189 145 qLYADKYGVKSLLLRI 160
Cdd:cd05254   137 -VAVLNANPRYLILRT 151
RmlD_sub_bind pfam04321
RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some ...
3-161 2.88e-10

RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some bacteria. Its precursor, dTDP-L-rhamnose, is synthesized by four different enzymes the final one of which is RmlD. The RmlD substrate binding domain is responsible for binding a sugar nucleotide.


Pssm-ID: 427865 [Multi-domain]  Cd Length: 284  Bit Score: 59.21  E-value: 2.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   3 ILITGGAGHVGRTLRRELAGRFELVrifdmvaaepIGPNEESVvgDIADIAAVENATRGM--DAVIHLAA---------E 71
Cdd:pfam04321   1 ILITGANGQLGTELRRLLAERGIEV----------VALTRAEL--DLTDPEAVARLLREIkpDVVVNAAAytavdkaesE 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  72 PNEApfgiiLQANVVGTWNVYEAARRCGAKrVIFGSSNH-----AVGFYPrsqrinETVPVKPDSRYGLSKCWGE-AVAq 145
Cdd:pfam04321  69 PDLA-----YAINALAPANLAEACAAVGAP-LIHISTDYvfdgtKPRPYE------EDDETNPLNVYGRTKLAGEqAVR- 135
                         170
                  ....*....|....*.
gi 1360496189 146 lyadKYGVKSLLLRIG 161
Cdd:pfam04321 136 ----AAGPRHLILRTS 147
PRK10217 PRK10217
dTDP-glucose 4,6-dehydratase; Provisional
2-162 5.65e-10

dTDP-glucose 4,6-dehydratase; Provisional


Pssm-ID: 182313 [Multi-domain]  Cd Length: 355  Bit Score: 58.89  E-value: 5.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   2 KILITGGAGHVGRTLRRELAGRF--------ELVRIFDMVAAEPIGPNE----ESVvgDIADIAAVENATRGM--DAVIH 67
Cdd:PRK10217    3 KILITGGAGFIGSALVRYIINETsdavvvvdKLTYAGNLMSLAPVAQSErfafEKV--DICDRAELARVFTEHqpDCVMH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  68 LAAEPN-----EAPFGIIlQANVVGTWNVYEAAR---------RCGAKRVIFGSSNHAVG-FYPRSQRINETVPVKPDSR 132
Cdd:PRK10217   81 LAAESHvdrsiDGPAAFI-ETNIVGTYTLLEAARaywnaltedKKSAFRFHHISTDEVYGdLHSTDDFFTETTPYAPSSP 159
                         170       180       190
                  ....*....|....*....|....*....|
gi 1360496189 133 YGLSKCWGEAVAQLYADKYGVKSLLLRIGN 162
Cdd:PRK10217  160 YSASKASSDHLVRAWLRTYGLPTLITNCSN 189
PRK05865 PRK05865
sugar epimerase family protein;
1-113 5.79e-10

sugar epimerase family protein;


Pssm-ID: 235630 [Multi-domain]  Cd Length: 854  Bit Score: 59.67  E-value: 5.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   1 MKILITGGAGHVGRTLRRELagrfeLVRIFDMVAAEPIGPNEES-----VVGDIADIAAVENATRGMDAVIHLAAEPNEA 75
Cdd:PRK05865    1 MRIAVTGASGVLGRGLTARL-----LSQGHEVVGIARHRPDSWPssadfIAADIRDATAVESAMTGADVVAHCAWVRGRN 75
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1360496189  76 PfgiilQANVVGTWNVYEAARRCGAKRVIFGSSNHAVG 113
Cdd:PRK05865   76 D-----HINIDGTANVLKAMAETGTGRIVFTSSGHQPR 108
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
2-194 7.54e-10

atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187554 [Multi-domain]  Cd Length: 203  Bit Score: 57.25  E-value: 7.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   2 KILITGGAGHVGRTLRRELAGRFELVRIfdMV-----AAEPIGPNEESVVGDIADIAAVENATRGMDAVIHLAA---EPN 73
Cdd:cd05243     1 KVLVVGATGKVGRHVVRELLDRGYQVRA--LVrdpsqAEKLEAAGAEVVVGDLTDAESLAAALEGIDAVISAAGsggKGG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  74 EAPFGIILQANVvgtwNVYEAARRCGAKRVIFGSSnhaVGFYPRSQRINETVPVkpdsryglskcwgeAVAQLYADKYGV 153
Cdd:cd05243    79 PRTEAVDYDGNI----NLIDAAKKAGVKRFVLVSS---IGADKPSHPLEALGPY--------------LDAKRKAEDYLR 137
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1360496189 154 KSLL----LRIGNAAATPGSARALAI---------WVSGRDLAQLVTIGLEHPD 194
Cdd:cd05243   138 ASGLdytiVRPGGLTDDPAGTGRVVLggdgtrldgPISRADVAEVLAEALDTPA 191
UGD_SDR_e cd05230
UDP-glucuronate decarboxylase (UGD) and related proteins, extended (e) SDRs; UGD catalyzes the ...
1-162 1.24e-09

UDP-glucuronate decarboxylase (UGD) and related proteins, extended (e) SDRs; UGD catalyzes the formation of UDP-xylose from UDP-glucuronate; it is an extended-SDR, and has the characteristic glycine-rich NAD-binding pattern, TGXXGXXG, and active site tetrad. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187541 [Multi-domain]  Cd Length: 305  Bit Score: 57.65  E-value: 1.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   1 MKILITGGAGHVGRTLRRELAGRFELVRIFDMVAA---EPIG-----PNEESVVGDIADIAAVEnatrgMDAVIHLAAEP 72
Cdd:cd05230     1 KRILITGGAGFLGSHLCDRLLEDGHEVICVDNFFTgrkRNIEhlighPNFEFIRHDVTEPLYLE-----VDQIYHLACPA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  73 N-----EAPFGIILqANVVGTWNVYEAARRCGAkRVIFGSSNHAVG---FYPRSQRINETV-PVKPDSRYGLSKCWGEAV 143
Cdd:cd05230    76 SpvhyqYNPIKTLK-TNVLGTLNMLGLAKRVGA-RVLLASTSEVYGdpeVHPQPESYWGNVnPIGPRSCYDEGKRVAETL 153
                         170
                  ....*....|....*....
gi 1360496189 144 AQLYADKYGVKSLLLRIGN 162
Cdd:cd05230   154 CMAYHRQHGVDVRIARIFN 172
TDH_SDR_e cd05272
L-threonine dehydrogenase, extended (e) SDRs; This subgroup contains members identified as ...
2-168 1.79e-09

