ID FAS_HUMAN Reviewed; 2511 AA.
AC P49327; Q13479; Q16702; Q4LE83; Q6P4U5; Q6SS02; Q969R1; Q96C68; Q96IT0;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 3.
DT 02-OCT-2024, entry version 246.
DE RecName: Full=Fatty acid synthase;
DE EC=2.3.1.85 {ECO:0000269|PubMed:16215233, ECO:0000269|PubMed:26851298, ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
DE AltName: Full=Type I fatty acid synthase;
DE Includes:
DE RecName: Full=[Acyl-carrier-protein] S-acetyltransferase;
DE EC=2.3.1.38 {ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
DE Includes:
DE RecName: Full=[Acyl-carrier-protein] S-malonyltransferase;
DE EC=2.3.1.39 {ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
DE Includes:
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase;
DE EC=2.3.1.41 {ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
DE Includes:
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase;
DE EC=1.1.1.100 {ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
DE Includes:
DE RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase;
DE EC=4.2.1.59 {ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
DE Includes:
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase;
DE EC=1.3.1.39 {ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
DE Includes:
DE RecName: Full=Acyl-[acyl-carrier-protein] hydrolase;
DE EC=3.1.2.14 {ECO:0000269|PubMed:15507492, ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
GN Name=FASN; Synonyms=FAS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, PHOSPHOPANTETHEINYLATION AT SER-2156, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=7567999; DOI=10.1073/pnas.92.19.8695;
RA Jayakumar A., Tai M.-H., Huang W.-Y., Al-Feel W., Hsu M., Abu-Elheiga L.,
RA Chirala S.S., Wakil S.J.;
RT "Human fatty acid synthase: properties and molecular cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:8695-8699(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hennigar R.A., Jenner K.H., Heine H.S., Kayler A.E., Wood F.D.,
RA Kuhajda F.P., Pasternack G.R.;
RT "Molecular cloning of tumor-associated human fatty acid synthase.";
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Mao J., Wakil S.J.;
RT "Recharacterization of the human fatty acid synthase (FAS) gene.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R.,
RA Okazaki N., Koga H., Nagase T., Ohara O.;
RT "Preparation of a set of expression-ready clones of mammalian long cDNAs
RT encoding large proteins by the ORF trap cloning method.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 1-12; 647-666; 791-802; 1242-1255; 1338-1349 AND
RP 2126-2138, ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUL-2005) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 753-758 AND 1285-1297.
RX PubMed=8022791; DOI=10.1073/pnas.91.14.6379;
RA Kuhajda F.P., Jenner K., Wood F.D., Hennigar R.A., Jacobs L.B., Dick J.D.,
RA Pasternack G.R.;
RT "Fatty acid synthesis: a potential selective target for antineoplastic
RT therapy.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:6379-6383(1994).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2047-2511, AND TISSUE SPECIFICITY.
RX PubMed=7595075;
RA Semenkovich C.F., Coleman T., Fiedorek F.T. Jr.;
RT "Human fatty acid synthase mRNA: tissue distribution, genetic mapping, and
RT kinetics of decay after glucose deprivation.";
RL J. Lipid Res. 36:1507-1521(1995).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8962082; DOI=10.1073/pnas.93.25.14509;
RA Jayakumar A., Huang W.Y., Raetz B., Chirala S.S., Wakil S.J.;
RT "Cloning and expression of the multifunctional human fatty acid synthase
RT and its subdomains in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:14509-14514(1996).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9356448; DOI=10.1073/pnas.94.23.12326;
RA Jayakumar A., Chirala S.S., Wakil S.J.;
RT "Human fatty acid synthase: assembling recombinant halves of the fatty acid
RT synthase subunit protein reconstitutes enzyme activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:12326-12330(1997).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16215233; DOI=10.1074/jbc.m507082200;
RA Carlisle-Moore L., Gordon C.R., Machutta C.A., Miller W.T., Tonge P.J.;
RT "Substrate recognition by the human fatty-acid synthase.";
RL J. Biol. Chem. 280:42612-42618(2005).
RN [13]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=16969344; DOI=10.1038/sj.bjc.6603350;
RA Zhao W., Kridel S., Thorburn A., Kooshki M., Little J., Hebbar S.,
RA Robbins M.;
RT "Fatty acid synthase: a novel target for antiglioma therapy.";
RL Br. J. Cancer 95:869-878(2006).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND S-NITROSYLATION AT
RP CYS-1471 AND CYS-2091.
RX PubMed=26851298; DOI=10.1194/jlr.m065805;
RA Choi M.S., Jung J.Y., Kim H.J., Ham M.R., Lee T.R., Shin D.W.;
RT "S-nitrosylation of fatty acid synthase regulates its activity through
RT dimerization.";
RL J. Lipid Res. 57:607-615(2016).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [16]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2198 AND THR-2204, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-2198; THR-2204 AND
RP SER-2236, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2204, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-298; LYS-436; LYS-528;
RP LYS-673; LYS-1704; LYS-1771; LYS-1847 AND LYS-1995, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63; SER-207; SER-1411;
RP SER-1584; SER-2198; THR-2204 AND THR-2215, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1174; SER-1411; SER-2198;
RP THR-2204 AND THR-2215, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [27]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-2449, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [29]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=34320401; DOI=10.1016/j.celrep.2021.109479;
RA Williams C.G., Jureka A.S., Silvas J.A., Nicolini A.M., Chvatal S.A.,
RA Carlson-Stevermer J., Oki J., Holden K., Basler C.F.;
RT "Inhibitors of VPS34 and fatty-acid metabolism suppress SARS-CoV-2
RT replication.";
RL Cell Rep. 36:109479-109479(2021).
RN [30]
RP 3D-STRUCTURE MODELING, AND STRUCTURE BY ELECTRON MICROSCOPY.
RX PubMed=11756679; DOI=10.1073/pnas.012589499;
RA Brink J., Ludtke S.J., Yang C.Y., Gu Z.-W., Wakil S.J., Chiu W.;
RT "Quaternary structure of human fatty acid synthase by electron
RT cryomicroscopy.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:138-143(2002).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 2218-2502, AND CATALYTIC ACTIVITY.
RX PubMed=15507492; DOI=10.1073/pnas.0406901101;
RA Chakravarty B., Gu Z., Chirala S.S., Wakil S.J., Quiocho F.A.;
RT "Human fatty acid synthase: structure and substrate selectivity of the
RT thioesterase domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15567-15572(2004).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2119-2207 IN COMPLEX WITH AASDHPPT
RP AND COENZYME A.
RX PubMed=18022563; DOI=10.1016/j.chembiol.2007.10.013;
RA Bunkoczi G., Pasta S., Joshi A., Wu X., Kavanagh K.L., Smith S.,
RA Oppermann U.;
RT "Mechanism and substrate recognition of human holo ACP synthase.";
RL Chem. Biol. 14:1243-1253(2007).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2200-2511 IN COMPLEX WITH
RP ORLISTAT, AND ACTIVE SITE FOR THIOESTERASE ACTIVITY.
