Difference between revisions of "HemA"

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|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1365 bp, 455 aa  
 
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1365 bp, 455 aa  
 
|-
 
|-
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yhfU]]'', ''[[yhfW]]''
+
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[hemX]]'', ''[[ysxD]]''
 
|-
 
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|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB14777&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
 
|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB14777&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''

Revision as of 08:32, 7 December 2009

  • Description: glutamyl-tRNA reductase

Gene name hemA
Synonyms
Essential no
Product glutamyl-tRNA reductase
Function porphyrin biosynthesis
MW, pI 50 kDa, 5.313
Gene length, protein length 1365 bp, 455 aa
Immediate neighbours hemX, ysxD
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
HemA context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU28170

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH (according to Swiss-Prot)
  • Protein family: glutamyl-tRNA reductase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization: cell membrane (according to Swiss-Prot)

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Operon:
  • Regulation:
    • repressed in the absence of hydrogen peroxide (PerR) PubMed
  • 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

A F Herbig, J D Helmann
Roles of metal ions and hydrogen peroxide in modulating the interaction of the Bacillus subtilis PerR peroxide regulon repressor with operator DNA.
Mol. Microbiol.: 2001, 41(4);849-59
[PubMed:11532148] [WorldCat.org] [DOI] (P p)

P Johansson, L Hederstedt
Organization of genes for tetrapyrrole biosynthesis in gram--positive bacteria.
Microbiology (Reading, Engl.): 1999, 145 ( Pt 3);529-38
[PubMed:10217486] [WorldCat.org] [DOI] (P p)

N Bsat, L Chen, J D Helmann
Mutation of the Bacillus subtilis alkyl hydroperoxide reductase (ahpCF) operon reveals compensatory interactions among hydrogen peroxide stress genes.
J. Bacteriol.: 1996, 178(22);6579-86
[PubMed:8932315] [WorldCat.org] [DOI] (P p)

L Chen, L Keramati, J D Helmann
Coordinate regulation of Bacillus subtilis peroxide stress genes by hydrogen peroxide and metal ions.
Proc. Natl. Acad. Sci. U.S.A.: 1995, 92(18);8190-4
[PubMed:7667267] [WorldCat.org] [DOI] (P p)

I Schröder, P Johansson, L Rutberg, L Hederstedt
The hemX gene of the Bacillus subtilis hemAXCDBL operon encodes a membrane protein, negatively affecting the steady-state cellular concentration of HemA (glutamyl-tRNA reductase).
Microbiology (Reading, Engl.): 1994, 140 ( Pt 4);731-40
[PubMed:8012594] [WorldCat.org] [DOI] (P p)

I Schröder, L Hederstedt, C G Kannangara, P Gough
Glutamyl-tRNA reductase activity in Bacillus subtilis is dependent on the hemA gene product.
Biochem. J.: 1992, 281 ( Pt 3);843-50
[PubMed:1536660] [WorldCat.org] [DOI] (P p)

M Hansson, L Rutberg, I Schröder, L Hederstedt
The Bacillus subtilis hemAXCDBL gene cluster, which encodes enzymes of the biosynthetic pathway from glutamate to uroporphyrinogen III.
J. Bacteriol.: 1991, 173(8);2590-9
[PubMed:1672867] [WorldCat.org] [DOI] (P p)