L-threonine dehydrogenase, extended (e) SDRs; This subgroup contains members identified as L-threonine dehydrogenase (TDH). TDH catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine via NAD(H)-dependent oxidation. This group is distinct from TDHs that are members of the medium chain dehydrogenase/reductase family. This group has the NAD-binding motif and active site tetrad of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187580 [Multi-domain]  Cd Length: 308  Bit Score: 57.32  E-value: 1.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   2 KILITGGAGHVGRTLRRELAGRF--ELVRIFDMV--AAEPI--GPNEESVVGDIADI-AAVENatRGMDAVIHLAA---- 70
Cdd:cd05272     1 RILITGGLGQIGSELAKLLRKRYgkDNVIASDIRkpPAHVVlsGPFEYLDVLDFKSLeEIVVN--HKITWIIHLAAllsa 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  71 ----EPNEApfgiiLQANVVGTWNVYEAARRCGAKrvIFGSSNHAVgFYPRSQRIN---ETVpVKPDSRYGLSKCWGEAV 143
Cdd:cd05272    79 vgekNPPLA-----WDVNMNGLHNVLELAREHNLR--IFVPSTIGA-FGPTTPRNNtpdDTI-QRPRTIYGVSKVAAELL 149
                         170       180
                  ....*....|....*....|....*...
gi 1360496189 144 AQLYADKYGVKSLLLR---IGNAAATPG 168
Cdd:cd05272   150 GEYYHHKFGVDFRSLRypgIISYDTLPG 177
YfcH COG1090
NAD dependent epimerase/dehydratase family enzyme [General function prediction only];
2-161 2.13e-09

NAD dependent epimerase/dehydratase family enzyme [General function prediction only];


Pssm-ID: 440707 [Multi-domain]  Cd Length: 298  Bit Score: 57.00  E-value: 2.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   2 KILITGGAGHVGRTLRRELAGRFE----LVRifdmvAAEPIGPNEESVVGDIADIAAVENATRGMDAVIHLAAEP-NEAP 76
Cdd:COG1090     1 KILITGGTGFIGSALVAALLARGHevvvLTR-----RPPKAPDEVTYVAWDPETGGIDAAALEGADAVINLAGASiADKR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  77 FG-----IILQANVVGTWNVYEAARRCGAK-RVIFGSSnhAVGFYPRS--QRINETVPVKPDSRYGLSKCWgEAVAQLyA 148
Cdd:COG1090    76 WTearkqEILDSRVDSTRLLVEAIAAAANPpKVLISAS--AIGYYGDRgdEVLTEDSPPGDGFLAEVCRAW-EAAAAP-A 151
                         170
                  ....*....|...
gi 1360496189 149 DKYGVKSLLLRIG 161
Cdd:COG1090   152 EEAGTRVVLLRTG 164
YwnB COG2910
Putative NADH-flavin reductase [General function prediction only];
2-105 1.15e-08

Putative NADH-flavin reductase [General function prediction only];


Pssm-ID: 442154 [Multi-domain]  Cd Length: 205  Bit Score: 53.71  E-value: 1.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   2 KILITGGAGHVGRTLRRELAGR-FE---LVRifDMVAAEPIGPNEESVVGDIADIAAVENATRGMDAVIHLAAepneAPF 77
Cdd:COG2910     1 KIAVIGATGRVGSLIVREALARgHEvtaLVR--NPEKLPDEHPGLTVVVGDVLDPAAVAEALAGADAVVSALG----AGG 74
                          90       100
                  ....*....|....*....|....*...
gi 1360496189  78 GIILQANVVGTWNVYEAARRCGAKRVIF 105
Cdd:COG2910    75 GNPTTVLSDGARALIDAMKAAGVKRLIV 102
3b-HSD_HSDB1_like_SDR_e cd09811
human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, ...
4-141 2.25e-08

human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, extended (e) SDRs; This extended-SDR subgroup includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7], and related proteins. These proteins have the characteristic active site tetrad and NAD(P)-binding motif of extended SDRs. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. C(27) 3beta-HSD is a membrane-bound enzyme of the endoplasmic reticulum, it catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187671 [Multi-domain]  Cd Length: 354  Bit Score: 54.05  E-value: 2.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   4 LITGGAGHVGRTLRRELAGRFEL---VRIFDMV--------AAEPIGPNEESVV-GDIADIAAVENATRGMDAVIHLAA- 70
Cdd:cd09811     3 LVTGGGGFLGQHIIRLLLERKEElkeIRVLDKAfgpeliehFEKSQGKTYVTDIeGDIKDLSFLFRACQGVSVVIHTAAi 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  71 -------EPNEapfgiILQANVVGTWNVYEAARRCGAKRVIFGSSNHAVG--FYPRS-QRINETVPVKPDSR--YGLSKC 138
Cdd:cd09811    83 vdvfgppNYEE-----LEEVNVNGTQAVLEACVQNNVKRLVYTSSIEVAGpnFKGRPiFNGVEDTPYEDTSTppYASSKL 157

                  ...
gi 1360496189 139 WGE 141
Cdd:cd09811   158 LAE 160
Lys2b COG3320
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary ...
1-149 2.33e-08

Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary metabolites biosynthesis, transport and catabolism]; Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 442549 [Multi-domain]  Cd Length: 265  Bit Score: 53.67  E-value: 2.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   1 MKILITGGAGHVGRTLRRELAGRFE-----LVR---------IFDMVAAEPIGPNEES------VVGDIA------DIAA 54
Cdd:COG3320     1 RTVLLTGATGFLGAHLLRELLRRTDarvycLVRasdeaaareRLEALLERYGLWLELDasrvvvVAGDLTqprlglSEAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  55 VENATRGMDAVIHLAAEPN-EAPFGIILQANVVGTWNVYEAARRCGAKRVIFGSSNHAVGFYPRSQRINETVPVKPDSR- 132
Cdd:COG3320    81 FQELAEEVDAIVHLAALVNlVAPYSELRAVNVLGTREVLRLAATGRLKPFHYVSTIAVAGPADRSGVFEEDDLDEGQGFa 160
                         170
                  ....*....|....*....
gi 1360496189 133 --YGLSKCWGEAVAQLYAD 149
Cdd:COG3320   161 ngYEQSKWVAEKLVREARE 179
CDP_GD_SDR_e cd05252
CDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains CDP-D-glucose 4, ...
43-172 3.34e-08

CDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains CDP-D-glucose 4,6-dehydratase, an extended SDR, which catalyzes the conversion of CDP-D-glucose to CDP-4-keto-6-deoxy-D-glucose. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187562 [Multi-domain]  Cd Length: 336  Bit Score: 53.47  E-value: 3.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  43 ESVVGDIADIAAVENATRGMDA--VIHLAAEP-----NEAPFGIIlQANVVGTWNVYEAARRCG-AKRVIFGSSNHAvgf 114
Cdd:cd05252    55 SSTRGDIRDLNALREAIREYEPeiVFHLAAQPlvrlsYKDPVETF-ETNVMGTVNLLEAIRETGsVKAVVNVTSDKC--- 130
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1360496189 115 YPRSQRI---NETVPVKPDSRYGLSKCWGEAVAQLYADKYGVKSLLLRIGNAAAtpgSARA 172
Cdd:cd05252   131 YENKEWGwgyRENDPLGGHDPYSSSKGCAELIISSYRNSFFNPENYGKHGIAIA---SARA 188
SDR_a7 cd05262
atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. ...
1-164 1.59e-07

atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. Members of this subgroup have a glycine-rich NAD(P)-binding motif consensus that matches the extended SDRs, TGXXGXXG, but lacks the characteristic active site residues of the SDRs. This subgroup has basic residues (HXXXR) in place of the active site motif YXXXK, these may have a catalytic role. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187572 [Multi-domain]  Cd Length: 291  Bit Score: 51.20  E-value: 1.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   1 MKILITGGAGHVGRTLRRELAGR----FELVRIfDMVAAEPIGPNEESVVGDIADIAAVENATRGMDAVIHLAAEPNEAP 76
Cdd:cd05262     1 MKVFVTGATGFIGSAVVRELVAAghevVGLARS-DAGAAKLEAAGAQVHRGDLEDLDILRKAAAEADAVIHLAFTHDFDN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  77 FGIILQANVVGTWNVYEAARRCGaKRVIFGSSNHAVGFYPRSQRINETVPVKPDSRYglsKCWGEAVAQLYADKyGVKSL 156
Cdd:cd05262    80 FAQACEVDRRAIEALGEALRGTG-KPLIYTSGIWLLGPTGGQEEDEEAPDDPPTPAA---RAVSEAAALELAER-GVRAS 154

                  ....*...
gi 1360496189 157 LLRIGNAA 164
Cdd:cd05262   155 VVRLPPVV 162
PRK10084 PRK10084
dTDP-glucose 4,6 dehydratase; Provisional
1-162 1.61e-07

dTDP-glucose 4,6 dehydratase; Provisional


Pssm-ID: 236649 [Multi-domain]  Cd Length: 352  Bit Score: 51.71  E-value: 1.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   1 MKILITGGAGHVGRTLRRELAGRFE--LVRIFDMVAAepigPNEESVVG------------DIADIAAVEN--ATRGMDA 64
Cdd:PRK10084    1 MKILVTGGAGFIGSAVVRHIINNTQdsVVNVDKLTYA----GNLESLADvsdseryvfehaDICDRAELDRifAQHQPDA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  65 VIHLAAEPN-----EAPFGIIlQANVVGTWNVYEAAR---------RCGAKRVIFGSSNHAVGFYPRSQRIN-------- 122
Cdd:PRK10084   77 VMHLAAESHvdrsiTGPAAFI-ETNIVGTYVLLEAARnywsaldedKKNAFRFHHISTDEVYGDLPHPDEVEnseelplf 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1360496189 123 -ETVPVKPDSRYGLSKCWGEAVAQLYADKYGVKSLLLRIGN 162
Cdd:PRK10084  156 tETTAYAPSSPYSASKASSDHLVRAWLRTYGLPTIVTNCSN 196
GDP_FS_SDR_e cd05239
GDP-fucose synthetase, extended (e) SDRs; GDP-fucose synthetase (aka 3, ...
2-199 2.63e-07

GDP-fucose synthetase, extended (e) SDRs; GDP-fucose synthetase (aka 3, 5-epimerase-4-reductase) acts in the NADP-dependent synthesis of GDP-fucose from GDP-mannose. Two activities have been proposed for the same active site: epimerization and reduction. Proteins in this subgroup are extended SDRs, which have a characteristic active site tetrad and an NADP-binding motif, [AT]GXXGXXG, that is a close match to the archetypical form. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187550 [Multi-domain]  Cd Length: 300  Bit Score: 50.66  E-value: 2.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   2 KILITGGAGHVGRTLRRELAGRFElvrifdmvaAEPIGPNEESVvgDIADIAAVENATR--GMDAVIHLAAE-------- 71
Cdd:cd05239     1 KILVTGHRGLVGSAIVRVLARRGY---------ENVVFRTSKEL--DLTDQEAVRAFFEkeKPDYVIHLAAKvggivanm 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  72 PNEAPF---GIILQANVVgtwnvyEAARRCGAKRVIFGSSNHAvgfYPR--SQRINETV----PVKPDSR-YGLSKCWGE 141
Cdd:cd05239    70 TYPADFlrdNLLINDNVI------HAAHRFGVKKLVFLGSSCI---YPDlaPQPIDESDlltgPPEPTNEgYAIAKRAGL 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189 142 AVAQLYADKYGVK-------------------------SLLLRIGNAAATpgSARALAIWVSGR---------DLAQLVT 187
Cdd:cd05239   141 KLCEAYRKQYGCDyisvmptnlygphdnfdpenshvipALIRKFHEAKLR--GGKEVTVWGSGTprreflysdDLARAIV 218
                         250
                  ....*....|....
gi 1360496189 188 IGLEHPD--IHCNV 199
Cdd:cd05239   219 FLLENYDepIIVNV 232
PLN02240 PLN02240
UDP-glucose 4-epimerase
3-162 2.71e-07

