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Entry: P0AAI5
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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   26-NOV-2014, entry version 91.
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 277:1453-1462(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   FUNCTION.
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   FUNCTION, AND CATALYTIC ACTIVITY.
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), AND ACTIVE SITE.
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. {ECO:0000269|PubMed:6988423,
CC       ECO:0000269|PubMed:9013860}.
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       {ECO:0000269|PubMed:9013860}.
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.
CC       {ECO:0000305}.
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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_000913.3.
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=2-413.
DR   PDB; 2GFW; X-ray; 2.40 A; A=2-413.
DR   PDB; 2GFX; X-ray; 2.59 A; A=2-413.
DR   PDB; 2GFY; X-ray; 2.85 A; A=2-413.
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   DrugBank; DB01034; Cerulenin.
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   InParanoid; P0AAI5; -.
DR   KO; K09458; -.
DR   OMA; CMANALR; -.
DR   OrthoDB; EOG6DG2SR; -.
DR   PhylomeDB; P0AAI5; -.
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   EvolutionaryTrace; P0AAI5; -.
DR   PRO; PR: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:CACAO.
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; SSF53901; 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. {ECO:0000269|PubMed:7972002}.
FT   CHAIN         2    413       3-oxoacyl-[acyl-carrier-protein] synthase
FT                                2.
FT                                /FTId=PRO_0000180314.
FT   ACT_SITE    164    164       {ECO:0000269|PubMed:10037680}.
FT   STRAND        6     15       {ECO:0000244|PDB:3HO9}.
FT   STRAND       18     20       {ECO:0000244|PDB:3HO9}.
FT   HELIX        21     29       {ECO:0000244|PDB:3HO9}.
FT   STRAND       35     37       {ECO:0000244|PDB:3HO9}.
FT   STRAND       50     52       {ECO:0000244|PDB:3HO9}.
FT   TURN         60     62       {ECO:0000244|PDB:3HO9}.
FT   HELIX        65     68       {ECO:0000244|PDB:3HO9}.
FT   HELIX        73     89       {ECO:0000244|PDB:3HO9}.
FT   TURN         95     97       {ECO:0000244|PDB:3HO9}.
FT   HELIX        98    100       {ECO:0000244|PDB:3HO9}.
FT   STRAND      101    106       {ECO:0000244|PDB:3HO9}.
FT   HELIX       112    125       {ECO:0000244|PDB:3HO9}.
FT   HELIX       127    129       {ECO:0000244|PDB:3HO9}.
FT   HELIX       134    138       {ECO:0000244|PDB:3HO9}.
FT   HELIX       142    151       {ECO:0000244|PDB:3HO9}.
FT   HELIX       163    165       {ECO:0000244|PDB:3HO9}.
FT   HELIX       166    180       {ECO:0000244|PDB:3HO9}.
FT   STRAND      184    192       {ECO:0000244|PDB:3HO9}.
FT   HELIX       197    205       {ECO:0000244|PDB:3HO9}.
FT   HELIX       216    219       {ECO:0000244|PDB:3HO9}.
FT   STRAND      235    243       {ECO:0000244|PDB:3HO9}.
FT   HELIX       244    249       {ECO:0000244|PDB:3HO9}.
FT   STRAND      256    265       {ECO:0000244|PDB:3HO9}.
FT   STRAND      270    272       {ECO:0000244|PDB:2GFV}.
FT   HELIX       278    291       {ECO:0000244|PDB:3HO9}.
FT   HELIX       295    297       {ECO:0000244|PDB:3HO9}.
FT   STRAND      300    302       {ECO:0000244|PDB:3HO9}.
FT   HELIX       309    323       {ECO:0000244|PDB:3HO9}.
FT   HELIX       324    328       {ECO:0000244|PDB:3HO9}.
FT   STRAND      330    333       {ECO:0000244|PDB:3HO9}.
FT   HELIX       336    339       {ECO:0000244|PDB:3HO9}.
FT   HELIX       343    345       {ECO:0000244|PDB:3HO9}.
FT   HELIX       346    360       {ECO:0000244|PDB:3HO9}.
FT   STRAND      370    372       {ECO:0000244|PDB:3HO9}.
FT   STRAND      382    384       {ECO:0000244|PDB:3HO9}.
FT   STRAND      393    400       {ECO:0000244|PDB:3HO9}.
FT   TURN        401    403       {ECO:0000244|PDB:3HO9}.
FT   STRAND      404    411       {ECO:0000244|PDB:3HO9}.
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
//
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