FAS_CHICK
ID FAS_CHICK Reviewed; 2512 AA.
AC P12276;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Fatty acid synthase;
DE EC=2.3.1.85 {ECO:0000269|PubMed:3182791, ECO:0000269|PubMed:6361031, ECO:0000269|PubMed:6654913, ECO:0000269|PubMed:6654914};
DE Includes:
DE RecName: Full=[Acyl-carrier-protein] S-acetyltransferase;
DE EC=2.3.1.38 {ECO:0000269|PubMed:6654913, ECO:0000269|PubMed:6654914};
DE Includes:
DE RecName: Full=[Acyl-carrier-protein] S-malonyltransferase;
DE EC=2.3.1.39 {ECO:0000269|PubMed:6654913, ECO:0000269|PubMed:6654914};
DE Includes:
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase;
DE EC=2.3.1.41 {ECO:0000305|PubMed:6654913};
DE Includes:
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase;
DE EC=1.1.1.100 {ECO:0000305|PubMed:3182791, ECO:0000305|PubMed:6361031, ECO:0000305|PubMed:6654913};
DE Includes:
DE RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase;
DE EC=4.2.1.59 {ECO:0000305|PubMed:3182791, ECO:0000305|PubMed:6654913};
DE Includes:
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase;
DE EC=1.3.1.39 {ECO:0000305|PubMed:6654913};
DE Includes:
DE RecName: Full=Acyl-[acyl-carrier-protein] hydrolase;
DE EC=3.1.2.14 {ECO:0000305|PubMed:1939144, ECO:0000305|PubMed:2681189, ECO:0000305|PubMed:6654913};
GN Name=FASN; Synonyms=FAS;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-12, AND ACETYLATION AT
RP GLU-2.
RC STRAIN=White leghorn; TISSUE=Liver;
RX PubMed=7944406; DOI=10.1006/abbi.1994.1410;
RA Huang W.-Y., Chirala S.S., Wakil S.J.;
RT "Amino-terminal blocking group and sequence of the animal fatty acid
RT synthase.";
RL Arch. Biochem. Biophys. 314:45-49(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 75-1775.
RC TISSUE=Liver;
RX PubMed=2734291; DOI=10.1073/pnas.86.12.4387;
RA Holzer K.P., Liu W., Hammes G.G.;
RT "Molecular cloning and sequencing of chicken liver fatty acid synthase
RT cDNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:4387-4391(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1568-2512, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2917973; DOI=10.1016/s0021-9258(19)84913-x;
RA Chirala S.S., Kasturi R., Pazirandeh M., Stolow D.T., Huang W.-Y.,
RA Wakil S.J.;
RT "A novel cDNA extension procedure. Isolation of chicken fatty acid synthase
RT cDNA clones.";
RL J. Biol. Chem. 264:3750-3757(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1752-2512.
RX PubMed=2842766; DOI=10.1073/pnas.85.17.6328;
RA Yuan Z., Liu W., Hammes G.G.;
RT "Molecular cloning and sequencing of DNA complementary to chicken liver
RT fatty acid synthase mRNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:6328-6331(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 2202-2512.
RX PubMed=3207710; DOI=10.1021/bi00420a029;
RA Kasturi R., Chirala S.S., Pazirandeh M., Wakil S.J.;
RT "Characterization of a genomic and cDNA clone coding for the thioesterase
RT domain and 3' noncoding region of the chicken liver fatty acid synthase
RT gene.";
RL Biochemistry 27:7778-7785(1988).
RN [6]
RP PROTEIN SEQUENCE OF 2122-2210.
RX PubMed=2648999; DOI=10.1016/0003-9861(89)90011-8;
RA Huang W.-Y., Stoops J.K., Wakil S.J.;
RT "Complete amino acid sequence of chicken liver acyl carrier protein derived
RT from the fatty acid synthase.";
RL Arch. Biochem. Biophys. 270:92-98(1989).
RN [7]
RP PROTEIN SEQUENCE OF 2210-2509.