UDP-glucose 4-epimerase


Pssm-ID: 177883 [Multi-domain]  Cd Length: 352  Bit Score: 50.73  E-value: 2.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   3 ILITGGAGHVG-RTLRRELAGRFELVRIFDMV---------AAEPIGPNEESVV---GDIADIAAVEN--ATRGMDAVIH 67
Cdd:PLN02240    8 ILVTGGAGYIGsHTVLQLLLAGYKVVVIDNLDnsseealrrVKELAGDLGDNLVfhkVDLRDKEALEKvfASTRFDAVIH 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  68 LAA-----EPNEAPFgIILQANVVGTWNVYEAARRCGAKRVIFGSSNHAVGfYPRSQRINETVPVKPDSRYGLSKCWGEA 142
Cdd:PLN02240   88 FAGlkavgESVAKPL-LYYDNNLVGTINLLEVMAKHGCKKLVFSSSATVYG-QPEEVPCTEEFPLSATNPYGRTKLFIEE 165
                         170       180
                  ....*....|....*....|.
gi 1360496189 143 VA-QLYADKYGVKSLLLRIGN 162
Cdd:PLN02240  166 ICrDIHASDPEWKIILLRYFN 186
NAD_binding_10 pfam13460
NAD(P)H-binding;
7-108 4.50e-07

NAD(P)H-binding;


Pssm-ID: 463885 [Multi-domain]  Cd Length: 183  Bit Score: 48.76  E-value: 4.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   7 GGAGHVGRTLRRELAGR-FE---LVRIFDMVAAEPIGPNEESVVGDIADIAAVENATRGMDAVI-HLAAEPNEAPFGIil 81
Cdd:pfam13460   1 GATGKIGRLLVKQLLARgHEvtaLVRNPEKLADLEDHPGVEVVDGDVLDPDDLAEALAGQDAVIsALGGGGTDETGAK-- 78
                          90       100
                  ....*....|....*....|....*..
gi 1360496189  82 qaNVVgtwnvyEAARRCGAKRVIFGSS 108
Cdd:pfam13460  79 --NII------DAAKAAGVKRFVLVSS 97
3b-HSD_like_1_SDR_e cd09812
3beta-hydroxysteroid dehydrogenase (3b-HSD)-like, subgroup1, extended (e) SDRs; An ...
2-129 4.73e-07

3beta-hydroxysteroid dehydrogenase (3b-HSD)-like, subgroup1, extended (e) SDRs; An uncharacterized subgroup of the 3b-HSD-like extended-SDR family. Proteins in this subgroup have the characteristic active site tetrad and NAD(P)-binding motif of extended-SDRs. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187672 [Multi-domain]  Cd Length: 339  Bit Score: 50.19  E-value: 4.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   2 KILITGGAGHVGRTLRRELAGRFELVRIFDMVA-AEPIGPNEESVVGDIADIAAVENATRGMDAVIHLAAepneapFGI- 79
Cdd:cd09812     1 SVLITGGGGYFGFRLGCALAKSGVHVILFDIRRpQQELPEGIKFIQADVRDLSQLEKAVAGVDCVFHIAS------YGMs 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  80 ---------ILQANVVGTWNVYEAARRCGAKRVIFGSS-NHAVGFYPRSQRiNETVPVKP 129
Cdd:cd09812    75 greqlnrelIEEINVRGTENIIQVCVRRRVPRLIYTSTfNVIFGGQPIRNG-DESLPYLP 133
SDR_a8 cd05242
atypical (a) SDRs, subgroup 8; This subgroup contains atypical SDRs of unknown function. ...
2-208 5.30e-07

atypical (a) SDRs, subgroup 8; This subgroup contains atypical SDRs of unknown function. Proteins in this subgroup have a glycine-rich NAD(P)-binding motif consensus that resembles that of the extended SDRs, (GXXGXXG or GGXGXXG), but lacks the characteristic active site residues of the SDRs. A Cys often replaces the usual Lys of the YXXXK active site motif, while the upstream Ser is generally present and Arg replaces the usual Asn. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187553 [Multi-domain]  Cd Length: 296  Bit Score: 49.92  E-value: 5.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   2 KILITGGAGHVGRTLRRELAGRFELVRIFDMVAAEPIGPNEESVVgdiADIAAVENATRGMDAVIHLAAEP------NEA 75
Cdd:cd05242     1 KIVITGGTGFIGRALTRRLTAAGHEVVVLSRRPGKAEGLAEVITW---DGLSLGPWELPGADAVINLAGEPiacrrwTEA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  76 PFGIILQANVVGTWNVYEAARRCGAK-RVIFGSSnhAVGFYPRSQRINETVPVKPDSRYG--LSKCWgEAVAQLyADKYG 152
Cdd:cd05242    78 NKKEILSSRIESTRVLVEAIANAPAPpKVLISAS--AVGYYGHSGDEVLTENSPSGKDFLaeVCKAW-EKAAQP-ASELG 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1360496189 153 VKSLLLRIGNAAATPGSARALAI-------------------WVSGRDLAQLVTIGLEHPDIHcnvvyGVSNNAA 208
Cdd:cd05242   154 TRVVILRTGVVLGPDGGALPKMLlpfrlglggplgsgrqwmsWIHIDDLVRLIEFAIENPDLS-----GPVNAVA 223
PRK10675 PRK10675
UDP-galactose-4-epimerase; Provisional
1-145 6.85e-07

UDP-galactose-4-epimerase; Provisional


Pssm-ID: 182639 [Multi-domain]  Cd Length: 338  Bit Score: 49.43  E-value: 6.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   1 MKILITGGAGHVG-RTLRRELAGRFELVrIFD---------MVAAEPIGPNEESVV-GDIADIAAVEN--ATRGMDAVIH 67
Cdd:PRK10675    1 MRVLVTGGSGYIGsHTCVQLLQNGHDVV-ILDnlcnskrsvLPVIERLGGKHPTFVeGDIRNEALLTEilHDHAIDTVIH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  68 LA---------AEPNEapfgiILQANVVGTWNVYEAARRCGAKRVIFGSSNHAVGFYPRSQRInETVPV-KPDSRYGLSK 137
Cdd:PRK10675   80 FAglkavgesvQKPLE-----YYDNNVNGTLRLISAMRAANVKNLIFSSSATVYGDQPKIPYV-ESFPTgTPQSPYGKSK 153

