FAS2_EMEND
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 03-AUG-2022, entry version 114.
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}.
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DR EMBL; U75347; AAB41493.1; -; Genomic_DNA.
DR AlphaFoldDB; P78615; -.
DR SMR; P78615; -.
DR PRIDE; 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: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; IPR002347; SDR_fam.
DR InterPro; IPR016039; Thiolase-like.
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; 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..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 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 REGION 1123..1337
FT /note="Beta-ketoacyl synthase"
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:0000250"
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
