O28305 · HEM2_ARCFU
- ProteinDelta-aminolevulinic acid dehydratase
- GenehemB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids322 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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 (By similarity).
Catalytic activity
- 2 5-aminolevulinate = porphobilinogen + 2 H2O + H+
Cofactor
Note: Binds 1 zinc ion per monomer.
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 | 120 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 122 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 130 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Active site | 195 | Schiff-base intermediate with substrate | ||||
Sequence: K | ||||||
Binding site | 205 | 5-aminolevulinate 1 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 217 | 5-aminolevulinate 1 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 233 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 248 | Schiff-base intermediate with substrate | ||||
Sequence: K | ||||||
Binding site | 274 | 5-aminolevulinate 2 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 312 | 5-aminolevulinate 2 (UniProtKB | ChEBI) | ||||
Sequence: Y |
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
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDelta-aminolevulinic acid dehydratase
- EC number
- Short namesALAD; ALADH
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Archaeoglobi > Archaeoglobales > Archaeoglobaceae > Archaeoglobus
Accessions
- Primary accessionO28305
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000140522 | 1-322 | Delta-aminolevulinic acid dehydratase | |||
Sequence: MAEFPKVRMRRLRKANLRWMFREARLSPENLITPIFVDENIKEKKPIESMPDYFRIPLEMVDKEVEECLEKDLRSFILFGIPSYKDETGSSAYDQNGVIQKAVRRIKAEFPDAVIVTDVCLCEYTTHGHCGVVKDGEIVNDETLPIIGKTAVSHAESGADIVAPSGMMDGMVKAIREALDAAGFESTPIMSYSAKYASNFYSPFRDAAESGFKFGDRRGYQMDIHNAREAMREIELDVKEGADIIMVKPALPYLDIIRMVRERFDLPLAAYNVSGEYSMIKAAIKNGWLSEEAIYEVLISIKRAGADLIITYHSKEIAEKLQ |
Proteomic databases
Interaction
Structure
Sequence
- Sequence statusComplete
- Length322
- Mass (Da)36,398
- Last updated1998-01-01 v1
- Checksum5FE684E6B394B509
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE000782 EMBL· GenBank· DDBJ | AAB89292.1 EMBL· GenBank· DDBJ | Genomic DNA |