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HAMAP rule MF_00850
General rule information
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| 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
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Identifier, protein and gene names
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| Identifier | POXB |
| Protein name | RecName: Full=Pyruvate dehydrogenase [ubiquinone]; EC=1.2.5.1; AltName: Full=Pyruvate oxidase; Short=POX; AltName: Full=Pyruvate:ubiquinone-8 oxidoreductase; |
| Gene name | Name=poxB; |
Comments
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| FUNCTION | A 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=1.2.5.1; |
| 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 REGULATION | The C-terminus inhibits activity; it has to move for the enzyme to be active. Activated by lipid-binding, which occurs via the C-terminus. |
| SUBUNIT | Homotetramer. |
| case not defined <Property:Membrane> or <Property:Membrane=1> | |
| SUBCELLULAR LOCATION | Cell membrane; Peripheral membrane protein; Cytoplasmic side. |
| else case <Property:Membrane=2> | |
| SUBCELLULAR LOCATION | Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. |
| end case | |
| DOMAIN | Has 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. |
| SIMILARITY | Belongs to the TPP enzyme family. |
Keywords
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| case defined <Property:Membrane> and <Property:Membrane=2> | |
| Cell inner membrane | |
| end case | |
| Cell membrane | |
| FAD | |
| Flavoprotein | |
| Lipid-binding | |
| Magnesium | |
| Membrane | |
| Metal-binding | |
| Nucleotide-binding | |
| Oxidoreductase | |
| Pyruvate | |
| Thiamine pyrophosphate | |
| Ubiquinone | |
Gene Ontology
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| 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
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| PROSITE | PS00187; TPP_ENZYMES; 1; |
| Pfam | PF02775; TPP_enzyme_C; 1; |
| Pfam | PF00205; TPP_enzyme_M; 1; |
| Pfam | PF02776; TPP_enzyme_N; 1; |
| General | Coiled_coil; -; 0-unlimited; |
Features
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| From: POXB_ECOLI (P07003) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 251 | 254 | /ligand="FAD" /ligand_id="ChEBI:CHEBI:57692" |
T-G-L-[IL] | ||||||||
| BINDING | 274 | 278 | /ligand="FAD" /ligand_id="ChEBI:CHEBI:57692" |
[TS]-x-[FL]-P-[YF] | ||||||||
| 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" /ligand_id="ChEBI:CHEBI:58937" |
[GA]-[ST]-M | ||||||||
| BINDING | 433 | 435 | /ligand="thiamine diphosphate" /ligand_id="ChEBI:CHEBI:58937" |
D-G-G | ||||||||
| BINDING | 460 | 466 | /ligand="thiamine diphosphate" /ligand_id="ChEBI:CHEBI:58937" |
|||||||||
| REGION | 531 | 572 | /note="Membrane-binding domain" | |||||||||
| BINDING | 433 | 433 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" |
D | ||||||||
| BINDING | 460 | 460 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" |
N | ||||||||
| BINDING | 50 | 50 | /ligand="thiamine diphosphate" /ligand_id="ChEBI:CHEBI:58937" |
E | ||||||||
| BINDING | 292 | 292 | /ligand="FAD" /ligand_id="ChEBI:CHEBI:57692" |
D | ||||||||
| SITE | 465 | 465 | /note="Moves into active site upon enzyme activation, plays a role in electron transfer" | F | ||||||||
Additional information
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| Size range | 528-616 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |