Difference between revisions of "HemL"

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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[spoVID]]'', ''[[hemB]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[spoVID]]'', ''[[hemB]]''
 
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU28120 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU28120 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU28120 Advanced_DNA]
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU28120 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU28120 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU28120 DNA_with_flanks]
 
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|colspan="2" | '''Genetic context''' <br/> [[Image:hemL_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:hemL_context.gif]]

Revision as of 10:54, 14 May 2013

  • Description: glutamate-1-semialdehyde aminotransferase

Gene name hemL
Synonyms hemK
Essential no
Product glutamate-1-semialdehyde aminotransferase
Function heme biosynthesis
Gene expression levels in SubtiExpress: hemL
MW, pI 46 kDa, 5.055
Gene length, protein length 1290 bp, 430 aa
Immediate neighbours spoVID, hemB
Sequences Protein DNA DNA_with_flanks
Genetic context
HemL context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
HemL expression.png
























Categories containing this gene/protein

biosynthesis of cofactors

This gene is a member of the following regulons

PerR regulon

The gene

Basic information

  • Locus tag: BSU28120

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: (S)-4-amino-5-oxopentanoate = 5-aminolevulinate (according to Swiss-Prot)
  • Protein family: HemL subfamily (according to Swiss-Prot)
  • Paralogous protein(s): GsaB

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]

Additional information

Expression and regulation

  • 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

Honghua Ge, Xinhuai Lv, Jun Fan, Yongxiang Gao, Maikun Teng, Liwen Niu
Crystal structure of glutamate-1-semialdehyde aminotransferase from Bacillus subtilis with bound pyridoxamine-5'-phosphate.
Biochem Biophys Res Commun: 2010, 402(2);356-60
[PubMed:20946885] [WorldCat.org] [DOI] (I p)

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)

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)