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Conserved domains on  [gi|1944548179|ref|WP_197812817|]
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Gfo/Idh/MocA family oxidoreductase [Serratia marcescens]

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];
1-373 2.25e-80

Predicted dehydrogenase [General function prediction only];


:

Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 247.91  E-value: 2.25e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944548179   1 MKQVRVGLIGTGYIGRCHAIAYAQAPtvfplkgDLVLEMLAEVTPELAAQRAAEFGfARSTGDWRQLVADPAIDVVDICA 80
Cdd:COG0673     1 MDKLRVGIIGAGGIGRAHAPALAALP-------GVELVAVADRDPERAEAFAEEYG-VRVYTDYEELLADPDIDAVVIAT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944548179  81 PNFLHKEMALEAIRHGKHVYSEKPLALDAADAAEMVQAARAKGVKTLVGFNYMKNPTSQLAREIIANGEIGEVVHFYGTH 160
Cdd:COG0673    73 PNHLHAELAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944548179 161 NEDYladPRTPIDWHCRRASAGLGALGDLAAHIVNMAHYLVG-DIVAVSGDMQTVIKQRpdpqdpsrmhpVENEDQASAL 239
Cdd:COG0673   153 GHPR---PAGPADWRFDPELAGGGALLDLGIHDIDLARWLLGsEPESVSATGGRLVPDR-----------VEVDDTAAAT 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944548179 240 LRFAGGAMGTIETSRIACGRKMGLTYVVTGTKGTLsytqermaelklyrhdepverqgfktllvgpkhpdyaafcisagh 319
Cdd:COG0673   219 LRFANGAVATLEASWVAPGGERDERLEVYGTKGTL--------------------------------------------- 253
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1944548179 320 gigfndqktveirdLVNGIAAGDRMWPDFEEGWKVSCVLDAIAASAEQRCWLEI 373
Cdd:COG0673   254 --------------FVDAIRGGEPPPVSLEDGLRALELAEAAYESARTGRRVEL 293
 
Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-373 2.25e-80

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 247.91  E-value: 2.25e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944548179   1 MKQVRVGLIGTGYIGRCHAIAYAQAPtvfplkgDLVLEMLAEVTPELAAQRAAEFGfARSTGDWRQLVADPAIDVVDICA 80
Cdd:COG0673     1 MDKLRVGIIGAGGIGRAHAPALAALP-------GVELVAVADRDPERAEAFAEEYG-VRVYTDYEELLADPDIDAVVIAT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944548179  81 PNFLHKEMALEAIRHGKHVYSEKPLALDAADAAEMVQAARAKGVKTLVGFNYMKNPTSQLAREIIANGEIGEVVHFYGTH 160
Cdd:COG0673    73 PNHLHAELAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944548179 161 NEDYladPRTPIDWHCRRASAGLGALGDLAAHIVNMAHYLVG-DIVAVSGDMQTVIKQRpdpqdpsrmhpVENEDQASAL 239
Cdd:COG0673   153 GHPR---PAGPADWRFDPELAGGGALLDLGIHDIDLARWLLGsEPESVSATGGRLVPDR-----------VEVDDTAAAT 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944548179 240 LRFAGGAMGTIETSRIACGRKMGLTYVVTGTKGTLsytqermaelklyrhdepverqgfktllvgpkhpdyaafcisagh 319
Cdd:COG0673   219 LRFANGAVATLEASWVAPGGERDERLEVYGTKGTL--------------------------------------------- 253
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1944548179 320 gigfndqktveirdLVNGIAAGDRMWPDFEEGWKVSCVLDAIAASAEQRCWLEI 373
Cdd:COG0673   254 --------------FVDAIRGGEPPPVSLEDGLRALELAEAAYESARTGRRVEL 293
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
3-256 2.49e-30

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: 118.48  E-value: 2.49e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944548179   3 QVRVGLIGTGYIGRCHAIAYAqapTVFPlkgDLVLEMLAEVTPELAAQRAAEFGFARSTGDWRQLVADPAIDVVDICAPN 82
Cdd:TIGR04380   1 KLKVGIIGAGRIGKVHAENLA---THVP---GARLKAIVDPFADAAAELAEKLGIEPVTQDPEAALADPEIDAVLIASPT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944548179  83 FLHKEMALEAIRHGKHVYSEKPLALDAADAAEMVQAARAKGVKTLVGFNYMKNPTSQLAREIIANGEIGEVVHFYGTHNe 162
Cdd:TIGR04380  75 DTHADLIIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKLQIGFNRRFDPNFRRVKQLVEAGKIGKPEILRITSR- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944548179 163 dylaDPRTPIDWHCrRASAGLGAlgDLAAHIVNMAHYLVGDIV----AVSGDMqtvikqrpdpqdpsrMHPVENE----D 234
Cdd:TIGR04380 154 ----DPAPPPVAYV-KVSGGLFL--DMTIHDFDMARFLLGSEVeevyAQGSVL---------------VDPAIGEagdvD 211
                         250       260
                  ....*....|....*....|..
gi 1944548179 235 QASALLRFAGGAMGTIETSRIA 256
Cdd:TIGR04380 212 TAVITLKFENGAIAVIDNSRRA 233
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
4-130 1.25e-22

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: 91.89  E-value: 1.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944548179   4 VRVGLIGTGYIGRCHAIAYAQAPtvfplkGDLVLEMLAEVTPELAAQRAAEFGfARSTGDWRQLVADPAIDVVDICAPNF 83
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNASQ------PGAELVAILDPNSERAEAVAESFG-VEVYSDLEELLNDPEIDAVIVATPNG 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1944548179  84 LHKEMALEAIRHGKHVYSEKPLALDAADAAEMVQAARAKGVKTLVGF 130
Cdd:pfam01408  74 LHYDLAIAALEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
PRK11579 PRK11579
putative oxidoreductase; Provisional
4-276 4.88e-14

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 72.44  E-value: 4.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944548179   4 VRVGLIGTGYIGRC-HAIAYAQAPTVfplkgdlvleMLAEVTPELAAQRAAEFGFARSTGDWRQLVADPAIDVVDICAPN 82
Cdd:PRK11579    5 IRVGLIGYGYASKTfHAPLIAGTPGL----------ELAAVSSSDATKVKADWPTVTVVSEPQHLFNDPNIDLIVIPTPN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944548179  83 FLHKEMALEAIRHGKHVYSEKPLALDAADAAEMVQAARAKGVKTLVGFNYMKNPTSQLAREIIANGEIGEVVHFyGTHNE 162
Cdd:PRK11579   75 DTHFPLAKAALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVLSVFHNRRWDSDFLTLKALLAEGVLGEVAYF-ESHFD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944548179 163 DYlaDPRTPIDWHcRRASAGLGALGDLAAHIVNMAHYLVGDIVAVSGDMQTVikqRPDPQDPSRMHPVENEDQASALLRf 242
Cdd:PRK11579  154 RF--RPQVRQRWR-EQGGPGSGIWYDLAPHLLDQAIQLFGLPVSITVDLAQL---RPGAQSTDYFHAILSYPQRRVVLH- 226
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1944548179 243 aGGAMGTIETSRiacgrkmgltYVVTGTKGtlSY 276
Cdd:PRK11579  227 -GTMLAAAESAR----------YIVHGSRG--SY 247
 
Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-373 2.25e-80

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 247.91  E-value: 2.25e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944548179   1 MKQVRVGLIGTGYIGRCHAIAYAQAPtvfplkgDLVLEMLAEVTPELAAQRAAEFGfARSTGDWRQLVADPAIDVVDICA 80
Cdd:COG0673     1 MDKLRVGIIGAGGIGRAHAPALAALP-------GVELVAVADRDPERAEAFAEEYG-VRVYTDYEELLADPDIDAVVIAT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944548179  81 PNFLHKEMALEAIRHGKHVYSEKPLALDAADAAEMVQAARAKGVKTLVGFNYMKNPTSQLAREIIANGEIGEVVHFYGTH 160
Cdd:COG0673    73 PNHLHAELAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944548179 161 NEDYladPRTPIDWHCRRASAGLGALGDLAAHIVNMAHYLVG-DIVAVSGDMQTVIKQRpdpqdpsrmhpVENEDQASAL 239
Cdd:COG0673   153 GHPR---PAGPADWRFDPELAGGGALLDLGIHDIDLARWLLGsEPESVSATGGRLVPDR-----------VEVDDTAAAT 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944548179 240 LRFAGGAMGTIETSRIACGRKMGLTYVVTGTKGTLsytqermaelklyrhdepverqgfktllvgpkhpdyaafcisagh 319
Cdd:COG0673   219 LRFANGAVATLEASWVAPGGERDERLEVYGTKGTL--------------------------------------------- 253
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1944548179 320 gigfndqktveirdLVNGIAAGDRMWPDFEEGWKVSCVLDAIAASAEQRCWLEI 373
Cdd:COG0673   254 --------------FVDAIRGGEPPPVSLEDGLRALELAEAAYESARTGRRVEL 293
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
3-256 2.49e-30

