Difference between revisions of "GcvH"

From SubtiWiki
Jump to: navigation, search
(References)
(References)
Line 125: Line 125:
  
 
=References=
 
=References=
<pubmed> 20882995,21338421 </pubmed>
+
'''Additonal publications:''' {{PubMed|21338421}}
 +
<pubmed> 20882995 </pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 19:22, 14 October 2011

  • Description: glycine cleavage system protein H, 2-oxo acid dehydrogenase, lipoyl-binding site

Gene name gcvH
Synonyms yusH
Essential no
Product glycine cleavage system protein H
Function glycine utilization
MW, pI 14 kDa, 3.888
Gene length, protein length 381 bp, 127 aa
Immediate neighbours yusG, yusI
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
GcvH context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

utilization of amino acids, Biosynthesis of cofactors

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU32800

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: gcvH family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s): lipoic acid, lipoylated by LipM PubMed
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Regulation:
  • Regulatory mechanism:
  • 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

Additonal publications: PubMed

Quin H Christensen, John E Cronan
Lipoic acid synthesis: a new family of octanoyltransferases generally annotated as lipoate protein ligases.
Biochemistry: 2010, 49(46);10024-36
[PubMed:20882995] [WorldCat.org] [DOI] (I p)