A0A2W4M849 · A0A2W4M849_UNCPS
- ProteinPQQ-dependent dehydrogenase, methanol/ethanol family
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids679 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 Ca2+ ion per subunit.
Note: Binds 1 heme c group per subunit.
Note: Binds 1 PQQ group per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 63 | pyrroloquinoline quinone (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 115 | pyrroloquinoline quinone (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 159 | pyrroloquinoline quinone (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 175-176 | pyrroloquinoline quinone (UniProtKB | ChEBI) | ||||
Sequence: GA | ||||||
Binding site | 233 | pyrroloquinoline quinone (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 253 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Active site | 298 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 298 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 325 | pyrroloquinoline quinone (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 385-386 | pyrroloquinoline quinone (UniProtKB | ChEBI) | ||||
Sequence: NW | ||||||
Binding site | 601 | heme c (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 604 | heme c (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 605 | Fe (UniProtKB | ChEBI) of heme c (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 644 | Fe (UniProtKB | ChEBI) of heme c (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: M |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Cellular Component | outer membrane-bounded periplasmic space | |
Molecular Function | calcium ion binding | |
Molecular Function | electron transfer activity | |
Molecular Function | heme binding | |
Molecular Function | oxidoreductase activity, acting on CH-OH group of donors |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota
Accessions
- Primary accessionA0A2W4M849
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Disulfide bond | 109↔110 | |||||
Sequence: CC |
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-34 | Disordered | ||||
Sequence: PAPPPTLPGAASREADPPHTAWPTPGRPDPGQRY | ||||||
Domain | 588-667 | Cytochrome c | ||||
Sequence: GNVLTGIRRYNQYCIMCHGRGAQSGPLMPDLRHSEAILEADAFGAIVLEGRLEAAGMAGFADVLSRADAEAIRAYLVWEA |
Sequence similarities
Belongs to the bacterial PQQ dehydrogenase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusFragment
- Length679
- Mass (Da)73,890
- Last updated2018-09-12 v1
- Checksum1036B61EFD529286
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: P |