RC STRAIN=White leghorn;
RX PubMed=3207709; DOI=10.1021/bi00420a028;
RA Yang C.-Y., Huang W.-Y., Chirala S.S., Wakil S.J.;
RT "Complete amino acid sequence of the thioesterase domain of chicken liver
RT fatty acid synthase.";
RL Biochemistry 27:7773-7777(1988).
RN [8]
RP PROTEIN SEQUENCE OF 668-675 AND 1699-1710.
RX PubMed=2751995; DOI=10.1021/bi00435a023;
RA Chang S.I., Hammes G.G.;
RT "Amino acid sequences of pyridoxal 5'-phosphate binding sites and
RT fluorescence resonance energy transfer in chicken liver fatty acid
RT synthase.";
RL Biochemistry 28:3781-3788(1989).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=6654913; DOI=10.1016/s0021-9258(17)43806-3;
RA Mattick J.S., Nickless J., Mizugaki M., Yang C.Y., Uchiyama S., Wakil S.J.;
RT "The architecture of the animal fatty acid synthetase. II. Separation of
RT the core and thioesterase functions and determination of the N-C
RT orientation of the subunit.";
RL J. Biol. Chem. 258:15300-15304(1983).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=6361031; DOI=10.1016/s0021-9258(17)43807-5;
RA Wong H., Mattick J.S., Wakil S.J.;
RT "The architecture of the animal fatty acid synthetase. III. Isolation and
RT characterization of beta-ketoacyl reductase.";
RL J. Biol. Chem. 258:15305-15311(1983).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND PATHWAY.
RX PubMed=6654914; DOI=10.1016/s0021-9258(17)43808-7;
RA Tsukamoto Y., Wong H., Mattick J.S., Wakil S.J.;
RT "The architecture of the animal fatty acid synthetase complex. IV. Mapping
RT of active centers and model for the mechanism of action.";
RL J. Biol. Chem. 258:15312-15322(1983).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=3182791; DOI=10.1016/s0021-9258(18)37582-3;
RA Tsukamoto Y., Wakil S.J.;
RT "Isolation and mapping of the beta-hydroxyacyl dehydratase activity of
RT chicken liver fatty acid synthase.";
RL J. Biol. Chem. 263:16225-16229(1988).
RN [13]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=2681189; DOI=10.1016/s0021-9258(19)84696-3;
RA Pazirandeh M., Chirala S.S., Huang W.Y., Wakil S.J.;
RT "Characterization of recombinant thioesterase and acyl carrier protein
RT domains of chicken fatty acid synthase expressed in Escherichia coli.";
RL J. Biol. Chem. 264:18195-18201(1989).
RN [14]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=1939144; DOI=10.1016/s0021-9258(18)54802-x;
RA Pazirandeh M., Chirala S.S., Wakil S.J.;
RT "Site-directed mutagenesis studies on the recombinant thioesterase domain
RT of chicken fatty acid synthase expressed in Escherichia coli.";
RL J. Biol. Chem. 266:20946-20952(1991).
