HemB
- Description: porphobilinogen synthase
Gene name | hemB |
Synonyms | |
Essential | no |
Product | porphobilinogen synthase |
Function | heme biosynthesis |
Gene expression levels in SubtiExpress: hemB | |
MW, pI | 36 kDa, 4.98 |
Gene length, protein length | 972 bp, 324 aa |
Immediate neighbours | hemL, hemD |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
biosynthesis of cofactors, phosphoproteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU28130
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
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:
- phosphorylated on Arg-217 PubMed
- Cofactor(s): zinc
- Effectors of protein activity:
- Localization:
- cytoplasm (according to Swiss-Prot)
Database entries
- Structure:
- UniProt: P30950
- KEGG entry: [3]
- E.C. number: 4.2.1.24
Additional information
Expression and regulation
- 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
Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742]
[WorldCat.org]
[DOI]
(I p)
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)