Difference between revisions of "HutU"
Line 29: | Line 29: | ||
<div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | ||
|- | |- | ||
− | |colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=hutU_4043574_4045232_1 Expression at a glance]'''   {{PubMed|22383849}}<br/>[[Image:hutU_expression.png|500px]] | + | |colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=hutU_4043574_4045232_1 Expression at a glance]'''   {{PubMed|22383849}}<br/>[[Image:hutU_expression.png|500px|link=http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU39360]] |
|- | |- | ||
|} | |} |
Revision as of 14:58, 16 May 2013
- Description: urocanase
Gene name | hutU |
Synonyms | |
Essential | no |
Product | urocanase |
Function | histidine utilization |
Gene expression levels in SubtiExpress: hutU | |
Metabolic function and regulation of this protein in SubtiPathways: His | |
MW, pI | 60 kDa, 5.664 |
Gene length, protein length | 1656 bp, 552 aa |
Immediate neighbours | hutH, hutI |
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: BSU39360
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
- A mutation was found in this gene after evolution under relaxed selection for sporulation PubMed
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: 3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate = urocanate + H2O (according to Swiss-Prot)
- Protein family: urocanase 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: 2FKN
- UniProt: P25503
- KEGG entry: [3]
- E.C. number: 4.2.1.49
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
Christopher T Brown, Laura K Fishwick, Binna M Chokshi, Marissa A Cuff, Jay M Jackson, Travis Oglesby, Alison T Rioux, Enrique Rodriguez, Gregory S Stupp, Austin H Trupp, James S Woollcombe-Clarke, Tracy N Wright, William J Zaragoza, Jennifer C Drew, Eric W Triplett, Wayne L Nicholson
Whole-genome sequencing and phenotypic analysis of Bacillus subtilis mutants following evolution under conditions of relaxed selection for sporulation.
Appl Environ Microbiol: 2011, 77(19);6867-77
[PubMed:21821766]
[WorldCat.org]
[DOI]
(I 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)