Difference between revisions of "TrpC"
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=Expression and regulation= | =Expression and regulation= | ||
− | + | * '''Operon:''' | |
− | * '''Operon:''' ''[[trpE]]-[[trpD]]-[[trpC]]-[[trpF]]-[[trpB]]-[[trpA]]-[[hisC]]-[[tyrA]]-[[aroE]]'' {{PubMed|3924737}} | + | ** ''[[aroF]]-[[aroB]]-[[aroH]]-[[trpE]]-[[trpD]]-[[trpC]]-[[trpF]]-[[trpB]]-[[trpA]]-[[hisC]]-[[tyrA]]-[[aroE]]'' (according to [http://dbtbs.hgc.jp/COG/prom/trpEDCFBA-hisC-tyrA-aroE.html DBTBS]) |
+ | ** ''[[trpE]]-[[trpD]]-[[trpC]]-[[trpF]]-[[trpB]]-[[trpA]]-[[hisC]]-[[tyrA]]-[[aroE]]'' {{PubMed|3924737}} | ||
* '''[[Sigma factor]]:''' [[SigA]] {{PubMed|6436812}} | * '''[[Sigma factor]]:''' [[SigA]] {{PubMed|6436812}} |
Revision as of 14:51, 1 August 2010
- Description: indole-3-glycerol-phosphate synthase
Gene name | trpC |
Synonyms | |
Essential | no |
Product | indole-3-glycerol-phosphate synthase |
Function | biosynthesis of tryptophan |
Metabolic function and regulation of this protein in SubtiPathways: Phe, Tyr, Trp | |
MW, pI | 27 kDa, 5.535 |
Gene length, protein length | 750 bp, 250 aa |
Immediate neighbours | trpF, trpD |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU22660
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO2 + H2O (according to Swiss-Prot)
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure: 1VC4 (from Thermus thermophilus, 36% identity, 49% similarity)
- UniProt: P03964
- KEGG entry: [3]
- E.C. number: 4.1.1.48
Additional information
Expression and regulation
- Operon:
- 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
Gintaras Deikus, Paul Babitzke, David H Bechhofer
Recycling of a regulatory protein by degradation of the RNA to which it binds.
Proc Natl Acad Sci U S A: 2004, 101(9);2747-51
[PubMed:14976255]
[WorldCat.org]
[DOI]
(P p)
J Otridge, P Gollnick
MtrB from Bacillus subtilis binds specifically to trp leader RNA in a tryptophan-dependent manner.
Proc Natl Acad Sci U S A: 1993, 90(1);128-32
[PubMed:8419914]
[WorldCat.org]
[DOI]
(P p)
P Babitzke, P Gollnick, C Yanofsky
The mtrAB operon of Bacillus subtilis encodes GTP cyclohydrolase I (MtrA), an enzyme involved in folic acid biosynthesis, and MtrB, a regulator of tryptophan biosynthesis.
J Bacteriol: 1992, 174(7);2059-64
[PubMed:1551827]
[WorldCat.org]
[DOI]
(P p)
H Shimotsu, M I Kuroda, C Yanofsky, D J Henner
Novel form of transcription attenuation regulates expression the Bacillus subtilis tryptophan operon.
J Bacteriol: 1986, 166(2);461-71
[PubMed:2422155]
[WorldCat.org]
[DOI]
(P p)
D J Henner, L Band, H Shimotsu
Nucleotide sequence of the Bacillus subtilis tryptophan operon.
Gene: 1985, 34(2-3);169-77
[PubMed:3924737]
[WorldCat.org]
[DOI]
(P p)
H Shimotsu, D J Henner
Characterization of the Bacillus subtilis tryptophan promoter region.
Proc Natl Acad Sci U S A: 1984, 81(20);6315-9
[PubMed:6436812]
[WorldCat.org]
[DOI]
(P p)