HemA

• Description: glutamyl-tRNA reductase
  
  

Gene name	hemA
Synonyms
Essential	no
Product	glutamyl-tRNA reductase
Function	porphyrin biosynthesis
Gene expression levels in SubtiExpress: hemA
MW, pI	50 kDa, 5.313
Gene length, protein length	1365 bp, 455 aa
Immediate neighbours	hemX, ysxD
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

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)