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Conserved domains on  [gi|2181801755|ref|WP_235424152|]
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Gfo/Idh/MocA family protein [Citrobacter koseri]

Protein Classification

Gfo/Idh/MocA family protein( domain architecture ID 11430574)

Gfo/Idh/MocA family protein belonging to the NAD(P)(+)-binding Rossmann-fold superfamily, may function as an oxidoreductase that catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-338 3.34e-71

Predicted dehydrogenase [General function prediction only];


:

Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 223.26  E-value: 3.34e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181801755   1 MNKIRAAVVGAGIYGKHHMNAYRHNPDTVLVAICDTVTERCDDLAMAYDVMGYTRLDVLLQEEAIDVLSVATPDPYHTES 80
Cdd:COG0673     1 MDKLRVGIIGAGGIGRAHAPALAALPGVELVAVADRDPERAEAFAEEYGVRVYTDYEELLADPDIDAVVIATPNHLHAEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181801755  81 ILTALRHGKHVLAEKPLATSVRECELIVEMAQQRDLLVGVDFHKRWDPAVMRIKAELEKPEAGRILRGHISMDDVISV-P 159
Cdd:COG0673    81 AIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRPAgP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181801755 160 TEW-LDWAGASS-PVWFLGSHCFDLVRHLSGQEVMSVYAVGQKRlmVECGLDTFDSVQSLLTMADGSSWVVENSWVLPEG 237
Cdd:COG0673   161 ADWrFDPELAGGgALLDLGIHDIDLARWLLGSEPESVSATGGRL--VPDRVEVDDTAAATLRFANGAVATLEASWVAPGG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181801755 238 FpkdNDGRIDILCEATYIrstsqhrgleittpgmtltpnsyfinyrngvasgfgidpindFVRAVIHKAPYPVTAVDGLA 317
Cdd:COG0673   239 E---RDERLEVYGTKGTL------------------------------------------FVDAIRGGEPPPVSLEDGLR 273
                         330       340
                  ....*....|....*....|.
gi 2181801755 318 VSRICEAVHQSLESQKPVLLK 338
Cdd:COG0673   274 ALELAEAAYESARTGRRVELP 294
 
Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-338 3.34e-71

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 223.26  E-value: 3.34e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181801755   1 MNKIRAAVVGAGIYGKHHMNAYRHNPDTVLVAICDTVTERCDDLAMAYDVMGYTRLDVLLQEEAIDVLSVATPDPYHTES 80
Cdd:COG0673     1 MDKLRVGIIGAGGIGRAHAPALAALPGVELVAVADRDPERAEAFAEEYGVRVYTDYEELLADPDIDAVVIATPNHLHAEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181801755  81 ILTALRHGKHVLAEKPLATSVRECELIVEMAQQRDLLVGVDFHKRWDPAVMRIKAELEKPEAGRILRGHISMDDVISV-P 159
Cdd:COG0673    81 AIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRPAgP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181801755 160 TEW-LDWAGASS-PVWFLGSHCFDLVRHLSGQEVMSVYAVGQKRlmVECGLDTFDSVQSLLTMADGSSWVVENSWVLPEG 237
Cdd:COG0673   161 ADWrFDPELAGGgALLDLGIHDIDLARWLLGSEPESVSATGGRL--VPDRVEVDDTAAATLRFANGAVATLEASWVAPGG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181801755 238 FpkdNDGRIDILCEATYIrstsqhrgleittpgmtltpnsyfinyrngvasgfgidpindFVRAVIHKAPYPVTAVDGLA 317
Cdd:COG0673   239 E---RDERLEVYGTKGTL------------------------------------------FVDAIRGGEPPPVSLEDGLR 273
                         330       340
                  ....*....|....*....|.
gi 2181801755 318 VSRICEAVHQSLESQKPVLLK 338
Cdd:COG0673   274 ALELAEAAYESARTGRRVELP 294
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
3-335 5.74e-39

inositol 2-dehydrogenase; All members of the seed alignment for this model are known or predicted inositol 2-dehydrogenase sequences co-clustered with other enzymes for catabolism of myo-inositol or closely related compounds. Inositol 2-dehydrogenase catalyzes the first step in inositol catabolism. Members of this family may vary somewhat in their ranges of acceptable substrates and some may act on analogs to myo-inositol rather than myo-inositol per se. [Energy metabolism, Sugars]


