HisA
- Description: phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, homologue to HisF
Gene name | hisA |
Synonyms | |
Essential | no |
Product | phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, homologue to HisF |
Function | biosynthesis of histidine |
Metabolic function and regulation of this protein in SubtiPathways: His | |
MW, pI | 26 kDa, 4.842 |
Gene length, protein length | 735 bp, 245 aa |
Immediate neighbours | hisF, hisH |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
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Contents
The gene
Basic information
- Locus tag: BSU34880
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide = 5-((5-phospho-1-deoxyribulos-1-ylamino)methylideneamino)-1-(5-phosphoribosyl)imidazole-4-carboxamide (according to Swiss-Prot)
- Protein family: hisA/hisF family (according to Swiss-Prot)
- Paralogous protein(s): HisF
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- Structure:
- UniProt: O35006
- KEGG entry: [2]
- E.C. number: 5.3.1.16
Additional information
Expression and regulation
- Regulation: repressed by casamino acids PubMed
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Ulrike Mäder, Georg Homuth, Christian Scharf, Knut Büttner, Rüdiger Bode, Michael Hecker
Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability.
J Bacteriol: 2002, 184(15);4288-95
[PubMed:12107147]
[WorldCat.org]
[DOI]
(P p)