Difference between revisions of "HemL"
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU28120 hemL] | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU28120 hemL] | ||
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+ | |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/subtipathways/search.php?enzyme=HemL HemL]''' | ||
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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 46 kDa, 5.055 | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 46 kDa, 5.055 |
Revision as of 11:47, 8 April 2014
- 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 | |
Metabolic function and regulation of this protein in SubtiPathways: 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 This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU28120
Phenotypes of a mutant
Database entries
- BsubCyc: BSU28120
- 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
- BsubCyc: BSU28120
- UniProt: P30949
- KEGG entry: [3]
- E.C. number: 5.4.3.8
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
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)