Pssm-ID: 275173 [Multi-domain]  Cd Length: 330  Bit Score: 140.43  E-value: 5.74e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181801755   3 KIRAAVVGAGIYGK-HHMNAYRHNPDTVLVAICDTVTERCDDLAMAYDVM-GYTRLDVLLQEEAIDVLSVATPDPYHTES 80
Cdd:TIGR04380   1 KLKVGIIGAGRIGKvHAENLATHVPGARLKAIVDPFADAAAELAEKLGIEpVTQDPEAALADPEIDAVLIASPTDTHADL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181801755  81 ILTALRHGKHVLAEKPLATSVRECELIVEMAQQRDLLVGVDFHKRWDPAVMRIKAELEKPEAGRILRGHISMDDVISVPT 160
Cdd:TIGR04380  81 IIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKLQIGFNRRFDPNFRRVKQLVEAGKIGKPEILRITSRDPAPPPV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181801755 161 EWLdwagASSPVWFL--GSHCFDLVRHLSGQEVMSVYAVG----QKRLMvECGLdtFDSVQSLLTMADGSSWVVENSWVL 234
Cdd:TIGR04380 161 AYV----KVSGGLFLdmTIHDFDMARFLLGSEVEEVYAQGsvlvDPAIG-EAGD--VDTAVITLKFENGAIAVIDNSRRA 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181801755 235 PEGFpkdnDGRIDIL-----------CEATYIRSTSQhrGLEITTPgMTLTPNSYFINYRNgvasgfgidPINDFVRAVI 303
Cdd:TIGR04380 234 AYGY----DQRVEVFgskgmlraendTESTVILYDAE--GVRGDKP-LNFFLERYRDAYRA---------EIQAFVDAIL 297
                         330       340       350
                  ....*....|....*....|....*....|..
gi 2181801755 304 HKAPYPVTAVDGLAVSRICEAVHQSLESQKPV 335
Cdd:TIGR04380 298 EGRPPPVTGEDGLKALLLALAAKRSLEEGRPV 329
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
4-122 4.68e-31

Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 426248 [Multi-domain]  Cd Length: 120  Bit Score: 113.46  E-value: 4.68e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181801755   4 IRAAVVGAGIYGKHHMNAYRHN-PDTVLVAICDTVTERCDDLAMAYDVMGYTRLDVLLQEEAIDVLSVATPDPYHTESIL 82
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNASqPGAELVAILDPNSERAEAVAESFGVEVYSDLEELLNDPEIDAVIVATPNGLHYDLAI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2181801755  83 TALRHGKHVLAEKPLATSVRECELIVEMAQQRDLLVGVDF 122
Cdd:pfam01408  81 AALEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
PRK11579 PRK11579
putative oxidoreductase; Provisional
59-201 1.37e-09

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 58.58  E-value: 1.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181801755  59 LLQEEAIDVLSVATPDPYHTESILTALRHGKHVLAEKPLATSVRECELIVEMAQQRDLLVGVdFH-KRWDPAVMRIKAEL 137
Cdd:PRK11579   59 LFNDPNIDLIVIPTPNDTHFPLAKAALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVLSV-FHnRRWDSDFLTLKALL 137
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2181801755 138 EKPEAGRILRGHISMDDV-ISVPTEWLDWAGASSPVWF-LGSHCFDLVRHLSGQEVMSVYAVGQKR 201
Cdd:PRK11579  138 AEGVLGEVAYFESHFDRFrPQVRQRWREQGGPGSGIWYdLAPHLLDQAIQLFGLPVSITVDLAQLR 203
 
Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-338 3.34e-71

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 223.26  E-value: 3.34e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181801755   1 MNKIRAAVVGAGIYGKHHMNAYRHNPDTVLVAICDTVTERCDDLAMAYDVMGYTRLDVLLQEEAIDVLSVATPDPYHTES 80
Cdd:COG0673     1 MDKLRVGIIGAGGIGRAHAPALAALPGVELVAVADRDPERAEAFAEEYGVRVYTDYEELLADPDIDAVVIATPNHLHAEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181801755  81 ILTALRHGKHVLAEKPLATSVRECELIVEMAQQRDLLVGVDFHKRWDPAVMRIKAELEKPEAGRILRGHISMDDVISV-P 159
Cdd:COG0673    81 AIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRPAgP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181801755 160 TEW-LDWAGASS-PVWFLGSHCFDLVRHLSGQEVMSVYAVGQKRlmVECGLDTFDSVQSLLTMADGSSWVVENSWVLPEG 237
Cdd:COG0673   161 ADWrFDPELAGGgALLDLGIHDIDLARWLLGSEPESVSATGGRL--VPDRVEVDDTAAATLRFANGAVATLEASWVAPGG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181801755 238 FpkdNDGRIDILCEATYIrstsqhrgleittpgmtltpnsyfinyrngvasgfgidpindFVRAVIHKAPYPVTAVDGLA 317
Cdd:COG0673   239 E---RDERLEVYGTKGTL------------------------------------------FVDAIRGGEPPPVSLEDGLR 273
                         330       340
                  ....*....|....*....|.
gi 2181801755 318 VSRICEAVHQSLESQKPVLLK 338
Cdd:COG0673   274 ALELAEAAYESARTGRRVELP 294
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
3-335 5.74e-39

inositol 2-dehydrogenase; All members of the seed alignment for this model are known or predicted inositol 2-dehydrogenase sequences co-clustered with other enzymes for catabolism of myo-inositol or closely related compounds. Inositol 2-dehydrogenase catalyzes the first step in inositol catabolism. Members of this family may vary somewhat in their ranges of acceptable substrates and some may act on analogs to myo-inositol rather than myo-inositol per se. [Energy metabolism, Sugars]


