Difference between revisions of "MtnU"
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− | * '''Description:''' | + | * '''Description:''' omega-amidase <br/><br/> |
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|style="background:#ABCDEF;" align="center"| '''Essential''' || no | |style="background:#ABCDEF;" align="center"| '''Essential''' || no | ||
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− | |style="background:#ABCDEF;" align="center"| '''Product''' || | + | |style="background:#ABCDEF;" align="center"| '''Product''' || omega-amidase |
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− | |style="background:#ABCDEF;" align="center"|'''Function''' || | + | |style="background:#ABCDEF;" align="center"|'''Function''' || methionine salvage |
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|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=BSU13570 mtnU] | |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=BSU13570 mtnU] | ||
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= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
− | {{SubtiWiki category|[[ | + | {{SubtiWiki category|[[biosynthesis/ acquisition of amino acids]]}} |
= This gene is a member of the following [[regulons]] = | = This gene is a member of the following [[regulons]] = | ||
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===Phenotypes of a mutant === | ===Phenotypes of a mutant === | ||
+ | * reduced growth with 5-methylthioribose as single sulfur source {{PubMed|24837359}} | ||
=== Database entries === | === Database entries === | ||
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* '''Catalyzed reaction/ biological activity:''' | * '''Catalyzed reaction/ biological activity:''' | ||
+ | ** 2-ketoglutaramate + H<sub>2</sub>O ---> 2-oxoglutarate + NH<sub>3</sub> {{PubMed|24837359}} | ||
* '''Protein family:''' CN hydrolase domain (according to Swiss-Prot) | * '''Protein family:''' CN hydrolase domain (according to Swiss-Prot) | ||
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=References= | =References= | ||
− | <pubmed> 15102328 12022921 11545674 </pubmed> | + | <pubmed> 15102328 12022921 11545674 24837359 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 08:55, 21 May 2014
- Description: omega-amidase
Gene name | mtnU |
Synonyms | ykrU |
Essential | no |
Product | omega-amidase |
Function | methionine salvage |
Gene expression levels in SubtiExpress: mtnU | |
Metabolic function and regulation of this protein in SubtiPathways: mtnU | |
MW, pI | 29 kDa, 5.099 |
Gene length, protein length | 777 bp, 259 aa |
Immediate neighbours | mtnK, mtnE |
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
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU13570
Phenotypes of a mutant
- reduced growth with 5-methylthioribose as single sulfur source PubMed
Database entries
- BsubCyc: BSU13570
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
the E.coli homolog: yafV
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- 2-ketoglutaramate + H2O ---> 2-oxoglutarate + NH3 PubMed
- Protein family: CN hydrolase domain (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- BsubCyc: BSU13570
- Structure:
- UniProt: O31664
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: mtnU PubMed
- 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
Kenneth W Ellens, Lynn G L Richardson, Océane Frelin, Joseph Collins, Cintia Leite Ribeiro, Yih-Feng Hsieh, Robert T Mullen, Andrew D Hanson
Evidence that glutamine transaminase and omega-amidase potentially act in tandem to close the methionine salvage cycle in bacteria and plants.
Phytochemistry: 2015, 113;160-9
[PubMed:24837359]
[WorldCat.org]
[DOI]
(I p)
Agnieszka Sekowska, Valérie Dénervaud, Hiroki Ashida, Karine Michoud, Dieter Haas, Akiho Yokota, Antoine Danchin
Bacterial variations on the methionine salvage pathway.
BMC Microbiol: 2004, 4;9
[PubMed:15102328]
[WorldCat.org]
[DOI]
(I e)
Agnieszka Sekowska, Antoine Danchin
The methionine salvage pathway in Bacillus subtilis.
BMC Microbiol: 2002, 2;8
[PubMed:12022921]
[WorldCat.org]
[DOI]
(I e)
A Sekowska, L Mulard, S Krogh, J K Tse, A Danchin
MtnK, methylthioribose kinase, is a starvation-induced protein in Bacillus subtilis.
BMC Microbiol: 2001, 1;15
[PubMed:11545674]
[WorldCat.org]
[DOI]
(I p)