ID FABF_ECOLI Reviewed; 413 AA.
AC P0AAI5; P39435;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 01-MAY-2013, entry version 79.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 2;
DE EC=2.3.1.179;
DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase II;
DE AltName: Full=Beta-ketoacyl-ACP synthase II;
DE Short=KAS II;
GN Name=fabF; Synonyms=fabJ; OrderedLocusNames=b1095, JW1081;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-32.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=7972002; DOI=10.1073/pnas.91.23.11027;
RA Siggaard-Andersen M., Wissenbach M., Chuck J.-A., Svendsen I.,
RA Olsen J.G., von Wettstein-Knowles P.V.;
RT "The fabJ-encoded beta-ketoacyl-[acyl carrier protein] synthase IV
RT from Escherichia coli is sensitive to cerulenin and specific for
RT short-chain substrates.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:11027-11031(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND IDENTITY OF FABF AND FABJ.
RC STRAIN=K12 / UB1005;
RX PubMed=7768872;
RA Magnuson K., Carey M.R., Cronan J.E. Jr.;
RT "The putative fabJ gene of Escherichia coli fatty acid synthesis is
RT the fabF gene.";
RL J. Bacteriol. 177:3593-3595(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
RA Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
RA Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
RA Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
RA Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
RA Yano M., Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome
RT corresponding to the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA Mau B., Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1474(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains
RT MG1655 and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP IDENTIFICATION OF FABF AS KASII.
RX PubMed=3549687;
RA Jackowski S., Rock C.O.;
RT "Altered molecular form of acyl carrier protein associated with beta-
RT ketoacyl-acyl carrier protein synthase II (fabF) mutants.";
RL J. Bacteriol. 169:1469-1473(1987).
RN [7]
RP CHARACTERIZATION.
RX PubMed=6988423;
RA Garwin J.L., Klages A.L., Cronan J.E. Jr.;
RT "Beta-ketoacyl-acyl carrier protein synthase II of Escherichia coli.
RT Evidence for function in the thermal regulation of fatty acid
RT synthesis.";
RL J. Biol. Chem. 255:3263-3265(1980).
RN [8]
RP CHARACTERIZATION.
RX PubMed=9013860; DOI=10.1016/S0014-5793(96)01437-8;
RA Edwards P., Nelsen J.S., Metz J.G., Dehesh K.;
RT "Cloning of the fabF gene in an expression vector and in vitro
RT characterization of recombinant fabF and fabB encoded enzymes from
RT Escherichia coli.";
RL FEBS Lett. 402:62-66(1997).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=9482715; DOI=10.1093/emboj/17.5.1183;
RA Huang W., Jia J., Edwards P., Dehesh K., Schneider G., Lindqvist Y.;
RT "Crystal structure of beta-ketoacyl-acyl carrier protein synthase II
RT from E.coli reveals the molecular architecture of condensing
RT enzymes.";
RL EMBO J. 17:1183-1191(1998).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).
RX PubMed=10037680; DOI=10.1074/jbc.274.10.6031;
RA Moche M., Schneider G., Edwards P., Dehesh K., Lindqvist Y.;
RT "Structure of the complex between the antibiotic cerulenin and its
RT target, beta-ketoacyl-acyl carrier protein synthase.";
RL J. Biol. Chem. 274:6031-6034(1999).
CC -!- FUNCTION: Catalyzes the condensation reaction of fatty acid
CC synthesis by the addition to an acyl acceptor of two carbons from
CC malonyl-ACP. Has a preference for short chain acid substrates and
CC may function to supply the octanoic substrates for lipoic acid
CC biosynthesis.
CC -!- CATALYTIC ACTIVITY: (Z)-hexadec-11-enoyl-[acyl-carrier-protein] +
CC malonyl-[acyl-carrier-protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-
CC carrier-protein] + CO(2) + [acyl-carrier-protein].
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC P0A6Y8:dnaK; NbExp=2; IntAct=EBI-542783, EBI-542092;
CC -!- SIMILARITY: Belongs to the beta-ketoacyl-ACP synthases family.
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DR EMBL; Z34979; CAA84431.1; -; Genomic_DNA.
DR EMBL; U20767; AAA83255.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74179.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35903.1; -; Genomic_DNA.
DR PIR; I41060; I41060.
DR RefSeq; NP_415613.1; NC_000913.2.
DR RefSeq; YP_489363.1; NC_007779.1.
DR PDB; 1B3N; X-ray; 2.65 A; A=2-413.
DR PDB; 1KAS; X-ray; 2.40 A; A=2-413.
DR PDB; 2GFV; X-ray; 2.29 A; A=2-412.
DR PDB; 2GFW; X-ray; 2.40 A; A=2-412.
DR PDB; 2GFX; X-ray; 2.59 A; A=2-412.
DR PDB; 2GFY; X-ray; 2.85 A; A=2-412.
DR PDB; 3G0Y; X-ray; 2.60 A; A=2-413.
DR PDB; 3G11; X-ray; 2.00 A; A=2-413.
DR PDB; 3HNZ; X-ray; 2.75 A; A=2-413.
DR PDB; 3HO2; X-ray; 2.00 A; A=2-413.
