P77165 · PAOA_ECOLI
- ProteinAldehyde oxidoreductase iron-sulfur-binding subunit PaoA
- GenepaoA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids229 (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
Note: Binds 2 [2Fe-2S] clusters.
Activity regulation
The complex requires PaoD for activity.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 99 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 104 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 105 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 107 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 119 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 158 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 161 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 208 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 210 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | outer membrane-bounded periplasmic space | |
Cellular Component | oxidoreductase complex | |
Cellular Component | periplasmic space | |
Molecular Function | 2 iron, 2 sulfur cluster binding | |
Molecular Function | carboxylate reductase activity | |
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 iron-sulfur-binding subunit PaoA
- EC number
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP77165
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Mutation results in complete impairment of cell growth in the presence of cinnamaldehyde.
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-53 | Tat-type signal | ||||
Sequence: MSNQGEYPEDNRVGKHEPHDLSLTRRDLIKVSAATAATAVVYPHSTLAASVPA | ||||||
Chain | PRO_0000189414 | 54-229 | Aldehyde oxidoreductase iron-sulfur-binding subunit PaoA | |||
Sequence: ATPAPEIMPLTLKVNGKTEQLEVDTRTTLLDTLRENLHLIGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLGSPDNLHPMQAAFIKHDGFQCGYCTSGQICSSVAVLKEIQDGIPSHVTVDLVSAPETTADEIRERMSGNICRCGAYANILAAIEDAAGEIKS |
Post-translational modification
Exported by the Tat system (PubMed:17218314).
The position of the signal peptide cleavage has not been experimentally proven (Probable)
The position of the signal peptide cleavage has not been experimentally proven (Probable)
Proteomic databases
Interaction
Subunit
Heterotrimer composed of PaoA, PaoB and PaoC.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P77165 | proX P0AFM2 | 2 | EBI-1115563, EBI-1129961 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-21 | Disordered | ||||
Sequence: MSNQGEYPEDNRVGKHEPHDL | ||||||
Domain | 61-137 | 2Fe-2S ferredoxin-type | ||||
Sequence: MPLTLKVNGKTEQLEVDTRTTLLDTLRENLHLIGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGL |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length229
- Mass (Da)24,343
- Last updated1997-02-01 v1
- Checksum216961D7BD21836C
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U73857 EMBL· GenBank· DDBJ | AAB18015.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC73389.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAE76070.1 EMBL· GenBank· DDBJ | Genomic DNA |