                  ....*...
gi 1360496189 138 CWGEAVAQ 145
Cdd:PRK10675  154 LMVEQILT 161
CAPF_like_SDR_e cd05261
capsular polysaccharide assembling protein (CAPF) like, extended (e) SDRs; This subgroup of ...
1-162 1.02e-06

capsular polysaccharide assembling protein (CAPF) like, extended (e) SDRs; This subgroup of extended SDRs, includes some members which have been identified as capsular polysaccharide assembling proteins, such as Staphylococcus aureus Cap5F which is involved in the biosynthesis of N-acetyl-l-fucosamine, a constituent of surface polysaccharide structures of S. aureus. This subgroup has the characteristic active site tetrad and NAD-binding motif of extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187571 [Multi-domain]  Cd Length: 248  Bit Score: 48.51  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   1 MKILITGGAGHVGRTLRRELAGRFElVRIFDmvaaepigpneesvVGDIADIAAVENATRGMDAVIHLAA-----EPNEa 75
Cdd:cd05261     1 MKILITGAKGFIGKNLIARLKEQKD-DDIFF--------------YDRESDESELDDFLQGADFIFHLAGvnrpkDEAE- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  76 pfgiILQANVVGTWNVYEAARRCGAK-RVIFGSSNHAVGfyprsqrinetvpvkpDSRYGLSKCWGEAVAQLYADKYGVK 154
Cdd:cd05261    65 ----FESGNVGLTERLLDALTRNGKKpPILLSSSIQAAL----------------DNPYGKSKLAAEELLQEYARETGAP 124

                  ....*...
gi 1360496189 155 SLLLRIGN 162
Cdd:cd05261   125 VYIYRLPN 132
BVR-B_like_SDR_a cd05244
biliverdin IX beta reductase (BVR-B, aka flavin reductase)-like proteins; atypical (a) SDRs; ...
2-108 7.64e-06

biliverdin IX beta reductase (BVR-B, aka flavin reductase)-like proteins; atypical (a) SDRs; Human BVR-B catalyzes pyridine nucleotide-dependent production of bilirubin-IX beta during fetal development; in the adult BVR-B has flavin and ferric reductase activities. Human BVR-B catalyzes the reduction of FMN, FAD, and riboflavin. Recognition of flavin occurs mostly by hydrophobic interactions, accounting for the broad substrate specificity. Atypical SDRs are distinct from classical SDRs. BVR-B does not share the key catalytic triad, or conserved tyrosine typical of SDRs. The glycine-rich NADP-binding motif of BVR-B is GXXGXXG, which is similar but not identical to the pattern seen in extended SDRs. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187555 [Multi-domain]  Cd Length: 207  Bit Score: 45.69  E-value: 7.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   2 KILITGGAGHVGRTLRRE-LAGRFE---LVRifDMVAAEPIGPNEESVVGDIADIAAVENATRGMDAVIH-LAAEPNEAP 76
Cdd:cd05244     1 KIAIIGATGRTGSAIVREaLARGHEvtaLVR--DPAKLPAEHEKLKVVQGDVLDLEDVKEALEGQDAVISaLGTRNDLSP 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1360496189  77 FGIILQanvvGTWNVYEAARRCGAKRVIFGSS 108
Cdd:cd05244    79 TTLHSE----GTRNIVSAMKAAGVKRLIVVGG 106
NmrA_TMR_like_1_SDR_a cd05231
NmrA (a transcriptional regulator) and triphenylmethane reductase (TMR) like proteins, ...
3-108 1.04e-05

NmrA (a transcriptional regulator) and triphenylmethane reductase (TMR) like proteins, subgroup 1, atypical (a) SDRs; Atypical SDRs related to NMRa, TMR, and HSCARG (an NADPH sensor). This subgroup resembles the SDRs and has a partially conserved characteristic [ST]GXXGXXG NAD-binding motif, but lacks the conserved active site residues. NmrA is a negative transcriptional regulator of various fungi, involved in the post-translational modulation of the GATA-type transcription factor AreA. NmrA lacks the canonical GXXGXXG NAD-binding motif and has altered residues at the catalytic triad, including a Met instead of the critical Tyr residue. NmrA may bind nucleotides but appears to lack any dehydrogenase activity. HSCARG has been identified as a putative NADP-sensing molecule, and redistributes and restructures in response to NADPH/NADP ratios. Like NmrA, it lacks most of the active site residues of the SDR family, but has an NAD(P)-binding motif similar to the extended SDR family, GXXGXXG. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Atypical SDRs are distinct from classical SDRs. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187542 [Multi-domain]  Cd Length: 259  Bit Score: 45.78  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   3 ILITGGAGHVGRTLRRELAGRFELVRIF---DMVAAEPIGPNEESVVGDIADIAAVENATRGMDAVIHLAA-EPNEAPFG 78
Cdd:cd05231     1 ILVTGATGRIGSKVATTLLEAGRPVRALvrsDERAAALAARGAEVVVGDLDDPAVLAAALAGVDAVFFLAPpAPTADARP 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 1360496189  79 IILQANVVgtwnVYEAARRCGAKRVIFGSS 108
Cdd:cd05231    81 GYVQAAEA----FASALREAGVKRVVNLSS 106
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
1-123 1.38e-05

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs; This subgroup of extended SDR-like proteins are atypical SDRs. They have a glycine-rich NAD(P)-binding motif similar to the typical SDRs, GXXGXXG, and have the YXXXK active site motif (though not the other residues of the SDR tetrad). Members identified include NDUFA9 (mitochondrial) and putative nucleoside-diphosphate-sugar epimerase. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187579 [Multi-domain]  Cd Length: 273  Bit Score: 45.31  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   1 MKILITGGAGHVGRTLRRELAGRFELVRIF-----DMVAAEPIGPNEESVV--GDIADIAAVENATRGMDAVIHLAAEPN 73
Cdd:cd05271     1 MVVTVFGATGFIGRYVVNRLAKRGSQVIVPyrceaYARRLLVMGDLGQVLFveFDLRDDESIRKALEGSDVVINLVGRLY 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1360496189  74 EAPFGIILQANVVGTWNVYEAARRCGAKRVI----FGSSNHAVGFYPRSQRINE 123
Cdd:cd05271    81 ETKNFSFEDVHVEGPERLAKAAKEAGVERLIhisaLGADANSPSKYLRSKAEGE 134
PLN02166 PLN02166
dTDP-glucose 4,6-dehydratase
1-162 4.33e-05

