ID K3VEF2_FUSPC Unreviewed; 1856 AA.
AC K3VEF2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 69.
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=FPSE_07169 {ECO:0000313|EMBL:EKJ72532.1};
OS Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=1028729 {ECO:0000313|EMBL:EKJ72532.1, ECO:0000313|Proteomes:UP000007978};
RN [1] {ECO:0000313|EMBL:EKJ72532.1, ECO:0000313|Proteomes:UP000007978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS3096 {ECO:0000313|EMBL:EKJ72532.1,
RC ECO:0000313|Proteomes:UP000007978};
RX PubMed=23028337; DOI=10.1371/journal.ppat.1002952;
RA Gardiner D.M., McDonald M.C., Covarelli L., Solomon P.S., Rusu A.G.,
RA Marshall M., Kazan K., Chakraborty S., McDonald B.A., Manners J.M.;
RT "Comparative pathogenomics reveals horizontally acquired novel virulence
RT genes in fungi infecting cereal hosts.";
RL PLoS Pathog. 8:E1002952-E1002952(2012).
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; EC=2.3.1.86;
CC 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:EKJ72532.1}.
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DR EMBL; AFNW01000191; EKJ72532.1; -; Genomic_DNA.
DR RefSeq; XP_009258562.1; XM_009260287.1.
DR EnsemblFungi; EKJ72532; EKJ72532; FPSE_07169.
DR GeneID; 20365787; -.
DR KEGG; fpu:FPSE_07169; -.
DR eggNOG; ENOG502QQJX; Eukaryota.
DR HOGENOM; CLU_000114_0_0_1; -.
DR OrthoDB; 2783039at2759; -.
DR Proteomes; UP000007978; Chromosome 3.
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; 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.
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000454}.
FT DOMAIN 139..217
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1088..1625
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT ACT_SITE 1271
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-1"
FT BINDING 1742
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT BINDING 1743
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT BINDING 1744
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT BINDING 1842
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT BINDING 1843
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT MOD_RES 177
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-4"
SQ SEQUENCE 1856 AA; 204147 MW; E089C8BCD457DD5F CRC64;
MRPEVEQELA HTLLVELLAY QFASPVRWIE TQDVFLGERT AERVVEIGPA DTLGVMAKRT
LKSKYEAYDA AKSVQRNILC YNKDAKEIYY DVDPVEEEPE PAAASSSEAS ASAPAASAAA
PAAAAAPAPS SGPVAQVADE PVQAVDIVRA LIAQKLKKPL LEVPLSKAIK DLVGGKSTLQ
NEILGDLGKE FGSTPEKPED TPLDELGASM QATFDGNLGK QSLSLIARLI SSKMPGGFNI
TAARKYLESR WGLGPGRQDG ALLLALTMEP PARLGSEGDA KGFFDSVANK YATNAGISLS
TAAATGPAGG SSGGMMMDPA AIDALTKDQR ALFKQQLELL ARYLKIDLRE GEKAHINSQK
SEKVLQAQID LWTAEHGDFY ASGIEPVFTP LKARTYDSSW NWARQDALSM YFDIIFGRLQ
AIDREIVSQC IRLMNRSNPK LLEFMQYHID NCPTERGETY KLAKELGQQL IENIQDVLEI
APVYKDVAVP TGPRTTVDAR GNLNYEEVPR ASCRKLEHYV QQMAEGGKIS EYGNRTKVQS
DLSRIYRLIK QQHKLSKTSQ LEIKSLYGDV LRSLAMNESQ ILPKDNKGRK VLKNSQSKGK
VETIPFLHLK KKGLHGWDYS KKLTGVYLNC LEDAAKSGVT FQNKHVLMTG AGAGSIGAEV
LQGLVSGGAK VIVTTSRFSR EVTEYYQAMY TRYGSRGSQI VVVPFNQGSK QDVEALVEYI
YDTKEGLGWD LDFIIPFAAI PENGRQIDDI DSKSELAHRI MLTNLIRLLG CVKSQKTERG
FETRPAQVVL PLSPNHGTFG SDGLYSESKL GLETLFNRWH SESWANYLTI CGAVIGWTRG
TGLMSGNNIV AEGVEAFGVR TFSQQEMAFN LLGLMSPTLV DLCQNEPVFA DLNGGLQFIP
NLNETMTKLR KDIMETSEVR RAVAKESAIE NTIVNGAASE VLYKKKTIDP RANIKFDFPK
RPDWKTEVEP LNDSLKGMVD LEKVVVVTGF AEVGPWGNSR TRWEMEAYGE FSLEGCVEMA
WIMGLIKNHN GPIKGKPYSG WVDSKTGEPV DDKDVKQKYE KFVLEHSGIR LIEPELFDGY
DPNKKQLLHE VVIEEDLEPF ESSKETAEEF KREHGDKVEV FEIPDSGEYI IRLRKGASLW
IPKALRFDRL VAGQIPTGWD PKRYGVPDDI VSQVDPVTLF LLVSTAEALL SSGITDPYEF
YKYVHVSEVG NCVGSGMGGA AALRDMHRTR FLDQPVQNDI LQESFINTMA AWVNMLLMSS
SGPIKTPVGA CATAVESIDT GYETIMEGKA RVCFVGGFDD LGEEGSYEFA NMKATSNTVD
EFAHGRTPKE MSRPTTTTRN GFMESQGCGI QIIMTAKLAL EMGVPIHGII ALTTTASDKI
GRSVPAPGQG VLTTARENPG KFPSPLLDIN YRRRQIERRK KTIKQWQESE LEYVHDEIDA
MKSQGATFDE KEYAQDRFAH IEREAARQEK ELLRSMGNNF WKSDPSIAPL RGALATWGLT
VDDIGVASFH GTSTKANDKN ESNVICQQLR HLGRKKGNAV LGIFQKYLTG HPKGAAGAWM
MNGCLQVLDT GLVPGNRNAD NVDPIMEQYD LIVYPSRSIQ TDGVKAFSVT SFGFGQKGAQ
AIGIHPKYLF ATLDEKTYND YCAKVDSRQK KAYRYFHDGF INNKLFVAKN NSPYADDQLS
KVLLNPDARV TEDKKSSELK YGADFMKQSE KVVSSTKAKE TEQVMEALAL KVANKNSQVG
VDVEDISAVN IDNETFVERN FTANEISYCR QAPSPQSSFA GRWSAKEAVF KSLGVASQGA
GAAMKDIEIV KGENGAPTVS LHGDAAAAAQ KAGVKDITLS ISHSDSQAIA VAVANF
//