P37063 · POXB_LACPL
- ProteinPyruvate oxidase
- Genepox5
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids603 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Important for the aerobic growth. Decarboxylates pyruvate in four steps. The energy released is partially stored in acetyl phosphate.
Catalytic activity
- H+ + O2 + phosphate + pyruvate = acetyl phosphate + CO2 + H2O2
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 FAD per subunit.
Note: Binds 1 Mg2+ ion per subunit.
Note: Binds 1 thiamine pyrophosphate per subunit.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | magnesium ion binding | |
Molecular Function | pyruvate oxidase activity | |
Molecular Function | thiamine pyrophosphate binding |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePyruvate oxidase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Lactobacillaceae > Lactiplantibacillus
Accessions
- Primary accessionP37063
- Secondary accessions
Proteomes
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000090818 | 1-603 | Pyruvate oxidase | |||
Sequence: MVMKQTKQTNILAGAAVIKVLEAWGVDHLYGIPGGSINSIMDALSAERDRIHYIQVRHEEVGAMAAAADAKLTGKIGVCFGSAGPGGTHLMNGLYDAREDHVPVLALIGQFGTTGMNMDTFQEMNENPIYADVADYNVTAVNAATLPHVIDEAIRRAYAHQGVAVVQIPVDLPWQQIPAEDWYASANSYQTPLLPEPDVQAVTRLTQTLLAAERPLIYYGIGARKAGKELEQLSKTLKIPLMSTYPAKGIVADRYPAYLGSANRVAQKPANEALAQADVVLFVGNNYPFAEVSKAFKNTRYFLQIDIDPAKLGKRHKTDIAVLADAQKTLAAILAQVSERESTPWWQANLANVKNWRAYLASLEDKQEGPLQAYQVLRAVNKIAEPDAIYSIDVGDINLNANRHLKLTPSNRHITSNLFATMGVGIPGAIAAKLNYPERQVFNLAGDGGASMTMQDLATQVQYHLPVINVVFTNCQYGFIKDEQEDTNQNDFIGVEFNDIDFSKIADGVHMQAFRVNKIEQLPDVFEQAKAIAQHEPVLIDAVITGDRPLPAEKLRLDSATSSAADIEAFKQRYEAQDLQPLSTYLKQFGLDDLQHQIGQGGF |
Interaction
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-191 | Core | ||||
Sequence: MVMKQTKQTNILAGAAVIKVLEAWGVDHLYGIPGGSINSIMDALSAERDRIHYIQVRHEEVGAMAAAADAKLTGKIGVCFGSAGPGGTHLMNGLYDAREDHVPVLALIGQFGTTGMNMDTFQEMNENPIYADVADYNVTAVNAATLPHVIDEAIRRAYAHQGVAVVQIPVDLPWQQIPAEDWYASANSYQT | ||||||
Region | 192-342 | FAD-binding | ||||
Sequence: PLLPEPDVQAVTRLTQTLLAAERPLIYYGIGARKAGKELEQLSKTLKIPLMSTYPAKGIVADRYPAYLGSANRVAQKPANEALAQADVVLFVGNNYPFAEVSKAFKNTRYFLQIDIDPAKLGKRHKTDIAVLADAQKTLAAILAQVSERES | ||||||
Region | 343-603 | Thiamine pyrophosphate binding | ||||
Sequence: TPWWQANLANVKNWRAYLASLEDKQEGPLQAYQVLRAVNKIAEPDAIYSIDVGDINLNANRHLKLTPSNRHITSNLFATMGVGIPGAIAAKLNYPERQVFNLAGDGGASMTMQDLATQVQYHLPVINVVFTNCQYGFIKDEQEDTNQNDFIGVEFNDIDFSKIADGVHMQAFRVNKIEQLPDVFEQAKAIAQHEPVLIDAVITGDRPLPAEKLRLDSATSSAADIEAFKQRYEAQDLQPLSTYLKQFGLDDLQHQIGQGGF |
Domain
Each monomer is divided into three domains, each of which contains a six-stranded parallel beta sheet surrounded by alpha helices.
Sequence similarities
Belongs to the TPP enzyme family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length603
- Mass (Da)66,111
- Last updated2003-03-25 v3
- Checksum71BEDD006EEB0FBE
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL935263 EMBL· GenBank· DDBJ | CCC80550.1 EMBL· GenBank· DDBJ | Genomic DNA |