ID FAS2_EMEND Reviewed; 1858 AA. AC P78615; DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 13-SEP-2023, entry version 119. DE RecName: Full=Fatty acid synthase subunit alpha; DE EC=2.3.1.86; DE Includes: DE RecName: Full=Acyl carrier; DE Includes: DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase; DE EC=1.1.1.100; DE AltName: Full=Beta-ketoacyl reductase; DE Includes: DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase; DE EC=2.3.1.41; DE AltName: Full=Beta-ketoacyl synthase; GN Name=fasA; OS Emericella nidulans (Aspergillus nidulans). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Nidulantes. OX NCBI_TaxID=162425; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE. RC STRAIN=FGSC 89; RX PubMed=8962148; DOI=10.1073/pnas.93.25.14873; RA Brown D.W., Adams T.H., Keller N.P.; RT "Aspergillus has distinct fatty acid synthases for primary and secondary RT metabolism."; RL Proc. Natl. Acad. Sci. U.S.A. 93:14873-14877(1996). CC -!- FUNCTION: Fatty acid synthetase catalyzes the formation of long-chain CC fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit CC contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier- CC protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase. CC {ECO:0000269|PubMed:8962148}. CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain CC fatty acyl-CoA + n CO2 + n CoA + H2O + 2n NADP(+); CC Xref=Rhea:RHEA:22896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:83139; EC=2.3.1.86; 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; 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 -!- SUBUNIT: Fatty acid synthase is composed of alpha and beta subunits. CC {ECO:0000250}. CC -!- DISRUPTION PHENOTYPE: Unable to grow on minimal medium unless CC supplemented with myristic acid. {ECO:0000269|PubMed:8962148}. CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Fungal fatty acid CC synthetase subunit alpha family. {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; U75347; AAB41493.1; -; Genomic_DNA. DR AlphaFoldDB; P78615; -. DR SMR; P78615; -. DR GO; GO:0005835; C:fatty acid synthase complex; IEA:InterPro. 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:0004312; F:fatty acid synthase activity; IEA:InterPro. DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt. DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IEA:InterPro. DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt. DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt. DR CDD; cd00828; elong_cond_enzymes; 1. DR CDD; cd08950; KR_fFAS_SDR_c_like; 1. DR Gene3D; 3.30.70.2490; -; 1. DR Gene3D; 3.40.47.10; -; 1. DR Gene3D; 3.90.25.70; -; 1. DR Gene3D; 6.10.140.1390; -; 1. DR Gene3D; 6.10.140.1410; -; 1. DR Gene3D; 6.10.250.1930; -; 1. DR Gene3D; 6.10.250.1940; -; 1. DR Gene3D; 3.90.470.20; 4'-phosphopantetheinyl transferase domain; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR HAMAP; MF_00101; AcpS; 1. DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom. DR InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf. DR InterPro; IPR002582; ACPS. DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase. DR InterPro; IPR040899; Fas_alpha_ACP. DR InterPro; IPR047224; FAS_alpha_su_C. DR InterPro; IPR026025; FAS_alpha_yeast. DR InterPro; IPR041550; FASI_helical. DR InterPro; IPR018201; Ketoacyl_synth_AS. DR InterPro; IPR014031; Ketoacyl_synth_C. DR InterPro; IPR014030; Ketoacyl_synth_N. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom. DR InterPro; IPR009081; PP-bd_ACP. DR InterPro; IPR004568; Ppantetheine-prot_Trfase_dom. DR InterPro; IPR002347; SDR_fam. DR InterPro; IPR016039; Thiolase-like. DR NCBIfam; TIGR00556; pantethn_trn; 1. DR PANTHER; PTHR10982:SF23; FATTY ACID SYNTHASE SUBUNIT ALPHA; 1. DR PANTHER; PTHR10982; MALONYL COA-ACYL CARRIER PROTEIN TRANSACYLASE; 1. DR Pfam; PF01648; ACPS; 1. DR Pfam; PF00106; adh_short; 1. DR Pfam; PF18325; Fas_alpha_ACP; 1. DR Pfam; PF18314; FAS_I_H; 1. DR Pfam; PF00109; ketoacyl-synt; 1. DR Pfam; PF02801; Ketoacyl-synt_C; 1. DR PIRSF; PIRSF000454; FAS_yeast_alpha; 1. DR SUPFAM; SSF56214; 4'-phosphopantetheinyl transferase; 1. DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR SUPFAM; SSF53901; Thiolase-like; 2. DR