3-oxoacyl-[acyl-carrier-protein] synthase 2

Name3-oxoacyl-[acyl-carrier-protein] synthase 2
Synonyms
  • 2.3.1.179
  • 3-oxoacyl-[acyl-carrier-protein] synthase II
  • Beta-ketoacyl-ACP synthase II
  • fabJ
  • KAS II
Gene NamefabF
OrganismEscherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0010563|3-oxoacyl-[acyl-carrier-protein] synthase 2
MSKRRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCE
DIISRKEQRKMDAFIQYGIVAGVQAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHT
SLMNGGPRKISPFFVPSTIVNMVAGHLTIMYGLRGPSISIATACTSGVHNIGHAARIIAY
GDADVMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKERDGFVLGDGAGMLV
LEEYEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMANALRDAGIEASQIGY
VNAHGTSTPAGDKAEAQAVKTIFGEAASRVLVSSTKSMTGHLLGAAGAVESIYSILALRD
QAVPPTINLDNPDEGCDLDFVPHEARQVSGMEYTLCNSFGFGGTNGSLIFKKI
Number of residuesNone
Molecular Weight43045.39
Theoretical pI6.0
GO Classification
Functions
  • 3-oxoacyl-[acyl-carrier-protein] synthase activity
  • beta-ketoacyl-acyl-carrier-protein synthase II activity
Processes
  • fatty acid biosynthetic process
Components
  • cytosol
General FunctionBeta-ketoacyl-acyl-carrier-protein synthase ii activity
Specific FunctionCatalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Has a preference for short chain acid substrates and may function to supply the octanoic substrates for lipoic acid biosynthesis.
Transmembrane Regions
GenBank Protein ID
UniProtKB IDP0AAI5
UniProtKB Entry Name
Cellular LocationNone
Gene sequence
>lcl|BSEQ0010564|3-oxoacyl-[acyl-carrier-protein] synthase 2 (fabF)
GTGTCTAAGCGTCGTGTAGTTGTGACCGGACTGGGCATGTTGTCTCCTGTCGGCAATACC
GTAGAGTCTACCTGGAAAGCTCTGCTTGCCGGTCAGAGTGGCATCAGCCTAATCGACCAT
TTCGATACTAGCGCCTATGCAACGAAATTTGCTGGCTTAGTAAAGGATTTTAACTGTGAG
GACATTATCTCGCGCAAAGAACAGCGCAAGATGGATGCCTTCATTCAATATGGAATTGTC
GCTGGCGTTCAGGCCATGCAGGATTCTGGCCTTGAAATAACGGAAGAGAACGCAACCCGC
ATTGGTGCCGCAATTGGCTCCGGGATTGGCGGCCTCGGACTGATCGAAGAAAACCACACA
TCTCTGATGAACGGTGGTCCACGTAAGATCAGCCCATTCTTCGTTCCGTCAACGATTGTG
AACATGGTGGCAGGTCATCTGACTATCATGTATGGCCTGCGTGGCCCGAGCATCTCTATC
GCGACTGCCTGTACTTCCGGCGTGCACAACATTGGCCATGCTGCGCGTATTATCGCGTAT
GGCGATGCTGACGTGATGGTTGCAGGTGGCGCAGAGAAAGCCAGTACGCCGCTGGGCGTT
GGTGGTTTTGGCGCGGCACGTGCATTATCTACCCGCAATGATAACCCGCAAGCGGCGAGC
CGCCCGTGGGATAAAGAGCGTGATGGTTTCGTACTGGGCGATGGTGCCGGTATGCTGGTA
CTTGAAGAGTACGAACACGCGAAAAAACGCGGTGCGAAAATTTACGCTGAACTCGTCGGC
TTTGGTATGAGCAGCGATGCTTATCATATGACGTCACCGCCAGAAAATGGCGCAGGCGCA
GCTCTGGCGATGGCAAATGCTCTGCGTGATGCAGGCATTGAAGCGAGTCAGATTGGCTAC
GTTAACGCGCACGGTACTTCTACGCCGGCTGGCGATAAAGCTGAAGCGCAGGCGGTGAAA
ACCATCTTCGGTGAAGCTGCAAGCCGTGTGTTGGTAAGCTCCACGAAATCTATGACCGGT
CACCTGTTAGGTGCGGCGGGTGCAGTAGAATCTATCTACTCCATCCTGGCGCTGCGCGAT
CAGGCTGTTCCGCCAACCATCAACCTGGATAACCCGGATGAAGGTTGCGATCTGGATTTC
GTACCGCACGAAGCGCGTCAGGTTAGCGGAATGGAATACACTCTGTGTAACTCCTTCGGC
TTCGGTGGCACTAATGGTTCTTTGATCTTTAAAAAGATCTAA
GenBank Gene ID
GeneCard IDNone
GenAtlas ID
HGNC ID
Chromosome LocationNone
LocusNone
References
  1. Siggaard-Andersen M, Wissenbach M, Chuck JA, Svendsen I, Olsen JG, von Wettstein-Knowles P: The fabJ-encoded beta-ketoacyl-[acyl carrier protein] synthase IV from Escherichia coli is sensitive to cerulenin and specific for short-chain substrates. Proc Natl Acad Sci U S A. 1994 Nov 8;91(23):11027-31. [7972002 ]
  2. Magnuson K, Carey MR, Cronan JE Jr: The putative fabJ gene of Escherichia coli fatty acid synthesis is the fabF gene. J Bacteriol. 1995 Jun;177(12):3593-5. [7768872 ]
  3. 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. [8905232 ]
  4. 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. [9278503 ]
  5. 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. [16738553 ]
  6. Jackowski S, Rock CO: Altered molecular form of acyl carrier protein associated with beta-ketoacyl-acyl carrier protein synthase II (fabF) mutants. J Bacteriol. 1987 Apr;169(4):1469-73. [3549687 ]
  7. Garwin JL, Klages AL, Cronan JE Jr: Beta-ketoacyl-acyl carrier protein synthase II of Escherichia coli. Evidence for function in the thermal regulation of fatty acid synthesis. J Biol Chem. 1980 Apr 25;255(8):3263-5. [6988423 ]
  8. Edwards P, Nelsen JS, Metz JG, Dehesh K: Cloning of the fabF gene in an expression vector and in vitro characterization of recombinant fabF and fabB encoded enzymes from Escherichia coli. FEBS Lett. 1997 Jan 27;402(1):62-6. [9013860 ]
  9. Huang W, Jia J, Edwards P, Dehesh K, Schneider G, Lindqvist Y: Crystal structure of beta-ketoacyl-acyl carrier protein synthase II from E.coli reveals the molecular architecture of condensing enzymes. EMBO J. 1998 Mar 2;17(5):1183-91. [9482715 ]
  10. Moche M, Schneider G, Edwards P, Dehesh K, Lindqvist Y: Structure of the complex between the antibiotic cerulenin and its target, beta-ketoacyl-acyl carrier protein synthase. J Biol Chem. 1999 Mar 5;274(10):6031-4. [10037680 ]

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