RX PubMed=17618296; DOI=10.1038/nsmb1265;
RA Pemble C.W. IV, Johnson L.C., Kridel S.J., Lowther W.T.;
RT "Crystal structure of the thioesterase domain of human fatty acid synthase
RT inhibited by Orlistat.";
RL Nat. Struct. Mol. Biol. 14:704-709(2007).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 422-831 IN COMPLEX WITH
RP MALONYL-COENZYME A.
RG Structural genomics consortium (SGC);
RT "Structure of the MAT domain of human FAS with malonyl-CoA.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [35] {ECO:0007744|PDB:2JFD}
RP X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 422-823.
RX PubMed=19549604; DOI=10.1016/j.chembiol.2009.04.011;
RA Bunkoczi G., Misquitta S., Wu X., Lee W.H., Rojkova A., Kochan G.,
RA Kavanagh K.L., Oppermann U., Smith S.;
RT "Structural basis for different specificities of acyltransferases
RT associated with the human cytosolic and mitochondrial fatty acid
RT synthases.";
RL Chem. Biol. 16:667-675(2009).
RN [36]
RP VARIANT HIS-477.
RX PubMed=28472301; DOI=10.1093/hmg/ddx175;
RA Pinggera A., Mackenroth L., Rump A., Schallner J., Beleggia F., Wollnik B.,
RA Striessnig J.;
RT "New gain-of-function mutation shows CACNA1D as recurrently mutated gene in
RT autism spectrum disorders and epilepsy.";
RL Hum. Mol. Genet. 26:2923-2932(2017).
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:16215233,
CC ECO:0000269|PubMed:16969344, ECO:0000269|PubMed:26851298,
CC ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448}.
CC -!- FUNCTION: (Microbial infection) Fatty acid synthetase activity is
CC required for SARS coronavirus-2/SARS-CoV-2 replication.
CC {ECO:0000269|PubMed:34320401}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + n malonyl-CoA + 2n NADPH + 2n H(+) = a long-chain
CC fatty acid + (n+1) CoA + n CO2 + 2n NADP(+).; EC=2.3.1.85;
CC Evidence={ECO:0000269|PubMed:16215233, ECO:0000269|PubMed:26851298,
CC ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
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;
CC Evidence={ECO:0000269|PubMed:26851298, ECO:0000269|PubMed:7567999,
CC ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41789;
CC Evidence={ECO:0000269|PubMed:26851298, ECO:0000269|PubMed:7567999,
CC ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
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;
CC Evidence={ECO:0000269|PubMed:26851298, ECO:0000269|PubMed:7567999,
CC ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41793;
CC Evidence={ECO:0000269|PubMed:26851298, ECO:0000269|PubMed:7567999,
CC ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
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:0000269|PubMed:26851298,
CC ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22837;
CC Evidence={ECO:0000269|PubMed:26851298, ECO:0000269|PubMed:7567999,
CC ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
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:0000269|PubMed:26851298, ECO:0000269|PubMed:7567999,
CC ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17399;
CC Evidence={ECO:0000269|PubMed:26851298, ECO:0000269|PubMed:7567999,
CC ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
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:0000269|PubMed:26851298, ECO:0000269|PubMed:7567999,
CC ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13098;
CC Evidence={ECO:0000269|PubMed:26851298, ECO:0000269|PubMed:7567999,
CC ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
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:0000269|PubMed:26851298, ECO:0000269|PubMed:7567999,
CC ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22566;
CC Evidence={ECO:0000269|PubMed:26851298, ECO:0000269|PubMed:7567999,
CC ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
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:0000269|PubMed:15507492, ECO:0000269|PubMed:7567999,
CC ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41933;
CC Evidence={ECO:0000269|PubMed:15507492, ECO:0000269|PubMed:7567999,
CC ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
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:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41801;
CC Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
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:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41805;
CC Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
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:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41809;
CC Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
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:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41813;
CC Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
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:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41821;
CC Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
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:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41825;
CC Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
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:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41829;
CC Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
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:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41833;
CC Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
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:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41837;
CC Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
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:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41841;
CC Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
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:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41845;
CC Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
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:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41849;
CC Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
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:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41853;
CC Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
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:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41857;
CC Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
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:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41861;
CC Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
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:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41865;
CC Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
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:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41869;
CC Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
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:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41873;
CC Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
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:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41877;
CC Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
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:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41881;
CC Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
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:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41885;
CC Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
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:0000269|PubMed:7567999,
CC ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41889;
CC Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
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:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41893;
CC Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
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:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41897;
CC Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
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:0000269|PubMed:7567999,
CC ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41901;
CC Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
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:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41905;
CC Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
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:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41909;
CC Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
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:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41913;
CC Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448};
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:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41917;
CC Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082};
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:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41921;
CC Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082};
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:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41925;
CC Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082};
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:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41929;
CC Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082};
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:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30124;
CC Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082};
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:0000269|PubMed:15507492, ECO:0000269|PubMed:7567999,
CC ECO:0000269|PubMed:8962082};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63205;
CC Evidence={ECO:0000269|PubMed:15507492, ECO:0000269|PubMed:7567999,
CC ECO:0000269|PubMed:8962082};
CC -!- ACTIVITY REGULATION: Activated by S-nitrosylation which promotes enzyme
CC dimerization (PubMed:26851298). 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 (PubMed:16969344). {ECO:0000269|PubMed:16969344,
CC ECO:0000269|PubMed:26851298}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8 uM for acetyl-CoA {ECO:0000269|PubMed:7567999};
CC KM=20 uM for malonyl-CoA {ECO:0000269|PubMed:7567999};
CC KM=25 uM for NADPH {ECO:0000269|PubMed:7567999};
CC KM=4 uM for butanoyl-CoA {ECO:0000269|PubMed:7567999};
CC KM=7 uM for acetyl-CoA {ECO:0000269|PubMed:16215233};
CC KM=6 uM for malonyl-CoA {ECO:0000269|PubMed:16215233};
CC KM=5 uM for NADPH {ECO:0000269|PubMed:16215233};
CC Vmax=29.6 nmol/min/mg enzyme for the incorporation of acetyl-CoA into
CC fatty acids {ECO:0000269|PubMed:7567999};
CC Vmax=220.6 nmol/min/mg enzyme for the incorporation of malonyl-CoA
CC into fatty acids {ECO:0000269|PubMed:7567999};
CC Vmax=462 nmol/min/mg enzyme for the oxidation of NADPH
CC {ECO:0000269|PubMed:7567999};
CC Vmax=440 nmol/min/mg enzyme for the oxidation of NADPH (at pH 7.0)
CC {ECO:0000269|PubMed:16215233};
CC pH dependence:
CC Optimum pH is 6.5 to 6.7. {ECO:0000269|PubMed:7567999};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC ECO:0000269|PubMed:9356448}.
