ID A0A0C4EBX6_MAGP6 Unreviewed; 2085 AA.
AC A0A0C4EBX6;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Ketosynthase family 3 (KS3) domain-containing protein {ECO:0000259|PROSITE:PS52004};
GN ORFNames=MAPG_10188 {ECO:0000313|EMBL:KLU91670.1};
OS Magnaporthiopsis poae (strain ATCC 64411 / 73-15) (Kentucky bluegrass
OS fungus) (Magnaporthe poae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Magnaporthaceae; Magnaporthiopsis.
OX NCBI_TaxID=644358 {ECO:0000313|EnsemblFungi:MAPG_10188T0, ECO:0000313|Proteomes:UP000011715};
RN [1] {ECO:0000313|Proteomes:UP000011715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 64411 / 73-15 {ECO:0000313|Proteomes:UP000011715};
RA Ma L.-J., Dead R., Young S., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Magnaporthe poae strain ATCC 64411.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KLU91670.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64411 {ECO:0000313|EMBL:KLU91670.1};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Genome Sequencing Center for Infectious Disease;
RA Ma L.-J., Dead R., Young S., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Magnaporthe poae strain ATCC 64411.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KLU91670.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64411 {ECO:0000313|EMBL:KLU91670.1};
RA Ma L.-J., Dead R., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Yandava C., Wortman J., Nusbaum C., Birren B.;
RT "Annotation of Magnaporthe poae ATCC 64411.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EnsemblFungi:MAPG_10188T0}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64411 / 73-15 {ECO:0000313|EnsemblFungi:MAPG_10188T0};
RX PubMed=26416668; DOI=10.1534/g3.115.020057;
RA Okagaki L.H., Nunes C.C., Sailsbery J., Clay B., Brown D., John T., Oh Y.,
RA Young N., Fitzgerald M., Haas B.J., Zeng Q., Young S., Adiconis X., Fan L.,
RA Levin J.Z., Mitchell T.K., Okubara P.A., Farman M.L., Kohn L.M., Birren B.,
RA Ma L.-J., Dean R.A.;
RT "Genome sequences of three phytopathogenic species of the Magnaporthaceae
RT family of fungi.";
RL G3 (Bethesda) 5:2539-2545(2015).
RN [5] {ECO:0000313|EnsemblFungi:MAPG_10188T0}
RP IDENTIFICATION.
RC STRAIN=ATCC 64411 {ECO:0000313|EnsemblFungi:MAPG_10188T0};
RG EnsemblFungi;
RL Submitted (JUN-2015) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ADBL01002621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADBL01002622; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADBL01002623; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GL876977; KLU91670.1; -; Genomic_DNA.
DR STRING; 644358.A0A0C4EBX6; -.
DR EnsemblFungi; MAPG_10188T0; MAPG_10188T0; MAPG_10188.
DR VEuPathDB; FungiDB:MAPG_10188; -.
DR eggNOG; KOG1202; Eukaryota.
DR OMA; QTTMLEH; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000011715; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF20; HYBRID PKS-NRPS SYNTHETASE APDA; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000011715}.
