3-oxoacyl-[acyl-carrier-protein] synthase 1

Details

Name
3-oxoacyl-[acyl-carrier-protein] synthase 1
Synonyms
  • 2.3.1.41
  • 3-oxoacyl-[acyl-carrier-protein] synthase I
  • Beta-ketoacyl-ACP synthase I
  • fabC
  • KAS I
Gene Name
fabB
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0010565|3-oxoacyl-[acyl-carrier-protein] synthase 1
MKRAVITGLGIVSSIGNNQQEVLASLREGRSGITFSQELKDSGMRSHVWGNVKLDTTGLI
DRKVVRFMSDASIYAFLSMEQAIADAGLSPEAYQNNPRVGLIAGSGGGSPRFQVFGADAM
RGPRGLKAVGPYVVTKAMASGVSACLATPFKIHGVNYSISSACATSAHCIGNAVEQIQLG
KQDIVFAGGGEELCWEMACEFDAMGALSTKYNDTPEKASRTYDAHRDGFVIAGGGGMVVV
EELEHALARGAHIYAEIVGYGATSDGADMVAPSGEGAVRCMKMAMHGVDTPIDYLNSHGT
STPVGDVKELAAIREVFGDKSPAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSIN
IEELDEQAAGLNIVTETTDRELTTVMSNSFGFGGTNATLVMRKLKD
Number of residues
406
Molecular Weight
42612.995
Theoretical pI
5.25
GO Classification
Functions
3-oxoacyl-[acyl-carrier-protein] synthase activity
Processes
fatty acid biosynthetic process / lipid biosynthetic process
Components
cytosol
General Function
3-oxoacyl-[acyl-carrier-protein] synthase activity
Specific Function
Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Specific for elongation from C-10 to unsaturated C-16 and C-18 fatty acids.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0010566|3-oxoacyl-[acyl-carrier-protein] synthase 1 (fabB)
ATGAAACGTGCAGTGATTACTGGCCTGGGCATTGTTTCCAGCATCGGTAATAACCAGCAG
GAAGTCCTGGCATCTCTGCGTGAAGGACGTTCAGGGATCACTTTCTCTCAGGAGCTGAAG
GATTCCGGCATGCGTAGCCACGTCTGGGGCAACGTAAAACTGGATACCACTGGCCTCATT
GACCGCAAAGTTGTGCGCTTTATGAGCGACGCATCCATTTATGCATTCCTTTCTATGGAG
CAGGCAATCGCTGATGCGGGCCTCTCTCCGGAAGCTTACCAGAATAACCCGCGCGTTGGC
CTGATTGCAGGTTCCGGCGGCGGCTCCCCGCGTTTCCAGGTGTTCGGCGCTGACGCAATG
CGCGGCCCGCGCGGCCTGAAAGCGGTTGGCCCGTATGTGGTCACCAAAGCGATGGCATCC
GGCGTTTCTGCCTGCCTCGCCACCCCGTTTAAAATTCATGGCGTTAACTACTCCATCAGC
TCCGCGTGTGCGACTTCCGCACACTGTATCGGTAACGCAGTAGAGCAGATCCAACTGGGC
AAACAGGACATCGTGTTTGCTGGCGGCGGCGAAGAGCTGTGCTGGGAAATGGCTTGCGAA
TTCGACGCAATGGGTGCGCTGTCTACTAAATACAACGACACCCCGGAAAAAGCCTCCCGT
ACTTACGACGCTCACCGTGACGGTTTCGTTATCGCTGGCGGCGGCGGTATGGTAGTGGTT
GAAGAGCTGGAACACGCGCTGGCGCGTGGTGCTCACATCTATGCTGAAATCGTTGGCTAC
GGCGCAACCTCTGATGGTGCAGACATGGTTGCTCCGTCTGGCGAAGGCGCAGTACGCTGC
ATGAAGATGGCGATGCATGGCGTTGATACCCCAATCGATTACCTGAACTCCCACGGTACT
TCGACTCCGGTTGGCGACGTGAAAGAGCTGGCAGCTATCCGTGAAGTGTTCGGCGATAAG
AGCCCGGCGATTTCTGCAACCAAAGCCATGACCGGTCACTCTCTGGGCGCTGCTGGCGTA
CAGGAAGCTATCTACTCTCTGCTGATGCTGGAACACGGCTTTATCGCCCCGAGCATCAAC
ATTGAAGAGCTGGACGAGCAGGCTGCGGGTCTGAACATCGTGACCGAAACGACCGATCGC
GAACTGACCACCGTTATGTCTAACAGCTTCGGCTTCGGCGGCACCAACGCCACGCTGGTA
ATGCGCAAGCTGAAAGATTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0A953
UniProtKB Entry NameFABB_ECOLI
GenBank Protein ID145884
GenBank Gene IDM24427
General References
  1. Kauppinen S, Siggaard-Andersen M, von Wettstein-Knowles P: beta-Ketoacyl-ACP synthase I of Escherichia coli: nucleotide sequence of the fabB gene and identification of the cerulenin binding residue. Carlsberg Res Commun. 1988;53(6):357-70. [Article]
  2. Yamamoto Y, Aiba H, Baba T, Hayashi K, Inada T, Isono K, Itoh T, Kimura S, Kitagawa M, Makino K, Miki T, Mitsuhashi N, Mizobuchi K, Mori H, Nakade S, Nakamura Y, Nashimoto H, Oshima T, Oyama S, Saito N, Sampei G, Satoh Y, Sivasundaram S, Tagami H, Horiuchi T, et al.: Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features. DNA Res. 1997 Apr 28;4(2):91-113. [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. Siggaard-Andersen M: Role of Escherichia coli beta-ketoacyl-ACP synthase I in unsaturated fatty acid synthesis. Carlsberg Res Commun. 1988;53(6):371-9. [Article]
  6. VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
  7. Olsen JG, Kadziola A, von Wettstein-Knowles P, Siggaard-Andersen M, Lindquist Y, Larsen S: The X-ray crystal structure of beta-ketoacyl [acyl carrier protein] synthase I. FEBS Lett. 1999 Oct 22;460(1):46-52. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01034CeruleninexperimentalyesinhibitorDetails
DB03017Lauric acidapproved, experimentalunknownDetails
DB03600Capric acidexperimentalunknownDetails
DB043024-Hydroxy-3,5-Dimethyl-5-(2-Methyl-Buta-1,3-Dienyl)-5h-Thiophen-2-OneexperimentalunknownDetails
DB04519Caprylic acidinvestigationalunknownDetails
DB083592-PHENYLAMINO-4-METHYL-5-ACETYL THIAZOLEexperimentalunknownDetails
DB08627(5R)-4-HYDROXY-3,5-DIMETHYL-5-[(1E,3E)-2-METHYLPENTA-1,3-DIENYL]THIOPHEN-2(5H)-ONEexperimentalunknownDetails
DB08628(5R)-5-[(1E)-BUTA-1,3-DIENYL]-4-HYDROXY-3,5-DIMETHYLTHIOPHEN-2(5H)-ONEexperimentalunknownDetails