CC -!- FUNCTION: Fatty acid synthetase is a multifunctional enzyme that
CC catalyzes the de novo biosynthesis of long-chain saturated fatty acids
CC starting from acetyl-CoA and malonyl-CoA in the presence of NADPH. This
CC multifunctional protein contains 7 catalytic activities and a site for
CC the binding of the prosthetic group 4'-phosphopantetheine of the acyl
CC carrier protein ([ACP]) domain. {ECO:0000269|PubMed:3182791,
CC ECO:0000269|PubMed:6361031, ECO:0000269|PubMed:6654913,
CC ECO:0000269|PubMed:6654914}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain
CC fatty acid + n CO2 + (n+1) CoA + 2n NADP(+); Xref=Rhea:RHEA:14993,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57560,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=2.3.1.85;
CC Evidence={ECO:0000269|PubMed:3182791, ECO:0000269|PubMed:6361031,
CC ECO:0000269|PubMed:6654913, ECO:0000269|PubMed:6654914};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14994;
CC Evidence={ECO:0000269|PubMed:3182791, ECO:0000269|PubMed:6361031,
CC ECO:0000269|PubMed:6654913, ECO:0000269|PubMed:6654914};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + holo-[ACP] = acetyl-[ACP] + CoA;
CC Xref=Rhea:RHEA:41788, Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78446; EC=2.3.1.38; Evidence={ECO:0000269|PubMed:6654913,
CC ECO:0000269|PubMed:6654914};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41789;
CC Evidence={ECO:0000269|PubMed:6654913, ECO:0000269|PubMed:6654914};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP];
CC Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449; EC=2.3.1.39; Evidence={ECO:0000269|PubMed:6654913,
CC ECO:0000269|PubMed:6654914};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41793;
CC Evidence={ECO:0000269|PubMed:6654913, ECO:0000269|PubMed:6654914};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP]
CC + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651;
CC EC=2.3.1.41; Evidence={ECO:0000305|PubMed:6654913};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22837;
CC Evidence={ECO:0000305|PubMed:6654913};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+)
CC + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-
CC COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;
CC Evidence={ECO:0000305|PubMed:3182791, ECO:0000305|PubMed:6361031,
CC ECO:0000305|PubMed:6654913};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17399;
CC Evidence={ECO:0000305|PubMed:3182791, ECO:0000305|PubMed:6361031,
CC ECO:0000305|PubMed:6654913};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O;
CC Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59;
CC Evidence={ECO:0000305|PubMed:3182791, ECO:0000305|PubMed:6654913};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13098;
CC Evidence={ECO:0000305|PubMed:3182791, ECO:0000305|PubMed:6654913};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-[ACP] + NADP(+) = a (2E)-enoyl-[ACP] +
CC H(+) + NADPH; Xref=Rhea:RHEA:22564, Rhea:RHEA-COMP:9925, Rhea:RHEA-
CC COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.39;
CC Evidence={ECO:0000305|PubMed:6654913};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22566;
CC Evidence={ECO:0000305|PubMed:6654913};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexadecanoyl-[ACP] = H(+) + hexadecanoate + holo-[ACP];
CC Xref=Rhea:RHEA:41932, Rhea:RHEA-COMP:9652, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78483; EC=3.1.2.14;
CC Evidence={ECO:0000305|PubMed:1939144, ECO:0000305|PubMed:2681189,
CC ECO:0000305|PubMed:6654913};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41933;
CC Evidence={ECO:0000305|PubMed:1939144, ECO:0000305|PubMed:2681189,
CC ECO:0000305|PubMed:6654913};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] +
CC CO2 + holo-[ACP]; Xref=Rhea:RHEA:41800, Rhea:RHEA-COMP:9621,
CC Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9625, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78446, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41801;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxobutanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxybutanoyl-
CC [ACP] + NADP(+); Xref=Rhea:RHEA:41804, Rhea:RHEA-COMP:9625,
CC Rhea:RHEA-COMP:9626, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:78450, ChEBI:CHEBI:78451;
CC Evidence={ECO:0000305|PubMed:3182791, ECO:0000305|PubMed:6361031,
CC ECO:0000305|PubMed:6654913};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41805;
CC Evidence={ECO:0000305|PubMed:3182791, ECO:0000305|PubMed:6361031,
CC ECO:0000305|PubMed:6654913};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxybutanoyl-[ACP] = (2E)-butenoyl-[ACP] + H2O;
CC Xref=Rhea:RHEA:41808, Rhea:RHEA-COMP:9626, Rhea:RHEA-COMP:9627,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78451, ChEBI:CHEBI:78453;
CC Evidence={ECO:0000305|PubMed:3182791, ECO:0000305|PubMed:6654913};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41809;
CC Evidence={ECO:0000305|PubMed:3182791, ECO:0000305|PubMed:6654913};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-butenoyl-[ACP] + H(+) + NADPH = butanoyl-[ACP] + NADP(+);
CC Xref=Rhea:RHEA:41812, Rhea:RHEA-COMP:9627, Rhea:RHEA-COMP:9628,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78453, ChEBI:CHEBI:78454;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41813;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxohexanoyl-[ACP] +