dTDP-glucose 4,6-dehydratase


Pssm-ID: 165812 [Multi-domain]  Cd Length: 436  Bit Score: 44.23  E-value: 4.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   1 MKILITGGAGHVGRTLRRELAGRFELVRIFDMV---AAEPI-----GPNEESVVGDIADIAAVEnatrgMDAVIHLA--A 70
Cdd:PLN02166  121 LRIVVTGGAGFVGSHLVDKLIGRGDEVIVIDNFftgRKENLvhlfgNPRFELIRHDVVEPILLE-----VDQIYHLAcpA 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  71 EPNEAPFGII--LQANVVGTWNVYEAARRCGAkRVIFGSSNHAVGfYPRSQRINETV-----PVKPDSRYGLSKCWGEAV 143
Cdd:PLN02166  196 SPVHYKYNPVktIKTNVMGTLNMLGLAKRVGA-RFLLTSTSEVYG-DPLEHPQKETYwgnvnPIGERSCYDEGKRTAETL 273
                         170
                  ....*....|....*....
gi 1360496189 144 AQLYADKYGVKSLLLRIGN 162
Cdd:PLN02166  274 AMDYHRGAGVEVRIARIFN 292
PCBER_SDR_a cd05259
phenylcoumaran benzylic ether reductase (PCBER) like, atypical (a) SDRs; PCBER and ...
2-116 4.36e-05

phenylcoumaran benzylic ether reductase (PCBER) like, atypical (a) SDRs; PCBER and pinoresinol-lariciresinol reductases are NADPH-dependent aromatic alcohol reductases, and are atypical members of the SDR family. Other proteins in this subgroup are identified as eugenol synthase. These proteins contain an N-terminus characteristic of NAD(P)-binding proteins and a small C-terminal domain presumed to be involved in substrate binding, but they do not have the conserved active site Tyr residue typically found in SDRs. Numerous other members have unknown functions. The glycine rich NADP-binding motif in this subgroup is of 2 forms: GXGXXG and G[GA]XGXXG; it tends to be atypical compared with the forms generally seen in classical or extended SDRs. The usual SDR active site tetrad is not present, but a critical active site Lys at the usual SDR position has been identified in various members, though other charged and polar residues are found at this position in this subgroup. Atypical SDR-related proteins retain the Rossmann fold of the SDRs, but have limited sequence identity and generally lack the catalytic properties of the archetypical members. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187569 [Multi-domain]  Cd Length: 282  Bit Score: 43.83  E-value: 4.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   2 KILITGGAGHVGRTLRREL--AGRFE---LVRIFDMVAAEPIGPNEESVVGDIADIAAVENATRGMDAVIHLAaepneAP 76
Cdd:cd05259     1 KIAIAGATGTLGGPIVSALlaSPGFTvtvLTRPSSTSSNEFQPSGVKVVPVDYASHESLVAALKGVDAVISAL-----GG 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1360496189  77 FGIILQANVVgtwnvyEAARRCGAKRVI---FGSSNHAVGFYP 116
Cdd:cd05259    76 AAIGDQLKLI------DAAIAAGVKRFIpseFGVDYDRIGALP 112
SDR_a2 cd05245
atypical (a) SDRs, subgroup 2; This subgroup contains atypical SDRs, one member is identified ...
3-108 5.17e-05

atypical (a) SDRs, subgroup 2; This subgroup contains atypical SDRs, one member is identified as Escherichia coli protein ybjT, function unknown. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif consensus that generally matches the extended SDRs, TGXXGXXG, but lacks the characteristic active site residues of the SDRs. This subgroup has basic residues (HXXXR) in place of the active site motif YXXXK, these may have a catalytic role. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187556 [Multi-domain]  Cd Length: 293  Bit Score: 43.87  E-value: 5.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   3 ILITGGAGHVGRTLRRELAGRFELVRIF----DMVAAEPIGPNEESVVGDIADIAAVENATRGMDAVIHLAAEPNEApfG 78
Cdd:cd05245     1 VLVTGATGYVGGRLVPRLLQEGHQVRALvrspEKLADRPWSERVTVVRGDLEDPESLRAALEGIDTAYYLVHSMGSG--G 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 1360496189  79 IILQANVVGTWNVYEAARRCGAKRVIFGSS 108
Cdd:cd05245    79 DFEEADRRAARNFARAARAAGVKRIIYLGG 108
PLN02206 PLN02206
UDP-glucuronate decarboxylase
1-162 5.57e-05

UDP-glucuronate decarboxylase


Pssm-ID: 177856 [Multi-domain]  Cd Length: 442  Bit Score: 43.82  E-value: 5.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   1 MKILITGGAGHVGRTLRRELAGRFELVRIFD--------MVAAEPIGPNEESVVGDIADIAAVEnatrgMDAVIHLA--A 70
Cdd:PLN02206  120 LRVVVTGGAGFVGSHLVDRLMARGDSVIVVDnfftgrkeNVMHHFSNPNFELIRHDVVEPILLE-----VDQIYHLAcpA 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  71 EPNEAPFGII--LQANVVGTWNVYEAARRCGAkRVIFGSSNHAVG---FYPRSQRINETV-PVKPDSRYGLSKCWGEAVA 144
Cdd:PLN02206  195 SPVHYKFNPVktIKTNVVGTLNMLGLAKRVGA-RFLLTSTSEVYGdplQHPQVETYWGNVnPIGVRSCYDEGKRTAETLT 273
                         170
                  ....*....|....*...
gi 1360496189 145 QLYADKYGVKSLLLRIGN 162
Cdd:PLN02206  274 MDYHRGANVEVRIARIFN 291
PRK12320 PRK12320
hypothetical protein; Provisional
1-107 1.99e-04

hypothetical protein; Provisional


Pssm-ID: 138873 [Multi-domain]  Cd Length: 699  Bit Score: 42.67  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   1 MKILITGGAGHVGRTLRRELAGRFELVRIFDMVAAEPIGPNEESVVGDIADIAAVENATRGmDAVIHLAAEPNEAPFGii 80
Cdd:PRK12320    1 MQILVTDATGAVGRSVTRQLIAAGHTVSGIAQHPHDALDPRVDYVCASLRNPVLQELAGEA-DAVIHLAPVDTSAPGG-- 77
                          90       100
                  ....*....|....*....|....*..
gi 1360496189  81 lqANVVGTWNVYEAARRCGAkRVIFGS 107
Cdd:PRK12320   78 --VGITGLAHVANAAARAGA-RLLFVS 101
PLN02725 PLN02725
GDP-4-keto-6-deoxymannose-3,5-epimerase-4-reductase
4-152 2.12e-04

