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Fatty acid synthase (EC 2.3.1.85) [Includes: [Acyl-carrier-protein] S-acetyltransferase (EC 2.3.1.38); [Acyl-carrier-protein] S-malonyltransferase (EC 2.3.1.39); 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41); 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100); 3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.59); Enoyl-[acyl-carrier-protein] reductase (EC 1.3.1.39); Oleoyl-[acyl-carrier-protein] hydrolase (EC 3.1.2.14)]

 FAS_CHICK               Reviewed;        2512 AA.
P12276;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 5.
23-MAY-2018, entry version 168.
RecName: Full=Fatty acid synthase;
EC=2.3.1.85;
Includes:
RecName: Full=[Acyl-carrier-protein] S-acetyltransferase;
EC=2.3.1.38;
Includes:
RecName: Full=[Acyl-carrier-protein] S-malonyltransferase;
EC=2.3.1.39;
Includes:
RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase;
EC=2.3.1.41;
Includes:
RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase;
EC=1.1.1.100;
Includes:
RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase;
EC=4.2.1.59;
Includes:
RecName: Full=Enoyl-[acyl-carrier-protein] reductase;
EC=1.3.1.39;
Includes:
RecName: Full=Oleoyl-[acyl-carrier-protein] hydrolase;
EC=3.1.2.14;
Name=FASN; Synonyms=FAS;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-12, AND ACETYLATION
AT GLU-2.
STRAIN=White leghorn; TISSUE=Liver;
PubMed=7944406; DOI=10.1006/abbi.1994.1410;
Huang W.-Y., Chirala S.S., Wakil S.J.;
"Amino-terminal blocking group and sequence of the animal fatty acid
synthase.";
Arch. Biochem. Biophys. 314:45-49(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 75-1775.
TISSUE=Liver;
PubMed=2734291; DOI=10.1073/pnas.86.12.4387;
Holzer K.P., Liu W., Hammes G.G.;
"Molecular cloning and sequencing of chicken liver fatty acid synthase
cDNA.";
Proc. Natl. Acad. Sci. U.S.A. 86:4387-4391(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1568-2512, AND PARTIAL PROTEIN SEQUENCE.
PubMed=2917973;
Chirala S.S., Kasturi R., Pazirandeh M., Stolow D.T., Huang W.-Y.,
Wakil S.J.;
"A novel cDNA extension procedure. Isolation of chicken fatty acid
synthase cDNA clones.";
J. Biol. Chem. 264:3750-3757(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1752-2512.
PubMed=2842766; DOI=10.1073/pnas.85.17.6328;
Yuan Z., Liu W., Hammes G.G.;
"Molecular cloning and sequencing of DNA complementary to chicken
liver fatty acid synthase mRNA.";
Proc. Natl. Acad. Sci. U.S.A. 85:6328-6331(1988).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 2202-2512.
PubMed=3207710; DOI=10.1021/bi00420a029;
Kasturi R., Chirala S.S., Pazirandeh M., Wakil S.J.;
"Characterization of a genomic and cDNA clone coding for the
thioesterase domain and 3' noncoding region of the chicken liver fatty
acid synthase gene.";
Biochemistry 27:7778-7785(1988).
[6]
PROTEIN SEQUENCE OF 2122-2210.
PubMed=2648999; DOI=10.1016/0003-9861(89)90011-8;
Huang W.-Y., Stoops J.K., Wakil S.J.;
"Complete amino acid sequence of chicken liver acyl carrier protein
derived from the fatty acid synthase.";
Arch. Biochem. Biophys. 270:92-98(1989).
[7]
PROTEIN SEQUENCE OF 2210-2509.
STRAIN=White leghorn;
PubMed=3207709; DOI=10.1021/bi00420a028;
Yang C.-Y., Huang W.-Y., Chirala S.S., Wakil S.J.;
"Complete amino acid sequence of the thioesterase domain of chicken
liver fatty acid synthase.";
Biochemistry 27:7773-7777(1988).
[8]
PROTEIN SEQUENCE OF 668-675 AND 1699-1710.
PubMed=2751995; DOI=10.1021/bi00435a023;
Chang S.I., Hammes G.G.;
"Amino acid sequences of pyridoxal 5'-phosphate binding sites and
fluorescence resonance energy transfer in chicken liver fatty acid
synthase.";
Biochemistry 28:3781-3788(1989).
-!- FUNCTION: Fatty acid synthetase catalyzes the formation of long-
chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This
multifunctional protein has 7 catalytic activities as an acyl
carrier protein.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + n malonyl-CoA + 2n NADPH = a
long-chain fatty acid + (n+1) CoA + n CO(2) + 2n NADP(+).
-!- CATALYTIC ACTIVITY: Acetyl-CoA + [acyl-carrier-protein] = CoA +
acetyl-[acyl-carrier-protein].
