P77324 · PAOB_ECOLI
- ProteinAldehyde oxidoreductase FAD-binding subunit PaoB
- GenepaoB
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids318 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Oxidizes aldehydes to the corresponding carboxylic acids with a preference for aromatic aldehydes. It might play a role in the detoxification of aldehydes to avoid cell damage.
Catalytic activity
- A + an aldehyde + H2O = a carboxylate + AH2 + H+
Cofactor
Protein has several cofactor binding sites:
Activity regulation
The complex requires PaoD for activity.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 26-34 | FAD (UniProtKB | ChEBI) | ||||
Sequence: KFIAGGTNL | ||||||
Binding site | 108 | FAD (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 119 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 129 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 138 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 157 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 164 | FAD (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 213 | FAD (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 230 | FAD (UniProtKB | ChEBI) | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | outer membrane-bounded periplasmic space | |
Cellular Component | oxidoreductase complex | |
Cellular Component | periplasmic space | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | carboxylate reductase activity | |
Molecular Function | FAD binding | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | metal ion binding | |
Molecular Function | oxidoreductase activity, acting on the aldehyde or oxo group of donors | |
Biological Process | catabolic process | |
Biological Process | cellular detoxification of aldehyde |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAldehyde oxidoreductase FAD-binding subunit PaoB
- EC number
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP77324
- Secondary accessions
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000166094 | 1-318 | Aldehyde oxidoreductase FAD-binding subunit PaoB | |||
Sequence: MKAFTYERVNTPAEAALSAQRVPGAKFIAGGTNLLDLMKLEIETPTHLIDVNGLGLDKIEVTDAGGLRIGALVRNTDLAAHERVRRDYAVLSRALLAGASGQLRNQATTAGNLLQRTRCPYFYDTNQPCNKRLPGSGCAALEGFSRQHAVVGVSEACIATHPSDMAVAMRLLDAVVETITPEGKTRSITLADFYHPPGKTPHIETALLPGELIVAVTLPPPLGGKHIYRKVRDRASYAFALVSVAAIIQPDGSGRVALGGVAHKPWRIEAADAQLSQGAQAVYDTLFASAHPTAENTFKLLLAKRTLASVLAEARAQA |
Proteomic databases
Interaction
Subunit
Heterotrimer composed of PaoA, PaoB and PaoC.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-223 | FAD-binding PCMH-type | ||||
Sequence: MKAFTYERVNTPAEAALSAQRVPGAKFIAGGTNLLDLMKLEIETPTHLIDVNGLGLDKIEVTDAGGLRIGALVRNTDLAAHERVRRDYAVLSRALLAGASGQLRNQATTAGNLLQRTRCPYFYDTNQPCNKRLPGSGCAALEGFSRQHAVVGVSEACIATHPSDMAVAMRLLDAVVETITPEGKTRSITLADFYHPPGKTPHIETALLPGELIVAVTLPPPLG |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length318
- Mass (Da)33,858
- Last updated1997-02-01 v1
- Checksum7D51C2B30C9BB222
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U73857 EMBL· GenBank· DDBJ | AAB18014.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC73388.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAE76069.1 EMBL· GenBank· DDBJ | Genomic DNA |