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Conserved domains on  [gi|302394273|gb|ADL33178|]
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oxidoreductase GFO/IDH/MOCA family [Butyrivibrio proteoclasticus B316]

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];
1-242 3.25e-20

Predicted dehydrogenase [General function prediction only];


:

Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 88.83  E-value: 3.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302394273   1 MNVVVIGLGSMGKRRIRLIKALyPEYTVYGV-DSREDRRNVAKEELGVDSFESVD-LLQN--VDCAFVCTSPLSHAAIIR 76
Cdd:COG0673    4 LRVGIIGAGGIGRAHAPALAAL-PGVELVAVaDRDPERAEAFAEEYGVRVYTDYEeLLADpdIDAVVIATPNHLHAELAI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302394273  77 DCLSKKWNVFTE----INLvdDGYDDNIELARNNGCKLFLSSTFLYRDETRYIRSKVDD-------SCKWNYVYHIGQYL 145
Cdd:COG0673   83 AALEAGKHVLCEkplaLTL--EEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSgaigeirSVRARFGHPRPAGP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302394273 146 PDWHPWENYKDyfVGNKRTNGCREI-LAIelpWLvetFGN-VNKYSAVADRITALGIDYDDNYAIQLLHENGNKGLLMVD 223
Cdd:COG0673  161 ADWRFDPELAG--GGALLDLGIHDIdLAR---WL---LGSePESVSATGGRLVPDRVEVDDTAAATLRFANGAVATLEAS 232
                        250       260
                 ....*....|....*....|..
gi 302394273 224 VVSPVAVRK--FEAY-SEGKYL 242
Cdd:COG0673  233 WVAPGGERDerLEVYgTKGTLF 254
 
Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-242 3.25e-20

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 88.83  E-value: 3.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302394273   1 MNVVVIGLGSMGKRRIRLIKALyPEYTVYGV-DSREDRRNVAKEELGVDSFESVD-LLQN--VDCAFVCTSPLSHAAIIR 76
Cdd:COG0673    4 LRVGIIGAGGIGRAHAPALAAL-PGVELVAVaDRDPERAEAFAEEYGVRVYTDYEeLLADpdIDAVVIATPNHLHAELAI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302394273  77 DCLSKKWNVFTE----INLvdDGYDDNIELARNNGCKLFLSSTFLYRDETRYIRSKVDD-------SCKWNYVYHIGQYL 145
Cdd:COG0673   83 AALEAGKHVLCEkplaLTL--EEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSgaigeirSVRARFGHPRPAGP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302394273 146 PDWHPWENYKDyfVGNKRTNGCREI-LAIelpWLvetFGN-VNKYSAVADRITALGIDYDDNYAIQLLHENGNKGLLMVD 223
Cdd:COG0673  161 ADWRFDPELAG--GGALLDLGIHDIdLAR---WL---LGSePESVSATGGRLVPDRVEVDDTAAATLRFANGAVATLEAS 232
                        250       260
                 ....*....|....*....|..
gi 302394273 224 VVSPVAVRK--FEAY-SEGKYL 242
Cdd:COG0673  233 WVAPGGERDerLEVYgTKGTLF 254
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
1-111 1.44e-11

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: 60.69  E-value: 1.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302394273    1 MNVVVIGLGSMGKRRIRLIKALYPEYTVYGV-DSREDRRNVAKEELGVDSFESVDLL---QNVDCAFVCTSPLSHAAIIR 76
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNASQPGAELVAIlDPNSERAEAVAESFGVEVYSDLEELlndPEIDAVIVATPNGLHYDLAI 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 302394273   77 DCLSKKWNVFTE--INL-VDDGyDDNIELARNNGCKLF 111
Cdd:pfam01408  81 AALEAGKHVLCEkpLATtVEEA-KELVELAKKKGVRVS 117
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
1-87 6.82e-05

N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) and similar proteins; The family corresponds to a group of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) that catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. nat-AmDHs can naturally catalyze the amination of 'neutral' carbonyl compounds using ammonia. They possess tremendous potential for the efficient asymmetric synthesis of alpha-chiral amines. The family also contains 2,4-diaminopentanoate dehydrogenase (DAPDH) and similar proteins. DAPDH, also known as ORD, is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). Although DAPDH is more efficient with (2R,4S)-DAP, the diastereoisomer (2R,4R)-DAP can also be metabolized. Different forms of DAPDH exist which utilize NAD(+) (EC 1.4.1.26) or NAD(+)/NADP(+) (EC 1.4.1.12). Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.


Pssm-ID: 467616 [Multi-domain]  Cd Length: 157  Bit Score: 42.53  E-value: 6.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302394273   1 MNVVVIGLGSMGKRRIRLIkALYPEYTVYG-VDSREDRRNVAKEELG---------VDSFESVDLLQNVDCAFVCT-SPL 69
Cdd:cd24146    1 IRVVVWGLGAMGRGIARYL-LEKPGLEIVGaVDRDPAKVGKDLGELGggaplgvkvTDDLDAVLAATKPDVVVHATtSFL 79
                         90
                 ....*....|....*....
gi 302394273  70 SHAAI-IRDCLSKKWNVFT 87
Cdd:cd24146   80 ADVAPqIERLLEAGLNVIT 98
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
1-68 4.93e-04

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 40.90  E-value: 4.93e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302394273   1 MNVVVIGLGSMGKRRIR-LIKALYPEYTVYGVDSREDRRNVAKEELGVDSFES-VDLLQNVDCAFVCTSP 68
Cdd:PRK11880   3 KKIGFIGGGNMASAIIGgLLASGVPAKDIIVSDPSPEKRAALAEEYGVRAATDnQEAAQEADVVVLAVKP 72
 
Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-242 3.25e-20

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 88.83  E-value: 3.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302394273   1 MNVVVIGLGSMGKRRIRLIKALyPEYTVYGV-DSREDRRNVAKEELGVDSFESVD-LLQN--VDCAFVCTSPLSHAAIIR 76
Cdd:COG0673    4 LRVGIIGAGGIGRAHAPALAAL-PGVELVAVaDRDPERAEAFAEEYGVRVYTDYEeLLADpdIDAVVIATPNHLHAELAI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302394273  77 DCLSKKWNVFTE----INLvdDGYDDNIELARNNGCKLFLSSTFLYRDETRYIRSKVDD-------SCKWNYVYHIGQYL 145
Cdd:COG0673   83 AALEAGKHVLCEkplaLTL--EEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSgaigeirSVRARFGHPRPAGP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302394273 146 PDWHPWENYKDyfVGNKRTNGCREI-LAIelpWLvetFGN-VNKYSAVADRITALGIDYDDNYAIQLLHENGNKGLLMVD 223
Cdd:COG0673  161 ADWRFDPELAG--GGALLDLGIHDIdLAR---WL---LGSePESVSATGGRLVPDRVEVDDTAAATLRFANGAVATLEAS 232
                        250       260
                 ....*....|....*....|..
gi 302394273 224 VVSPVAVRK--FEAY-SEGKYL 242
Cdd:COG0673  233 WVAPGGERDerLEVYgTKGTLF 254
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
1-111 1.44e-11

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: 60.69  E-value: 1.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302394273    1 MNVVVIGLGSMGKRRIRLIKALYPEYTVYGV-DSREDRRNVAKEELGVDSFESVDLL---QNVDCAFVCTSPLSHAAIIR 76
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNASQPGAELVAIlDPNSERAEAVAESFGVEVYSDLEELlndPEIDAVIVATPNGLHYDLAI 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 302394273   77 DCLSKKWNVFTE--INL-VDDGyDDNIELARNNGCKLF 111
Cdd:pfam01408  81 AALEAGKHVLCEkpLATtVEEA-KELVELAKKKGVRVS 117
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
1-66 5.56e-06

Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440056 [Multi-domain]  Cd Length: 278  Bit Score: 47.04  E-value: 5.56e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 302394273   1 MNVVVIGLG----SMGKRrirlIKALYPEYTVYGVDSREDRRNVAKeELGV-DSFES--VDLLQNVDCAFVCT 66
Cdd:COG0287    2 MRIAIIGLGliggSLALA----LKRAGLAHEVVGVDRSPETLERAL-ELGViDRAATdlEEAVADADLVVLAV 69
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
1-78 3.56e-05

Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 440114 [Multi-domain]  Cd Length: 267  Bit Score: 44.67  E-value: 3.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302394273   1 MNVVVIGLGSMGKRRIR-LIKALYPEYTVYGVDSREDRRNVAKEELGVDSFES-VDLLQNVDCAFVCTSPLSHAAIIRDC 78
Cdd:COG0345    3 MKIGFIGAGNMGSAIIKgLLKSGVPPEDIIVSDRSPERLEALAERYGVRVTTDnAEAAAQADVVVLAVKPQDLAEVLEEL 82
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
1-87 6.82e-05

N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) and similar proteins; The family corresponds to a group of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) that catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. nat-AmDHs can naturally catalyze the amination of 'neutral' carbonyl compounds using ammonia. They possess tremendous potential for the efficient asymmetric synthesis of alpha-chiral amines. The family also contains 2,4-diaminopentanoate dehydrogenase (DAPDH) and similar proteins. DAPDH, also known as ORD, is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). Although DAPDH is more efficient with (2R,4S)-DAP, the diastereoisomer (2R,4R)-DAP can also be metabolized. Different forms of DAPDH exist which utilize NAD(+) (EC 1.4.1.26) or NAD(+)/NADP(+) (EC 1.4.1.12). Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.


Pssm-ID: 467616 [Multi-domain]  Cd Length: 157  Bit Score: 42.53  E-value: 6.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302394273   1 MNVVVIGLGSMGKRRIRLIkALYPEYTVYG-VDSREDRRNVAKEELG---------VDSFESVDLLQNVDCAFVCT-SPL 69
Cdd:cd24146    1 IRVVVWGLGAMGRGIARYL-LEKPGLEIVGaVDRDPAKVGKDLGELGggaplgvkvTDDLDAVLAATKPDVVVHATtSFL 79
                         90
                 ....*....|....*....
gi 302394273  70 SHAAI-IRDCLSKKWNVFT 87
Cdd:cd24146   80 ADVAPqIERLLEAGLNVIT 98
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
1-68 4.93e-04

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 40.90  E-value: 4.93e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302394273   1 MNVVVIGLGSMGKRRIR-LIKALYPEYTVYGVDSREDRRNVAKEELGVDSFES-VDLLQNVDCAFVCTSP 68
Cdd:PRK11880   3 KKIGFIGGGNMASAIIGgLLASGVPAKDIIVSDPSPEKRAALAEEYGVRAATDnQEAAQEADVVVLAVKP 72
PRK08507 PRK08507
prephenate dehydrogenase; Validated
1-64 4.28e-03

prephenate dehydrogenase; Validated


Pssm-ID: 181452 [Multi-domain]  Cd Length: 275  Bit Score: 38.34  E-value: 4.28e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 302394273   1 MNVVVIGLGSMGKRRIRLIKALYPEYTVYGVDSREDRRNVAKeELG-VDSFESVDLLQNVDCAFV 64
Cdd:PRK08507   1 MKIGIIGLGLMGGSLGLALKEKGLISKVYGYDHNELHLKKAL-ELGlVDEIVSFEELKKCDVIFL 64
 
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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