Difference between revisions of "MccB"
(50 intermediate revisions by 8 users not shown) | |||
Line 1: | Line 1: | ||
− | * '''Description:''' | + | * '''Description:''' cystathionine lyase/ homocysteine gamma-lyase <br/><br/> |
{| align="right" border="1" cellpadding="2" | {| align="right" border="1" cellpadding="2" | ||
|- | |- | ||
|style="background:#ABCDEF;" align="center"|'''Gene name''' | |style="background:#ABCDEF;" align="center"|'''Gene name''' | ||
− | |'' | + | |''mccB '' |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' | + | |style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''yrhB'' |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"| '''Essential''' || | + | |style="background:#ABCDEF;" align="center"| '''Essential''' || no |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"| '''Product''' || | + | |style="background:#ABCDEF;" align="center"| '''Product''' || cystathionine lyase/ homocysteine gamma-lyase |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"|'''Function''' || | + | |style="background:#ABCDEF;" align="center"|'''Function''' || methionine-to-cysteine conversion |
+ | |- | ||
+ | |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=BSU27250 mccB] | ||
+ | |- | ||
+ | |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/subtipathways/search.php?enzyme=mccB mccB]''' | ||
|- | |- | ||
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 40 kDa, 5.215 | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 40 kDa, 5.215 | ||
Line 18: | Line 22: | ||
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1137 bp, 379 aa | |style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1137 bp, 379 aa | ||
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || | + | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yrhC]]'', ''[[mccA]]'' |
|- | |- | ||
− | |style="background:#FAF8CC;" align="center"|'''[http:// | + | |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU27250 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU27250 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU27250 DNA_with_flanks] |
− | |||
|- | |- | ||
|colspan="2" | '''Genetic context''' <br/> [[Image:yrhB_context.gif]] | |colspan="2" | '''Genetic context''' <br/> [[Image:yrhB_context.gif]] | ||
+ | <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | ||
+ | |- | ||
+ | |colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=mccB_2785001_2786140_-1 Expression at a glance]'''   {{PubMed|22383849}}<br/>[[Image:mccB_expression.png|500px|link=http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU27250]] | ||
|- | |- | ||
|} | |} | ||
__TOC__ | __TOC__ | ||
+ | <br/><br/><br/><br/> | ||
+ | <br/><br/><br/><br/> | ||
+ | <br/><br/><br/><br/> | ||
+ | <br/><br/><br/><br/> | ||
+ | <br/><br/><br/><br/> | ||
+ | |||
+ | |||
+ | <br/><br/><br/><br/><br/><br/> | ||
+ | |||
+ | = [[Categories]] containing this gene/protein = | ||
+ | {{SubtiWiki category|[[biosynthesis/ acquisition of amino acids]]}}, | ||
+ | {{SubtiWiki category|[[membrane proteins]]}} | ||
− | + | = This gene is a member of the following [[regulons]] = | |
+ | {{SubtiWiki regulon|[[CymR regulon]]}}, | ||
+ | {{SubtiWiki regulon|[[Spx regulon]]}} | ||
=The gene= | =The gene= | ||
Line 35: | Line 55: | ||
=== Basic information === | === Basic information === | ||
− | * ''' | + | * '''Locus tag:''' BSU27250 |
===Phenotypes of a mutant === | ===Phenotypes of a mutant === | ||
=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU27250&redirect=T BSU27250] | ||
− | * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/ | + | * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/yrrT-mtn-yrhABC.html] |
* '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG12291] | * '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG12291] | ||
=== Additional information=== | === Additional information=== | ||
+ | |||
+ | |||
Line 52: | Line 75: | ||
=== Basic information/ Evolution === | === Basic information/ Evolution === | ||
− | * '''Catalyzed reaction/ biological activity:''' | + | * '''Catalyzed reaction/ biological activity:''' L-cystathionine + H<sub>2</sub>O = L-cysteine + NH<sub>3</sub> + 2-oxobutanoate (according to Swiss-Prot) |
− | * '''Protein family:''' | + | * '''Protein family:''' trans-sulfuration enzymes family (according to Swiss-Prot) |
* '''Paralogous protein(s):''' | * '''Paralogous protein(s):''' | ||
Line 70: | Line 93: | ||
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
− | * '''Interactions:''' | + | * '''[[SubtInteract|Interactions]]:''' |
− | * '''Localization:''' | + | * '''[[Localization]]:''' |
