Difference between revisions of "PyrK"
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<div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | ||
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+ | |colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=pyrK_1626948_1627718_1 Expression at a glance]'''   {{PubMed|22383849}}<br/>[[Image:pyrK_expression.png|500px]] | ||
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Revision as of 09:13, 19 April 2012
- 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 |
Metabolic function and regulation of this protein in SubtiPathways: Pyrimidines, Nucleotides (regulation) | |
MW, pI | 27 kDa, 5.582 |
Gene length, protein length | 768 bp, 256 aa |
Immediate neighbours | pyrAB, pyrD |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
biosynthesis/ acquisition of nucleotides
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:
- Domains:
- Modification:
- Cofactor(s): 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:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
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)