HAMAP rule MF_01169
General rule information
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PURL | https://purl.expasy.org/hamap/rule/MF_01169 |
Accession | MF_01169 |
Dates | 17-DEC-2005 (Created)
17-DEC-2024 (Last updated, Version 19) |
Name | SucA_OdhA |
Scope(s) |
Bacteria Bacillales Brucellaceae Leptospiraceae |
Template(s) | P23129 (ODO1_BACSU); [ Recover all ] |
Triggered by |
HAMAP; MF_01169 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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Identifier | ODO1 |
Protein name | RecName: Full=2-oxoglutarate dehydrogenase E1 component; EC=1.2.4.2; AltName: Full=Alpha-ketoglutarate dehydrogenase; |
case <OC:Bacillota> | |
Gene name | Name=odhA; |
end case | |
case not <OC:Bacillota> | |
Gene name | Name=sucA; Synonyms=odhA; |
end case |
Comments
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FUNCTION | E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2). |
CATALYTIC ACTIVITY | Reaction=N(6)-[(R)-lipoyl]-L-lysyl-[protein] + 2-oxoglutarate + H(+) = N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[protein] + CO2; Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:20092, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:83099, ChEBI:CHEBI:83120; EC=1.2.4.2; |
COFACTOR | Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; |
SUBUNIT | Homodimer. Part of the 2-oxoglutarate dehydrogenase (OGDH) complex composed of E1 (2-oxoglutarate dehydrogenase), E2 (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide dehydrogenase); the complex contains multiple copies of the three enzymatic components (E1, E2 and E3). |
SIMILARITY | Belongs to the alpha-ketoglutarate dehydrogenase family. |
Keywords
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Gene Ontology
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GO:0004591; Molecular function:oxoglutarate dehydrogenase (succinyl-transferring) activity |
GO:0030976; Molecular function:thiamine pyrophosphate binding |
GO:0006096; Biological process:glycolytic process |
Cross-references
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Features
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Additional information
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Size range | 910-1004 amino acids |
Related rules |
None |
Fusion | Nter: None Cter: None |
Comments | This family is restricted taxonomically to some bacteria so as to avoid overlap with proteins that have similarity to alpha-ketoglutarate dehydrogenase but may be a different enzyme. |