3-oxoacyl-[acyl-carrier-protein] synthase 2
Details
- Name
- 3-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 Name
- fabF
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0010563|3-oxoacyl-[acyl-carrier-protein] synthase 2 MSKRRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCE DIISRKEQRKMDAFIQYGIVAGVQAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHT SLMNGGPRKISPFFVPSTIVNMVAGHLTIMYGLRGPSISIATACTSGVHNIGHAARIIAY GDADVMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKERDGFVLGDGAGMLV LEEYEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMANALRDAGIEASQIGY VNAHGTSTPAGDKAEAQAVKTIFGEAASRVLVSSTKSMTGHLLGAAGAVESIYSILALRD QAVPPTINLDNPDEGCDLDFVPHEARQVSGMEYTLCNSFGFGGTNGSLIFKKI
- Number of residues
- 413
- Molecular Weight
- 43045.39
- Theoretical pI
- 6.0
- GO Classification
- Functions3-oxoacyl-[acyl-carrier-protein] synthase activity / beta-ketoacyl-acyl-carrier-protein synthase II activityProcessesfatty acid biosynthetic processComponentscytosol
- General Function
- Beta-ketoacyl-acyl-carrier-protein synthase ii activity
- Specific Function
- Catalyzes 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.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- 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
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0AAI5 UniProtKB Entry Name FABF_ECOLI GenBank Protein ID 572680 GenBank Gene ID Z34979 - General References
- 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. [Article]
- 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. [Article]
- 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]
- 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]
- 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]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB01034 Cerulenin experimental yes inhibitor Details DB03017 Lauric acid approved, experimental unknown Details DB08366 3-({3-[(1S,4aS,6S,7S,9S,9aR)-1,6-dimethyl-2-oxodecahydro-6,9-epoxy-4a,7-methanobenzo[7]annulen-1-yl]propanoyl}amino)-2,4-dihydroxybenzoic acid experimental unknown Details DB08407 Platensimycin experimental unknown Details