ID A0A4Q4X7Z3_9PEZI Unreviewed; 1866 AA. AC A0A4Q4X7Z3; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 24-JUL-2024, entry version 20. DE RecName: Full=Fatty acid synthase subunit alpha {ECO:0000256|ARBA:ARBA00014008}; DE EC=1.1.1.100 {ECO:0000256|ARBA:ARBA00012948}; DE EC=2.3.1.41 {ECO:0000256|ARBA:ARBA00013191}; DE EC=2.3.1.86 {ECO:0000256|ARBA:ARBA00012878}; GN ORFNames=DL771_011976 {ECO:0000313|EMBL:RYP56324.1}; OS Monosporascus sp. 5C6A. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Xylariomycetidae; Xylariales; Xylariales incertae sedis; Monosporascus. OX NCBI_TaxID=2211642 {ECO:0000313|EMBL:RYP56324.1, ECO:0000313|Proteomes:UP000292526}; RN [1] {ECO:0000313|EMBL:RYP56324.1, ECO:0000313|Proteomes:UP000292526} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=5C6A {ECO:0000313|EMBL:RYP56324.1, RC ECO:0000313|Proteomes:UP000292526}; RA Robinson A.J., Natvig D.O.; RT "Complete Genomes of Monosporascus."; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. 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:0000256|ARBA:ARBA00001572}; 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:0000256|ARBA:ARBA00001402}; 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; Evidence={ECO:0000256|ARBA:ARBA00000343}; CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Fungal fatty acid CC synthetase subunit alpha family. {ECO:0000256|ARBA:ARBA00007485, CC ECO:0000256|PIRNR:PIRNR000454}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RYP56324.1}. 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; QJOB01000783; RYP56324.1; -; Genomic_DNA. DR STRING; 2211642.A0A4Q4X7Z3; -. DR Proteomes; UP000292526; Unassembled WGS sequence. 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:0042759; P:long-chain fatty acid biosynthetic process; IEA:UniProtKB-UniRule. 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; IPR050830; Fungal_FAS. 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; 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; 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. PE 3: Inferred from homology; KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160}; KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832}; KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR000454-3}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR000454-3}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Phosphopantetheine {ECO:0000256|PIRNR:PIRNR000454, KW ECO:0000256|PIRSR:PIRSR000454-4}; KW Reference proteome {ECO:0000313|Proteomes:UP000292526}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000454}. FT DOMAIN 143..218 FT /note="Carrier" FT /evidence="ECO:0000259|PROSITE:PS50075" FT DOMAIN 1098..1635 FT /note="Ketosynthase family 3 (KS3)" FT /evidence="ECO:0000259|PROSITE:PS52004" FT