FAS2_PENPA
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 03-AUG-2022, entry version 134.
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 PRIDE; 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: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:InterPro.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.90.470.20; -; 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; 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; IPR009081; PP-bd_ACP.
DR InterPro; IPR004568; Ppantetheine-prot_Trfase_dom.
DR InterPro; IPR016039; Thiolase-like.
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; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR SUPFAM; SSF56214; SSF56214; 1.
DR TIGRFAMs; TIGR00556; pantethn_trn; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 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 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 REGION ?..1857
FT /note="Beta-ketoacyl synthase"
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:0000250"
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
