A0A7J7EPE3 · A0A7J7EPE3_DICBM
- ProteinDelta-aminolevulinic acid dehydratase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids325 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen.
Catalytic activity
- 2 5-aminolevulinate = porphobilinogen + 2 H2O + H+
Pathway
Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 122 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 124 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 131 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 132 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Active site | 199 | Schiff-base intermediate with substrate | ||||
Sequence: K | ||||||
Binding site | 223 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Active site | 252 | Schiff-base intermediate with substrate | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | porphobilinogen synthase activity | |
Molecular Function | zinc ion binding | |
Biological Process | protoporphyrinogen IX biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDelta-aminolevulinic acid dehydratase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Perissodactyla > Rhinocerotidae > Diceros
Accessions
- Primary accessionA0A7J7EPE3
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Homooctamer; active form. Homohexamer; low activity form.
Structure
Sequence
- Sequence statusComplete
- Length325
- Mass (Da)35,349
- Last updated2021-04-07 v1
- Checksum4FEB869572C1395C
Keywords
- Technical term