-!- CATALYTIC ACTIVITY: Malonyl-CoA + an [acyl-carrier-protein] = CoA
+ a malonyl-[acyl-carrier-protein].
-!- CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + malonyl-[acyl-
carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO(2) +
[acyl-carrier-protein].
-!- CATALYTIC ACTIVITY: (3R)-3-hydroxyacyl-[acyl-carrier-protein] +
NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH.
-!- CATALYTIC ACTIVITY: A (3R)-3-hydroxyacyl-[acyl-carrier protein] =
a trans-2-enoyl-[acyl-carrier protein] + H(2)O.
-!- CATALYTIC ACTIVITY: An acyl-[acyl-carrier protein] + NADP(+) = a
trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH.
-!- CATALYTIC ACTIVITY: Oleoyl-[acyl-carrier-protein] + H(2)O = [acyl-
carrier-protein] + oleate.
-!- SUBUNIT: Homodimer which is arranged in a head to tail fashion.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=2;
IsoId=P12276-1; Sequence=Displayed;
Name=1;
IsoId=P12276-2; Sequence=VSP_000149;
-!- SEQUENCE CAUTION:
Sequence=AAA82106.1; Type=Frameshift; Positions=2352; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; J03860; AAA48767.1; -; mRNA.
EMBL; J04485; AAB46389.1; -; mRNA.
EMBL; J02839; AAA82106.1; ALT_FRAME; Genomic_DNA.
PIR; S57248; XYCHFA.
UniGene; Gga.8951; -.
ProteinModelPortal; P12276; -.
SMR; P12276; -.
STRING; 9031.ENSGALP00000038133; -.
BindingDB; P12276; -.
ChEMBL; CHEMBL1795136; -.
ESTHER; chick-fas; Thioesterase.
iPTMnet; P12276; -.
PaxDb; P12276; -.
PRIDE; P12276; -.
eggNOG; KOG1202; Eukaryota.
eggNOG; COG3321; LUCA.
HOGENOM; HOG000019642; -.
HOVERGEN; HBG005640; -.
InParanoid; P12276; -.
PhylomeDB; P12276; -.
SABIO-RK; P12276; -.
PRO; PR:P12276; -.
Proteomes; UP000000539; Unplaced.
GO; GO:0005623; C:cell; IDA:AgBase.
GO; GO:0047451; F:3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
GO; GO:0102131; F:3-oxo-glutaryl-[acp] methyl ester reductase activity; IEA:UniProtKB-EC.
GO; GO:0102132; F:3-oxo-pimeloyl-[acp] methyl ester reductase activity; IEA:UniProtKB-EC.
GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC.
GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
GO; GO:0004313; F:[acyl-carrier-protein] S-acetyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0047117; F:enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) activity; IEA:UniProtKB-EC.
GO; GO:0004312; F:fatty acid synthase activity; TAS:AgBase.
GO; GO:0016295; F:myristoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0004320; F:oleoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0016296; F:palmitoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
GO; GO:0003697; F:single-stranded DNA binding; IDA:AgBase.
GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0006089; P:lactate metabolic process; IMP:AgBase.
GO; GO:0032100; P:positive regulation of appetite; IMP:AgBase.
Gene3D; 1.10.1200.10; -; 1.
Gene3D; 1.10.1470.20; -; 1.
Gene3D; 3.40.366.10; -; 1.
Gene3D; 3.40.47.10; -; 1.
Gene3D; 3.40.50.1820; -; 2.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR001227; Ac_transferase_dom_sf.
InterPro; IPR036736; ACP-like_sf.
InterPro; IPR014043; Acyl_transferase.
InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
InterPro; IPR013149; ADH_C.
InterPro; IPR023102; Fatty_acid_synthase_dom_2.
InterPro; IPR011032; GroES-like_sf.
InterPro; IPR032821; KAsynt_C_assoc.
InterPro; IPR018201; Ketoacyl_synth_AS.
InterPro; IPR014031; Ketoacyl_synth_C.
InterPro; IPR014030; Ketoacyl_synth_N.
InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020801; PKS_acyl_transferase.
InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
InterPro; IPR020807; PKS_dehydratase.
InterPro; IPR020843; PKS_ER.
InterPro; IPR013968; PKS_KR.
InterPro; IPR020806; PKS_PP-bd.
InterPro; IPR009081; PP-bd_ACP.
InterPro; IPR006162; Ppantetheine_attach_site.
InterPro; IPR029063; SAM-dependent_MTases.
InterPro; IPR001031; Thioesterase.
InterPro; IPR016039; Thiolase-like.
Pfam; PF00698; Acyl_transf_1; 1.
Pfam; PF00107; ADH_zinc_N; 1.
Pfam; PF16197; KAsynt_C_assoc; 1.
Pfam; PF00109; ketoacyl-synt; 1.