CC -!- SUBUNIT: Homodimer which is arranged in a head to tail fashion
CC (PubMed:17618296, PubMed:18022563, Ref.34). Interacts with CEACAM1;
CC this interaction is insulin and phosphorylation-dependent; reduces
CC fatty-acid synthase activity. {ECO:0000269|PubMed:17618296,
CC ECO:0000269|PubMed:18022563, ECO:0000269|Ref.34}.
CC -!- INTERACTION:
CC P49327; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-356658, EBI-10827839;
CC P49327; Q16665: HIF1A; NbExp=4; IntAct=EBI-356658, EBI-447269;
CC P49327; P42858: HTT; NbExp=13; IntAct=EBI-356658, EBI-466029;
CC P49327; Q8IV20: LACC1; NbExp=8; IntAct=EBI-356658, EBI-12508070;
CC P49327; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-356658, EBI-739832;
CC P49327; PRO_0000045603 [Q99IB8]; Xeno; NbExp=6; IntAct=EBI-356658, EBI-6927928;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17081065}.
CC Melanosome {ECO:0000269|PubMed:17081065}. Note=Identified by mass
CC spectrometry in melanosome fractions from stage I to stage IV.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Prominent expression in brain, lung,
CC liver and mammary gland. {ECO:0000269|PubMed:7567999,
CC ECO:0000269|PubMed:7595075}.
CC -!- PTM: S-nitrosylation of Fatty acid synthase at cysteine residues Cys-
CC 1471 or Cys-2091 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:0000269|PubMed:26851298}.
CC -!- MISCELLANEOUS: The relatively low beta-ketoacyl synthase activity may
CC be attributable to the low 4'-phosphopantetheine content of the
CC protein.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB35516.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC50259.1; Type=Miscellaneous discrepancy; Note=Several sequencing errors.; Evidence={ECO:0000305};
CC Sequence=BAE06070.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U26644; AAC50259.1; ALT_SEQ; mRNA.
DR EMBL; U29344; AAA73576.1; -; mRNA.
DR EMBL; AY451392; AAS09886.1; -; mRNA.
DR EMBL; AB209988; BAE06070.1; ALT_INIT; mRNA.
DR EMBL; AC135056; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007267; AAH07267.1; -; mRNA.
DR EMBL; BC007909; AAH07909.1; -; mRNA.
DR EMBL; BC014634; AAH14634.2; -; mRNA.
DR EMBL; BC063242; AAH63242.1; -; mRNA.
DR EMBL; S80437; AAB35516.1; ALT_INIT; mRNA.
DR CCDS; CCDS11801.1; -.
DR PIR; A57788; A57788.
DR PIR; G01880; G01880.
DR RefSeq; NP_004095.4; NM_004104.4.
DR RefSeq; XP_011521840.1; XM_011523538.2.
DR PDB; 1XKT; X-ray; 2.60 A; A/B=2218-2502.
DR PDB; 2CG5; X-ray; 2.70 A; B=2119-2207.
DR PDB; 2JFD; X-ray; 2.81 A; A/B/C/D=422-823.
DR PDB; 2JFK; X-ray; 2.40 A; A/B/C/D=422-831.
DR PDB; 2PX6; X-ray; 2.30 A; A/B=2200-2511.
DR PDB; 3HHD; X-ray; 2.15 A; A/B/C/D=2-963.
DR PDB; 3TJM; X-ray; 1.48 A; A=2218-2500.
DR PDB; 4PIV; X-ray; 2.30 A; A/B=1110-2114.
DR PDB; 4W82; X-ray; 1.70 A; A/B=1529-1867.
DR PDB; 4W9N; X-ray; 1.84 A; A/B/C/D=1529-1867.
DR PDB; 4Z49; X-ray; 1.70 A; A/B=2221-2502.
DR PDB; 5C37; X-ray; 2.30 A; A/C=1108-1523, A/C=1877-2122.
DR PDB; 6NNA; X-ray; 2.26 A; A/B=1109-2114.
DR PDB; 7MHD; X-ray; 2.03 A; A=2215-2503.
DR PDB; 7MHE; X-ray; 2.80 A; AAA=2215-2503.
DR PDB; 8EYI; EM; 2.70 A; E/F=855-2511.
DR PDB; 8EYK; EM; 2.70 A; E/F=855-2511.
DR PDB; 8G7X; X-ray; 1.81 A; A/B=858-1103.
DR PDB; 8GKC; EM; 2.45 A; A/D=855-2511.
DR PDBsum; 1XKT; -.
DR PDBsum; 2CG5; -.
DR PDBsum; 2JFD; -.
DR PDBsum; 2JFK; -.
DR PDBsum; 2PX6; -.
DR PDBsum; 3HHD; -.
DR PDBsum; 3TJM; -.
DR PDBsum; 4PIV; -.
DR PDBsum; 4W82; -.
DR PDBsum; 4W9N; -.
DR PDBsum; 4Z49; -.
DR PDBsum; 5C37; -.
DR PDBsum; 6NNA; -.
DR PDBsum; 7MHD; -.
DR PDBsum; 7MHE; -.
DR PDBsum; 8EYI; -.
DR PDBsum; 8EYK; -.
DR PDBsum; 8G7X; -.
DR PDBsum; 8GKC; -.
DR AlphaFoldDB; P49327; -.
DR EMDB; EMD-28690; -.
DR EMDB; EMD-28691; -.
DR EMDB; EMD-40182; -.
DR SMR; P49327; -.
DR BioGRID; 108488; 1066.
DR DIP; DIP-33681N; -.
DR IntAct; P49327; 135.
DR MINT; P49327; -.
DR STRING; 9606.ENSP00000304592; -.
DR BindingDB; P49327; -.
DR ChEMBL; CHEMBL4158; -.
DR DrugBank; DB01034; Cerulenin.
DR DrugBank; DB01083; Orlistat.
DR DrugCentral; P49327; -.
DR GuidetoPHARMACOLOGY; 2608; -.
DR SwissLipids; SLP:000000765; -.
DR ESTHER; human-FASN; Thioesterase.
DR CarbonylDB; P49327; -.
DR GlyCosmos; P49327; 2 sites, 1 glycan.
DR GlyGen; P49327; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; P49327; -.
DR MetOSite; P49327; -.
DR PhosphoSitePlus; P49327; -.
DR SwissPalm; P49327; -.
DR BioMuta; FASN; -.
DR DMDM; 269849686; -.
DR CPTAC; CPTAC-369; -.
DR CPTAC; CPTAC-370; -.
DR CPTAC; CPTAC-371; -.
DR CPTAC; CPTAC-372; -.
DR jPOST; P49327; -.
DR MassIVE; P49327; -.
DR PaxDb; 9606-ENSP00000304592; -.
DR PeptideAtlas; P49327; -.
DR PRIDE; P49327; -.
