Difference between revisions of "CysH"
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= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
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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]]:''' |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
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=== Database entries === | === Database entries === | ||
| − | * '''Structure:''' | + | * '''Structure:''' [http://pdb.org/pdb/explore/explore.do?structureId=2goy 2GOY] (from ''Pseudomonas aeruginosa'', 35% identity) {{PubMed|17010373}} |
* '''UniProt:''' [http://www.uniprot.org/uniprot/P94498 P94498] | * '''UniProt:''' [http://www.uniprot.org/uniprot/P94498 P94498] | ||
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=cysH_1630382_1631083_1 cysH] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=cysH_1630382_1631083_1 cysH] {{PubMed|22383849}} | ||
| − | * '''Sigma factor:''' [[SigA]] {{PubMed|11004190}} | + | * '''[[Sigma factor]]:''' [[SigA]] {{PubMed|11004190}} |
* '''Regulation:''' | * '''Regulation:''' | ||
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=References= | =References= | ||
| − | <pubmed>10094622,16267287,11004190 ,12107147, 18039762 9006060 </pubmed> | + | <pubmed>10094622,16267287,11004190 ,12107147, 18039762 9006060 17010373 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 15:43, 16 March 2014
- Description: phosphoadenosine phosphosulfate sulfotransferase
| Gene name | cysH |
| Synonyms | |
| Essential | no |
| Product | phosphoadenosine phosphosulfate sulfotransferase |
| Function | sulfate reduction |
| Gene expression levels in SubtiExpress: cysH | |
| Metabolic function and regulation of this protein in SubtiPathways: cysH | |
| MW, pI | 26 kDa, 5.462 |
| Gene length, protein length | 699 bp, 233 aa |
| Immediate neighbours | pyrE, cysP |
| 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
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU15570
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin (according to Swiss-Prot)
- Protein family: CysH subfamily (according to Swiss-Prot)
- Paralogous protein(s): YitB
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
- Localization:
- cytoplasm (according to Swiss-Prot)
Database entries
- UniProt: P94498
- KEGG entry: [3]
- E.C. number: 1.8.4.8
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- S-box: transcription termination/ antitermination, the S-box riboswitch binds S-adenosylmethionine resulting in termination PubMed
- CymR: transcription repression
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Isabelle Martin-Verstraete, Institute Pasteur, Paris, France
Your additional remarks
References
Jerneja Tomsic, Brooke A McDaniel, Frank J Grundy, Tina M Henkin
Natural variability in S-adenosylmethionine (SAM)-dependent riboswitches: S-box elements in bacillus subtilis exhibit differential sensitivity to SAM In vivo and in vitro.
J Bacteriol: 2008, 190(3);823-33
[PubMed:18039762]
[WorldCat.org]
[DOI]
(I p)
Justin Chartron, Kate S Carroll, Carrie Shiau, Hong Gao, Julie A Leary, Carolyn R Bertozzi, C David Stout
Substrate recognition, protein dynamics, and iron-sulfur cluster in Pseudomonas aeruginosa adenosine 5'-phosphosulfate reductase.
J Mol Biol: 2006, 364(2);152-69
[PubMed:17010373]
[WorldCat.org]
[DOI]
(P p)
Daniela Albanesi, Maria Cecilia Mansilla, Gustavo E Schujman, Diego de Mendoza
Bacillus subtilis cysteine synthetase is a global regulator of the expression of genes involved in sulfur assimilation.
J Bacteriol: 2005, 187(22);7631-8
[PubMed:16267287]
[WorldCat.org]
[DOI]
(P p)
Ulrike Mäder, Georg Homuth, Christian Scharf, Knut Büttner, Rüdiger Bode, Michael Hecker
Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability.
J Bacteriol: 2002, 184(15);4288-95
[PubMed:12107147]
[WorldCat.org]
[DOI]
(P p)
M C Mansilla, D Albanesi, D de Mendoza
Transcriptional control of the sulfur-regulated cysH operon, containing genes involved in L-cysteine biosynthesis in Bacillus subtilis.
J Bacteriol: 2000, 182(20);5885-92
[PubMed:11004190]
[WorldCat.org]
[DOI]
(P p)
F J Grundy, T M Henkin
The S box regulon: a new global transcription termination control system for methionine and cysteine biosynthesis genes in gram-positive bacteria.
Mol Microbiol: 1998, 30(4);737-49
[PubMed:10094622]
[WorldCat.org]
[DOI]
(P p)
M C Mansilla, D de Mendoza
L-cysteine biosynthesis in Bacillus subtilis: identification, sequencing, and functional characterization of the gene coding for phosphoadenylylsulfate sulfotransferase.
J Bacteriol: 1997, 179(3);976-81
[PubMed:9006060]
[WorldCat.org]
[DOI]
(P p)
