A0A3V1N9X2 · A0A3V1N9X2_SALET
- Protein4-hydroxy-2-oxo-heptane-1,7-dioate aldolase
- GenehpaI
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids263 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the reversible retro-aldol cleavage of 4-hydroxy-2-ketoheptane-1,7-dioate (HKHD) to pyruvate and succinic semialdehyde.
Catalytic activity
- 4-hydroxy-2-oxoheptanedioate = pyruvate + succinate semialdehyde
Cofactor
Note: Binds 1 divalent metal cation per subunit.
Pathway
Aromatic compound metabolism; 4-hydroxyphenylacetate degradation; pyruvate and succinate semialdehyde from 4-hydroxyphenylacetate: step 7/7.
Features
Showing features for active site, site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 45 | Proton acceptor | ||||
Sequence: H | ||||||
Site | 70 | Transition state stabilizer | ||||
Sequence: R | ||||||
Site | 84 | Increases basicity of active site His | ||||
Sequence: D | ||||||
Binding site | 147 | substrate | ||||
Sequence: Q | ||||||
Binding site | 149 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 174 | substrate | ||||
Sequence: A | ||||||
Binding site | 175 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 175 | substrate | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 2,4-dihydroxyhept-2-ene-1,7-dioate aldolase activity | |
Molecular Function | aldehyde-lyase activity | |
Molecular Function | metal ion binding | |
Biological Process | phenylacetate catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name4-hydroxy-2-oxo-heptane-1,7-dioate aldolase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Salmonella
Accessions
- Primary accessionA0A3V1N9X2
Proteomes
Interaction
Subunit
Homohexamer; trimer of dimers.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 15-240 | HpcH/HpaI aldolase/citrate lyase | ||||
Sequence: QIGLWLGLANSYSAELLAGAGFDWLLIDGEHAPNNVQTVLTQLQAIAPYPSQPVVRPSWNDPVQIKQLLDVGAQTLLIPMVQNADEARNAVAATRYPPAGIRGVGSALARASRWNRIPDYLHLANDAMCVLVQIETREAMSNLASILDVDGIDGVFIGPADLSADMGFAGNPQHPEVQAAIENAIVQIRAAGKAPGILMANEALAKRYLELGALFVAVGVDTTLLA |
Sequence similarities
Belongs to the HpcH/HpaI aldolase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length263
- Mass (Da)27,758
- Last updated2019-12-11 v1
- Checksum52CC25BC0244BBB9
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AAIYPR010000006 EMBL· GenBank· DDBJ | ECJ5164795.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAKIYB010000006 EMBL· GenBank· DDBJ | ECS2351704.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAKTCM010000003 EMBL· GenBank· DDBJ | ECV1971136.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAAODK010000001 EMBL· GenBank· DDBJ | HAD2565895.1 EMBL· GenBank· DDBJ | Genomic DNA |