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Conserved domains on  [gi|515756120|ref|WP_017188720|]
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Gfo/Idh/MocA family protein [Vibrio harveyi]

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];
1-256 5.56e-65

Predicted dehydrogenase [General function prediction only];


:

Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 206.70  E-value: 5.56e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515756120   1 MFKLAVIGTNWISQQFVEAALQTKEFCLQAVYSRDVEKACEFGKPYNAQsYYDSLEALGADNDIDAVYIASPNSLHAPQA 80
Cdd:COG0673    3 KLRVGIIGAGGIGRAHAPALAALPGVELVAVADRDPERAEAFAEEYGVR-VYTDYEELLADPDIDAVVIATPNHLHAELA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515756120  81 MQMLKAGKHVICEKPMASNYPLAQAMFKTAEENNVVLFEAFMSPYTPNFQVLKDSL--PAIAPLRHATISYCQYSSRyqk 158
Cdd:COG0673   82 IAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIdsGAIGEIRSVRARFGHPRPA--- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515756120 159 ylnGENPNTFNPEF-SNGSIMDIGYYCVGSAIELFG-EPNSIEASAHIL---PSGVDGCGSVTLAY-DGFNVNLLHSKVS 232
Cdd:COG0673  159 ---GPADWRFDPELaGGGALLDLGIHDIDLARWLLGsEPESVSATGGRLvpdRVEVDDTAAATLRFaNGAVATLEASWVA 235
                        250       260
                 ....*....|....*....|....*..
gi 515756120 233 DSLIPS---EFQGEQGSVLVDMIATGR 256
Cdd:COG0673  236 PGGERDerlEVYGTKGTLFVDAIRGGE 262
 
Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-256 5.56e-65

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 206.70  E-value: 5.56e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515756120   1 MFKLAVIGTNWISQQFVEAALQTKEFCLQAVYSRDVEKACEFGKPYNAQsYYDSLEALGADNDIDAVYIASPNSLHAPQA 80
Cdd:COG0673    3 KLRVGIIGAGGIGRAHAPALAALPGVELVAVADRDPERAEAFAEEYGVR-VYTDYEELLADPDIDAVVIATPNHLHAELA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515756120  81 MQMLKAGKHVICEKPMASNYPLAQAMFKTAEENNVVLFEAFMSPYTPNFQVLKDSL--PAIAPLRHATISYCQYSSRyqk 158
Cdd:COG0673   82 IAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIdsGAIGEIRSVRARFGHPRPA--- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515756120 159 ylnGENPNTFNPEF-SNGSIMDIGYYCVGSAIELFG-EPNSIEASAHIL---PSGVDGCGSVTLAY-DGFNVNLLHSKVS 232
Cdd:COG0673  159 ---GPADWRFDPELaGGGALLDLGIHDIDLARWLLGsEPESVSATGGRLvpdRVEVDDTAAATLRFaNGAVATLEASWVA 235
                        250       260
                 ....*....|....*....|....*..
gi 515756120 233 DSLIPS---EFQGEQGSVLVDMIATGR 256
Cdd:COG0673  236 PGGERDerlEVYGTKGTLFVDAIRGGE 262
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
2-121 2.03e-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: 114.23  E-value: 2.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515756120    2 FKLAVIGTNWISQQFVEAALQTKEFC-LQAVYSRDVEKACEFGKPYNAqSYYDSLEALGADNDIDAVYIASPNSLHAPQA 80
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNASQPGAeLVAILDPNSERAEAVAESFGV-EVYSDLEELLNDPEIDAVIVATPNGLHYDLA 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 515756120   81 MQMLKAGKHVICEKPMASNYPLAQAMFKTAEENNVVLFEAF 121
Cdd:pfam01408  80 IAALEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
1-134 8.38e-23

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: 96.52  E-value: 8.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515756120    1 MFKLAVIGTNWISQqfVEA---ALQTKEFCLQAVYSRDVEKACEFGKPYNAQSYYDSLEALGADNDIDAVYIASPNSLHA 77
Cdd:TIGR04380   1 KLKVGIIGAGRIGK--VHAenlATHVPGARLKAIVDPFADAAAELAEKLGIEPVTQDPEAALADPEIDAVLIASPTDTHA 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 515756120   78 PQAMQMLKAGKHVICEKPMASNYPLAQAMFKTAEENNVVLFEAFMSPYTPNFQVLKD 134
Cdd:TIGR04380  79 DLIIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKLQIGFNRRFDPNFRRVKQ 135
PRK11579 PRK11579
putative oxidoreductase; Provisional
28-229 5.80e-08

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 53.57  E-value: 5.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515756120  28 LQAVYSRDVEKAcefGKPYNAQSYYDSLEALGADNDIDAVYIASPNSLHAPQAMQMLKAGKHVICEKPMASNYPLAQAMF 107
Cdd:PRK11579  32 LAAVSSSDATKV---KADWPTVTVVSEPQHLFNDPNIDLIVIPTPNDTHFPLAKAALEAGKHVVVDKPFTVTLSQARELD 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515756120 108 KTAEENNVVLFEAFMSPYTPNFQVLKdSLpaIAPLRHATISYcqYSSRYQKylngenpntFNPEFSN----------GSI 177
Cdd:PRK11579 109 ALAKSAGRVLSVFHNRRWDSDFLTLK-AL--LAEGVLGEVAY--FESHFDR---------FRPQVRQrwreqggpgsGIW 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 515756120 178 MDIGYYCVGSAIELFGEPNSIEASAHILPSGVDGCG--SVTLAYDGFNVnLLHS 229
Cdd:PRK11579 175 YDLAPHLLDQAIQLFGLPVSITVDLAQLRPGAQSTDyfHAILSYPQRRV-VLHG 227
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
3-117 2.19e-06