REGION 96..136 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 1281 FT /note="For beta-ketoacyl synthase activity" FT /evidence="ECO:0000256|PIRSR:PIRSR000454-1" FT BINDING 1752 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3" FT BINDING 1753 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3" FT BINDING 1754 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3" FT BINDING 1852 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3" FT BINDING 1853 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3" FT MOD_RES 178 FT /note="O-(pantetheine 4'-phosphoryl)serine" FT /evidence="ECO:0000256|PIRSR:PIRSR000454-4" SQ SEQUENCE 1866 AA; 203885 MW; 4A6AA1556C63A9FF CRC64; MRPEVEQELA HTLLVELLAY QFASPVRWIE TQDVLLAEQQ AERIVEIGPA DTLGVMAKRT IASKYEAFDA AKSLQRQILC SAKDGKEIYY EGDPIEEESE PAAAAQPGSS GTAPAPAPAA AAAPAAAPAP SAGPAAAVPD APIPAMDVVR ALIAQKLKKP FLEIPLSKAI KDLVGGKSTL QNEILGDLGK EFGSTPEKPE DTPLDELGGL MQATFNGQLG KTTQGLIARV ISSKMPGGFN ITTARKYLES RWGLGPGRQD GVLVFAITME PASRLGSEAD AKAFFDDVTQ KYASHAGVSL STAAAAGPAG GSGGAMMMDP EALEALTKDQ KVLYKNQLEL LARYLKIDLR AGEKAAQATQ QSQAVLQAQI DLWTAEHGDF YASGIEPSFS PLKARSYDSS WNWARQDVLS MYYDVLFGKL KVVDREIVSQ CIRIMSKSNP KLLEFMQYHI DNCPTERGET YRLAKELGEQ LIENCRDVLS VPPVYKDVNV PTGPHTTVDA RGNLAYEEVP RANCRKLEHY VQQMAEGGKI SEYGGRTKVQ NDLGRLVKLI KEQHKMSKTA KLEFKALYGN VLRSLAMNES QILNKDSGKA NGLVKKSSSL KGSSQASKGK METIPFLHLK RSTLHGWEYS KKLTGVYLDV LEAAARNGIS YEGKYALMTG AGAGSIGAEV LSGLISGGAK VIVTTSRFSP EVTQYYQAMY AKFGARGSQL VVVPFNGGSK QDVEALVNYI YDTKNGLGWD LDYIVPFAAI PEQGRQIDGI DSRSELAHRI MLTNVVRLLG AVKSQKDEHG YLTRPAQVIL PLSPNHGTFG NDGLYSESKL GLETLFNRWH SEDWANYLSI TGAVIGWTRG TGLMSGNNIV AEGVEAFGVR TFSQQEMAFN LLGLMSPDIA DICQNEPVFA DLNGGLQFIP NLNETMTRLR KDIMETSEIR RAVTKETAIE NKVVNGENSE ALYKKKVIAP RANIKFDFPT LPDWKTEIEP LNKSLEGMVD LERVVVVTGF AEVGPWGNAR TRWEMEAYGH FSLEGCVEMA WIMGLIKNHN GPIKGQPYSG WVDAKTGEPV DDKDIKQKYE SHILEHSGIR LVEPELFFGY NPEKKQLLQE VAIDEDLEPF EASKDLAQAY KREHGDKCEI FEIPESGEYI VRMKKGATLW IPKAIRFDRL VAGQIPTGWD AKRYGIEDDI ISQVDRSTLF VLVSVAEALV SAGITDPYEF YKYVHVSEVG NMIGAGMGGS NALHGMYVER KLDRPVQNDV LQETFINTAA AWVNMLLLSS SGPIKTPVGA CATAVESVDI GYDTIMEGKA RICIVGGYDE FSEEGSNEFA MMNATSNAID EFAHGRTPKE MSRPTTTTRN GFMESQGAGC QIIMTAKLAI EMGLPIYGIL ALTTTASDKI GRSVPAPGQG VLTTARENSS KFPSPLLDLN YRRRQIDIRK RQITSWKESE LEYLYEEVAA MKVQSPGFDE KAYTQERALH IEKEAARQET EAVRSLGNNF WKQDNSIAPL RGALATWGLT IDDLDVASFH GTSTKANDKN ESSVINKQLT HLGRKKGNAV LGIFQKYLTG HPKGAAGAWM MNGCLQVLNT GLVPGNRNAD NVDPVMEEFD LIVYPSRSIQ TDGVKAFSVT SFGFGQKGAQ AIGVHPKYLF AVLDQSTYAQ YAAKVTARQK KAYRFLHNGM INNSIFKAKN NSPYTDDQLR SVLLNPDART SDDKKTMAIT YAANFAKQTA EPQAAKTKKT KQVVESLAQT LRTGKNNKVG VDVEDISAIN IENATFIERN FTAHEIDYCR NAANPQSSFA GRWSAKEAVF KSLGVQSKGA GAALKEIEIL SNDVGAPIVS LHGDAETAAK KAGVKEISIS ISHSDDQAIA IAVATF //