Difference between revisions of "PatB"
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=== Database entries === | === Database entries === | ||
| − | * '''Structure:''' | + | * '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?structureId=3T32 3T32] (from ''B. anthracis'', 46% identity, 75% similarity) |
* '''UniProt:''' [http://www.uniprot.org/uniprot/Q08432 Q08432] | * '''UniProt:''' [http://www.uniprot.org/uniprot/Q08432 Q08432] | ||
Revision as of 19:13, 13 September 2011
- Description: cystathione-beta-lyase
| Gene name | patB |
| Synonyms | |
| Essential | no |
| Product | cystathione-beta-lyase |
| Function | biosynthesis of methionine |
| Metabolic function and regulation of this protein in SubtiPathways: Cys, Met & Sulfate assimilation | |
| MW, pI | 42 kDa, 5.439 |
| Gene length, protein length | 1161 bp, 387 aa |
| Immediate neighbours | yugE, kinB |
| 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
biosynthesis/ acquisition of amino acids
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU31440
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: L-cystathionine + H2O = L-homocysteine + NH3 + pyruvate (according to Swiss-Prot)
- Protein family: MalY/patB cystathionine beta-lyase subfamily (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure: 3T32 (from B. anthracis, 46% identity, 75% similarity)
- UniProt: Q08432
- KEGG entry: [3]
- E.C. number: 4.4.1.8
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- 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
S Auger, M P Gomez, A Danchin, I Martin-Verstraete
The PatB protein of Bacillus subtilis is a C-S-lyase.
Biochimie: 2005, 87(2);231-8
[PubMed:15760717]
[WorldCat.org]
[DOI]
(P p)
Bauke Oudega, Gregory Koningstein, Luísa Rodrigues, Maria de Sales Ramon, Helmut Hilbert, Andreas Düsterhöft, Thomas M Pohl, Thomas Weitzenegger
Analysis of the Bacillus subtilis genome: cloning and nucleotide sequence of a 62 kb region between 275 degrees (rrnB) and 284 degrees (pai).
Microbiology (Reading): 1997, 143 ( Pt 8);2769-2774
[PubMed:9274030]
[WorldCat.org]
[DOI]
(P p)
