Difference between revisions of "HemB"
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| + | = [[Categories]] containing this gene/protein = | ||
| + | {{SubtiWiki category|[[biosynthesis of cofactors]]}} | ||
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| + | = This gene is a member of the following [[regulons]] = | ||
| + | {{SubtiWiki regulon|[[PerR regulon]]}} | ||
=The gene= | =The gene= | ||
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=The protein= | =The protein= | ||
Revision as of 22:03, 8 December 2010
- 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
| |
Contents
Categories containing this gene/protein
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:
- 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
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
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)