CC CO2 + holo-[ACP]; Xref=Rhea:RHEA:41820, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9628, Rhea:RHEA-COMP:9629, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78454, ChEBI:CHEBI:78456;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41821;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxohexanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxyhexanoyl-
CC [ACP] + NADP(+); Xref=Rhea:RHEA:41824, Rhea:RHEA-COMP:9629,
CC Rhea:RHEA-COMP:9630, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:78456, ChEBI:CHEBI:78457;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41825;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxyhexanoyl-[ACP] = (2E)-hexenoyl-[ACP] + H2O;
CC Xref=Rhea:RHEA:41828, Rhea:RHEA-COMP:9630, Rhea:RHEA-COMP:9631,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78457, ChEBI:CHEBI:78458;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41829;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-hexenoyl-[ACP] + H(+) + NADPH = hexanoyl-[ACP] + NADP(+);
CC Xref=Rhea:RHEA:41832, Rhea:RHEA-COMP:9631, Rhea:RHEA-COMP:9632,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78458, ChEBI:CHEBI:78459;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41833;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexanoyl-[ACP] + malonyl-[ACP] = 3-oxooctanoyl-[ACP] +
CC CO2 + holo-[ACP]; Xref=Rhea:RHEA:41836, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9632, Rhea:RHEA-COMP:9633, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78459, ChEBI:CHEBI:78460;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41837;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxooctanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxyoctanoyl-
CC [ACP] + NADP(+); Xref=Rhea:RHEA:41840, Rhea:RHEA-COMP:9633,
CC Rhea:RHEA-COMP:9634, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:78460, ChEBI:CHEBI:78461;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41841;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxyoctanoyl-[ACP] = (2E)-octenoyl-[ACP] + H2O;
CC Xref=Rhea:RHEA:41844, Rhea:RHEA-COMP:9634, Rhea:RHEA-COMP:9635,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78461, ChEBI:CHEBI:78462;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41845;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-octenoyl-[ACP] + H(+) + NADPH = NADP(+) + octanoyl-[ACP];
CC Xref=Rhea:RHEA:41848, Rhea:RHEA-COMP:9635, Rhea:RHEA-COMP:9636,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78462, ChEBI:CHEBI:78463;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41849;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + malonyl-[ACP] + octanoyl-[ACP] = 3-oxodecanoyl-[ACP] +
CC CO2 + holo-[ACP]; Xref=Rhea:RHEA:41852, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9636, Rhea:RHEA-COMP:9637, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78463, ChEBI:CHEBI:78464;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41853;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxodecanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxydecanoyl-
CC [ACP] + NADP(+); Xref=Rhea:RHEA:41856, Rhea:RHEA-COMP:9637,
CC Rhea:RHEA-COMP:9638, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:78464, ChEBI:CHEBI:78466;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41857;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O;
CC Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41861;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-decenoyl-[ACP] + H(+) + NADPH = decanoyl-[ACP] + NADP(+);
CC Xref=Rhea:RHEA:41864, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9640,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78467, ChEBI:CHEBI:78468;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41865;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxododecanoyl-[ACP]
CC + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41868, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9640, Rhea:RHEA-COMP:9641, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78468, ChEBI:CHEBI:78469;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41869;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxododecanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxydodecanoyl-
CC [ACP] + NADP(+); Xref=Rhea:RHEA:41872, Rhea:RHEA-COMP:9641,
CC Rhea:RHEA-COMP:9642, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:78469, ChEBI:CHEBI:78470;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41873;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxydodecanoyl-[ACP] = (2E)-dodecenoyl-[ACP] + H2O;
CC Xref=Rhea:RHEA:41876, Rhea:RHEA-COMP:9642, Rhea:RHEA-COMP:9643,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78470, ChEBI:CHEBI:78472;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41877;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-dodecenoyl-[ACP] + H(+) + NADPH = dodecanoyl-[ACP] +
CC NADP(+); Xref=Rhea:RHEA:41880, Rhea:RHEA-COMP:9643, Rhea:RHEA-
CC COMP:9644, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:65264, ChEBI:CHEBI:78472;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41881;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxotetradecanoyl-
