Difference between revisions of "HutI"
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Revision as of 14:58, 16 May 2013
- Description: imidazolone-5-propionate hydrolase
Gene name | hutI |
Synonyms | |
Essential | no |
Product | imidazolone-5-propionate hydrolase |
Function | histidine utilization |
Gene expression levels in SubtiExpress: hutI | |
Metabolic function and regulation of this protein in SubtiPathways: His | |
MW, pI | 45 kDa, 5.215 |
Gene length, protein length | 1263 bp, 421 aa |
Immediate neighbours | hutU, hutG |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
CcpA regulon, CodY regulon, HutP regulon
The gene
Basic information
- Locus tag: BSU39370
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate + H2O = N-formimidoyl-L-glutamate + H+ (according to Swiss-Prot)
- Protein family: hutI family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- Structure: 2BB0
- UniProt: P42084
- KEGG entry: [3]
- E.C. number: 3.5.2.7
Additional information
Expression and regulation
- Regulation:
- 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
Reviews
Robert A Bender
Regulation of the histidine utilization (hut) system in bacteria.
Microbiol Mol Biol Rev: 2012, 76(3);565-84
[PubMed:22933560]
[WorldCat.org]
[DOI]
(I p)
Original publications
Yamei Yu, Yu-He Liang, Erik Brostromer, Jun-Min Quan, Santosh Panjikar, Yu-Hui Dong, Xiao-Dong Su
A catalytic mechanism revealed by the crystal structures of the imidazolonepropionase from Bacillus subtilis.
J Biol Chem: 2006, 281(48);36929-36
[PubMed:16990261]
[WorldCat.org]
[DOI]
(P p)
Ken-Ichi Yoshida, Izumi Ishio, Eishi Nagakawa, Yoshiyuki Yamamoto, Mami Yamamoto, Yasutaro Fujita
Systematic study of gene expression and transcription organization in the gntZ-ywaA region of the Bacillus subtilis genome.
Microbiology (Reading): 2000, 146 ( Pt 3);573-579
[PubMed:10746760]
[WorldCat.org]
[DOI]
(P p)
J M Zalieckas, L V Wray, S H Fisher
trans-acting factors affecting carbon catabolite repression of the hut operon in Bacillus subtilis.
J Bacteriol: 1999, 181(9);2883-8
[PubMed:10217782]
[WorldCat.org]
[DOI]
(P p)
S H Fisher, K Rohrer, A E Ferson
Role of CodY in regulation of the Bacillus subtilis hut operon.
J Bacteriol: 1996, 178(13);3779-84
[PubMed:8682780]
[WorldCat.org]
[DOI]
(P p)
L V Wray, S H Fisher
Analysis of Bacillus subtilis hut operon expression indicates that histidine-dependent induction is mediated primarily by transcriptional antitermination and that amino acid repression is mediated by two mechanisms: regulation of transcription initiation and inhibition of histidine transport.
J Bacteriol: 1994, 176(17);5466-73
[PubMed:8071225]
[WorldCat.org]
[DOI]
(P p)