A0A2V3EIF8 · A0A2V3EIF8_ECOLX
- ProteinHistidine biosynthesis bifunctional protein HisB
- GenehisB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids355 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Cofactor
Protein has several cofactor binding sites:
Pathway
Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 9 | Nucleophile | ||||
Sequence: D | ||||||
Binding site | 9 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 11 | Proton donor | ||||
Sequence: D | ||||||
Binding site | 11 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 93 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 95 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 101 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 103 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 130 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | histidinol-phosphatase activity | |
Molecular Function | imidazoleglycerol-phosphate dehydratase activity | |
Molecular Function | metal ion binding | |
Biological Process | L-histidine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHistidine biosynthesis bifunctional protein HisB
Including 2 domains:
- Recommended nameHistidinol-phosphatase
- EC number
- Recommended nameImidazoleglycerol-phosphate dehydratase
- EC number
- Short namesIGPD
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionA0A2V3EIF8
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-166 | Histidinol-phosphatase | ||||
Sequence: MSQKYLFIDRDGTLISEPPSDFQVDRFDKLAFEPGVIPELLKLQKAGYKLVMITNQDGLGTQSFPQADFDGPHNLMMQIFTSQGVQFDEVLICPHLPADECDCRKPKVKLVERYLAEQAMDRANSYVIGDRATDIQLAENMGINGLRYDRETLNWPMIGEQLTKRD | ||||||
Region | 167-355 | Imidazoleglycerol-phosphate dehydratase | ||||
Sequence: RYAHVVRNTKETQIDVQVWLDREGGSKINTGVGFFDHMLDQIATHGGFRMEINVKGDLYIDDHHTVEDTALALGEALKIALGDKRGICRFGFVLPMDECLARCALDISGRPHLEYKAEFTYQRVGDLSTEMIEHFFRSLSYTMGVTLHLKTKGKNDHHRVESLFKAFGRTLRQAIRVEGDTLPSSKGVL |
Sequence similarities
In the C-terminal section; belongs to the imidazoleglycerol-phosphate dehydratase family.
In the N-terminal section; belongs to the histidinol-phosphatase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length355
- Mass (Da)40,277
- Last updated2018-09-12 v1
- Checksum0A4ECC2941D91DD1