CC [ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41884, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9644, Rhea:RHEA-COMP:9645, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:65264, ChEBI:CHEBI:78449, ChEBI:CHEBI:78473;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41885;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxotetradecanoyl-[ACP] + H(+) + NADPH = (3R)-
CC hydroxytetradecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41888,
CC Rhea:RHEA-COMP:9645, Rhea:RHEA-COMP:9646, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78473,
CC ChEBI:CHEBI:78474; Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41889;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxytetradecanoyl-[ACP] = (2E)-tetradecenoyl-[ACP] +
CC H2O; Xref=Rhea:RHEA:41892, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9647,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78474, ChEBI:CHEBI:78475;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41893;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-tetradecenoyl-[ACP] + H(+) + NADPH = NADP(+) +
CC tetradecanoyl-[ACP]; Xref=Rhea:RHEA:41896, Rhea:RHEA-COMP:9647,
CC Rhea:RHEA-COMP:9648, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:78475, ChEBI:CHEBI:78477;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41897;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + malonyl-[ACP] + tetradecanoyl-[ACP] = 3-
CC oxohexadecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41900,
CC Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9648, Rhea:RHEA-COMP:9649,
CC Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78477,
CC ChEBI:CHEBI:78478; Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41901;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxohexadecanoyl-[ACP] + H(+) + NADPH = (3R)-
CC hydroxyhexadecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41904, Rhea:RHEA-
CC COMP:9649, Rhea:RHEA-COMP:9650, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:78478, ChEBI:CHEBI:78480;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41905;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxyhexadecanoyl-[ACP] = (2E)-hexadecenoyl-[ACP] +
CC H2O; Xref=Rhea:RHEA:41908, Rhea:RHEA-COMP:9650, Rhea:RHEA-COMP:9651,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78480, ChEBI:CHEBI:78481;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41909;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-hexadecenoyl-[ACP] + H(+) + NADPH = hexadecanoyl-[ACP] +
CC NADP(+); Xref=Rhea:RHEA:41912, Rhea:RHEA-COMP:9651, Rhea:RHEA-
CC COMP:9652, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78481, ChEBI:CHEBI:78483;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41913;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexadecanoyl-[ACP] + malonyl-[ACP] = 3-oxooctadecanoyl-
CC [ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41916, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9652, Rhea:RHEA-COMP:9653, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78483, ChEBI:CHEBI:78487;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41917;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxooctadecanoyl-[ACP] + H(+) + NADPH = (3R)-
CC hydroxyoctadecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41920, Rhea:RHEA-
CC COMP:9653, Rhea:RHEA-COMP:9654, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:78487, ChEBI:CHEBI:78488;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41921;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxyoctadecanoyl-[ACP] = (2E)-octadecenoyl-[ACP] +
CC H2O; Xref=Rhea:RHEA:41924, Rhea:RHEA-COMP:9654, Rhea:RHEA-COMP:9655,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78488, ChEBI:CHEBI:78489;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41925;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-octadecenoyl-[ACP] + H(+) + NADPH = NADP(+) +
CC octadecanoyl-[ACP]; Xref=Rhea:RHEA:41928, Rhea:RHEA-COMP:9655,
CC Rhea:RHEA-COMP:9656, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:78489, ChEBI:CHEBI:78495;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41929;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + tetradecanoyl-[ACP] = H(+) + holo-[ACP] +
CC tetradecanoate; Xref=Rhea:RHEA:30123, Rhea:RHEA-COMP:9648, Rhea:RHEA-
CC COMP:9685, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78477; EC=3.1.2.14;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30124;
CC Evidence={ECO:0000250|UniProtKB:P49327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + octadecanoyl-[ACP] = H(+) + holo-[ACP] + octadecanoate;
CC Xref=Rhea:RHEA:63204, Rhea:RHEA-COMP:9656, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78495;
CC Evidence={ECO:0000305|PubMed:2681189};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63205;
CC Evidence={ECO:0000305|PubMed:2681189};
CC -!- ACTIVITY REGULATION: Cerulenin, a potent non-competitive
CC pharmacological inhibitor of FAS, binds covalently to the active site
CC of the condensing enzyme region, inactivating a key enzyme step in
CC fatty acid synthesis. {ECO:0000269|PubMed:6654914}.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000269|PubMed:3182791, ECO:0000269|PubMed:6361031,
CC ECO:0000269|PubMed:6654913, ECO:0000269|PubMed:6654914}.