+ | ** cell membrane (according to Swiss-Prot) | ||
=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU27250&redirect=T BSU27250] | ||
* '''Structure:''' | * '''Structure:''' | ||
− | * ''' | + | * '''UniProt:''' [http://www.uniprot.org/uniprot/O05394 O05394] |
− | * '''KEGG entry:''' | + | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU27250] |
− | * '''E.C. number:''' | + | * '''E.C. number:''' [http://www.expasy.org/enzyme/4.4.1.1 4.4.1.1] |
=== Additional information=== | === Additional information=== | ||
Line 88: | Line 113: | ||
=Expression and regulation= | =Expression and regulation= | ||
− | * '''Operon:''' | + | * '''Operon:''' ''[[yrrT]]-[[mtnN]]-[[mccA]]-[[mccB]]-[[yrhC]]'' [http://www.ncbi.nlm.nih.gov/sites/entrez/17056751 PubMed] |
− | * '''Sigma factor:''' | + | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=mccB_2785001_2786140_-1 mccB] {{PubMed|22383849}} |
+ | |||
+ | * '''Sigma factor:''' [[SigA]] {{PubMed|16513748}} | ||
* '''Regulation:''' | * '''Regulation:''' | ||
+ | ** repressed in the presence of cysteine ([[CymR]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/16513748 PubMed] | ||
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
+ | ** [[CymR]]: transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/16513748 PubMed] | ||
+ | ** [[Spx]]: transcription activation {{PubMed|12642660,16885442}} | ||
− | * '''Additional information:''' | + | * '''Additional information:''' |
+ | ** number of protein molecules per cell (minimal medium with glucose and ammonium): 164 {{PubMed|24696501}} | ||
=Biological materials = | =Biological materials = | ||
* '''Mutant:''' | * '''Mutant:''' | ||
+ | ** 1A942 ( ''mccB''::''kan''), {{PubMed|17056751}}, available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1A942&Search=1A942 BGSC] | ||
+ | ** 1A945 ( ''mccB''::''kan''), {{PubMed|17056751}}, available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1A945&Search=1A945 BGSC] | ||
* '''Expression vector:''' | * '''Expression vector:''' | ||
Line 118: | Line 151: | ||
=References= | =References= | ||
− | + | <pubmed>17056751,16513748,16885442, 12642660, </pubmed> | |
+ | |||
+ | [[Category:Protein-coding genes]] |
Latest revision as of 09:59, 17 April 2014
- Description: cystathionine lyase/ homocysteine gamma-lyase
Gene name | mccB |
Synonyms | yrhB |
Essential | no |
Product | cystathionine lyase/ homocysteine gamma-lyase |
Function | methionine-to-cysteine conversion |
Gene expression levels in SubtiExpress: mccB | |
Metabolic function and regulation of this protein in SubtiPathways: mccB | |
MW, pI | 40 kDa, 5.215 |
Gene length, protein length | 1137 bp, 379 aa |
Immediate neighbours | yrhC, mccA |
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 amino acids, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU27250
Phenotypes of a mutant
Database entries
- BsubCyc: BSU27250
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: L-cystathionine + H2O = L-cysteine + NH3 + 2-oxobutanoate (according to Swiss-Prot)
- Protein family: trans-sulfuration enzymes family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
- cell membrane (according to Swiss-Prot)
Database entries
- BsubCyc: BSU27250
- Structure:
- UniProt: O05394
- KEGG entry: [3]
- E.C. number: 4.4.1.1
Additional information
Expression and regulation
- Additional information:
- number of protein molecules per cell (minimal medium with glucose and ammonium): 164 PubMed
Biological materials
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Marie-Françoise Hullo, Sandrine Auger, Olga Soutourina, Octavian Barzu, Mireille Yvon, Antoine Danchin, Isabelle Martin-Verstraete
Conversion of methionine to cysteine in Bacillus subtilis and its regulation.
J Bacteriol: 2007, 189(1);187-97
[PubMed:17056751]
[WorldCat.org]
[DOI]
(P p)
Soon-Yong Choi, Dindo Reyes, Montira Leelakriangsak, Peter Zuber
The global regulator Spx functions in the control of organosulfur metabolism in Bacillus subtilis.
J Bacteriol: 2006, 188(16);5741-51
[PubMed:16885442]
[WorldCat.org]
[DOI]
(P p)
Sergine Even, Pierre Burguière, Sandrine Auger, Olga Soutourina, Antoine Danchin, Isabelle Martin-Verstraete
Global control of cysteine metabolism by CymR in Bacillus subtilis.
J Bacteriol: 2006, 188(6);2184-97
[PubMed:16513748]
[WorldCat.org]
[DOI]
(P p)
Shunji Nakano, Michiko M Nakano, Ying Zhang, Montira Leelakriangsak, Peter Zuber
A regulatory protein that interferes with activator-stimulated transcription in bacteria.
Proc Natl Acad Sci U S A: 2003, 100(7);4233-8
[PubMed:12642660]
[WorldCat.org]
[DOI]
(P p)