DR ProteomicsDB; 55989; -.
DR Pumba; P49327; -.
DR Antibodypedia; 1650; 831 antibodies from 41 providers.
DR DNASU; 2194; -.
DR Ensembl; ENST00000306749.4; ENSP00000304592.2; ENSG00000169710.9.
DR GeneID; 2194; -.
DR KEGG; hsa:2194; -.
DR MANE-Select; ENST00000306749.4; ENSP00000304592.2; NM_004104.5; NP_004095.4.
DR UCSC; uc002kdu.4; human.
DR AGR; HGNC:3594; -.
DR CTD; 2194; -.
DR DisGeNET; 2194; -.
DR GeneCards; FASN; -.
DR HGNC; HGNC:3594; FASN.
DR HPA; ENSG00000169710; Tissue enhanced (adipose tissue, breast).
DR MIM; 600212; gene.
DR neXtProt; NX_P49327; -.
DR OpenTargets; ENSG00000169710; -.
DR PharmGKB; PA28006; -.
DR VEuPathDB; HostDB:ENSG00000169710; -.
DR eggNOG; KOG1202; Eukaryota.
DR GeneTree; ENSGT00940000157276; -.
DR HOGENOM; CLU_000022_31_7_1; -.
DR InParanoid; P49327; -.
DR OMA; KMRGGEF; -.
DR OrthoDB; 3378513at2759; -.
DR PhylomeDB; P49327; -.
DR TreeFam; TF300549; -.
DR BioCyc; MetaCyc:HS09992-MONOMER; -.
DR BRENDA; 2.3.1.39; 2681.
DR BRENDA; 2.3.1.85; 2681.
DR PathwayCommons; P49327; -.
DR Reactome; R-HSA-163765; ChREBP activates metabolic gene expression.
DR Reactome; R-HSA-199220; Vitamin B5 (pantothenate) metabolism.
DR Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
DR Reactome; R-HSA-75105; Fatty acyl-CoA biosynthesis.
DR Reactome; R-HSA-9029558; NR1H2 & NR1H3 regulate gene expression linked to lipogenesis.
DR SABIO-RK; P49327; -.
DR SignaLink; P49327; -.
DR SIGNOR; P49327; -.
DR UniPathway; UPA00094; -.
DR BioGRID-ORCS; 2194; 173 hits in 1172 CRISPR screens.
DR ChiTaRS; FASN; human.
DR EvolutionaryTrace; P49327; -.
DR GeneWiki; Fatty_acid_synthase; -.
DR GenomeRNAi; 2194; -.
DR Pharos; P49327; Tchem.
DR PRO; PR:P49327; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P49327; protein.
DR Bgee; ENSG00000169710; Expressed in right hemisphere of cerebellum and 185 other cell types or tissues.
DR ExpressionAtlas; P49327; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0042587; C:glycogen granule; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0047450; F:(3R)-3-hydroxybutanoyl-[acyl-carrier-protein] hydratase activity; IEA:RHEA.
DR GO; GO:0008693; F:(3R)-3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity; IEA:RHEA.
DR GO; GO:0008659; F:(3R)-3-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity; IEA:RHEA.
DR GO; GO:0047451; F:(3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity; IEA:RHEA.
DR GO; GO:0004317; F:(3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity; IEA:RHEA.
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; IDA:FlyBase.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0141148; F:enoyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR GO; GO:0016297; F:fatty acyl-[ACP] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0071353; P:cellular response to interleukin-4; IEA:Ensembl.
DR GO; GO:0090557; P:establishment of endothelial intestinal barrier; IEA:Ensembl.
DR GO; GO:0008611; P:ether lipid biosynthetic process; IEA:Ensembl.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0006631; P:fatty acid metabolic process; TAS:ProtInc.
DR GO; GO:0002068; P:glandular epithelial cell development; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0030879; P:mammary gland development; IEA:Ensembl.
DR GO; GO:0044788; P:modulation by host of viral process; IDA:UniProtKB.
DR GO; GO:0030224; P:monocyte differentiation; IEA:Ensembl.
DR GO; GO:0030223; P:neutrophil differentiation; IEA:Ensembl.
DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd08954; KR_1_FAS_SDR_x; 2.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 2.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
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; IPR049391; FAS_pseudo-KR.
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; IPR013217; Methyltransf_12.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR049900; PKS_mFAS_DH.
DR InterPro; IPR050091; PKS_NRPS_Biosynth_Enz.
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 PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF7; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR Pfam; PF21149; FAS_pseudo-KR; 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; PF08242; Methyltransf_12; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 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; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
DR PROSITE; PS52019; PKS_MFAS_DH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Fatty acid biosynthesis; Fatty acid metabolism; Hydrolase; Isopeptide bond;
KW Lipid biosynthesis; Lipid metabolism; Lyase; Multifunctional enzyme; NAD;
KW NADP; Oxidoreductase; Phosphopantetheine; Phosphoprotein;
KW Proteomics identification; Pyridoxal phosphate; Reference proteome;
KW S-nitrosylation; Transferase; Ubl conjugation.
