N9Z0C5 · N9Z0C5_9FIRM
- ProteinHistidine biosynthesis bifunctional protein HisIE
- GenehisI
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids437 (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
Including 2 domains:
- Recommended namePhosphoribosyl-AMP cyclohydrolase
- EC number
- Short namesPRA-CH
- Recommended namePhosphoribosyl-ATP pyrophosphatase
- EC number
- Short namesPRA-PH
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Lachnospirales > Lachnospiraceae > Enterocloster
Accessions
- Primary accessionN9Z0C5
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-350 | Phosphoribosyl-AMP cyclohydrolase | ||||
Sequence: MTDCKKLIMGFGYRNGKTFSWNGKLEYEGGLKELARTACDNGADEIFICDRSFSDEDHEAVIGAIKETARTVDEPILAGGRIRRLEDVKKYLYAGASAVFLDVSYEDNVDMMKEAADRFGSEKIYAYMPDLSYLNRVEEYIQLGASVMICRASGPVLSLAELGEIGEISCRSLIFCGGHENVQEMAGDLKLSLGCPQVEGAVLTLAEDNLDKVMELKQILKGAGIVTDTFESSLEWKNFKLGSDGLIPVIVQDYKTLEVLMMAYMNEESFQATLASGRMTYFSRSRQKLWLKGETSGHFQYVKSLKIDCDNDTILASVKQVGAACHTGNRSCFFTTLAEKEYKETNPLKV | ||||||
Domain | 261-334 | Phosphoribosyl-AMP cyclohydrolase | ||||
Sequence: MMAYMNEESFQATLASGRMTYFSRSRQKLWLKGETSGHFQYVKSLKIDCDNDTILASVKQVGAACHTGNRSCFF | ||||||
Region | 351-437 | Phosphoribosyl-ATP pyrophosphohydrolase | ||||
Sequence: FEEVFGVILDRKEHPKEGSYTNYLFDKGIDKILKKLGEEATEIVIAAKNPNPEEIKYEISDFLYHMMVLMADRGITWEEITEELANR |
Sequence similarities
Belongs to the HisA/HisF family.
In the C-terminal section; belongs to the PRA-PH family.
In the N-terminal section; belongs to the PRA-CH family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length437
- Mass (Da)49,041
- Last updated2013-06-26 v1
- Checksum910468DA030CCC48
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AGYG01000030 EMBL· GenBank· DDBJ | ENZ33135.1 EMBL· GenBank· DDBJ | Genomic DNA |