ID   FAS2_PENPA              Reviewed;        1857 AA.
AC   P15368;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   13-SEP-2023, entry version 139.
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=FAS2;
OS   Penicillium patulum (Penicillium griseofulvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5078;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3053172; DOI=10.1111/j.1432-1033.1988.tb14346.x;
RA   Wiesner P., Beck J., Beck K.-F., Ripka S., Mueller G., Luecke S.,
RA   Schweizer E.;
RT   "Isolation and sequence analysis of the fatty acid synthetase FAS2 gene
RT   from Penicillium patulum.";
RL   Eur. J. Biochem. 177:69-79(1988).
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   -!- 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: [Alpha(6)beta(6)] hexamers of two multifunctional subunits
CC       (alpha and beta).
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Fungal fatty acid
CC       synthetase subunit alpha family. {ECO:0000305}.
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DR   EMBL; M37461; AAA33695.1; -; Genomic_DNA.
DR   PIR; S01787; S01787.
DR   AlphaFoldDB; P15368; -.
DR   SMR; P15368; -.
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; 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.
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..1857
FT                   /note="Fatty acid synthase subunit alpha"
FT                   /id="PRO_0000180285"
FT   DOMAIN          139..214
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          1092..1633
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   REGION          96..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          577..604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          648..845
FT                   /note="Beta-ketoacyl reductase"
FT   COMPBIAS        116..131
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1275
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        1518
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        1559
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   BINDING         1743..1745
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250"
FT   BINDING         1743
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         1744
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         1745
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         1769
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250"
FT   BINDING         1779
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250"
FT   BINDING         1788..1798
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250"
FT   BINDING         1812..1815
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250"
FT   BINDING         1842..1844
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250"
FT   BINDING         1843
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         1844
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         174
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   1857 AA;  204466 MW;  34BAFD547D93FEE6 CRC64;
     MRPEVEQELA HTLLVELLAY QFASPVRWIE TQDVILAEQR TERIVEIGPA DTLGGMARRT
     LASKYEAYDA ATSVQRQILC YNKDAKEIYY DVDPVEEEPE ATEPAPSATP AAPAAAPAAG
     APPPPPSAGP AASVEDIPVT AVDILRTLVA QKLKKSLADV PLSKAIKDLV GGKSTLQNEI
     LGDLGKEFGS TPEKPEDVPL DELGASMQAT FNGQLGKQSS SLIARMVSSK MPGGFNITSV
     RKYLETRWGL GSGRQDGVLL LALTMEPAAR LGSEVDAKAY LDDVTNKYAA SAGVNLSAPV
     AGGDSGGAGG GMVMDPAAID ALTKDQRALF KQQLEIIARY LKMDLRGGEK AHVISQETQK
     ALQAQLDLWQ AEHGDFYASG IEPSFDQLKA RVYDSSWNWA RQDALSMYYD IIFGRLQVVD
     REIVSQCIRI MNRSNPLLLD FMQYHIDNCP TERGETYQLA KELGQQLIEN CREVLEVAPV
     YKDVAVPTGP QTTIDARGNI SYKETPRTSA RKLEHYVKHM AEGGPISEYS NRTKVQNDLK
     SVYKLIRKQH RLSKSSQLQF DALYKDVVHA LGMNESQIIP QENGHSKKGG RSAAKRNTPT
     RPGKVETIPF LHLKKKTEHG WDYNKKLTGI YLNVTESAAK DGLSFQGKNV LMTGAGAGSI
     GAEVLQGLIS GGAQVIVTTS RFSREVTEYY QAMYARYGAR GSQLVVVPFN QGSKQDVEAL
     VEYIYDTKKG LGWDLDFVVP FAAIPENGRE IDSIDSKSEL AHRIMLTNLL RLLGSVKTQK
     QAHGFETRPA QVILPLSPNH GTFGNDGLYS ESKLALETLF NRWYSENWGH YLTICGAVIG
     WTRGTGLMSG NNMVAEGVEK LGVRTFSQQE MAFNLLGLMS PAIVNLCQLD PVFADLNGGL
     QFIPDLKGLM TKLRTDIMET SDVRQAVMKE TAIEHNIVNG EDSGVLYKKV IAEPRANIKF
     EFPNLPDWEK EVKPLNENLK GMVNLDKVVV VTGFSEVGPW GNSRTRWEME SKGKFSLEGC
     VEMAWIMGLI KHHNGPLKGQ AYSGWVDAKT GEPVDDKDVK PKYEKHILEH TGIRLIEPEL
     FKGYDPKKKQ LLQEIVIQED LEPFEASKET AEEFKREHGD KVEIFEIPES GEYTVRLCKG
     ATMLIPKALQ FDRLVAGQVP TGWDASRYGI PDDIISQVDP VTLFVLVCTA EAMLSAGVTD
     PYEFYKYVHL SEVGNCIGSG IGGTHRLRGM YKDRFLDKPL QKDILQESFI NTMSAWVNML
     LLSSTGPIKT PVGCCATAVE SVDIGYETIV EGKARVCFVG GFDDFQEEGS YEFANMKATS
     NAEDEFAHGR TPQEMSRPTT TTRAGFMESQ GCGMQLIMTA QLALDMGVPI HGIIALTTTA
     TDKIGRSVRS VPAPGQGVLT TARENPGKFP SPLLDIKYRR RQLDLRKKQI NEWQEAELLY
     LQEEAEAMKA QSDETFNEAE YMQERAQHIE REAIRQEKDA QYSLGNNFWK QDSRIAPLRG
     AMATWGLTVD DIDVASFHGT STVANDKNES DVICQQMKHL GRSKGNAVMG IFQKYLTGHP
     KGAAGAWMFN GCLQVLDSGL VPGNRNADNV DKVMEKFDYI VYPSRSIQTD GVKAFSVTSF
     GFGQKGAQVI GIHPKYLYAT LDQAQYEAYK TKVEARQKKA YRYFHNGLIN NSIFVAKSKA
     PYEDEQQSKV FLNPDYRVSV DKKTSELKFS TTAPEAKQSE STRQTLESLA KANATENSKI
     GVDVEHIDSV NIENETFVER NFTQSEQDYC RKAASPQSSF AGRWSAKEAV FKSLGVSSKG
     AGAALKDIEI GVDANGAPVV NLHGAAAAAA KQAGVKQVSV SISHSDSQAV AVAVSQF
//