GDP-4-keto-6-deoxymannose-3,5-epimerase-4-reductase


Pssm-ID: 178326 [Multi-domain]  Cd Length: 306  Bit Score: 41.99  E-value: 2.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   4 LITGGAGHVGRTLRRELAGRfelvrifdmvaaepigPNEESVV-----GDIADIAAVEN--ATRGMDAVIHLAAE----- 71
Cdd:PLN02725    1 FVAGHRGLVGSAIVRKLEAL----------------GFTNLVLrthkeLDLTRQADVEAffAKEKPTYVILAAAKvggih 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  72 -PNEAP---FGIILQANVvgtwNVYEAARRCGAKRVIF-GSSnhavGFYPR--SQRINETV----PVKPDSR-YGLSKCW 139
Cdd:PLN02725   65 aNMTYPadfIRENLQIQT----NVIDAAYRHGVKKLLFlGSS----CIYPKfaPQPIPETAlltgPPEPTNEwYAIAKIA 136
                         170
                  ....*....|...
gi 1360496189 140 GEAVAQLYADKYG 152
Cdd:PLN02725  137 GIKMCQAYRIQYG 149
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
4-107 2.14e-04

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: 41.99  E-value: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   4 LITGGAG----HVGRTLRRELAGRFELV--------RIFDMVAAEPIGPNEESVVGDIADIAAVENATR------GMDAV 65
Cdd:cd05274   154 LITGGLGglglLVARWLAARGARHLVLLsrrgpaprAAARAALLRAGGARVSVVRCDVTDPAALAALLAelaaggPLAGV 233
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1360496189  66 IHLA--------AEPNEAPFGIILQANVVGTWNVYEAARRCGAKR-VIFGS 107
Cdd:cd05274   234 IHAAgvlrdallAELTPAAFAAVLAAKVAGALNLHELTPDLPLDFfVLFSS 284
NmrA_like_SDR_a cd05251
NmrA (a transcriptional regulator) and HSCARG (an NADPH sensor) like proteins, atypical (a) ...
3-107 2.54e-04

NmrA (a transcriptional regulator) and HSCARG (an NADPH sensor) like proteins, atypical (a) SDRs; NmrA and HSCARG like proteins. NmrA is a negative transcriptional regulator of various fungi, involved in the post-translational modulation of the GATA-type transcription factor AreA. NmrA lacks the canonical GXXGXXG NAD-binding motif and has altered residues at the catalytic triad, including a Met instead of the critical Tyr residue. NmrA may bind nucleotides but appears to lack any dehydrogenase activity. HSCARG has been identified as a putative NADP-sensing molecule, and redistributes and restructures in response to NADPH/NADP ratios. Like NmrA, it lacks most of the active site residues of the SDR family, but has an NAD(P)-binding motif similar to the extended SDR family, GXXGXXG. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Atypical SDRs are distinct from classical SDRs. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187561 [Multi-domain]  Cd Length: 242  Bit Score: 41.49  E-value: 2.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   3 ILITGGAGHVGRTLRRELAGRFE-----LVRIFDMVAA-EPIGPNEESVVGDIADIAAVENATRGMDAVIHLAAEPNEAP 76
Cdd:cd05251     1 ILVFGATGKQGGSVVRALLKDPGfkvraLTRDPSSPAAkALAAPGVEVVQGDLDDPESLEAALKGVYGVFLVTDFWEAGG 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1360496189  77 FGIILQANvvgtwNVYEAARRCGAKRVIFGS 107
Cdd:cd05251    81 EDEIAQGK-----NVVDAAKRAGVQHFVFSS 106
PRK07201 PRK07201
SDR family oxidoreductase;
1-116 2.63e-04

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 42.25  E-value: 2.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   1 MKILITGGAGHVGRTLRRELAGRFELVRIFDMVAAEPIGPNEE-----------SVVGDIAD----IAAVENATRG-MDA 64
Cdd:PRK07201    1 MRYFVTGGTGFIGRRLVSRLLDRRREATVHVLVRRQSLSRLEAlaaywgadrvvPLVGDLTEpglgLSEADIAELGdIDH 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1360496189  65 VIHLAAEPN-EAPFGIILQANVVGTWNVYEAARRCGAKRVIFGSSNHAVGFYP 116
Cdd:PRK07201   81 VVHLAAIYDlTADEEAQRAANVDGTRNVVELAERLQAATFHHVSSIAVAGDYE 133
TMR_SDR_a cd05269
triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs; TMR is an ...
3-111 2.82e-04

triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs; TMR is an atypical NADP-binding protein of the SDR family. It lacks the active site residues of the SDRs but has a glycine rich NAD(P)-binding motif that matches the extended SDRs. Proteins in this subgroup however, are more similar in length to the classical SDRs. TMR was identified as a reducer of triphenylmethane dyes, important environmental pollutants. This subgroup also includes Escherichia coli NADPH-dependent quinine oxidoreductase (QOR2), which catalyzes two-electron reduction of quinone; but is unlikely to play a major role in protecting against quinone cytotoxicity. Atypical SDRs are distinct from classical SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187578 [Multi-domain]  Cd Length: 272  Bit Score: 41.49  E-value: 2.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   3 ILITGGAGHVGRTLRRELAGRFE----LVRIFDmVAAEPIGPNEESVVGDIADIAAVENATRGMDAV--IHLAAEPNEAP 76
Cdd:cd05269     1 ILVTGATGKLGTAVVELLLAKVAsvvaLVRNPE-KAKAFAADGVEVRQGDYDDPETLERAFEGVDRLllISPSDLEDRIQ 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1360496189  77 fgiiLQANVVgtwnvyEAARRCGAKRVIFGSSNHA 111
Cdd:cd05269    80 ----QHKNFI------DAAKQAGVKHIVYLSASGA 104
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
4-108 3.28e-04

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: 40.54  E-value: 3.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189    4 LITGGAGHVGRTL----------------RRELAGRFELVRIFDMVAAepiGPNEESVVGDIADIAAVENATRGM----- 62
Cdd:smart00822   4 LITGGLGGLGRALarwlaergarrlvllsRSGPDAPGAAALLAELEAA---GARVTVVACDVADRDALAAVLAAIpaveg 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1360496189   63 --DAVIHLAAEPNEAPFGII--------LQANVVGTWNVYEAARRCGAKRVIFGSS 108
Cdd:smart00822  81 plTGVIHAAGVLDDGVLASLtperfaavLAPKAAGAWNLHELTADLPLDFFVLFSS 136
PRK15181 PRK15181
Vi polysaccharide biosynthesis UDP-N-acetylglucosaminuronic acid C-4 epimerase TviC;
4-162 3.40e-04

Vi polysaccharide biosynthesis UDP-N-acetylglucosaminuronic acid C-4 epimerase TviC;


