Difference between revisions of "YwaA"
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|style="background:#ABCDEF;" align="center"|'''Function''' || biosynthesis of branched-chain amino acids | |style="background:#ABCDEF;" align="center"|'''Function''' || biosynthesis of branched-chain amino acids | ||
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− | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http:// | + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU38550 ywaA] |
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/fatty_acid_synthesis.html Lipid synthesis], [http://subtiwiki.uni-goettingen.de/pathways/ile_val_leu.html Ile, Leu, Val]''' | |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/fatty_acid_synthesis.html Lipid synthesis], [http://subtiwiki.uni-goettingen.de/pathways/ile_val_leu.html Ile, Leu, Val]''' | ||
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[dltE]]'', ''[[licH]]'' | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[dltE]]'', ''[[licH]]'' | ||
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− | | | + | |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU38550 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU38550 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU38550 Advanced_DNA] |
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Revision as of 14:11, 13 May 2013
- Description: branched-chain amino acid aminotransferase
Gene name | ywaA |
Synonyms | ipa-0r |
Essential | no |
Product | branched-chain amino acid aminotransferase |
Function | biosynthesis of branched-chain amino acids |
Gene expression levels in SubtiExpress: ywaA | |
Metabolic function and regulation of this protein in SubtiPathways: Lipid synthesis, Ile, Leu, Val | |
MW, pI | 40 kDa, 4.952 |
Gene length, protein length | 1089 bp, 363 aa |
Immediate neighbours | dltE, licH |
Sequences | Protein DNA Advanced_DNA |
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
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU38550
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate (according to Swiss-Prot)
- Protein family: class-IV pyridoxal-phosphate-dependent aminotransferase family (according to Swiss-Prot)
- Paralogous protein(s): YbgE
Extended information on the protein
- Kinetic information:
- Domains:
- Modification: S-cysteinylation after diamide stress (C104) PubMed
- Cofactor(s):
- Effectors of protein activity:
Database entries
- UniProt: P39576
- KEGG entry: [3]
- E.C. number: 2.6.1.42
Additional information
Expression and regulation
- Operon: ywaA PubMed
- Sigma factor:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- a ywaA::spc mutant and a bcd ybgE ywaA triple mutant are available in Linc Sonenshein's lab
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Falko Hochgräfe, Jörg Mostertz, Dierk-Christoph Pöther, Dörte Becher, John D Helmann, Michael Hecker
S-cysteinylation is a general mechanism for thiol protection of Bacillus subtilis proteins after oxidative stress.
J Biol Chem: 2007, 282(36);25981-5
[PubMed:17611193]
[WorldCat.org]
[DOI]
(P p)
Bradley J Berger, Shane English, Gene Chan, Marvin H Knodel
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis.
J Bacteriol: 2003, 185(8);2418-31
[PubMed:12670965]
[WorldCat.org]
[DOI]
(P p)