Difference between revisions of "CysH"
Line 14: | Line 14: | ||
|style="background:#ABCDEF;" align="center"|'''Function''' || sulfate reduction | |style="background:#ABCDEF;" align="center"|'''Function''' || sulfate reduction | ||
|- | |- | ||
− | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http:// | + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU15570 cysH] |
|- | |- | ||
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/cys_meth_and_sulfate_assimilation.html Cys, Met & Sulfate assimilation]''' | |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/cys_meth_and_sulfate_assimilation.html Cys, Met & Sulfate assimilation]''' | ||
Line 24: | Line 24: | ||
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[pyrE]]'', ''[[cysP]]'' | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[pyrE]]'', ''[[cysP]]'' | ||
|- | |- | ||
− | | | + | |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU15570 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU15570 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU15570 Advanced_DNA] |
|- | |- | ||
|colspan="2" | '''Genetic context''' <br/> [[Image:cysH_context.gif]] | |colspan="2" | '''Genetic context''' <br/> [[Image:cysH_context.gif]] |
Revision as of 12:47, 13 May 2013
- 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: Cys, Met & Sulfate assimilation | |
MW, pI | 26 kDa, 5.462 |
Gene length, protein length | 699 bp, 233 aa |
Immediate neighbours | pyrE, cysP |
Sequences | Protein DNA Advanced_DNA |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
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:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
- cytoplasm (according to Swiss-Prot)
Database entries
- Structure:
- 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)
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)