Pssm-ID: 185103 [Multi-domain]  Cd Length: 348  Bit Score: 41.62  E-value: 3.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   4 LITGGAGHVGRTLRRELAGRFELVRIFDMVAAE--------PIGPNEES------VVGDIADIAAVENATRGMDAVIHLA 69
Cdd:PRK15181   19 LITGVAGFIGSGLLEELLFLNQTVIGLDNFSTGyqhnlddvRTSVSEEQwsrfifIQGDIRKFTDCQKACKNVDYVLHQA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  70 A---EPNEAPFGIILQ-ANVVGTWNVYEAARRCGAKRVIFGSSNHAVGFYPRSQRINETVPvKPDSRYGLSKCWGEAVAQ 145
Cdd:PRK15181   99 AlgsVPRSLKDPIATNsANIDGFLNMLTAARDAHVSSFTYAASSSTYGDHPDLPKIEERIG-RPLSPYAVTKYVNELYAD 177
                         170
                  ....*....|....*..
gi 1360496189 146 LYADKYGVKSLLLRIGN 162
Cdd:PRK15181  178 VFARSYEFNAIGLRYFN 194
SQD1_like_SDR_e cd05255
UDP_sulfoquinovose_synthase (Arabidopsis thaliana SQD1 and related proteins), extended (e) ...
1-91 7.53e-04

UDP_sulfoquinovose_synthase (Arabidopsis thaliana SQD1 and related proteins), extended (e) SDRs; Arabidopsis thaliana UDP-sulfoquinovose-synthase ( SQD1), an extended SDR, catalyzes the transfer of SO(3)(-) to UDP-glucose in the biosynthesis of plant sulfolipids. Members of this subgroup share the conserved SDR catalytic residues, and a partial match to the characteristic extended-SDR NAD-binding motif. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187565 [Multi-domain]  Cd Length: 382  Bit Score: 40.45  E-value: 7.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   1 MKILITGGAGHVGRTLRRELAGRFELVRIFD------------MVAAEPIGPNEESV--------------VGDIADIAA 54
Cdd:cd05255     1 MKVLILGGDGYCGWPTALHLSKRGHEVCIVDnlvrrridvelgLESLTPIASIHERLrawkeltgktiefyVGDACDYEF 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1360496189  55 VENATRGM--DAVIHLAAEPNeAPFGII--------LQANVVGTWNV 91
Cdd:cd05255    81 LAELLASHepDAVVHFAEQRS-APYSMIdrehanytQHNNVIGTLNL 126
SDR_a1 cd05265
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ...
1-159 1.27e-03

atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been identified putatively as isoflavones reductase, sugar dehydratase, mRNA binding protein etc. Atypical SDRs are distinct from classical SDRs. Members of this subgroup retain the canonical active site triad (though not the upstream Asn found in most SDRs) but have an unusual putative glycine-rich NAD(P)-binding motif, GGXXXXG, in the usual location. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187575 [Multi-domain]  Cd Length: 250  Bit Score: 39.20  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   1 MKILITGGAGHVGRTLRRELAGRFELVRIFDM-VAAEPIGPNEESVVGDIADIAAVENA--TRGMDAVIH-LAAEPNEAp 76
Cdd:cd05265     1 MKILIIGGTRFIGKALVEELLAAGHDVTVFNRgRTKPDLPEGVEHIVGDRNDRDALEELlgGEDFDVVVDtIAYTPRQV- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  77 fgiilqanvvgtwnvyEAARRCGAKRV---IFGSSnhaVGFY-PRSQRINETVP--------VKPDSRYGLSKCWGEAVA 144
Cdd:cd05265    80 ----------------ERALDAFKGRVkqyIFISS---ASVYlKPGRVITESTPlrepdavgLSDPWDYGRGKRAAEDVL 140
                         170
                  ....*....|....*
gi 1360496189 145 QlyaDKYGVKSLLLR 159
Cdd:cd05265   141 I---EAAAFPYTIVR 152
SDR_a6 cd05267
atypical (a) SDRs, subgroup 6; These atypical SDR family members of unknown function have only ...
1-204 1.75e-03

atypical (a) SDRs, subgroup 6; These atypical SDR family members of unknown function have only a partial match to a prototypical glycine-rich NAD(P)-binding motif consensus, GXXG, which conserves part of the motif of extended SDR. Furthermore, they lack the characteristic active site residues of the SDRs. This subgroup is related to phenylcoumaran benzylic ether reductase, an NADPH-dependent aromatic alcohol reductase. One member is identified as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187577 [Multi-domain]  Cd Length: 203  Bit Score: 38.49  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   1 MKILITGGAGHVGRTLRRELA--GRFELVRIFDMVA--AEPIGPNEESVVGDIADIAAVENATRGMDAVIhlaaepneap 76
Cdd:cd05267     1 KKVLILGANGEIAREATTMLLenSNVELTLFLRNAHrlLHLKSARVTVVEGDALNSDDLKAAMRGQDVVY---------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189  77 fgiilqANVVG------TWNVYEAARRCGAKRVI--------------FGSSNHA-VGFYPRSQRINETVPVKPDSRYGL 135
Cdd:cd05267    71 ------ANLGGtdldqqAENVVQAMKAVGVKRLIwttslgiydevpgkFGEWNKEfIGNYLAPYRKSAAVIENSDLDYTL 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189 136 SKCwgeavaQLYADKYGVKSLLLRIGNA-AATPGSARAlaiwvsgrdLAQLVTIGLEHPDIHCNVVYGVS 204
Cdd:cd05267   145 LRP------AWLTNNDEIDYELTPKGEAfKGTEVSRKS---------VADLITDIINHPDYHVRESIGIN 199
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
4-108 2.39e-03

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


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 38.89  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360496189   4 LITGGAGHVGRTLRRELAGRFelVRIFDMVAAEPIGPNEES-----------------VVGDIADIAAVENATRGM---- 62
Cdd:cd08953   209 LVTGGAGGIGRALARALARRY--GARLVLLGRSPLPPEEEWkaqtlaalealgarvlyISADVTDAAAVRRLLEKVrery 286
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1360496189  63 ---DAVIHLAAEPNEAP--------FGIILQANVVGTWNVYEAARRCGAKRVIFGSS 108
Cdd:cd08953   287 gaiDGVIHAAGVLRDALlaqktaedFEAVLAPKVDGLLNLAQALADEPLDFFVLFSS 343
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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