Difference between revisions of "PabC"
(→References) |
|||
Line 140: | Line 140: | ||
=References= | =References= | ||
− | + | <pubmed>9084182,21815947 , </pubmed> | |
− | |||
− | |||
− | |||
− | <pubmed>9084182,, </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 16:06, 13 July 2013
- Description: aminodeoxychorismate lyase
Gene name | pabC |
Synonyms | |
Essential | no |
Product | aminodeoxychorismate lyase |
Function | biosynthesis of folate |
Gene expression levels in SubtiExpress: pabC | |
Metabolic function and regulation of this protein in SubtiPathways: Folate | |
MW, pI | 33 kDa, 6.119 |
Gene length, protein length | 879 bp, 293 aa |
Immediate neighbours | pabA, sul |
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: BSU00760
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: 4-amino-4-deoxychorismate = 4-aminobenzoate + pyruvate (according to Swiss-Prot)
- Protein family: class-IV pyridoxal-phosphate-dependent aminotransferase family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: P28821
- KEGG entry: [3]
- E.C. number: 4.1.3.38
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
Martin Lehnik-Habrink, Marc Schaffer, Ulrike Mäder, Christine Diethmaier, Christina Herzberg, Jörg Stülke
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y.
Mol Microbiol: 2011, 81(6);1459-73
[PubMed:21815947]
[WorldCat.org]
[DOI]
(I p)
Antoine de Saizieu, Pierre Vankan, Cassandra Vockler, Adolphus P G M van Loon
The trp RNA-binding attenuation protein (TRAP) regulates the steady-state levels of transcripts of the Bacillus subtilis folate operon.
Microbiology (Reading): 1997, 143 ( Pt 3);979-989
[PubMed:9084182]
[WorldCat.org]
[DOI]
(P p)