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: 118.48  E-value: 2.49e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944548179   3 QVRVGLIGTGYIGRCHAIAYAqapTVFPlkgDLVLEMLAEVTPELAAQRAAEFGFARSTGDWRQLVADPAIDVVDICAPN 82
Cdd:TIGR04380   1 KLKVGIIGAGRIGKVHAENLA---THVP---GARLKAIVDPFADAAAELAEKLGIEPVTQDPEAALADPEIDAVLIASPT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944548179  83 FLHKEMALEAIRHGKHVYSEKPLALDAADAAEMVQAARAKGVKTLVGFNYMKNPTSQLAREIIANGEIGEVVHFYGTHNe 162
Cdd:TIGR04380  75 DTHADLIIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKLQIGFNRRFDPNFRRVKQLVEAGKIGKPEILRITSR- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944548179 163 dylaDPRTPIDWHCrRASAGLGAlgDLAAHIVNMAHYLVGDIV----AVSGDMqtvikqrpdpqdpsrMHPVENE----D 234
Cdd:TIGR04380 154 ----DPAPPPVAYV-KVSGGLFL--DMTIHDFDMARFLLGSEVeevyAQGSVL---------------VDPAIGEagdvD 211
                         250       260
                  ....*....|....*....|..
gi 1944548179 235 QASALLRFAGGAMGTIETSRIA 256
Cdd:TIGR04380 212 TAVITLKFENGAIAVIDNSRRA 233
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
4-130 1.25e-22

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: 91.89  E-value: 1.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944548179   4 VRVGLIGTGYIGRCHAIAYAQAPtvfplkGDLVLEMLAEVTPELAAQRAAEFGfARSTGDWRQLVADPAIDVVDICAPNF 83
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNASQ------PGAELVAILDPNSERAEAVAESFG-VEVYSDLEELLNDPEIDAVIVATPNG 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1944548179  84 LHKEMALEAIRHGKHVYSEKPLALDAADAAEMVQAARAKGVKTLVGF 130
Cdd:pfam01408  74 LHYDLAIAALEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
GFO_IDH_MocA_C pfam02894
Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or ...
142-373 1.29e-16

Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 427044  Cd Length: 203  Bit Score: 77.46  E-value: 1.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944548179 142 REIIANGEIGEVVhFYGTHNEDYLADPRTPIDWHCRRASAGlGALGDLAAHIVNMAHYLVGDIVAVSgdmqTVIKQrpdp 221
Cdd:pfam02894   1 KELIENGVLGEVV-MVTVHTRDPFRPPQEFKRWRVDPEKSG-GALYDLGIHTIDLLIYLFGEPPSVV----AVYAS---- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944548179 222 qdpsrmhpvenEDQASALLRFAGGAMGTIETSRIACGRKMGLTYVVTGTKGTLSYTQERMAELKLYRHDEPVERQGFKTL 301
Cdd:pfam02894  71 -----------EDTAFATLEFKNGAVGTLETSGGSIVEANGHRISIHGTKGSIELDGIDDGLLSVTVVGEPGWATDDPMV 139
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1944548179 302 LVGPKH-PDYAAfcisaghgiGFNDQKTVEIRDLVNGIAAGDRMWPDFEEGWKVSCVLDAIAASAEQRCWLEI 373
Cdd:pfam02894 140 RKGGDEvPEFLG---------SFAGGYLLEYDAFLEAVRGGKVVLVDAEDGLYALAVIEAAYESAEEGRPVKL 203
PRK11579 PRK11579
putative oxidoreductase; Provisional
4-276 4.88e-14