DR PDB; 3HO9; X-ray; 1.90 A; A=2-413.
DR PDB; 3I8P; X-ray; 1.90 A; A=2-413.
DR PDBsum; 1B3N; -.
DR PDBsum; 1KAS; -.
DR PDBsum; 2GFV; -.
DR PDBsum; 2GFW; -.
DR PDBsum; 2GFX; -.
DR PDBsum; 2GFY; -.
DR PDBsum; 3G0Y; -.
DR PDBsum; 3G11; -.
DR PDBsum; 3HNZ; -.
DR PDBsum; 3HO2; -.
DR PDBsum; 3HO9; -.
DR PDBsum; 3I8P; -.
DR ProteinModelPortal; P0AAI5; -.
DR SMR; P0AAI5; 3-413.
DR DIP; DIP-29377N; -.
DR IntAct; P0AAI5; 6.
DR MINT; MINT-1231688; -.
DR STRING; 511145.b1095; -.
DR PaxDb; P0AAI5; -.
DR PRIDE; P0AAI5; -.
DR EnsemblBacteria; AAC74179; AAC74179; b1095.
DR EnsemblBacteria; BAA35903; BAA35903; BAA35903.
DR GeneID; 12931078; -.
DR GeneID; 946665; -.
DR KEGG; ecj:Y75_p1065; -.
DR KEGG; eco:b1095; -.
DR PATRIC; 32117431; VBIEscCol129921_1138.
DR EchoBASE; EB2490; -.
DR EcoGene; EG12606; fabF.
DR eggNOG; COG0304; -.
DR HOGENOM; HOG000060165; -.
DR KO; K09458; -.
DR OMA; INMISGF; -.
DR ProtClustDB; PRK07314; -.
DR BioCyc; EcoCyc:3-OXOACYL-ACP-SYNTHII-MONOMER; -.
DR BioCyc; ECOL316407:JW1081-MONOMER; -.
DR BioCyc; MetaCyc:3-OXOACYL-ACP-SYNTHII-MONOMER; -.
DR BRENDA; 2.3.1.179; 2026.
DR SABIO-RK; P0AAI5; -.
DR UniPathway; UPA00094; -.
DR DrugBank; DB01034; Cerulenin.
DR EvolutionaryTrace; P0AAI5; -.
DR Genevestigator; P0AAI5; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IDA:EcoCyc.
DR GO; GO:0033817; F:beta-ketoacyl-acyl-carrier-protein synthase II activity; IDA:EcoCyc.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR017568; 3-oxoacyl-ACP_synth-2.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR016038; Thiolase-like_subgr.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR PIRSF; PIRSF000447; KAS_II; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR TIGRFAMs; TIGR03150; fabF; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Complete proteome;
KW Direct protein sequencing; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism;
KW Reference proteome; Transferase.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 413 3-oxoacyl-[acyl-carrier-protein] synthase
FT 2.
FT /FTId=PRO_0000180314.
FT ACT_SITE 164 164
FT STRAND 6 15
FT STRAND 18 20
FT HELIX 21 29
FT STRAND 35 37
FT STRAND 50 52
FT TURN 60 62
FT HELIX 65 68
FT HELIX 73 89
FT TURN 95 97
FT HELIX 98 100
FT STRAND 101 106
FT HELIX 112 125
FT HELIX 127 129
FT HELIX 134 138
FT HELIX 142 151
FT HELIX 163 165
FT HELIX 166 180
FT STRAND 184 192
FT HELIX 197 205
FT HELIX 216 219
FT STRAND 235 243
FT HELIX 244 249
FT STRAND 256 265
FT STRAND 270 272
FT HELIX 278 291
FT HELIX 295 297
FT STRAND 300 302
FT HELIX 309 323
FT HELIX 324 328
FT STRAND 330 333
FT HELIX 336 339
FT HELIX 343 345
FT HELIX 346 360
FT STRAND 370 372
FT STRAND 382 384
FT STRAND 393 400
FT TURN 401 403
FT STRAND 404 411
SQ SEQUENCE 413 AA; 43046 MW; 5F60DB1F986B2EE5 CRC64;
MSKRRVVVTG LGMLSPVGNT VESTWKALLA GQSGISLIDH FDTSAYATKF AGLVKDFNCE
DIISRKEQRK MDAFIQYGIV AGVQAMQDSG LEITEENATR IGAAIGSGIG GLGLIEENHT
SLMNGGPRKI SPFFVPSTIV NMVAGHLTIM YGLRGPSISI ATACTSGVHN IGHAARIIAY
GDADVMVAGG AEKASTPLGV GGFGAARALS TRNDNPQAAS RPWDKERDGF VLGDGAGMLV
LEEYEHAKKR GAKIYAELVG FGMSSDAYHM TSPPENGAGA ALAMANALRD AGIEASQIGY
VNAHGTSTPA GDKAEAQAVK TIFGEAASRV LVSSTKSMTG HLLGAAGAVE SIYSILALRD
QAVPPTINLD NPDEGCDLDF VPHEARQVSG MEYTLCNSFG FGGTNGSLIF KKI
//
