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 27-MAR-2024, entry version 243. 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] 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 + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain CC fatty acid + n CO2 + (n+1) CoA + 2n NADP(+); Xref=Rhea:RHEA:14993, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57560, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=2.3.1.85; CC Evidence={ECO:0000269|PubMed:16215233, 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:14994; 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 1045. DR DIP; DIP-33681N; -. DR IntAct; P49327; 118. 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 EPD; P49327; -. DR jPOST; P49327; -. DR MassIVE; P49327; -. DR MaxQB; P49327; -. DR PaxDb; 9606-ENSP00000304592; -. DR PeptideAtlas; P49327; -. DR PRIDE; P49327; -. DR ProteomicsDB; 55989; -. DR Pumba; P49327; -. DR Antibodypedia; 1650; 854 antibodies from 40 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:0008693; F:(3R)-3-hydroxydecanoyl-[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:0047450; F:(3R)-hydroxybutanoyl-[acyl-carrier-protein] hydratase activity; IEA:RHEA. DR GO; GO:0008659; F:(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC. DR GO; GO:0004317; F:(3R)-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:0047117; F:enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) activity; IEA:UniProtKB-EC. DR GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central. DR GO; GO:0016295; F:myristoyl-[acyl-carrier-protein] hydrolase activity; IEA:RHEA. DR GO; GO:0016296; F:palmitoyl-[acyl-carrier-protein] hydrolase activity; IEA:RHEA. 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; 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. DR Genevisible; P49327; HS. 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 Pyridoxal phosphate; Reference proteome; S-nitrosylation; Transferase; KW 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 //