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 72.44  E-value: 4.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944548179   4 VRVGLIGTGYIGRC-HAIAYAQAPTVfplkgdlvleMLAEVTPELAAQRAAEFGFARSTGDWRQLVADPAIDVVDICAPN 82
Cdd:PRK11579    5 IRVGLIGYGYASKTfHAPLIAGTPGL----------ELAAVSSSDATKVKADWPTVTVVSEPQHLFNDPNIDLIVIPTPN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944548179  83 FLHKEMALEAIRHGKHVYSEKPLALDAADAAEMVQAARAKGVKTLVGFNYMKNPTSQLAREIIANGEIGEVVHFyGTHNE 162
Cdd:PRK11579   75 DTHFPLAKAALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVLSVFHNRRWDSDFLTLKALLAEGVLGEVAYF-ESHFD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944548179 163 DYlaDPRTPIDWHcRRASAGLGALGDLAAHIVNMAHYLVGDIVAVSGDMQTVikqRPDPQDPSRMHPVENEDQASALLRf 242
Cdd:PRK11579  154 RF--RPQVRQRWR-EQGGPGSGIWYDLAPHLLDQAIQLFGLPVSITVDLAQL---RPGAQSTDYFHAILSYPQRRVVLH- 226
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1944548179 243 aGGAMGTIETSRiacgrkmgltYVVTGTKGtlSY 276
Cdd:PRK11579  227 -GTMLAAAESAR----------YIVHGSRG--SY 247
PRK10206 PRK10206
putative oxidoreductase; Provisional
45-223 7.85e-06

putative oxidoreductase; Provisional


Pssm-ID: 182305 [Multi-domain]  Cd Length: 344  Bit Score: 47.51  E-value: 7.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944548179  45 PELAAQRAAEFGFarsTGDWRQLVADPAIDVVDICAPNFLHKEMALEAIRHGKHVYSEKPLALDAADAAEMVQAARAKGV 124
Cdd:PRK10206   40 PEEQAPIYSHIHF---TSDLDEVLNDPDVKLVVVCTHADSHFEYAKRALEAGKNVLVEKPFTPTLAEAKELFALAKSKGL 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944548179 125 kTLVGFNYMKNPTSQL-AREIIANGEIGEVV----HFygthneDYL-----ADPRTPIDwhcrrasaglGALGDLAAHIV 194
Cdd:PRK10206  117 -TVTPYQNRRFDSCFLtAKKAIESGKLGEIVevesHF------DYYrpvaeTKPGLPQD----------GAFYGLGVHTM 179
                         170       180
                  ....*....|....*....|....*....
gi 1944548179 195 NMAHYLVGDIVAVSGDMQTvIKQRPDPQD 223
Cdd:PRK10206  180 DQIISLFGRPDHVAYDIRS-LRNKANPDD 207
COG4091 COG4091
Predicted homoserine dehydrogenase, contains C-terminal SAF domain [Amino acid transport and ...
2-99 2.68e-05

Predicted homoserine dehydrogenase, contains C-terminal SAF domain [Amino acid transport and metabolism];


Pssm-ID: 443267 [Multi-domain]  Cd Length: 429  Bit Score: 45.91  E-value: 2.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944548179   2 KQVRVGLIGTGYIGRCHAiayAQAPTVfplKGdLVLEMLAEVTPELAAQRAAEFGFARS--------------------- 60
Cdd:COG4091    14 RPIRVGLIGAGQMGRGLL---AQIRRM---PG-MEVVAIADRNPERARAALREAGIPEEdirvvdtaaeadaaiaagktv 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1944548179  61 -TGDWRQLVADPAIDVVdICA---PNFLHKeMALEAIRHGKHV 99
Cdd:COG4091    87 vTDDAELLIAADGIDVV-VEAtgvPEAGAR-HALAAIEAGKHV 127
NAD_binding_3 pfam03447
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. ...
46-128 2.76e-05

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: 43.06  E-value: 2.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944548179  46 ELAAQRAAEFGFARSTGDWRQLVADPAIDVVDICAPNFLHKEMALEAIRHGKHVYS-EKPLALDAADAAEMVQAARAKGV 124
Cdd:pfam03447  32 LLSKDPLALLPDEPLTLDLDDLIAHPDPDVVVECASSEAVAELVLDALKAGKDVVTaSKGALADLALYEELREAAEANGA 111

                  ....
gi 1944548179 125 KTLV 128
Cdd:pfam03447 112 RIYV 115
 
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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