Difference between revisions of "PyrK"
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= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
| − | {{SubtiWiki category|[[biosynthesis/ acquisition of nucleotides]]}} | + | {{SubtiWiki category|[[biosynthesis/ acquisition of nucleotides]]}}, |
| + | [[most abundant proteins]] | ||
= This gene is a member of the following [[regulons]] = | = This gene is a member of the following [[regulons]] = | ||
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=== Additional information=== | === Additional information=== | ||
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=The protein= | =The protein= | ||
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* '''Kinetic information:''' | * '''Kinetic information:''' | ||
| − | * '''Domains:''' | + | * '''[[Domains]]:''' |
* '''Modification:''' | * '''Modification:''' | ||
| − | * ''' | + | * '''[[Cofactors]]:''' contains an iron-sulfur cluster |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=pyrK_1626948_1627718_1 pyrK] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=pyrK_1626948_1627718_1 pyrK] {{PubMed|22383849}} | ||
| − | * '''Sigma factor:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/sites/entrez/1709162 PubMed] | + | * '''[[Sigma factor]]:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/sites/entrez/1709162 PubMed] |
* '''Regulation:''' | * '''Regulation:''' | ||
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* '''Additional information:''' | * '''Additional information:''' | ||
| + | ** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}} | ||
=Biological materials = | =Biological materials = | ||
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=References= | =References= | ||
| − | <pubmed>8206849,8759868,1709162,10545205, </pubmed> | + | <pubmed>8206849,8759868,1709162,10545205, 15378759</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 17:16, 5 March 2014
- Description: dihydroorotic acid dehydrogenase (electron transfer subunit)
| Gene name | pyrK |
| Synonyms | pyrDII, ylxD |
| Essential | no |
| Product | dihydroorotic acid dehydrogenase (electron transfer subunit) |
| Function | pyrimidine biosynthesis |
| Gene expression levels in SubtiExpress: pyrK | |
| Metabolic function and regulation of this protein in SubtiPathways: pyrK | |
| MW, pI | 27 kDa, 5.582 |
| Gene length, protein length | 768 bp, 256 aa |
| Immediate neighbours | pyrAB, pyrD |
| Sequences | Protein DNA DNA_with_flanks |
Genetic context 
This image was kindly provided by SubtiList
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Expression at a glance PubMed
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Contents
Categories containing this gene/protein
biosynthesis/ acquisition of nucleotides, most abundant proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU15530
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: FAD-binding FR-type domain (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Modification:
- Cofactors: contains an iron-sulfur cluster
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: P25983
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulatory mechanism:
- PyrR: RNA switch, transcription termination/ antitermination (in the presence of uridine nucleotides: termination, in their absence: antitermination) PubMed
- Additional information:
- belongs to the 100 most abundant proteins PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
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)
A E Kahler, F S Nielsen, R L Switzer
Biochemical characterization of the heteromeric Bacillus subtilis dihydroorotate dehydrogenase and its isolated subunits.
Arch Biochem Biophys: 1999, 371(2);191-201
[PubMed:10545205]
[WorldCat.org]
[DOI]
(P p)
A E Kahler, R L Switzer
Identification of a novel gene of pyrimidine nucleotide biosynthesis, pyrDII, that is required for dihydroorotate dehydrogenase activity in Bacillus subtilis.
J Bacteriol: 1996, 178(16);5013-6
[PubMed:8759868]
[WorldCat.org]
[DOI]
(P p)
R J Turner, Y Lu, R L Switzer
Regulation of the Bacillus subtilis pyrimidine biosynthetic (pyr) gene cluster by an autogenous transcriptional attenuation mechanism.
J Bacteriol: 1994, 176(12);3708-22
[PubMed:8206849]
[WorldCat.org]
[DOI]
(P p)
C L Quinn, B T Stephenson, R L Switzer
Functional organization and nucleotide sequence of the Bacillus subtilis pyrimidine biosynthetic operon.
J Biol Chem: 1991, 266(14);9113-27
[PubMed:1709162]
[WorldCat.org]
(P p)