FT DOMAIN 12..426
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 2085 AA; 226728 MW; A4DC789483D32367 CRC64;
MGSISYNPKF AGEPIAIVGS SCRFPGDASS PSKLWELLKN PRDVVSEIPP SRFNTAGIYN
RDSQHHGSTN VCHAYLLSED PRVFDRDFFG ISPKEAESMD PQQRMLLETV YEGVESAGYS
MQQLRGSATA VFVGVMFLDY QNVSVRGIES LPQYHATGVA MSILANRVSY FYDWKGPSAA
VDTACSSSLV ALHQAVQSLR SGEAEMAVAA GSNLILGAEP FVSESSLNML SPNGRSYMWD
KDADGYTRGE GFSAVMLKRL SQAIADGDHI ECIIRETGVN QDGRTPGITM PSPSAQADLI
RATYARAGLD PRRERDRPQY FEAHGTGTQA GDPREAEAIS SVFFPKGCKS DGELIVGSIK
TIIGHLEGSA GLAGILKASL ALQHGQIPAN LHFKTLNPKI RPFYTHLRIG AAYAAGYLDA
HDAIRIAYLR GLHSKLAQGP DGRRGKMMAV GMSLDQAKTF CAEFDGAIKV AASNSARSCT
LAGDAPTIDA ARERLDEAGT FARVLQVDTA YHSHHMLPAA QPYLDSLRKC NIKIHKGLGE
SCPWYSSVWG SNGRIRSFAG EQDSLRGQYW VDNLTNTVLF SQAVQRAIGE SHVFDLALEV
GPHPALKGPA SEVITNMTGM GLPYSGVLKR GQADVEAFAD ALGLLWKSFP LQSGPPLVGF
ESLQRAFATG EKTSGRPAIL KDLPTYPFDH GTIHWKESRA SALVRTQGCP RHQLLGHANT
FGSGKRREVH WRQVLRISEI PWLNGHRIQG EYLFPATGFV TMAYEAAIRL VPSTEPIRMM
ELHDIDIFRA LNLPPDSSGT EVLFTMRVTD QTDDAVTARW ACYSASVDFE HGQGLGAAPP
QADAHAEGFV RIELGYPSHD VLPKRAEPVL CLTPIDVEEL YETLAGLGHG YTGDFQAPAM
LRRLNHAVVT MPAGWEGADQ MTSREMNPAS LDTVIHGLLA GYSCPGDGRQ RSVYLPGRID
SIRVNMMPLE HSGDNDNGLL EADAFVTRGD ANVISGDLDV FDPASGQTRV QVRGVHMSQL
PGSRKGDREL YAQEVWERDA QSGIEPGKEA QVSAERVEIG RLAARMALFY CRKMTMQIKS
FETMLMSKNR KALMSWVQKD LIGKAQAGEH PETEKEWMED ASEDVLDSEM DRLGAADSAD
IVLIRALGRN LASITRGLTP AIKVAEKDDA LARFYAGGVG FREAIQDAAT LAAQLSHRYP
AMKMVEVGAS FGPGLREAIL ESVGKRRYAS YTVTNAVEPP DEHDSKLLYK LLDMDKDPLR
QGFSEGSFDL AIAATSYSTM INTETLANAR KLLRPGGFLL IVALTGDSLP VRLVQSLLPG
SWMERDDGQP QILSVSECDN VLKQVGFSGV DTSSTPSFCS VMLSQAVDDA VMAVLDPIAT
AQQLEAEVLI VHDPSPSAGV TKLASQLATK LVQVATVRTA AGLEGISVPA GAVVLNLCDL
DTPTWHKMHE RRFQGLQEVM RQASALLWVT EGARTGTKPE NTMVLGWGRS ARVERTTMKL
QVLDIEQEAD TIDPDFVLKL LLRLADTREP SQEMLWTLEP ELVLRDNAFY VPRVWPIDEL
NGLADTRYKD VTVEVPATSP HIILDERGQL TVGRSYQDGA QAQDWEILAA SVHKLRLRDE
EQAKRLCVLR NSKSGESMLA LTYQKGSSFG TEVLWRYCND GRVASYSHQM HHLLAVATAE
AILQGVEGRV WVHGAPAWLV KELDLVATRQ DDLRLYQTTN DAEMSDAQTK FLHPFLTERE
LVLAKPASVS RFICLDDTHH SKALVGVIHK NWPAIKVECP DLSLESHEGV VSKNLSQAGF
AGLVEKKLGI SGQLPDSVVE GCIIPVQDIP NTTLSSVPPA GVFDRTTAAT VMAKLLPPNH
AGLFSADKTY LLLGLAGDLG ISIAHWLFDN GARHVVLASR NPVVPQAVVD HAATVKGANL
RFMAIDICSA TSLAAAWADI HETMPPIAGV MNGAMVMRDQ LFTDQPWANF SAVMAPKVAG
TQNLVELLDR SAKPGQLDFV MFFSSAVAVA GNAGQTAYGA SNWYMQGAAS ELRRRGTPAL
LPPVAMSRSR LICSTDPRAC AVPIAKGMVG EKTAIWSQLK LSMSS
//