Pfam; PF02801; Ketoacyl-synt_C; 1.
Pfam; PF08659; KR; 1.
Pfam; PF00550; PP-binding; 1.
Pfam; PF14765; PS-DH; 1.
Pfam; PF00975; Thioesterase; 1.
SMART; SM00827; PKS_AT; 1.
SMART; SM00826; PKS_DH; 1.
SMART; SM00829; PKS_ER; 1.
SMART; SM00825; PKS_KS; 1.
SMART; SM00823; PKS_PP; 1.
SUPFAM; SSF47336; SSF47336; 1.
SUPFAM; SSF50129; SSF50129; 1.
SUPFAM; SSF51735; SSF51735; 2.
SUPFAM; SSF52151; SSF52151; 2.
SUPFAM; SSF53335; SSF53335; 1.
SUPFAM; SSF53474; SSF53474; 1.
SUPFAM; SSF53901; SSF53901; 2.
SUPFAM; SSF55048; SSF55048; 1.
PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PROSITE; PS50075; CARRIER; 1.
PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome;
Direct protein sequencing; Fatty acid biosynthesis;
Fatty acid metabolism; Hydrolase; Lipid biosynthesis;
Lipid metabolism; Lyase; Multifunctional enzyme; NAD; NADP;
Oxidoreductase; Phosphopantetheine; Phosphoprotein;
Pyridoxal phosphate; Reference proteome; Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:7944406}.
CHAIN 2 2512 Fatty acid synthase.
/FTId=PRO_0000180273.
DOMAIN 2120 2200 Carrier. {ECO:0000255|PROSITE-
ProRule:PRU00258}.
NP_BIND 1675 1692 NADP (ER).
NP_BIND 1889 1904 NADP (KR).
REGION 2 ?412 Beta-ketoacyl synthase.
REGION 427 815 Acyl and malonyl transferases.
REGION 1638 1866 Enoyl reductase.
REGION 1867 2119 Beta-ketoacyl reductase.
REGION 2209 2511 Thioesterase.
ACT_SITE 161 161 For beta-ketoacyl synthase activity.
{ECO:0000255|PROSITE-ProRule:PRU10022}.
ACT_SITE 580 580 For acyl/malonyl transferase activity.
{ECO:0000255|PROSITE-ProRule:PRU10022}.
ACT_SITE 878 878 For beta-hydroxyacyl dehydratase
activity. {ECO:0000255|PROSITE-
ProRule:PRU10022}.
ACT_SITE 2309 2309 For thioesterase activity.
{ECO:0000255|PROSITE-ProRule:PRU10022}.
ACT_SITE 2482 2482 For thioesterase activity.
{ECO:0000255|PROSITE-ProRule:PRU10022}.
MOD_RES 2 2 N-acetylglutamate.
{ECO:0000269|PubMed:7944406}.
MOD_RES 1708 1708 N6-(pyridoxal phosphate)lysine.
{ECO:0000250}.
MOD_RES 2158 2158 O-(pantetheine 4'-phosphoryl)serine.
{ECO:0000255|PROSITE-ProRule:PRU00258}.
VAR_SEQ 2349 2349 T -> TQCFSFSLF (in isoform 1).
{ECO:0000305}.
/FTId=VSP_000149.
CONFLICT 78 79 QL -> PV (in Ref. 2; AAA48767).
{ECO:0000305}.
CONFLICT 117 117 L -> A (in Ref. 2; AAA48767).
{ECO:0000305}.
CONFLICT 676 676 R -> S (in Ref. 2; AAA48767).
{ECO:0000305}.
CONFLICT 1170 1170 K -> N (in Ref. 2; AAA48767).
{ECO:0000305}.
CONFLICT 1179 1179 A -> T (in Ref. 2; AAA48767).
{ECO:0000305}.
CONFLICT 1192 1192 R -> H (in Ref. 2; AAA48767).
{ECO:0000305}.
CONFLICT 1199 1199 P -> L (in Ref. 2; AAA48767).
{ECO:0000305}.
CONFLICT 1287 1288 DN -> ND (in Ref. 2; AAA48767).
{ECO:0000305}.
CONFLICT 1373 1373 K -> E (in Ref. 2; AAA48767).
{ECO:0000305}.
CONFLICT 1534 1534 C -> Y (in Ref. 2; AAA48767).
{ECO:0000305}.
CONFLICT 1578 1578 W -> R (in Ref. 2; AAA48767).
{ECO:0000305}.
CONFLICT 1686 1697 QAAIAIALSMGC -> ASSHCHRLEHGLA (in Ref. 2;
AAA48767). {ECO:0000305}.
CONFLICT 1733 1733 Q -> E (in Ref. 2; AAA48767).
{ECO:0000305}.
CONFLICT 1746 1746 S -> N (in Ref. 2; AAA48767).
{ECO:0000305}.
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


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