ID   FAS_ANSAN               Reviewed;         352 AA.
AC   P36189;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Fatty acid synthase;
DE            EC=2.3.1.85;
DE   Flags: Fragment;
GN   Name=FASN; Synonyms=FAS;
OS   Anser anser anser (Western greylag goose).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anserinae; Anser.
OX   NCBI_TaxID=8844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=1702426; DOI=10.1016/s0021-9258(18)52451-0;
RA   Kameda K., Goodridge A.G.;
RT   "Isolation and partial characterization of the gene for goose fatty acid
RT   synthase.";
RL   J. Biol. Chem. 266:419-426(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 152-173.
RX   PubMed=6712225; DOI=10.1016/0003-9861(84)90092-4;
RA   Pouloe A.J., Bonsall R.F., Kolattukudy P.E.;
RT   "Specific modification of the condensation domain of fatty acid synthase
RT   and the determination of the primary structure of the modified active site
RT   peptides.";
RL   Arch. Biochem. Biophys. 230:117-128(1984).
CC   -!- FUNCTION: Fatty acid synthetase catalyzes the formation of long-chain
CC       fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This
CC       multifunctional protein has 7 catalytic activities as an acyl carrier
CC       protein.
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   -!- SUBUNIT: Homodimer which monomers are arranged in a head to tail
CC       fashion.
CC   -!- INDUCTION: By triiodothyronine.
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DR   EMBL; M60622; AAA49316.1; -; mRNA.
DR   PIR; A39042; A39042.
DR   AlphaFoldDB; P36189; -.
DR   SMR; P36189; -.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.47.10; -; 1.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR016039; Thiolase-like.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF53901; SSF53901; 1.
DR   PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Hydrolase; Ligase; Lipid biosynthesis; Lipid metabolism;
KW   Multifunctional enzyme; NAD; NADP; Oxidoreductase; Phosphopantetheine;
KW   Transferase.
FT   CHAIN           1..>352
FT                   /note="Fatty acid synthase"
FT                   /id="PRO_0000180272"
FT   REGION          1..>352
FT                   /note="Beta-ketoacyl synthase"
FT   ACT_SITE        161
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   NON_TER         352
SQ   SEQUENCE   352 AA;  37912 MW;  908530BF76762335 CRC64;
     MEDVVIAGIA GKLPESENLQ EFWEKLLNGV DMVTEDDRRW KPGMYGLPKR NGKLKDISKF
     DASFFGVHPK QAHTMDPQLR LLLEVSYEAI LDGGINPATL RGTDTGVWVG ASGSEAGEAF
     SQDPEQLLGY SMIGCQRAMF ANRISYFYDF KGPSLSIDTA CSSSLMALEN AYKAIRNGRC
     SAAVVGGVNL LLKPNTSVQF MKLGMLSPDG ACKVFDASGD GYCRSEAVVV VLLTKKSMAK
     RIYATIVNAG SNTDGFKEQG VTFPSGDMQR QLVSSLHREC GIKPGDIEYV ETHGTGTKVG
     DPQEVNGLAD LFCQCEREPL LIGSTKSNMG HPEPASGLAA LAKVVLSLEH GL