CC -!- SUBUNIT: Homodimer which is arranged in a head to tail fashion.
CC {ECO:0000250|UniProtKB:P49327}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=P12276-1; Sequence=Displayed;
CC Name=1;
CC IsoId=P12276-2; Sequence=VSP_000149;
CC -!- PTM: S-nitrosylation of Fatty acid synthase at cysteine residues Cys-
CC 1475 or Cys-2093 is important for the enzyme dimerization. In
CC adipocytes, S-nitrosylation of Fatty acid synthase occurs under
CC physiological conditions and gradually increases during adipogenesis.
CC {ECO:0000250|UniProtKB:P49327}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA82106.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; J03860; AAA48767.1; -; mRNA.
DR EMBL; J04485; AAB46389.1; -; mRNA.
DR EMBL; J02839; AAA82106.1; ALT_FRAME; Genomic_DNA.
DR PIR; S57248; XYCHFA.
DR AlphaFoldDB; P12276; -.
DR SMR; P12276; -.
DR STRING; 9031.ENSGALP00000004327; -.
DR BindingDB; P12276; -.
DR ChEMBL; CHEMBL1795136; -.
DR ESTHER; chick-fas; Thioesterase.
DR iPTMnet; P12276; -.
DR PaxDb; P12276; -.
DR PRIDE; P12276; -.
DR VEuPathDB; HostDB:geneid_396061; -.
DR eggNOG; KOG1202; Eukaryota.
DR eggNOG; KOG2335; Eukaryota.
DR InParanoid; P12276; -.
DR OrthoDB; 993446at2759; -.
DR PhylomeDB; P12276; -.
DR SABIO-RK; P12276; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:P12276; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008659; F:(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0008693; F:3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0047451; F:3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0004317; F:3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004313; F:[acyl-carrier-protein] S-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0047117; F:enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR GO; GO:0016295; F:myristoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004320; F:oleoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016296; F:palmitoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:AgBase.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0006089; P:lactate metabolic process; IMP:AgBase.
DR GO; GO:0032100; P:positive regulation of appetite; IMP:AgBase.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR Gene3D; 3.40.50.1820; -; 2.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR001031; Thioesterase.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 2.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Direct protein sequencing;
KW Fatty acid biosynthesis; Fatty acid metabolism; Hydrolase;
KW Lipid biosynthesis; Lipid metabolism; Lyase; Multifunctional enzyme; NAD;
KW NADP; Oxidoreductase; Phosphopantetheine; Phosphoprotein;
KW Pyridoxal phosphate; Reference proteome; S-nitrosylation; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7944406"
FT CHAIN 2..2512
FT /note="Fatty acid synthase"
FT /id="PRO_0000180273"