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: 46.77  E-value: 2.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515756120   3 KLAVIGTNWISQQFVEAALQTKEFCLQAVYSRDVEKAcefGKPYNAQSY--------YDSLEALGADNDIDAVYIASPNS 74
Cdd:cd24146    2 RVVVWGLGAMGRGIARYLLEKPGLEIVGAVDRDPAKV---GKDLGELGGgaplgvkvTDDLDAVLAATKPDVVVHATTSF 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 515756120  75 LH--APQAMQMLKAGKHVI--CEK---PMASNYPLAQAMFKTAEENNVVL 117
Cdd:cd24146   79 LAdvAPQIERLLEAGLNVIttCEElfyPWARDPELAEELDALAKENGVTV 128
 
Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-256 5.56e-65

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 206.70  E-value: 5.56e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515756120   1 MFKLAVIGTNWISQQFVEAALQTKEFCLQAVYSRDVEKACEFGKPYNAQsYYDSLEALGADNDIDAVYIASPNSLHAPQA 80
Cdd:COG0673    3 KLRVGIIGAGGIGRAHAPALAALPGVELVAVADRDPERAEAFAEEYGVR-VYTDYEELLADPDIDAVVIATPNHLHAELA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515756120  81 MQMLKAGKHVICEKPMASNYPLAQAMFKTAEENNVVLFEAFMSPYTPNFQVLKDSL--PAIAPLRHATISYCQYSSRyqk 158
Cdd:COG0673   82 IAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIdsGAIGEIRSVRARFGHPRPA--- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515756120 159 ylnGENPNTFNPEF-SNGSIMDIGYYCVGSAIELFG-EPNSIEASAHIL---PSGVDGCGSVTLAY-DGFNVNLLHSKVS 232
Cdd:COG0673  159 ---GPADWRFDPELaGGGALLDLGIHDIDLARWLLGsEPESVSATGGRLvpdRVEVDDTAAATLRFaNGAVATLEASWVA 235
                        250       260
                 ....*....|....*....|....*..
gi 515756120 233 DSLIPS---EFQGEQGSVLVDMIATGR 256
Cdd:COG0673  236 PGGERDerlEVYGTKGTLFVDAIRGGE 262
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
2-121 2.03e-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: 114.23  E-value: 2.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515756120    2 FKLAVIGTNWISQQFVEAALQTKEFC-LQAVYSRDVEKACEFGKPYNAqSYYDSLEALGADNDIDAVYIASPNSLHAPQA 80
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNASQPGAeLVAILDPNSERAEAVAESFGV-EVYSDLEELLNDPEIDAVIVATPNGLHYDLA 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 515756120   81 MQMLKAGKHVICEKPMASNYPLAQAMFKTAEENNVVLFEAF 121
Cdd:pfam01408  80 IAALEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
1-134 8.38e-23

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: 96.52  E-value: 8.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515756120    1 MFKLAVIGTNWISQqfVEA---ALQTKEFCLQAVYSRDVEKACEFGKPYNAQSYYDSLEALGADNDIDAVYIASPNSLHA 77
Cdd:TIGR04380   1 KLKVGIIGAGRIGK--VHAenlATHVPGARLKAIVDPFADAAAELAEKLGIEPVTQDPEAALADPEIDAVLIASPTDTHA 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 515756120   78 PQAMQMLKAGKHVICEKPMASNYPLAQAMFKTAEENNVVLFEAFMSPYTPNFQVLKD 134
Cdd:TIGR04380  79 DLIIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKLQIGFNRRFDPNFRRVKQ 135
PRK11579 PRK11579
putative oxidoreductase; Provisional
28-229 5.80e-08

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 53.57  E-value: 5.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515756120  28 LQAVYSRDVEKAcefGKPYNAQSYYDSLEALGADNDIDAVYIASPNSLHAPQAMQMLKAGKHVICEKPMASNYPLAQAMF 107
Cdd:PRK11579  32 LAAVSSSDATKV---KADWPTVTVVSEPQHLFNDPNIDLIVIPTPNDTHFPLAKAALEAGKHVVVDKPFTVTLSQARELD 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515756120 108 KTAEENNVVLFEAFMSPYTPNFQVLKdSLpaIAPLRHATISYcqYSSRYQKylngenpntFNPEFSN----------GSI 177
Cdd:PRK11579 109 ALAKSAGRVLSVFHNRRWDSDFLTLK-AL--LAEGVLGEVAY--FESHFDR---------FRPQVRQrwreqggpgsGIW 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 515756120 178 MDIGYYCVGSAIELFGEPNSIEASAHILPSGVDGCG--SVTLAYDGFNVnLLHS 229
Cdd:PRK11579 175 YDLAPHLLDQAIQLFGLPVSITVDLAQLRPGAQSTDyfHAILSYPQRRV-VLHG 227
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
3-117 2.19e-06

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: 46.77  E-value: 2.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515756120   3 KLAVIGTNWISQQFVEAALQTKEFCLQAVYSRDVEKAcefGKPYNAQSY--------YDSLEALGADNDIDAVYIASPNS 74
Cdd:cd24146    2 RVVVWGLGAMGRGIARYLLEKPGLEIVGAVDRDPAKV---GKDLGELGGgaplgvkvTDDLDAVLAATKPDVVVHATTSF 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 515756120  75 LH--APQAMQMLKAGKHVI--CEK---PMASNYPLAQAMFKTAEENNVVL 117
Cdd:cd24146   79 LAdvAPQIERLLEAGLNVIttCEElfyPWARDPELAEELDALAKENGVTV 128
 
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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