S0DFG8 · S0DFG8_9ZZZZ
- ProteinHistidine biosynthesis bifunctional protein HisIE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids216 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Pathway
Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | phosphoribosyl-AMP cyclohydrolase activity | |
Molecular Function | phosphoribosyl-ATP diphosphatase activity | |
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 HisIE
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageunclassified sequences > metagenomes > organismal metagenomes
Accessions
- Primary accessionS0DFG8
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 30-102 | Phosphoribosyl-AMP cyclohydrolase | |||
Sequence similarities
In the C-terminal section; belongs to the PRA-PH family.
In the N-terminal section; belongs to the PRA-CH family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length216
- Mass (Da)24,167
- Last updated2013-09-18 v1
- Checksum0E55ACF58C3AD892
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
HF548275 EMBL· GenBank· DDBJ | CCO20910.1 EMBL· GenBank· DDBJ | Genomic DNA |