ID B2W1Q2_PYRTR Unreviewed; 2386 AA.
AC B2W1Q2;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 24-JAN-2024, entry version 93.
DE SubName: Full=Phenolpthiocerol synthesis polyketide synthase ppsB {ECO:0000313|EMBL:EDU47225.1};
GN ORFNames=PTRG_04387 {ECO:0000313|EMBL:EDU47225.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU47225.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
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DR EMBL; DS231617; EDU47225.1; -; Genomic_DNA.
DR RefSeq; XP_001934720.1; XM_001934685.1.
DR STRING; 426418.B2W1Q2; -.
DR EnsemblFungi; EDU47225; EDU47225; PTRG_04387.
DR GeneID; 6342625; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR InParanoid; B2W1Q2; -.
DR OMA; QPICSVL; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000001471; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd05274; KR_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 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 InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
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; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775:SF29; ASPERFURANONE POLYKETIDE SYNTHASE AFOG-RELATED; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 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; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-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; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001471};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..433
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2299..2376
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2386 AA; 259858 MW; 9141E9FE7FE69EE7 CRC64;
MPSATTSIDV PIAVVGLACR FPGDASSPSK FWDMLKNGRD AYSPTSSRWN SDAFYHPFNG
KLNSLPTKGG HFLKEDPYVF DASFFNITAA EAIALDPKQR MALEVAYEAF ENANMPLQQV
SGTQTACYMG SGASDYRGAV ERDFLNNPKY HLLGTGDEMI SNRISHFFNI HGPSATVQTA
CSSSLMATHL ACQSLKSGES EMAVTGGVSL MLTPDFTTHL NNLTFLNPQG RSKAFDESAG
GYGRGEGCGI IILKRLDKAI QDGDSIRAVI RATGANSDGF TQGITMPSFE AQAALIKYVY
ESNGLDYNSA QYVEAHGTGT KVGDPIETRA IYSTIGKGSS KSRKLYVGSV KPNIGHLESA
AGVSGIIKGI LAMEHNLIPP NVHFTKGNPN IPFDEWNVAV PLKPTPWPVS QTKRMSVSGF
GMGGTNGHAV IESFNSSRLA DVPVKLGDFT KFQKARNKKR LFVFSSHDQA GFKRNADALA
HHIDDLGSAS SSSEFLANLA HTLSGAKSSL SWRATCLTEN TTELRDYLYT KPGDNASREA
SSRHTAPRIG FVFTGQGAQW ARMGVEMLDR QVFRDSVEQS ATYLRDMGCL WDPIAELEKA
QVDSRLSHPE ISQPICSVLQ IALVDELQSW GVVPSRVVGH SSGEIAAAYS IGALSHRDAI
AAAYFRGIAA TKLQTDAPDL KGGMMAVGCS RDEADGVIEQ SKLSGTAVVA CVNSPSSVTL
SGDMDALEQL RAIFDERKVF ARRLKVEMAY HSRHMNRVFG SYSASIADLE PITQDDTDEE
GDVKIQAMIS SVTGQEVAPE LLGPYYWVRN LVSPVLFSDA VKELVSPADQ DANDNSISTV
DLLIEVGPHS ALSGPVEQIL DHYGIKNVGY KSMLIRGRNA LDTSLELASE LYLDGVPLDI
SQVNGDLKVR RLTDLPPYQW NHSKIFRHET RIQRELMTRQ FPPRSLIGAQ VPMMDESQHV
WRNFLRLSDE PWLRGHKIGS TVLLPAAGLV SMAIEAARQL VEPGKKARSL RFREVCFSAA
MALSEDVATE VILHMRPHLL ATSGSTPSSW WEFTISSCVG TSQLRDNCQG LVTIDYADTT
SEQMAKEDAN FEESIISEYH RVHKECPDTY SKEDFYGQFE KISWEYGEAF QGAENVHLGD
GESTYDVRLV DIGETSSKGQ TDRPFLIHAG TLDSILQGCL GSTYKNGRFE KDKPALPTFI
GEMEISLDMP GDIGYVMPGL CKSKRHGFKE LSSDINTFDT SLSKVVLSVV DFRISELEND
TDAQDTEQLE VDPAEITSVI RWKSSLAIAT QEELQKLVLA SAPEARLVLL YIHNNPSATV
IELTPNIEPP NHTVMSELPS GTIQSSHVHY AAICAETSLE GNSANAHLSG IPFYLGELDD
PMPGGVTPAD LLIVPQAFSD CENMEKLLDR LVTLGKPDAA LLLEPKKDFD QLTSILKAKE
FQCVLNVENS VALFKRQVSQ PTNGSTNCTS AKCDFTIVES LAPTQDSKAF SHALRATLED
QGYTASVATW TEMSACTETE LEGKTHISLL ELDMPMLSSL SEPDFHNFRK LVLSSKRLLW
VNAGDDPSMG VIDGIRRTMW SEVAGIDFQV LHLSGLKAAL HFGPSLVSRI LTTEAQDDEY
RERNGMLEVA RIYNSPKGNA DVRHCLEDSV RVQRLADQVK PLTLTIGKPG LLDTLTFIED
DRTKTALGEM EIEVDIKATG INFKDIMAAM GLVGVSVIGH EASGIVTATG SAAASRFKPG
DRVTLLWEGM HTTKIQIDHR LAVHIPDSMS FEEAAALPMV HVTAYHALIN IAKLRRGQSI
LIHAAAGGVG QAALQLAAYL GLTVYVTVGS DDKRRLLMDK YNIPDAHIFY SRDASFLKAI
KRVTGGRGVD CVLNSLSGEL LRVSWACLAP FGTFVEIGLR DITNNMRLDM RPFSQSTTFA
FINIANFFCA EGLDTLGNII SDTFALVHRG VLRSAYPLTV YPVSELGTAF RTMQQGKHRG
KLVLSFEENA QAPVLCKSKD ALRLNPDATY LFVGGLGGLG RSLAREFIAC GARHIAFVSR
SGNAGEKAKA TIDDLTALGA VVKAYQADIT DEDAFLSTMQ QCAADLPPIA GVLQMAMLLR
DSLFEKMSYE DWTGPTRPKI QGTLNLHHYF SDTRPLDFFL ICSSISGIFG NTGQTAYAAG
NTFQDAFAQH RRNQGLKAVA INLGIMRDVG VLAEQGSTGK LALWEAALGI REKPFHALMK
SIINRECKGE ASPTQICTGL GTADVMKNFG LELPEHFSDP RFGPLNVLSI DATSSTNTDG
SSVASSPSAR LTTASTFHEA VSIITDALVH KTAEILLMPV SEVDPSRPMY RYGVDSLVAL
EVRNWITREL QANMALLEIL AAVPMGEFAE KIAGKSKLVM MGDAGK
//