FT DOMAIN 2120..2200
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 2..?412
FT /note="Beta-ketoacyl synthase"
FT REGION 427..815
FT /note="Acyl and malonyl transferases"
FT REGION 1638..1866
FT /note="Enoyl reductase"
FT REGION 1867..2119
FT /note="Beta-ketoacyl reductase"
FT REGION 2209..2511
FT /note="Thioesterase"
FT ACT_SITE 161
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 580
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 878
FT /note="For beta-hydroxyacyl dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 2309
FT /note="For thioesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 2482
FT /note="For thioesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT BINDING 646..647
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P19096"
FT BINDING 670
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P19096"
FT BINDING 772
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P19096"
FT BINDING 1675..1692
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="1"
FT /ligand_note="for enoyl reductase activity"
FT BINDING 1889..1904
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /ligand_note="for ketoreductase activity"
FT MOD_RES 2
FT /note="N-acetylglutamate"
FT /evidence="ECO:0000269|PubMed:7944406"
FT MOD_RES 1475
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P49327"
FT MOD_RES 1708
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT MOD_RES 2093
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P49327"
FT MOD_RES 2158
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT VAR_SEQ 2349
FT /note="T -> TQCFSFSLF (in isoform 1)"
FT /evidence="ECO:0000305"
FT /id="VSP_000149"
FT CONFLICT 78..79
FT /note="QL -> PV (in Ref. 2; AAA48767)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="L -> A (in Ref. 2; AAA48767)"
FT /evidence="ECO:0000305"
FT CONFLICT 676
FT /note="R -> S (in Ref. 2; AAA48767)"
FT /evidence="ECO:0000305"
FT CONFLICT 1170
FT /note="K -> N (in Ref. 2; AAA48767)"
FT /evidence="ECO:0000305"
FT CONFLICT 1179
FT /note="A -> T (in Ref. 2; AAA48767)"
FT /evidence="ECO:0000305"
FT CONFLICT 1192
FT /note="R -> H (in Ref. 2; AAA48767)"
FT /evidence="ECO:0000305"
FT CONFLICT 1199
FT /note="P -> L (in Ref. 2; AAA48767)"
FT /evidence="ECO:0000305"
FT CONFLICT 1287..1288
FT /note="DN -> ND (in Ref. 2; AAA48767)"
FT /evidence="ECO:0000305"
FT CONFLICT 1373
FT /note="K -> E (in Ref. 2; AAA48767)"
FT /evidence="ECO:0000305"
FT CONFLICT 1534
FT /note="C -> Y (in Ref. 2; AAA48767)"
FT /evidence="ECO:0000305"
FT CONFLICT 1578
FT /note="W -> R (in Ref. 2; AAA48767)"
FT /evidence="ECO:0000305"
FT CONFLICT 1686..1697
FT /note="QAAIAIALSMGC -> ASSHCHRLEHGLA (in Ref. 2; AAA48767)"
FT /evidence="ECO:0000305"
FT CONFLICT 1733
FT /note="Q -> E (in Ref. 2; AAA48767)"
FT /evidence="ECO:0000305"
FT CONFLICT 1746
