AC MF_00850; DC Protein; auto TR HAMAP; MF_00850; -; 1; level=0 XX Names: POX XX ID POXB DE RecName: Full=Pyruvate dehydrogenase [ubiquinone]; DE EC=1.2.5.1; DE AltName: Full=Pyruvate oxidase; DE Short=POX; DE AltName: Full=Pyruvate:ubiquinone-8 oxidoreductase; GN Name=poxB; XX CC -!- FUNCTION: A peripheral cell membrane enzyme that catalyzes the CC oxidative decarboxylation of pyruvate to form acetate and CO(2). It CC channels electrons from the cytoplasm to the respiratory chain at the CC cell membrane via ubiquinone. CC -!- CATALYTIC ACTIVITY: CC Reaction=a ubiquinone + H2O + pyruvate = a ubiquinol + acetate + CO2; CC Xref=Rhea:RHEA:27405, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:16389, CC ChEBI:CHEBI:16526, ChEBI:CHEBI:17976, ChEBI:CHEBI:30089; EC=1.2.5.1; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Note=Binds 1 FAD per subunit.; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Note=Binds 1 Mg(2+) ion per subunit.; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Note=Binds 1 thiamine pyrophosphate per subunit.; CC -!- ACTIVITY REGULATION: The C-terminus inhibits activity; it has to move CC for the enzyme to be active. Activated by lipid-binding, which occurs CC via the C-terminus. CC -!- SUBUNIT: Homotetramer. case not defined or CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; CC Cytoplasmic side. else case CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; CC Cytoplasmic side. end case CC -!- DOMAIN: Has 4 domains; the Pyr domain which binds the pyrimidine moiety CC of the thiamine pyrophosphate cofactor, the FAD-binding domain, the PP- CC binding domain which binds the pyrophosphate portion of thiamine CC pyrophosphate and the C-terminal membrane binding region. The C- CC terminus is held closely against the rest of the protein and covers the CC active site; during activation it unfolds from the rest of the protein CC and forms an amphipathic helix upon membrane binding, exposing the CC active site. CC -!- SIMILARITY: Belongs to the TPP enzyme family. XX DR PROSITE; PS00187; TPP_ENZYMES; 1; trigger=no DR Pfam; PF02775; TPP_enzyme_C; 1; trigger=no DR Pfam; PF00205; TPP_enzyme_M; 1; trigger=no DR Pfam; PF02776; TPP_enzyme_N; 1; trigger=no DR General; Coiled_coil; -; 0-unlimited; trigger=yes XX case defined and KW Cell inner membrane end case KW Cell membrane KW FAD KW Flavoprotein KW Lipid-binding KW Magnesium KW Membrane KW Metal-binding KW Nucleotide-binding KW Oxidoreductase KW Pyruvate KW Thiamine pyrophosphate KW Ubiquinone XX GO GO:0005886; C:plasma membrane GO GO:0050660; F:flavin adenine dinucleotide binding GO GO:0008289; F:lipid binding GO GO:0000287; F:magnesium ion binding GO GO:0052737; F:pyruvate dehydrogenase (quinone) activity GO GO:0030976; F:thiamine pyrophosphate binding GO GO:0042867; P:pyruvate catabolic process GO GO:0048039; F:ubiquinone binding XX FT From: POXB_ECOLI (P07003) FT BINDING 251..254 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT Condition: T-G-L-[IL] FT BINDING 274..278 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT Condition: [TS]-x-[FL]-P-[YF] FT REGION 1..182 FT /note="Pyr domain" FT REGION 183..334 FT /note="FAD-binding domain" FT REGION 335..530 FT /note="PP-binding domain" FT BINDING 406..408 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT Condition: [GA]-[ST]-M FT BINDING 433..435 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT Condition: D-G-G FT BINDING 460..466 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT REGION 531..572 FT /note="Membrane-binding domain" FT BINDING 433 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Condition: D FT BINDING 460 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Condition: N FT BINDING 50 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT Condition: E FT BINDING 292 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT Condition: D FT SITE 465 FT /note="Moves into active site upon enzyme activation, plays FT a role in electron transfer" FT Condition: F XX Size: 528-616; Related: None; Template: P07003; Scope: Bacteria Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.5 2022/11/19 //