Difference between revisions of "HemL"
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=== Database entries === | === Database entries === | ||
| − | * '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=3BS8 3BS8] | + | * '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=3BS8 3BS8] {{PubMed|20946885}} |
* '''UniProt:''' [http://www.uniprot.org/uniprot/P30949 P30949] | * '''UniProt:''' [http://www.uniprot.org/uniprot/P30949 P30949] | ||
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=References= | =References= | ||
| − | <pubmed>10217486,1672867,,11532148, </pubmed> | + | <pubmed>10217486,1672867,20946885 ,11532148, </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 14:16, 16 October 2010
- Description: glutamate-1-semialdehyde aminotransferase
| Gene name | hemL |
| Synonyms | hemK |
| Essential | no |
| Product | glutamate-1-semialdehyde aminotransferase |
| Function | heme biosynthesis |
| MW, pI | 46 kDa, 5.055 |
| Gene length, protein length | 1290 bp, 430 aa |
| Immediate neighbours | spoVID, hemB |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Contents
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:
- Interactions:
- Localization:
Database entries
- 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)