FT /note="S -> N (in Ref. 2; AAA48767)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2512 AA; 274782 MW; 66FDE22F5CCF603C CRC64;
MEDVVIAGIA GKLPESENLQ EFWENLLNGV DMVTEDDRRW KPGIYGLPKR NGKLKDIKKF
DASFFGVHPK QAHTMDPQLR LLLEVSYEAI LDGGINPTAL RGTDTGVWVG ASGSEALEAL
SQDPEELLGY SMTGCQRAML ANRISYFYDF TGPSLTIDTA CSSSLMALEN AYKAIRHGQC
SAALVGGVNI LLKPNTSVQF MKLGMLSPDG ACKAFDVSGN GYCRSEAVVV VLLTKKSMAK
RVYATIVNAG SNTDGFKEQG VTFPSGEMQQ QLVGSLYREC GIKPGDVEYV EAHGTGTKVG
DPQEVNGIVN VFCQCEREPL LIGSTKSNMG HPEPASGLAA LAKVILSLEH GLWAPNLHFN
DPNPDIPALH DGSLKVVCKP TPVKGGLVSI NSFGFGGSNA HVILRPNEKK CQPQETCNLP
RLVQVCGRTQ EAVEILIEES RKHGGCSPFL SLLSDISAVP VSSMPYRGYT LVGTESDITE
IQQVQASGRP LWYICSGMGT QWKGMGLSLM KLDLFRQSIL RSDEALKSTG LKVSDLLLNA
DENTFDDTVH AFVGLAAIQI AQIDVLKAAG LQPDGILGHS VGELACGYAD NSLSHEEAVL
AAYWRGRCVK EAKLPPGGMA AVGLTWEECK QRCPPNVVPA CHNSEDTVTV SGPLDSVSEF
VTKLKKDGVF AKEVRRAGVA FHSYYMASIA PALLSALKKV IPHPKPRSAR WISTSIPESQ
WQSDLARNSS AEYHVNNLVN PVLFHEGLKH IPENAVVVEI APHALLQAIL RRTLKPTCTI
LPLMKKDHKN NLEFFLTQTG KIHLTGINVL GNNLFPPVEY PVPVGTPLIS PYIKWDHSQD
WDVPKAEDFP SGSKGSASAS VYNIDVSPDS PDHYLVGHCI DGRVLYPATG YLVLAWRTLA
RSLGMVMEQT AVMFEEVTIH QATILPKKGS TQLEVRIMPA SHSFEVSGNG NLAVSGKISL
LENDALKNFH NQLADFQSQA NVTAKSGLLM EDVYQELHLR GYNYGPTFQG VLECNSEGSA
GKILWNGNWV TFLDTLLHLI VLAETGRSLR LPTRIRSVYI DPVLHQEQVY QYQDNVEAFD
VVVDRCLDSL KAGGVQINGL HASVAPRRQQ ERISPTLEKF SFVPYIESDC LSSSTQLHAY
LEHCKGLIQK LQAKMALHGV KLVIHGLETK GAAAGSPPAQ KGLQHILTEI CRLELNGNPH
SELEQIVTQE KMHLQDDPLL NGLLDSSELK TCLDVAKENT TSHRMKIVEA LAGSGRLFSR
VQSILNTQPL LQLDYIATDC TPETLSDNET ELHDAGISFS QWDPSSLPSG NLTNADLAVC
NCSTSVLGNT AEIISNLAAA VKEGGFVLLH TLLKEETLGE IVSFLTSPDL QQKHSFLSQA
QWEELFSKAS LNLVAMKRSF FGSVIFLCRR QSPAKAPILL PVDDTHYKWV DSLKEILADS
SEQPLWLTAT NCGNSGILGM VNCLRLEAEG HRIRCVFVSN LSPSSTVPAT SLSSLEMQKI
IERDLVMNVY RDGKWGSFRH LPLQQAQPQE LTECAYVNVL TRGDLSSLRW IVSPLRHFQT
TNPNVQLCKV YYASLNFWDI MLATGKLSPD AIPGNWTLQQ CMLGMEFSGR DLAGRRVMGL
LPAKGLATVV DCDKRFLWEV PENWTLEEAA SVPVVYATAY YALVVRGGMK KGESVLIHSG
SGGVGQAAIA IALSMGCRVF ATVGSAEKRE YLQARFPQLD ANSFASSRNT TFQQHILRVT
NGKGVSLVLN SLAEEKLQAS LRCLAQHGRF LEIGKFDLSN NSQLGMALFL KNVAFHGILL
DSIFEEGNQE WEVVSELLTK GIKDGVVKPL RTTVFGKEEV EAAFRFMAQG KHIGKVMIKI
QEEEKQYPLR SEPVKLSAIS RTSCPPTKSY IITGGLGGFG LELAQWLIER GAQKLVLTSR
SGIRTGYQAK CVREWKALGI QVLVSTSDVG TLEGTQLLIE EALKLGPVGG IFNLAVVLKD
AMIENQTPEL FWEVNKPKYS GTLHLDWVTR KKCPDLDYFV VFSSVSCGRG NAGQSNYGFA
NSAMERICEQ RHHDGLPGLA VQWGAIGDVG ILKAMGNREV VIGGTVLQQI SSCLEVLDMF
LNQPHPVMSS FVLAEKVSVK SEGGSQRDLV EAVAHILGVR DVSSLNAESS LADLGLDSLM
GVEVRQTLER DYDIVMTMRE IRLLTINKLR ELSSKTGTAE ELKPSQVLKT GPGEPPKLDL
NNLLVNPEGP TITRLNEVQS TERPLFLVHP IEGSIAVFYT LASKLHMPCY GLQCTKAAPL
DSIQSLASYY IDCMKQIQPE GPYRIAGYSF GACVAFEMCS QLQAQQNASH ALNSLFLFDG
SHSFVAAYTQ SYRAKLTQGN EAALETEALC AFVQQFTGIE YNKLLEILLP LEDLEARVNA
AADLITQIHK NINREALSFA AASFYHKLKA ADKYIPESKY HGNVTLMRAK THNEYEEGLG
GDYRLSEVCD GKVSVHIIEG DHRTLLEGDG VESIIGIIHG SLAEPRVSVR EG
