ID X0AQ78_FUSOX Unreviewed; 1856 AA.
AC X0AQ78;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=FOMG_10447 {ECO:0000313|EMBL:EXK35261.1};
OS Fusarium oxysporum f. sp. melonis 26406.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089452 {ECO:0000313|EMBL:EXK35261.1};
RN [1] {ECO:0000313|EMBL:EXK35261.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=26406 {ECO:0000313|EMBL:EXK35261.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum melonis.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EXK35261.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=26406 {ECO:0000313|EMBL:EXK35261.1};
RG The Broad Institute Genomics Platform;
RA Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "Annotation of the Genome Sequence of Fusarium oxysporum f. sp. melonis
RT 26406.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; JH659335; EXK35261.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:FOMG_10447; -.
DR HOGENOM; CLU_000114_0_0_1; -.
DR Proteomes; UP000030703; Unassembled WGS sequence.
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; 203863 MW; 737EF3D86BC96CB8 CRC64;
MRPEVEQELA HTLLVELLAY QFASPVRWIE TQDVFLGERT AERVVEIGPA DTLGVMAKRT
LKSKYEAYDA AKSVQRNILC YNKDAKEIYY DVDPVEEEPE PAAASSSDAP AAPAAAAAAP
AAAAAAPAPS SGPVAQVADE PVQAVDIVRA LIAQKLKKPL LEVPLSKAIK DLVGGKSTLQ
NEILGDLGKE FGSTPEKPED TPLDELGASM QATFDGNLGK QSLSLIARLI SSKMPGGFNI
TAARKYLESR WGLGPGRQDG ALLLALTMEP PARLGSEGDA KAFFDSVANK YATNAGISLS
TATAAGPAGG SSGGMMMDPA AIDALTKDQR ALFKQQLELL ARYLKIDLRE GEKAHLNSQK
SEKVLQAQLD LWTAEHGDFY ASGIEPVFTP LKARTYDSSW NWARQDALSM YFDIIFGRLQ
AVDREIVSQC IRLMNRSNPK LLDFMQYHID NCPTERGETY KLAQELGQQL IENCKDVLDV
APVYKDVSLP TGPRTTVDAR GNLNYEEVPR TSCRKLEHYV QQMAEGGKIS EYGNRTKVQS
DLSRIYRLIK QQHKLSKTSQ LEIKSLYGEV LRSLAMNESQ ILPKDNKGRK VLKNSQSKGK
VETIPFLHLK KKGLHGWDYS KKLTGVYLNC LEDAAKSGVT FQDKHVLMTG AGAGSIGAEV
LQGLISGGAK VIVTTSRFSR EVTEYYQAMY TRYGSRGSQI VVVPFNQGSK QDVEALVEYI
YDTKEGLGWD LDFIVPFAAI PENGREIDSI DSKSELAHRI MLTNLVRLLG CVKAQKTERG
FETRPAQVVL PLSPNHGTFG NDGLYSESKL GLETLFNRWH SESWANYLTI CGAVIGWTRG
TGLMSGNNIV AEGVEAFGVR TFSQQEMAFN LLGLMSPTLV DLCQNEPVFA DLNGGLQFIP
NLNETMTKLR KDIMETSEVR RAVAKESAIE NTIVNGAASE VLYKKKTIDP RANIKLDFPN
RPDWKTEIEP LNENLKGMVD LEKVVVVTGF AEVGPWGNSR TRWEMEAYGE FSLEGCVEMA
WIMGLIKNHN GLIKGKPYSG WVDAKTGEPV DDKDVKPKYE KYVLEHSGIR LIEPELFEGY
DPNKKQLLHE VVIEEDLEPF EASKETAEEF KREHGDKVEV FEIPDSGEYI IRLRKGASLW
IPKALRFDRL VAGQIPTGWD PKRYGVPEDI VSQVDPVTLF LLVSTAEALL SCGITDPYEF
YKYVHVSEVG NCVGSGMGGA AALRDMHRTR FLDQPVQNDI LQESFINTMA AWVNMLLMSS
SGPIKTPVGA CATAVESIDT GYETIMEGKA RVCFVGGFDD LGEEGSYEFA NMKATSNTVD
EFAHGRTPKE MSRPTTTTRN GFMESQGCGI QVIMTAKLAL DMGVPIHGIV ALTTTASDKI
GRSVPAPGQG VLTTARENPG KFPSPLLDIN YRRRQIERRK KTIKQWQESE LEYVHDEIDA
MKAQGASFDE KEYAADRFAH IEKEAARQEK ELLRSMGNNF WKSDPSIAPL RGALATWGLT
VDDIGVASFH GTSTKANDKN ESSVICQQLR HLGRKKGNAV LGIFQKYLTG HPKGAAGAWM
MNGCLQVLDT GLVPGNRNAD NVDPVMEQYD LIVYPSRSIQ TDGVKAFSVT SFGFGQKGAQ
AIGVHPKYLF ATLDEKTYAE YCAKVDARQK KAYRYFHDGF INNKLFVAKN NSPYSDDQLS
KVLLNPDARV SEDKKSSELK YAPDFMKKSE KVVSSAKAKE TEQVMEALAL KVTNKNSQVG
VDVEDIAAVN IDNDTFVERN FTANEISYCR QAPSPQSSFA GRWSAKEAVF KSLGVASQGA
GAAMKDIEIV KGENGAPAVS LHGEAAAAAK KAGVKDITLS ISHSDSQAIA VAVANF
//
