HemA

• 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 This image was kindly provided by SubtiList

Categories containing this gene/protein

biosynthesis of cofactors, membrane proteins

This gene is a member of the following regulons

PerR regulon

The gene

Basic information

• Locus tag: BSU28170

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• UniProt: P16618

• KEGG entry: [3]

• E.C. number: 1.2.1.70

Expression and regulation

• Operon: hemA-hemX-hemC-hemD-hemB-hemL PubMed

• Expression browser: hemA PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • induced by hydrogen peroxide (PerR) PubMed

• Regulatory mechanism:
  • PerR: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)

Per Johansson, Lars Hederstedt
Organization of genes for tetrapyrrole biosynthesis in gram--positive bacteria.
Microbiology (Reading): 1999, 145 ( Pt 3);529-538
[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): 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)(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)