Difference between revisions of "AccB"
| Line 13: | Line 13: | ||
|- | |- | ||
|style="background:#ABCDEF;" align="center"|'''Function''' || production of malonyl-CoA, the substrate for fatty acid biosynthesis | |style="background:#ABCDEF;" align="center"|'''Function''' || production of malonyl-CoA, the substrate for fatty acid biosynthesis | ||
| − | |||
| − | |||
|- | |- | ||
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 17 kDa, 4.394 | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 17 kDa, 4.394 | ||
Revision as of 10:18, 16 February 2010
- Description: acetyl-CoA carboxylase (biotin carboxyl carrier subunit)
| Gene name | accB |
| Synonyms | fabE, yqhW |
| Essential | yes PubMed |
| Product | acetyl-CoA carboxylase (biotin carboxyl carrier subunit) |
| Function | production of malonyl-CoA, the substrate for fatty acid biosynthesis |
| MW, pI | 17 kDa, 4.394 |
| Gene length, protein length | 477 bp, 159 aa |
| Immediate neighbours | accC, spoIIIAH |
| 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: BSU24350
Phenotypes of a mutant
essential PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
Database entries
- UniProt: P49786
- KEGG entry: [3]
- E.C. number: 6.4.1.2
Additional information
AccB binds to StrepTactin, and may be co-purified when purifying Strep-tagged proteins by SPINE.
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
Reviews
Stephen W White, Jie Zheng, Yong-Mei Zhang, Rock
The structural biology of type II fatty acid biosynthesis.
Annu Rev Biochem: 2005, 74;791-831
[PubMed:15952903]
[WorldCat.org]
[DOI]
(P p)
Original Publications
F K Athappilly, W A Hendrickson
Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing.
Structure: 1995, 3(12);1407-19
[PubMed:8747466]
[WorldCat.org]
[DOI]
(P p)
P Marini, S J Li, D Gardiol, J E Cronan, D de Mendoza
The genes encoding the biotin carboxyl carrier protein and biotin carboxylase subunits of Bacillus subtilis acetyl coenzyme A carboxylase, the first enzyme of fatty acid synthesis.
J Bacteriol: 1995, 177(23);7003-6
[PubMed:7592499]
[WorldCat.org]
[DOI]
(P p)
