Difference between revisions of "GuaD"
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| − | * '''Description:''' guanine deaminase, general stress protein, important for survival of ethanol | + | * '''Description:''' guanine deaminase, general stress protein, important for survival of ethanol and paraquat stresses <br/><br/> |
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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|[[general stress proteins (controlled by SigB)]]}} | + | {{SubtiWiki category|[[general stress proteins (controlled by SigB)]]}}, |
| + | {{SubtiWiki category|[[resistance against oxidative and electrophile stress]]}} | ||
= This gene is a member of the following [[regulons]] = | = This gene is a member of the following [[regulons]] = | ||
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=guaD_1382677_1383147_-1 guaD] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=guaD_1382677_1383147_-1 guaD] {{PubMed|22383849}} | ||
| − | * '''Sigma factor:''' [[SigA]] {{PubMed|11101664}}, [[SigB]] [http://www.ncbi.nlm.nih.gov/pubmed/15805528 PubMed] | + | * '''[[Sigma factor]]:''' [[SigA]] {{PubMed|11101664}}, [[SigB]] [http://www.ncbi.nlm.nih.gov/pubmed/15805528 PubMed] |
* '''Regulation:''' | * '''Regulation:''' | ||
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=References= | =References= | ||
| − | <pubmed>11101664,,12029039,15180998 ,15805528, 11344136 </pubmed> | + | <pubmed>11101664,,12029039,15180998 ,15805528, 11344136 22582280</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 19:19, 15 September 2013
- Description: guanine deaminase, general stress protein, important for survival of ethanol and paraquat stresses
| Gene name | guaD |
| Synonyms | gde, yknA |
| Essential | no |
| Product | guanine deaminase |
| Function | deamination of guanine to xanthine, purine salvage and interconversion |
| Gene expression levels in SubtiExpress: guaD | |
| Metabolic function and regulation of this protein in SubtiPathways: Purine salvage, Purine catabolism, Nucleotides (regulation) | |
| MW, pI | 17 kDa, 4.999 |
| Gene length, protein length | 468 bp, 156 aa |
| Immediate neighbours | ykzN, metE |
| Sequences | Protein DNA DNA_with_flanks |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
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Contents
Categories containing this gene/protein
biosynthesis/ acquisition of nucleotides, general stress proteins (controlled by SigB), resistance against oxidative and electrophile stress
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU13170
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Guanine + H2O = xanthine + NH3 (according to Swiss-Prot)
- Protein family: cytidine and deoxycytidylate deaminase family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure: 1WKQ
- UniProt: O34598
- KEGG entry: [3]
- E.C. number: 3.5.4.3
Additional information
Expression and regulation
- Operon: guaD PubMed
- Regulation:
- 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
Alexander Reder, Dirk Höper, Ulf Gerth, Michael Hecker
Contributions of individual σB-dependent general stress genes to oxidative stress resistance of Bacillus subtilis.
J Bacteriol: 2012, 194(14);3601-10
[PubMed:22582280]
[WorldCat.org]
[DOI]
(I p)
Dirk Höper, Uwe Völker, Michael Hecker
Comprehensive characterization of the contribution of individual SigB-dependent general stress genes to stress resistance of Bacillus subtilis.
J Bacteriol: 2005, 187(8);2810-26
[PubMed:15805528]
[WorldCat.org]
[DOI]
(P p)
Shwu-Huey Liaw, Yu-Jui Chang, Cheng-Tsung Lai, Hui-Chuan Chang, Gu-Gang Chang
Crystal structure of Bacillus subtilis guanine deaminase: the first domain-swapped structure in the cytidine deaminase superfamily.
J Biol Chem: 2004, 279(34);35479-85
[PubMed:15180998]
[WorldCat.org]
[DOI]
(P p)
Lars Beier, Per Nygaard, Hanne Jarmer, Hans H Saxild
Transcription analysis of the Bacillus subtilis PucR regulon and identification of a cis-acting sequence required for PucR-regulated expression of genes involved in purine catabolism.
J Bacteriol: 2002, 184(12);3232-41
[PubMed:12029039]
[WorldCat.org]
[DOI]
(P p)
A C Schultz, P Nygaard, H H Saxild
Functional analysis of 14 genes that constitute the purine catabolic pathway in Bacillus subtilis and evidence for a novel regulon controlled by the PucR transcription activator.
J Bacteriol: 2001, 183(11);3293-302
[PubMed:11344136]
[WorldCat.org]
[DOI]
(P p)
Per Nygaard, Søren M Bested, Kasper A K Andersen, Hans H Saxild
Bacillus subtilis guanine deaminase is encoded by the yknA gene and is induced during growth with purines as the nitrogen source.
Microbiology (Reading): 2000, 146 Pt 12;3061-3069
[PubMed:11101664]
[WorldCat.org]
[DOI]
(P p)
