Difference between revisions of "FabI"
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=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU11720&redirect=T BSU11720] | ||
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/fabI.html] | * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/fabI.html] | ||
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=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU11720&redirect=T BSU11720] | ||
* '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?structureId=3OIF 3OIF] (complex with NAD and inhibitor triclosan) {{PubMed|21185310}} | * '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?structureId=3OIF 3OIF] (complex with NAD and inhibitor triclosan) {{PubMed|21185310}} |
Revision as of 13:26, 2 April 2014
- Description: enoyl-acyl carrier protein reductase
Gene name | fabI |
Synonyms | yjbW |
Essential | no |
Product | enoyl-acyl carrier protein reductase |
Function | fatty acid biosynthesis |
Gene expression levels in SubtiExpress: fabI | |
Metabolic function and regulation of this protein in SubtiPathways: fabI | |
MW, pI | 27 kDa, 5.605 |
Gene length, protein length | 774 bp, 258 aa |
Immediate neighbours | thiD, cotO |
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
biosynthesis of lipids, most abundant proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU11720
Phenotypes of a mutant
Database entries
- BsubCyc: BSU11720
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Acyl-[acyl-carrier-protein] + NAD+ = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADH (according to Swiss-Prot)
- Protein family: FabI subfamily (according to Swiss-Prot)
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
- inhibited by triclosan PubMed
Database entries
- BsubCyc: BSU11720
- UniProt: P54616
- KEGG entry: [3]
- E.C. number: 1.3.1.9
Additional information
Expression and regulation
- Regulation:
- Additional information:
- belongs to the 100 most abundant proteins PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
Yasutaro Fujita, Hiroshi Matsuoka, Kazutake Hirooka
Regulation of fatty acid metabolism in bacteria.
Mol Microbiol: 2007, 66(4);829-39
[PubMed:17919287]
[WorldCat.org]
[DOI]
(P p)
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
Michaela Wenzel, Malay Patra, Dirk Albrecht, David Y-K Chen, K C Nicolaou, Nils Metzler-Nolte, Julia E Bandow
Proteomic signature of fatty acid biosynthesis inhibition available for in vivo mechanism-of-action studies.
Antimicrob Agents Chemother: 2011, 55(6);2590-6
[PubMed:21383089]
[WorldCat.org]
[DOI]
(I p)
Kook-Han Kim, Byung Hak Ha, Su Jin Kim, Seung Kon Hong, Kwang Yeon Hwang, Eunice Eunkyeong Kim
Crystal structures of Enoyl-ACP reductases I (FabI) and III (FabL) from B. subtilis.
J Mol Biol: 2011, 406(3);403-15
[PubMed:21185310]
[WorldCat.org]
[DOI]
(I p)
Helena B Thomaides, Ella J Davison, Lisa Burston, Hazel Johnson, David R Brown, Alison C Hunt, Jeffery Errington, Lloyd Czaplewski
Essential bacterial functions encoded by gene pairs.
J Bacteriol: 2007, 189(2);591-602
[PubMed:17114254]
[WorldCat.org]
[DOI]
(P p)
Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759]
[WorldCat.org]
[DOI]
(P p)
Gustavo E Schujman, Luciana Paoletti, Alan D Grossman, Diego de Mendoza
FapR, a bacterial transcription factor involved in global regulation of membrane lipid biosynthesis.
Dev Cell: 2003, 4(5);663-72
[PubMed:12737802]
[WorldCat.org]
[DOI]
(P p)
R J Heath, N Su, C K Murphy, C O Rock
The enoyl-[acyl-carrier-protein] reductases FabI and FabL from Bacillus subtilis.
J Biol Chem: 2000, 275(51);40128-33
[PubMed:11007778]
[WorldCat.org]
[DOI]
(P p)
C Baldock, J B Rafferty, S E Sedelnikova, P J Baker, A R Stuitje, A R Slabas, T R Hawkes, D W Rice
A mechanism of drug action revealed by structural studies of enoyl reductase.
Science: 1996, 274(5295);2107-10
[PubMed:8953047]
[WorldCat.org]
[DOI]
(P p)