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
- Functions3-oxoacyl-[acyl-carrier-protein] synthase activityProcessesfatty acid biosynthetic process / lipid biosynthetic processComponentscytosol
- 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
Resource Link UniProtKB ID P0A953 UniProtKB Entry Name FABB_ECOLI GenBank Protein ID 145884 GenBank Gene ID M24427 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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 ID Name Drug group Pharmacological action? Actions Details DB01034 Cerulenin experimental yes inhibitor Details DB03017 Lauric acid approved, experimental unknown Details DB03600 Capric acid experimental unknown Details DB04302 4-Hydroxy-3,5-Dimethyl-5-(2-Methyl-Buta-1,3-Dienyl)-5h-Thiophen-2-One experimental unknown Details DB04519 Caprylic acid investigational unknown Details DB08359 2-PHENYLAMINO-4-METHYL-5-ACETYL THIAZOLE experimental unknown Details DB08627 (5R)-4-HYDROXY-3,5-DIMETHYL-5-[(1E,3E)-2-METHYLPENTA-1,3-DIENYL]THIOPHEN-2(5H)-ONE experimental unknown Details DB08628 (5R)-5-[(1E)-BUTA-1,3-DIENYL]-4-HYDROXY-3,5-DIMETHYLTHIOPHEN-2(5H)-ONE experimental unknown Details