Difference between revisions of "ThrC"
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=== Database entries === | === Database entries === | ||
| + | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU32250&redirect=T BSU32250] | ||
* '''DBTBS entry:''' no entry | * '''DBTBS entry:''' no entry | ||
| Line 90: | Line 91: | ||
=== Database entries === | === Database entries === | ||
| + | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU32250&redirect=T BSU32250] | ||
* '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1UIN 1UIN] (from ''Thermus thermophilus'', 51% identity, 69% similarity) {{PubMed|12952961}} | * '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1UIN 1UIN] (from ''Thermus thermophilus'', 51% identity, 69% similarity) {{PubMed|12952961}} | ||
Revision as of 14:40, 2 April 2014
- Description: threonine synthase
| Gene name | thrC |
| Synonyms | thrB |
| Essential | no |
| Product | threonine synthase |
| Function | biosynthesis of threonine |
| Gene expression levels in SubtiExpress: thrC | |
| Metabolic function and regulation of this protein in SubtiPathways: thrC | |
| MW, pI | 37 kDa, 5.185 |
| Gene length, protein length | 1056 bp, 352 aa |
| Immediate neighbours | thrB, hom |
| 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
biosynthesis/ acquisition of amino acids, most abundant proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU32250
Phenotypes of a mutant
Database entries
- BsubCyc: BSU32250
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: O-phospho-L-homoserine + H2O = L-threonine + phosphate (according to Swiss-Prot)
- Protein family: serine/threonine dehydratase family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
Database entries
- BsubCyc: BSU32250
- UniProt: P04990
- KEGG entry: [2]
- E.C. number: 4.2.3.1
Additional information
Expression and regulation
- Regulation:
- Additional information:
- belongs to the 100 most abundant proteins PubMed
Biological materials
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Allison Kriel, Shaun R Brinsmade, Jessica L Tse, Ashley K Tehranchi, Alycia N Bittner, Abraham L Sonenshein, Jue D Wang
GTP dysregulation in Bacillus subtilis cells lacking (p)ppGpp results in phenotypic amino acid auxotrophy and failure to adapt to nutrient downshift and regulate biosynthesis genes.
J Bacteriol: 2014, 196(1);189-201
[PubMed:24163341]
[WorldCat.org]
[DOI]
(I p)
Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759]
[WorldCat.org]
[DOI]
(P p)
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)
C Parsot
Evolution of biosynthetic pathways: a common ancestor for threonine synthase, threonine dehydratase and D-serine dehydratase.
EMBO J: 1986, 5(11);3013-9
[PubMed:3098560]
[WorldCat.org]
[DOI]
(P p)