PROSITE; PS50075; CARRIER; 1. DR PROSITE; PS00606; KS3_1; 1. DR PROSITE; PS52004; KS3_2; 1. DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1. PE 3: Inferred from homology; KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis; KW Lipid metabolism; Magnesium; Metal-binding; Multifunctional enzyme; NAD; KW NADP; Oxidoreductase; Phosphopantetheine; Phosphoprotein; Transferase. FT CHAIN 1..1858 FT /note="Fatty acid synthase subunit alpha" FT /id="PRO_0000419254" FT DOMAIN 143..218 FT /note="Carrier" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258" FT DOMAIN 1097..1634 FT /note="Ketosynthase family 3 (KS3)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" FT REGION 580..606 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 651..848 FT /note="Beta-ketoacyl reductase" FT /evidence="ECO:0000250" FT COMPBIAS 580..597 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 1279 FT /note="For beta-ketoacyl synthase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" FT ACT_SITE 1519 FT /note="For beta-ketoacyl synthase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" FT ACT_SITE 1560 FT /note="For beta-ketoacyl synthase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" FT BINDING 1746..1748 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250" FT BINDING 1746 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 1747 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 1748 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 1772 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250" FT BINDING 1782 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250" FT BINDING 1791..1801 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250" FT BINDING 1815..1818 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250" FT BINDING 1843..1845 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250" FT BINDING 1844 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 1845 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT MOD_RES 178 FT /note="O-(pantetheine 4'-phosphoryl)serine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258" SQ SEQUENCE 1858 AA; 204732 MW; 3D961E8716C9E24D CRC64; MRPEIEQELA HTLLVELLAY QFASPVRWIE TQDVILAEKR TERIVEIGPA DTLGGMARRT LASKYEAYDA ATSVQRQILC YNKDAKEIYY DVDPVEEETE SAPEAAAAPP TSAAPAAAVV AAPAPAASAP SAGPAAPVED APVTALDIVR TLVAQKLKKA LSDVPLNKAI KDLVGGKSTL QNEILGDLGK EFGSTPEKPE DTPLDELGAS MQATFNGQLG KQSSSLIARL VSSKMPGGFN ITAVRKYLET RWGLGPGRQD GVLLLALTME PASRIGSEPD AKVFLDDVAN KYAANSGISL NVPTASGDGG ASAGGMLMDP AAIDALTKDQ RALFKQQLEI IARYLKMDLR DGQKAFVASQ ETQKTLQAQL DLWQAEHGDF YASGIEPSFD PLKARVYDSS WNWARQDALS MYYDIIFGRL KVVDREIVSQ CIRIMNRSNP LLLEFMQYHI DNCPTERGET YQLAKELGEQ LIENCKEVLG VSPVYKDVAV PTGPQTTIDA RGNIEYQEVP RASARKLEHY VKQMAEGGPI SEYSNRAKVQ NDLRSVYKLI RRQHRLSKSS QLQFNALYKD VVRALSMNEN QIMPQENGST KKPGRNGSVR NGSPRAGKVE TIPFLHLKKK NEHGWDYSKK LTGIYLDVLE SAARSGLTFQ GKNVLMTGAG AGSIGAEVLQ GLISGGAKVI VTTSRYSREV TEYYQAMYAR YGARGSQLVV VPFNQGSKQD VEALVDYIYD TKKGLGWDLD FIVPFAAIPE NGREIDSIDS KSELAHRIML TNLLRLLGSV KAQKQANGFE TRPAQVILPL SPNHGTFGND GLYSESKLAL ETLFNRWYSE NWSNYLTICG AVIGWTRGTG LMSGNNMVAE GVEKLGVRTF SQQEMAFNLL GLMAPAIVNL CQLDPVWADL NGGLQFIPDL KDLMTRLRTE IMETSDVRRA VIKETAIENK VVNGEDSEVL YKKVIAEPRA NIKFQFPNLP TWDEDIKPLN ENLKGMVNLD KVVVVTGFSE VGPWGNSRTR WEMEASGKFS LEGCVEMAWI MGLIRHHNGP IKGKTYSGWV DSKTGEPVDD KDVKAKYEKY ILEHSGIRLI EPELFKGYDP KKKQLLQEIV IEEDLEPFEA SKETAEEFKR EHGEKVEIFE VLESGEYTVR LKKGATLLIP KALQFDRLVA GQVPTGWDAR RYGIPEDIIE QVDPVTLFVL VCTAEAMLSA GVTDPYEFYK YVHLSEVGNC IGSGIGGTHA LRGMYKDRYL DKPLQKDILQ ESFINTMSAW VNMLLLSSTG PIKTPVGACA TAVESVDIGY ETIVEGKARV CFVGGFDDFQ EEGSYEFANM KATSNAEDEF AHGRTPQEMS RPTTTTRAGF MESQGCGMQL IMSAQLALDM GVPIYGIIAL TTTATDKIGR SVPAPGQGVL TTARENPGKF PSPLLDIKYR RRQLELRKRQ IREWQESELL YLQEEAEAIK AQNPADFVVE EYLQERAQHI NREAIRQEKD AQFSLGNNFW KQDSRIAPLR GALATWGLTV DEIGVASFHG TSTVANDKNE SDVICQQMKH LGRKKGNALL GIFQKYLTGH PKGAAGAWMF NGCLQVLDSG LVPGNRNADN VDKVMEKFDY IVYPSRSIQT DGIKAFSVTS FGFGQKGAQV IGIHPKYLYA TLDRAQFEAY RAKVETRQKK AYRYFHNGLV NNSIFVAKNK APYEDELQSK VFLNPDYRVA ADKKTSELKY PPKPPVATDA GSESTKAVIE SLAKAHATEN SKIGVDVESI DSINISNETF IERILPASEQ QYCQNAPSPQ SSFAGRWSAK EAVFKSLGVC SKGAGAPLKD IEIENDSNGA PTLHGVAAEA AKEAGVKHIS VSISHSDMQA VAVAISQF //