3-oxoacyl-[acyl-carrier-protein] reductase FabG

Details

Name
3-oxoacyl-[acyl-carrier-protein] reductase FabG
Synonyms
  • 1.1.1.100
  • 3-ketoacyl-acyl carrier protein reductase
  • Beta-ketoacyl-ACP reductase
  • Beta-Ketoacyl-acyl carrier protein reductase
Gene Name
fabG
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0011499|3-oxoacyl-[acyl-carrier-protein] reductase FabG
MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLNV
TDPASIESVLEKIRAEFGEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKA
VMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSKSLAREVASRGITVNVVA
PGFIETDMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVNGG
MYMV
Number of residues
244
Molecular Weight
25560.065
Theoretical pI
7.67
GO Classification
Functions
3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity / identical protein binding / metal ion binding / NAD binding / NADP binding
Processes
biotin biosynthetic process / fatty acid biosynthetic process / fatty acid elongation / lipid biosynthetic process
Components
cytosol
General Function
Nadp binding
Specific Function
Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0011500|3-oxoacyl-[acyl-carrier-protein] reductase FabG (fabG)
ATGAATTTTGAAGGAAAAATCGCACTGGTAACCGGTGCAAGCCGCGGAATTGGCCGCGCA
ATTGCTGAAACGCTCGCAGCCCGTGGCGCGAAAGTTATTGGCACTGCGACCAGTGAAAAT
GGCGCTCAGGCGATCAGTGATTATTTAGGTGCCAACGGCAAAGGTCTGATGTTGAATGTG
ACCGACCCGGCATCTATCGAATCTGTTCTGGAAAAAATTCGCGCAGAATTTGGTGAAGTG
GATATCCTGGTCAATAATGCCGGTATCACTCGTGATAACCTGTTAATGCGAATGAAAGAT
GAAGAGTGGAACGATATTATCGAAACCAACCTTTCATCTGTTTTCCGTCTGTCAAAAGCG
GTAATGCGCGCTATGATGAAAAAGCGTCATGGTCGTATTATCACTATCGGTTCTGTGGTT
GGTACCATGGGAAATGGCGGTCAGGCCAACTACGCTGCGGCGAAAGCGGGCTTGATCGGC
TTCAGTAAATCACTGGCGCGCGAAGTTGCGTCACGCGGTATTACTGTAAACGTTGTTGCT
CCGGGCTTTATTGAAACGGACATGACACGTGCGCTGAGCGATGACCAGCGTGCGGGTATC
CTGGCGCAGGTTCCTGCGGGTCGCCTCGGCGGCGCACAGGAAATCGCCAACGCGGTTGCA
TTCCTGGCATCCGACGAAGCAGCTTACATCACGGGTGAAACTTTGCATGTGAACGGCGGG
ATGTACATGGTCTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0AEK2
UniProtKB Entry NameFABG_ECOLI
GenBank Gene IDM84991
General References
  1. Rawlings M, Cronan JE Jr: The gene encoding Escherichia coli acyl carrier protein lies within a cluster of fatty acid biosynthetic genes. J Biol Chem. 1992 Mar 25;267(9):5751-4. [Article]
  2. Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. 1996 Jun 30;3(3):137-55. [Article]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  4. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  5. Verwoert II, Verbree EC, van der Linden KH, Nijkamp HJ, Stuitje AR: Cloning, nucleotide sequence, and expression of the Escherichia coli fabD gene, encoding malonyl coenzyme A-acyl carrier protein transacylase. J Bacteriol. 1992 May;174(9):2851-7. [Article]
  6. Toomey RE, Wakil SJ: Studies on the mechanism of fatty acid synthesis. XV. Preparation and general properties of beta-ketoacyl acyl carrier protein reductase from Escherichia coli. Biochim Biophys Acta. 1966 Apr 4;116(2):189-97. [Article]
  7. Heath RJ, Rock CO: Inhibition of beta-ketoacyl-acyl carrier protein synthase III (FabH) by acyl-acyl carrier protein in Escherichia coli. J Biol Chem. 1996 May 3;271(18):10996-1000. [Article]
  8. Lai CY, Cronan JE: Isolation and characterization of beta-ketoacyl-acyl carrier protein reductase (fabG) mutants of Escherichia coli and Salmonella enterica serovar Typhimurium. J Bacteriol. 2004 Mar;186(6):1869-78. [Article]
  9. Kristan K, Bratkovic T, Sova M, Gobec S, Prezelj A, Urleb U: Novel inhibitors of beta-ketoacyl-ACP reductase from Escherichia coli. Chem Biol Interact. 2009 Mar 16;178(1-3):310-6. doi: 10.1016/j.cbi.2008.09.030. Epub 2008 Oct 9. [Article]
  10. Price AC, Zhang YM, Rock CO, White SW: Structure of beta-ketoacyl-[acyl carrier protein] reductase from Escherichia coli: negative cooperativity and its structural basis. Biochemistry. 2001 Oct 30;40(43):12772-81. [Article]
  11. Price AC, Zhang YM, Rock CO, White SW: Cofactor-induced conformational rearrangements establish a catalytically competent active site and a proton relay conduit in FabG. Structure. 2004 Mar;12(3):417-28. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03461Nicotinamide adenine dinucleotide phosphateexperimentalunknownDetails