Pssm-ID: 275173 [Multi-domain]  Cd Length: 330  Bit Score: 140.43  E-value: 5.74e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181801755   3 KIRAAVVGAGIYGK-HHMNAYRHNPDTVLVAICDTVTERCDDLAMAYDVM-GYTRLDVLLQEEAIDVLSVATPDPYHTES 80
Cdd:TIGR04380   1 KLKVGIIGAGRIGKvHAENLATHVPGARLKAIVDPFADAAAELAEKLGIEpVTQDPEAALADPEIDAVLIASPTDTHADL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181801755  81 ILTALRHGKHVLAEKPLATSVRECELIVEMAQQRDLLVGVDFHKRWDPAVMRIKAELEKPEAGRILRGHISMDDVISVPT 160
Cdd:TIGR04380  81 IIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKLQIGFNRRFDPNFRRVKQLVEAGKIGKPEILRITSRDPAPPPV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181801755 161 EWLdwagASSPVWFL--GSHCFDLVRHLSGQEVMSVYAVG----QKRLMvECGLdtFDSVQSLLTMADGSSWVVENSWVL 234
Cdd:TIGR04380 161 AYV----KVSGGLFLdmTIHDFDMARFLLGSEVEEVYAQGsvlvDPAIG-EAGD--VDTAVITLKFENGAIAVIDNSRRA 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181801755 235 PEGFpkdnDGRIDIL-----------CEATYIRSTSQhrGLEITTPgMTLTPNSYFINYRNgvasgfgidPINDFVRAVI 303
Cdd:TIGR04380 234 AYGY----DQRVEVFgskgmlraendTESTVILYDAE--GVRGDKP-LNFFLERYRDAYRA---------EIQAFVDAIL 297
                         330       340       350
                  ....*....|....*....|....*....|..
gi 2181801755 304 HKAPYPVTAVDGLAVSRICEAVHQSLESQKPV 335
Cdd:TIGR04380 298 EGRPPPVTGEDGLKALLLALAAKRSLEEGRPV 329
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
4-122 4.68e-31

Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 426248 [Multi-domain]  Cd Length: 120  Bit Score: 113.46  E-value: 4.68e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181801755   4 IRAAVVGAGIYGKHHMNAYRHN-PDTVLVAICDTVTERCDDLAMAYDVMGYTRLDVLLQEEAIDVLSVATPDPYHTESIL 82
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNASqPGAELVAILDPNSERAEAVAESFGVEVYSDLEELLNDPEIDAVIVATPNGLHYDLAI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2181801755  83 TALRHGKHVLAEKPLATSVRECELIVEMAQQRDLLVGVDF 122
Cdd:pfam01408  81 AALEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
PRK11579 PRK11579
putative oxidoreductase; Provisional
59-201 1.37e-09

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 58.58  E-value: 1.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181801755  59 LLQEEAIDVLSVATPDPYHTESILTALRHGKHVLAEKPLATSVRECELIVEMAQQRDLLVGVdFH-KRWDPAVMRIKAEL 137
Cdd:PRK11579   59 LFNDPNIDLIVIPTPNDTHFPLAKAALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVLSV-FHnRRWDSDFLTLKALL 137
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2181801755 138 EKPEAGRILRGHISMDDV-ISVPTEWLDWAGASSPVWF-LGSHCFDLVRHLSGQEVMSVYAVGQKR 201
Cdd:PRK11579  138 AEGVLGEVAYFESHFDRFrPQVRQRWREQGGPGSGIWYdLAPHLLDQAIQLFGLPVSITVDLAQLR 203
PRK10206 PRK10206
putative oxidoreductase; Provisional
54-146 1.71e-06

putative oxidoreductase; Provisional


Pssm-ID: 182305 [Multi-domain]  Cd Length: 344  Bit Score: 49.05  E-value: 1.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181801755  54 TRLDVLLQEEAIDVLSVATPDPYHTESILTALRHGKHVLAEKPLATSVRECELIVEMAQQRDLLVGVDFHKRWDPAVMRI 133
Cdd:PRK10206   54 SDLDEVLNDPDVKLVVVCTHADSHFEYAKRALEAGKNVLVEKPFTPTLAEAKELFALAKSKGLTVTPYQNRRFDSCFLTA 133
                          90
                  ....*....|...
gi 2181801755 134 KAELEKPEAGRIL 146
Cdd:PRK10206  134 KKAIESGKLGEIV 146
NAD_binding_3 pfam03447
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. ...
8-92 2.41e-03

Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. The C-terminal domain of homoserine dehydrogenase contributes a single helix to this structural domain, which is not included in the Pfam model.


Pssm-ID: 281446 [Multi-domain]  Cd Length: 116  Bit Score: 37.28  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181801755   8 VVGAGIYGkhHMNAYRHNPDTVLVAICDTVTERCDDLAMAYDVMGYTRLDVLLQEEAIDVLSVATPDPYHTESILTALRH 87
Cdd:pfam03447   4 AIGSGVLE--QLLRQQSEIPLELVAVADRDLLSKDPLALLPDEPLTLDLDDLIAHPDPDVVVECASSEAVAELVLDALKA 81

                  ....*
gi 2181801755  88 GKHVL 92
Cdd:pfam03447  82 GKDVV 86
 
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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