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Database: UniProt
Entry: K3VEF2_FUSPC
LinkDB: K3VEF2_FUSPC
Original site: K3VEF2_FUSPC 
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
//
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