Difference between revisions of "PurA"
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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]]}}, | ||
| − | {{SubtiWiki category|[[phosphoproteins]]}} | + | {{SubtiWiki category|[[phosphoproteins]]}}, |
| + | [[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:''' | ||
** phosphorylated on Arg-97 {{PubMed|22517742}} | ** phosphorylated on Arg-97 {{PubMed|22517742}} | ||
| − | * ''' | + | * '''[[Cofactors]]:''' |
* '''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=purA_4155433_4156725_-1 purA] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=purA_4155433_4156725_-1 purA] {{PubMed|22383849}} | ||
| − | * '''Sigma factor:''' [[SigA]] {{PubMed|1312531}} | + | * '''[[Sigma factor]]:''' [[SigA]] {{PubMed|1312531}} |
* '''Regulation:''' expression activated by glucose (4.9 fold) ([[CcpA]]) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed] | * '''Regulation:''' expression activated by glucose (4.9 fold) ([[CcpA]]) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed] | ||
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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>1722815,1312531 ,7638212,12850135, 21424839 22517742</pubmed> | + | <pubmed>1722815,1312531 ,7638212,12850135, 21424839 22517742 15378759</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 16:56, 5 March 2014
- Description: adenylosuccinate synthetase
| Gene name | purA |
| Synonyms | |
| Essential | no |
| Product | adenylosuccinate synthetase |
| Function | purine biosynthesis |
| Gene expression levels in SubtiExpress: purA | |
| Metabolic function and regulation of this protein in SubtiPathways: purA | |
| MW, pI | 47 kDa, 5.459 |
| Gene length, protein length | 1290 bp, 430 aa |
| Immediate neighbours | trnY-Lys, yycE |
| 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 nucleotides, phosphoproteins, most abundant proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU40420
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP (according to Swiss-Prot)
- Protein family: adenylosuccinate synthetase family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Modification:
- phosphorylated on Arg-97 PubMed
- Effectors of protein activity:
- Localization:
- cytoplasm (according to Swiss-Prot)
Database entries
- UniProt: P29726
- KEGG entry: [3]
- E.C. number: 6.3.4.4
Additional information
Expression and regulation
- Operon: purA 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
Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742]
[WorldCat.org]
[DOI]
(I p)
Haojian Li, Guoqiang Zhang, Aihua Deng, Ning Chen, Tingyi Wen
De novo engineering and metabolic flux analysis of inosine biosynthesis in Bacillus subtilis.
Biotechnol Lett: 2011, 33(8);1575-80
[PubMed:21424839]
[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)
Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135]
[WorldCat.org]
[DOI]
(P p)
M Weng, P L Nagy, H Zalkin
Identification of the Bacillus subtilis pur operon repressor.
Proc Natl Acad Sci U S A: 1995, 92(16);7455-9
[PubMed:7638212]
[WorldCat.org]
[DOI]
(P p)
P Mäntsälä, H Zalkin
Cloning and sequence of Bacillus subtilis purA and guaA, involved in the conversion of IMP to AMP and GMP.
J Bacteriol: 1992, 174(6);1883-90
[PubMed:1312531]
[WorldCat.org]
[DOI]
(P p)
H H Saxild, P Nygaard
Regulation of levels of purine biosynthetic enzymes in Bacillus subtilis: effects of changing purine nucleotide pools.
J Gen Microbiol: 1991, 137(10);2387-94
[PubMed:1722815]
[WorldCat.org]
[DOI]
(P p)