FT CHAIN 1..2511
FT /note="Fatty acid synthase"
FT /id="PRO_0000180276"
FT DOMAIN 1..406
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT DOMAIN 838..1108
FT /note="PKS/mFAS DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT DOMAIN 2121..2198
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 429..817
FT /note="Acyl and malonyl transferases"
FT /evidence="ECO:0000250"
FT REGION 838..966
FT /note="N-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT REGION 981..1108
FT /note="C-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT REGION 1635..1863
FT /note="Enoyl reductase"
FT /evidence="ECO:0000250"
FT REGION 1864..2118
FT /note="Beta-ketoacyl reductase"
FT /evidence="ECO:0000250"
FT REGION 2207..2511
FT /note="Thioesterase"
FT /evidence="ECO:0000250"
FT ACT_SITE 161
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 293
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 331
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 581
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 878
FT /note="Proton acceptor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT ACT_SITE 1031
FT /note="Proton donor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT ACT_SITE 2308
FT /note="For thioesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022,
FT ECO:0000269|PubMed:17618296"
FT ACT_SITE 2481
FT /note="For thioesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT BINDING 647..648
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P19096"
FT BINDING 671
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P19096"
FT BINDING 773
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P19096"
FT BINDING 1671..1688
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="1"
FT /ligand_note="for enoyl reductase activity"
FT /evidence="ECO:0000250"
FT BINDING 1886..1901
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /ligand_note="for ketoreductase activity"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 70
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 298
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 436
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 528
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 673
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 725
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19096"
FT MOD_RES 992
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19096"
FT MOD_RES 1174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1471
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000269|PubMed:26851298"
FT MOD_RES 1584
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1594
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19096"
FT MOD_RES 1704
FT /note="N6-(pyridoxal phosphate)lysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 1704
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1771
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1847
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1995
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 2091
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000269|PubMed:26851298"
FT MOD_RES 2156
FT /note="O-(pantetheine 4'-phosphoryl)serine; alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000269|PubMed:7567999"
FT MOD_RES 2156
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P12785"
FT MOD_RES 2198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 2204
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 2215
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 2236
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 2391
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19096"
FT CROSSLNK 2449
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25114211"
FT VARIANT 477
FT /note="R -> H (in dbSNP:rs113931914)"
FT /evidence="ECO:0000269|PubMed:28472301"
FT /id="VAR_079534"
FT VARIANT 1483
FT /note="V -> I (in dbSNP:rs2228305)"
FT /id="VAR_055479"
FT VARIANT 1694
FT /note="R -> H (in dbSNP:rs561903908)"
FT /id="VAR_055480"
FT VARIANT 1888
FT /note="I -> V (in dbSNP:rs2228307)"
FT /id="VAR_055481"
FT CONFLICT 459..462
FT /note="AVPA -> LSPT (in Ref. 2; AAA73576)"
FT /evidence="ECO:0000305"
FT CONFLICT 528..529
FT /note="KP -> NR (in Ref. 2; AAA73576)"
FT /evidence="ECO:0000305"
FT CONFLICT 637
FT /note="G -> A (in Ref. 2; AAA73576)"
FT /evidence="ECO:0000305"
FT CONFLICT 801
FT /note="G -> R (in Ref. 2; AAA73576)"
FT /evidence="ECO:0000305"
FT CONFLICT 902
FT /note="A -> P (in Ref. 2; AAA73576)"
FT /evidence="ECO:0000305"
FT CONFLICT 958
FT /note="V -> M (in Ref. 3; AAS09886)"
FT /evidence="ECO:0000305"
FT CONFLICT 1121
FT /note="P -> S (in Ref. 2; AAA73576 and 3; AAS09886)"
FT /evidence="ECO:0000305"
FT CONFLICT 1151
FT /note="K -> T (in Ref. 6; AAH63242)"
FT /evidence="ECO:0000305"
FT CONFLICT 1353..1356
FT /note="LGDI -> SGH (in Ref. 2; AAA73576)"
FT /evidence="ECO:0000305"
FT CONFLICT 1386
FT /note="L -> V (in Ref. 2; AAA73576)"
FT /evidence="ECO:0000305"
FT CONFLICT 1467..1468
FT /note="NR -> T (in Ref. 2; AAA73576)"
FT /evidence="ECO:0000305"
FT CONFLICT 1827
FT /note="K -> E (in Ref. 3; AAS09886)"
FT /evidence="ECO:0000305"
FT CONFLICT 1934
FT /note="R -> A (in Ref. 2; AAA73576)"
FT /evidence="ECO:0000305"
FT CONFLICT 2065
FT /note="D -> H (in Ref. 9; AAB35516)"
FT /evidence="ECO:0000305"
FT CONFLICT 2087
FT /note="R -> A (in Ref. 2; AAA73576)"
