HemB

• Description: porphobilinogen synthase
  
  

Gene name	hemB
Synonyms
Essential	no
Product	porphobilinogen synthase
Function	heme biosynthesis
MW, pI	36 kDa, 4.98
Gene length, protein length	972 bp, 324 aa
Immediate neighbours	hemL, hemD
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

This gene is a member of the following regulons

PerR regulon

The gene

Basic information

• Locus tag: BSU28130

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: 2 5-aminolevulinate = porphobilinogen + 2 H₂O (according to Swiss-Prot)

• Protein family: ALADH family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s): zinc

• Effectors of protein activity:

• Interactions:

• Localization:
  • cytoplasm (according to Swiss-Prot)

Database entries

• Structure:

• UniProt: P30950

• KEGG entry: [3]

• E.C. number: 4.2.1.24

Expression and regulation

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

Qianda Lu, Jinming Ma, Hui Rong, Jun Fan, Ye Yuan, Kuai Li, Yongxiang Gao, Xiao Zhang, Maikun Teng, Liwen Niu
Cloning, expression, purification, crystallization and preliminary crystallographic analysis of 5-aminolaevulinic acid dehydratase from Bacillus subtilis.
Acta Crystallogr Sect F Struct Biol Cryst Commun: 2010, 66(Pt 9);1053-5
[PubMed:20823524] [WorldCat.org] [DOI] (I p)

Catherine E Goodwin, Finian J Leeper
Stereochemistry and mechanism of the conversion of 5-aminolaevulinic acid into porphobilinogen catalysed by porphobilinogen synthase.
Org Biomol Chem: 2003, 1(9);1443-6
[PubMed:12926268] [WorldCat.org] [DOI] (P 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)

I Berek, A Miczák, I Kiss, G Ivánovics, I Durkó
Genetic and biochemical analysis of haemin dependent mutants of Bacillus subtilis.
Acta Microbiol Acad Sci Hung: 1975, 22(2);157-67
[PubMed:804803] [WorldCat.org] (P p)

I Berek, A Miczák, G Ivánovics
Mapping the delta-aminolaevulinic acid dehydrase and porphobilinogen deaminase loci in Bacillus subtilis.
Mol Gen Genet: 1974, 132(3);233-9
[PubMed:4214010] [WorldCat.org] [DOI] (P p)