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HAMAP rule MF_00850

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General rule information [?]

Accession MF_00850
Dates 23-MAR-2020 (Created)
19-NOV-2022 (Last updated, Version 5)
Name POX
Scope(s) Bacteria
Template(s) P07003 (POXB_ECOLI); [ Recover all ]
Triggered by HAMAP; MF_00850 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier POXB
Protein name RecName: Full=Pyruvate dehydrogenase [ubiquinone];
AltName: Full=Pyruvate oxidase;
AltName: Full=Pyruvate:ubiquinone-8 oxidoreductase;
Gene name Name=poxB;

Comments [?]

FUNCTIONA peripheral cell membrane enzyme that catalyzes the oxidative decarboxylation of pyruvate to form acetate and CO(2). It channels electrons from the cytoplasm to the respiratory chain at the cell membrane via ubiquinone.
CATALYTIC ACTIVITY Reaction=a ubiquinone + H2O + pyruvate = a ubiquinol + acetate + CO2; Xref=Rhea:RHEA:27405, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:16389, ChEBI:CHEBI:16526, ChEBI:CHEBI:17976, ChEBI:CHEBI:30089; EC=;
COFACTOR Name=FAD; Xref=ChEBI:CHEBI:57692; Note=Binds 1 FAD per subunit.;
COFACTOR Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) ion per subunit.;
COFACTOR Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Note=Binds 1 thiamine pyrophosphate per subunit.;
ACTIVITY REGULATIONThe C-terminus inhibits activity; it has to move for the enzyme to be active. Activated by lipid-binding, which occurs via the C-terminus.
case not defined <Property:Membrane> or <Property:Membrane=1>
SUBCELLULAR LOCATIONCell membrane; Peripheral membrane protein; Cytoplasmic side.
else case <Property:Membrane=2>
SUBCELLULAR LOCATIONCell inner membrane; Peripheral membrane protein; Cytoplasmic side.
end case
DOMAINHas 4 domains; the Pyr domain which binds the pyrimidine moiety of the thiamine pyrophosphate cofactor, the FAD-binding domain, the PP- binding domain which binds the pyrophosphate portion of thiamine pyrophosphate and the C-terminal membrane binding region. The C- terminus is held closely against the rest of the protein and covers the active site; during activation it unfolds from the rest of the protein and forms an amphipathic helix upon membrane binding, exposing the active site.
SIMILARITYBelongs to the TPP enzyme family.

Keywords [?]

Gene Ontology [?]

GO:0005886; Cellular component:plasma membrane
GO:0050660; Molecular function:flavin adenine dinucleotide binding
GO:0008289; Molecular function:lipid binding
GO:0000287; Molecular function:magnesium ion binding
GO:0052737; Molecular function:pyruvate dehydrogenase (quinone) activity
GO:0030976; Molecular function:thiamine pyrophosphate binding
GO:0042867; Biological process:pyruvate catabolic process
GO:0048039; Molecular function:ubiquinone binding

Cross-references [?]

Pfam PF02775; TPP_enzyme_C; 1;
Pfam PF00205; TPP_enzyme_M; 1;
Pfam PF02776; TPP_enzyme_N; 1;
General Coiled_coil; -; 0-unlimited;

Features [?]

From: POXB_ECOLI (P07003)
Key From To Description Tag Condition FTGroup
BINDING 251 254 /ligand="FAD"
BINDING 274 278 /ligand="FAD"
REGION 1 182 /note="Pyr domain"
REGION 183 334 /note="FAD-binding domain"
REGION 335 530 /note="PP-binding domain"
BINDING 406 408 /ligand="thiamine diphosphate"
BINDING 433 435 /ligand="thiamine diphosphate"
BINDING 460 466 /ligand="thiamine diphosphate"
REGION 531 572 /note="Membrane-binding domain"
BINDING 433 433 /ligand="Mg(2+)"
BINDING 460 460 /ligand="Mg(2+)"
BINDING 50 50 /ligand="thiamine diphosphate"
BINDING 292 292 /ligand="FAD"
SITE 465 465 /note="Moves into active site upon enzyme activation, plays a role in electron transfer" F

Additional information [?]

Size range 528-616 amino acids
Related rules None
Fusion Nter: None Cter: None

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