FT /evidence="ECO:0000305"
FT CONFLICT 2363
FT /note="A -> P (in Ref. 9; AAB35516)"
FT /evidence="ECO:0000305"
FT CONFLICT 2428
FT /note="R -> G (in Ref. 2; AAA73576)"
FT /evidence="ECO:0000305"
FT CONFLICT 2453
FT /note="A -> T (in Ref. 9; AAB35516)"
FT /evidence="ECO:0000305"
FT CONFLICT 2456
FT /note="E -> Q (in Ref. 9; AAB35516)"
FT /evidence="ECO:0000305"
FT STRAND 4..13
FT /evidence="ECO:0007829|PDB:3HHD"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 19..27
FT /evidence="ECO:0007829|PDB:3HHD"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:3HHD"
FT TURN 62..66
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 69..73
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 77..92
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:3HHD"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 115..120
FT /evidence="ECO:0007829|PDB:3HHD"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 130..135
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 139..148
FT /evidence="ECO:0007829|PDB:3HHD"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 163..176
FT /evidence="ECO:0007829|PDB:3HHD"
FT STRAND 181..189
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 194..202
FT /evidence="ECO:0007829|PDB:3HHD"
FT STRAND 227..235
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:3HHD"
FT STRAND 243..253
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 266..279
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:3HHD"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 300..312
FT /evidence="ECO:0007829|PDB:3HHD"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 326..329
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 336..350
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 367..370
FT /evidence="ECO:0007829|PDB:3HHD"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:3HHD"
FT STRAND 387..393
FT /evidence="ECO:0007829|PDB:3HHD"
FT STRAND 397..406
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 416..419
FT /evidence="ECO:0007829|PDB:3HHD"
FT STRAND 422..430
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 431..443
FT /evidence="ECO:0007829|PDB:3HHD"
FT TURN 444..446
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 448..457
FT /evidence="ECO:0007829|PDB:3HHD"
FT TURN 462..464
FT /evidence="ECO:0007829|PDB:3HHD"
FT STRAND 467..477
FT /evidence="ECO:0007829|PDB:3HHD"
FT STRAND 481..484
FT /evidence="ECO:0007829|PDB:3HHD"
FT STRAND 492..496
FT /evidence="ECO:0007829|PDB:3HHD"
FT TURN 504..509
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 510..512
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 514..527
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 528..530
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 534..539
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 545..547
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 549..569
FT /evidence="ECO:0007829|PDB:3HHD"
FT STRAND 575..579
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 583..590
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 596..611
FT /evidence="ECO:0007829|PDB:3HHD"
FT STRAND 618..625
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 627..633
FT /evidence="ECO:0007829|PDB:3HHD"
FT STRAND 639..645
FT /evidence="ECO:0007829|PDB:3HHD"
FT STRAND 648..654
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 655..667
FT /evidence="ECO:0007829|PDB:3HHD"
FT STRAND 672..675
FT /evidence="ECO:0007829|PDB:3HHD"
FT STRAND 677..679
FT /evidence="ECO:0007829|PDB:2JFD"
FT HELIX 685..690
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 691..701
FT /evidence="ECO:0007829|PDB:3HHD"
FT STRAND 702..704
FT /evidence="ECO:0007829|PDB:2JFD"
FT STRAND 715..717
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 719..721
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 725..728
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 732..740
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 745..749
FT /evidence="ECO:0007829|PDB:3HHD"
FT STRAND 757..764
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 768..774
FT /evidence="ECO:0007829|PDB:3HHD"
FT STRAND 780..783
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 792..805
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 812..815
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 831..833
FT /evidence="ECO:0007829|PDB:3HHD"
FT HELIX 847..849
FT /evidence="ECO:0007829|PDB:3HHD"
FT STRAND 858..865
FT /evidence="ECO:0007829|PDB:8G7X"
FT STRAND 867..870
FT /evidence="ECO:0007829|PDB:8EYI"
FT HELIX 873..877
FT /evidence="ECO:0007829|PDB:8G7X"
FT STRAND 878..880
FT /evidence="ECO:0007829|PDB:8GKC"
FT STRAND 883..885
FT /evidence="ECO:0007829|PDB:8G7X"
FT HELIX 888..903
FT /evidence="ECO:0007829|PDB:8G7X"
FT HELIX 907..909
FT /evidence="ECO:0007829|PDB:8G7X"
FT STRAND 912..919
FT /evidence="ECO:0007829|PDB:8G7X"
FT STRAND 927..938
FT /evidence="ECO:0007829|PDB:8G7X"
FT TURN 939..942
FT /evidence="ECO:0007829|PDB:8G7X"
FT STRAND 943..948
FT /evidence="ECO:0007829|PDB:8G7X"
FT STRAND 951..960
FT /evidence="ECO:0007829|PDB:8G7X"
FT HELIX 966..969
FT /evidence="ECO:0007829|PDB:8G7X"
FT STRAND 981..983
FT /evidence="ECO:0007829|PDB:8EYI"
FT STRAND 984..986
FT /evidence="ECO:0007829|PDB:8G7X"
FT HELIX 987..996
FT /evidence="ECO:0007829|PDB:8G7X"
FT STRAND 999..1001
FT /evidence="ECO:0007829|PDB:8GKC"
FT HELIX 1003..1005
FT /evidence="ECO:0007829|PDB:8G7X"
FT STRAND 1008..1012
FT /evidence="ECO:0007829|PDB:8G7X"
FT STRAND 1015..1021
FT /evidence="ECO:0007829|PDB:8G7X"
FT HELIX 1026..1039
FT /evidence="ECO:0007829|PDB:8G7X"
FT STRAND 1047..1057
FT /evidence="ECO:0007829|PDB:8G7X"
FT HELIX 1059..1065
FT /evidence="ECO:0007829|PDB:8G7X"
FT STRAND 1074..1081
FT /evidence="ECO:0007829|PDB:8G7X"
FT TURN 1082..1085
FT /evidence="ECO:0007829|PDB:8G7X"
FT STRAND 1086..1089
FT /evidence="ECO:0007829|PDB:8G7X"
FT STRAND 1092..1101
FT /evidence="ECO:0007829|PDB:8G7X"
FT STRAND 1113..1127
FT /evidence="ECO:0007829|PDB:6NNA"
FT TURN 1128..1130
FT /evidence="ECO:0007829|PDB:6NNA"
FT HELIX 1132..1149
FT /evidence="ECO:0007829|PDB:6NNA"
FT HELIX 1173..1175
FT /evidence="ECO:0007829|PDB:5C37"
FT HELIX 1177..1187
FT /evidence="ECO:0007829|PDB:6NNA"
FT HELIX 1200..1205
FT /evidence="ECO:0007829|PDB:6NNA"
FT HELIX 1206..1211
FT /evidence="ECO:0007829|PDB:6NNA"
FT TURN 1213..1217
FT /evidence="ECO:0007829|PDB:6NNA"
FT HELIX 1218..1220
FT /evidence="ECO:0007829|PDB:6NNA"
FT HELIX 1222..1233
FT /evidence="ECO:0007829|PDB:6NNA"
FT STRAND 1236..1246
FT /evidence="ECO:0007829|PDB:6NNA"
FT HELIX 1247..1250
FT /evidence="ECO:0007829|PDB:6NNA"
FT TURN 1253..1255
FT /evidence="ECO:0007829|PDB:6NNA"
FT HELIX 1256..1260
FT /evidence="ECO:0007829|PDB:6NNA"
FT STRAND 1263..1265
FT /evidence="ECO:0007829|PDB:5C37"
FT STRAND 1267..1276
FT /evidence="ECO:0007829|PDB:6NNA"
FT HELIX 1277..1283
FT /evidence="ECO:0007829|PDB:6NNA"
FT HELIX 1284..1289
FT /evidence="ECO:0007829|PDB:6NNA"
FT STRAND 1293..1296
FT /evidence="ECO:0007829|PDB:6NNA"
FT HELIX 1305..1307
FT /evidence="ECO:0007829|PDB:6NNA"
FT STRAND 1309..1316
FT /evidence="ECO:0007829|PDB:6NNA"
FT TURN 1317..1319
FT /evidence="ECO:0007829|PDB:6NNA"
FT HELIX 1325..1334
FT /evidence="ECO:0007829|PDB:6NNA"
FT STRAND 1336..1347
FT /evidence="ECO:0007829|PDB:6NNA"
FT HELIX 1352..1360
FT /evidence="ECO:0007829|PDB:6NNA"
FT HELIX 1374..1383
FT /evidence="ECO:0007829|PDB:6NNA"
FT STRAND 1387..1394
FT /evidence="ECO:0007829|PDB:6NNA"
FT STRAND 1397..1404
FT /evidence="ECO:0007829|PDB:6NNA"
FT STRAND 1413..1416
FT /evidence="ECO:0007829|PDB:6NNA"
FT HELIX 1424..1433
FT /evidence="ECO:0007829|PDB:6NNA"
FT STRAND 1441..1445
FT /evidence="ECO:0007829|PDB:6NNA"
FT HELIX 1453..1460
FT /evidence="ECO:0007829|PDB:6NNA"
FT HELIX 1466..1468
FT /evidence="ECO:0007829|PDB:6NNA"
FT STRAND 1469..1474
FT /evidence="ECO:0007829|PDB:6NNA"
FT STRAND 1479..1482
FT /evidence="ECO:0007829|PDB:8EYI"
FT HELIX 1491..1499
FT /evidence="ECO:0007829|PDB:6NNA"
FT STRAND 1502..1507
FT /evidence="ECO:0007829|PDB:6NNA"
FT STRAND 1510..1518
FT /evidence="ECO:0007829|PDB:6NNA"
FT STRAND 1525..1529
FT /evidence="ECO:0007829|PDB:8GKC"
FT STRAND 1531..1537
FT /evidence="ECO:0007829|PDB:4W82"
FT HELIX 1541..1543
FT /evidence="ECO:0007829|PDB:4W82"
FT STRAND 1544..1548
FT /evidence="ECO:0007829|PDB:4W82"
FT HELIX 1550..1553
FT /evidence="ECO:0007829|PDB:8GKC"
FT STRAND 1562..1570
FT /evidence="ECO:0007829|PDB:4W82"
FT HELIX 1573..1579
FT /evidence="ECO:0007829|PDB:4W82"
FT HELIX 1585..1587
FT /evidence="ECO:0007829|PDB:4W82"
FT HELIX 1589..1592
FT /evidence="ECO:0007829|PDB:4W82"
FT STRAND 1602..1606
FT /evidence="ECO:0007829|PDB:4W82"
FT STRAND 1612..1616
FT /evidence="ECO:0007829|PDB:4W82"
FT STRAND 1622..1628
FT /evidence="ECO:0007829|PDB:4W82"
FT HELIX 1630..1632
FT /evidence="ECO:0007829|PDB:4W82"
FT STRAND 1633..1635
FT /evidence="ECO:0007829|PDB:4W82"
FT HELIX 1642..1645
FT /evidence="ECO:0007829|PDB:4W82"
FT HELIX 1649..1659
FT /evidence="ECO:0007829|PDB:4W82"
FT TURN 1660..1663
FT /evidence="ECO:0007829|PDB:4W82"
FT STRAND 1670..1675
FT /evidence="ECO:0007829|PDB:4W82"
FT HELIX 1679..1690
FT /evidence="ECO:0007829|PDB:4W82"
FT STRAND 1694..1701
FT /evidence="ECO:0007829|PDB:4W82"
FT HELIX 1702..1711
FT /evidence="ECO:0007829|PDB:4W82"
FT HELIX 1717..1719
FT /evidence="ECO:0007829|PDB:4W82"
FT STRAND 1720..1722
FT /evidence="ECO:0007829|PDB:4W82"
FT STRAND 1723..1726
FT /evidence="ECO:0007829|PDB:4W9N"
FT HELIX 1728..1735
FT /evidence="ECO:0007829|PDB:4W82"
FT TURN 1736..1738
FT /evidence="ECO:0007829|PDB:4W82"
FT STRAND 1741..1746
FT /evidence="ECO:0007829|PDB:4W82"
FT TURN 1747..1751
FT /evidence="ECO:0007829|PDB:4W9N"
FT HELIX 1753..1757
FT /evidence="ECO:0007829|PDB:4W82"
FT STRAND 1760..1769
FT /evidence="ECO:0007829|PDB:4W82"
FT HELIX 1772..1775
FT /evidence="ECO:0007829|PDB:8GKC"
FT STRAND 1779..1781
FT /evidence="ECO:0007829|PDB:8GKC"
FT TURN 1784..1788
FT /evidence="ECO:0007829|PDB:4W82"
FT STRAND 1790..1794
FT /evidence="ECO:0007829|PDB:4W82"
FT HELIX 1796..1799
FT /evidence="ECO:0007829|PDB:4W82"
FT TURN 1801..1803
FT /evidence="ECO:0007829|PDB:4W9N"
FT HELIX 1805..1819
FT /evidence="ECO:0007829|PDB:4W82"
FT STRAND 1828..1832
FT /evidence="ECO:0007829|PDB:4W82"
FT HELIX 1833..1835
FT /evidence="ECO:0007829|PDB:4W82"
FT HELIX 1836..1845
FT /evidence="ECO:0007829|PDB:4W82"
FT STRAND 1849..1857
FT /evidence="ECO:0007829|PDB:4W82"
FT STRAND 1873..1876
FT /evidence="ECO:0007829|PDB:8GKC"
FT STRAND 1885..1890
FT /evidence="ECO:0007829|PDB:6NNA"
FT TURN 1891..1893
FT /evidence="ECO:0007829|PDB:6NNA"
FT HELIX 1895..1906
FT /evidence="ECO:0007829|PDB:6NNA"
FT STRAND 1911..1915
FT /evidence="ECO:0007829|PDB:6NNA"
FT HELIX 1923..1934
FT /evidence="ECO:0007829|PDB:6NNA"
FT STRAND 1938..1942
FT /evidence="ECO:0007829|PDB:6NNA"
FT HELIX 1949..1962
FT /evidence="ECO:0007829|PDB:6NNA"
FT STRAND 1963..1970
FT /evidence="ECO:0007829|PDB:6NNA"
FT HELIX 1980..1982
FT /evidence="ECO:0007829|PDB:6NNA"
FT HELIX 1985..2009
FT /evidence="ECO:0007829|PDB:6NNA"
FT STRAND 2015..2021
FT /evidence="ECO:0007829|PDB:6NNA"
FT HELIX 2022..2025
FT /evidence="ECO:0007829|PDB:6NNA"
FT HELIX 2032..2050
FT /evidence="ECO:0007829|PDB:6NNA"
FT STRAND 2056..2060
FT /evidence="ECO:0007829|PDB:6NNA"
FT STRAND 2065..2067
FT /evidence="ECO:0007829|PDB:6NNA"
FT TURN 2068..2070
FT /evidence="ECO:0007829|PDB:6NNA"
FT STRAND 2075..2077
FT /evidence="ECO:0007829|PDB:5C37"
FT HELIX 2088..2099
FT /evidence="ECO:0007829|PDB:6NNA"
FT STRAND 2104..2111
FT /evidence="ECO:0007829|PDB:6NNA"
FT HELIX 2127..2134
FT /evidence="ECO:0007829|PDB:2CG5"
FT TURN 2149..2153
FT /evidence="ECO:0007829|PDB:2CG5"
FT HELIX 2156..2170
FT /evidence="ECO:0007829|PDB:2CG5"
FT HELIX 2176..2180
FT /evidence="ECO:0007829|PDB:2CG5"
FT HELIX 2184..2192
FT /evidence="ECO:0007829|PDB:2CG5"
FT HELIX 2219..2222
FT /evidence="ECO:0007829|PDB:3TJM"
FT STRAND 2230..2233
FT /evidence="ECO:0007829|PDB:3TJM"
FT STRAND 2239..2241
FT /evidence="ECO:0007829|PDB:3TJM"
FT STRAND 2244..2247
FT /evidence="ECO:0007829|PDB:3TJM"
FT HELIX 2255..2257
FT /evidence="ECO:0007829|PDB:3TJM"
FT HELIX 2258..2263
FT /evidence="ECO:0007829|PDB:3TJM"
FT STRAND 2268..2271
FT /evidence="ECO:0007829|PDB:3TJM"
FT HELIX 2282..2293
FT /evidence="ECO:0007829|PDB:3TJM"
FT TURN 2294..2296
FT /evidence="ECO:0007829|PDB:3TJM"
FT STRAND 2303..2307
FT /evidence="ECO:0007829|PDB:3TJM"
FT HELIX 2309..2325
FT /evidence="ECO:0007829|PDB:3TJM"
FT STRAND 2333..2338
FT /evidence="ECO:0007829|PDB:3TJM"
FT HELIX 2343..2352
FT /evidence="ECO:0007829|PDB:3TJM"
FT HELIX 2360..2375
FT /evidence="ECO:0007829|PDB:3TJM"
FT HELIX 2380..2387
FT /evidence="ECO:0007829|PDB:3TJM"
FT STRAND 2390..2392
FT /evidence="ECO:0007829|PDB:3TJM"
FT HELIX 2393..2407
FT /evidence="ECO:0007829|PDB:3TJM"
FT HELIX 2413..2432
FT /evidence="ECO:0007829|PDB:3TJM"
FT STRAND 2443..2447
FT /evidence="ECO:0007829|PDB:3TJM"
FT STRAND 2453..2458
FT /evidence="ECO:0007829|PDB:4Z49"
FT TURN 2459..2463
FT /evidence="ECO:0007829|PDB:3TJM"
FT HELIX 2464..2466
FT /evidence="ECO:0007829|PDB:3TJM"
FT STRAND 2468..2470
FT /evidence="ECO:0007829|PDB:7MHD"
FT STRAND 2472..2476
FT /evidence="ECO:0007829|PDB:3TJM"
FT HELIX 2483..2485
FT /evidence="ECO:0007829|PDB:3TJM"
FT HELIX 2487..2499
FT /evidence="ECO:0007829|PDB:3TJM"
SQ SEQUENCE 2511 AA; 273427 MW; 7A07171FEFA3287B CRC64;
MEEVVIAGMS GKLPESENLQ EFWDNLIGGV DMVTDDDRRW KAGLYGLPRR SGKLKDLSRF
DASFFGVHPK QAHTMDPQLR LLLEVTYEAI VDGGINPDSL RGTHTGVWVG VSGSETSEAL
SRDPETLVGY SMVGCQRAMM ANRLSFFFDF RGPSIALDTA CSSSLMALQN AYQAIHSGQC
PAAIVGGINV LLKPNTSVQF LRLGMLSPEG TCKAFDTAGN GYCRSEGVVA VLLTKKSLAR
RVYATILNAG TNTDGFKEQG VTFPSGDIQE QLIRSLYQSA GVAPESFEYI EAHGTGTKVG
DPQELNGITR ALCATRQEPL LIGSTKSNMG HPEPASGLAA LAKVLLSLEH GLWAPNLHFH
SPNPEIPALL DGRLQVVDQP LPVRGGNVGI NSFGFGGSNV HIILRPNTQP PPAPAPHATL
PRLLRASGRT PEAVQKLLEQ GLRHSQDLAF LSMLNDIAAV PATAMPFRGY AVLGGERGGP
EVQQVPAGER PLWFICSGMG TQWRGMGLSL MRLDRFRDSI LRSDEAVKPF GLKVSQLLLS
TDESTFDDIV HSFVSLTAIQ IGLIDLLSCM GLRPDGIVGH SLGEVACGYA DGCLSQEEAV
LAAYWRGQCI KEAHLPPGAM AAVGLSWEEC KQRCPPGVVP ACHNSKDTVT ISGPQAPVFE
FVEQLRKEGV FAKEVRTGGM AFHSYFMEAI APPLLQELKK VIREPKPRSA RWLSTSIPEA
QWHSSLARTS SAEYNVNNLV SPVLFQEALW HVPEHAVVLE IAPHALLQAV LKRGLKPSCT
IIPLMKKDHR DNLEFFLAGI GRLHLSGIDA NPNALFPPVE FPAPRGTPLI SPLIKWDHSL
AWDVPAAEDF PNGSGSPSAA IYNIDTSSES PDHYLVDHTL DGRVLFPATG YLSIVWKTLA
RALGLGVEQL PVVFEDVVLH QATILPKTGT VSLEVRLLEA SRAFEVSENG NLVVSGKVYQ
WDDPDPRLFD HPESPTPNPT EPLFLAQAEV YKELRLRGYD YGPHFQGILE ASLEGDSGRL
LWKDNWVSFM DTMLQMSILG SAKHGLYLPT RVTAIHIDPA THRQKLYTLQ DKAQVADVVV
SRWLRVTVAG GVHISGLHTE SAPRRQQEQQ VPILEKFCFT PHTEEGCLSE RAALQEELQL
CKGLVQALQT KVTQQGLKMV VPGLDGAQIP RDPSQQELPR LLSAACRLQL NGNLQLELAQ
VLAQERPKLP EDPLLSGLLD SPALKACLDT AVENMPSLKM KVVEVLAGHG HLYSRIPGLL
SPHPLLQLSY TATDRHPQAL EAAQAELQQH DVAQGQWDPA DPAPSALGSA DLLVCNCAVA
ALGDPASALS NMVAALREGG FLLLHTLLRG HPLGDIVAFL TSTEPQYGQG ILSQDAWESL
FSRVSLRLVG LKKSFYGSTL FLCRRPTPQD SPIFLPVDDT SFRWVESLKG ILADEDSSRP
VWLKAINCAT SGVVGLVNCL RREPGGNRLR CVLLSNLSST SHVPEVDPGS AELQKVLQGD
LVMNVYRDGA WGAFRHFLLE EDKPEEPTAH AFVSTLTRGD LSSIRWVCSS LRHAQPTCPG
AQLCTVYYAS LNFRDIMLAT GKLSPDAIPG KWTSQDSLLG MEFSGRDASG KRVMGLVPAK
GLATSVLLSP DFLWDVPSNW TLEEAASVPV VYSTAYYALV VRGRVRPGET LLIHSGSGGV
GQAAIAIALS LGCRVFTTVG SAEKRAYLQA RFPQLDSTSF ANSRDTSFEQ HVLWHTGGKG
VDLVLNSLAE EKLQASVRCL ATHGRFLEIG KFDLSQNHPL GMAIFLKNVT FHGVLLDAFF
NESSADWREV WALVQAGIRD GVVRPLKCTV FHGAQVEDAF RYMAQGKHIG KVVVQVLAEE
PEAVLKGAKP KLMSAISKTF CPAHKSYIIA GGLGGFGLEL AQWLIQRGVQ KLVLTSRSGI
RTGYQAKQVR RWRRQGVQVQ VSTSNISSLE GARGLIAEAA QLGPVGGVFN LAVVLRDGLL
ENQTPEFFQD VCKPKYSGTL NLDRVTREAC PELDYFVVFS SVSCGRGNAG QSNYGFANSA
MERICEKRRH EGLPGLAVQW GAIGDVGILV ETMSTNDTIV SGTLPQRMAS CLEVLDLFLN
QPHMVLSSFV LAEKAAAYRD RDSQRDLVEA VAHILGIRDL AAVNLDSSLA DLGLDSLMSV
EVRQTLEREL NLVLSVREVR QLTLRKLQEL SSKADEASEL ACPTPKEDGL AQQQTQLNLR
SLLVNPEGPT LMRLNSVQSS ERPLFLVHPI EGSTTVFHSL ASRLSIPTYG LQCTRAAPLD
SIHSLAAYYI DCIRQVQPEG PYRVAGYSYG ACVAFEMCSQ LQAQQSPAPT HNSLFLFDGS
PTYVLAYTQS YRAKLTPGCE AEAETEAICF FVQQFTDMEH NRVLEALLPL KGLEERVAAA
VDLIIKSHQG LDRQELSFAA RSFYYKLRAA EQYTPKAKYH GNVMLLRAKT GGAYGEDLGA
DYNLSQVCDG KVSVHVIEGD HRTLLEGSGL ESIISIIHSS LAEPRVSVRE G
//