UniProt: W6QMT3

Database: UniProt
Entry: W6QMT3_PENRF

LinkDB:  W6QMT3_PENRF 
Original site:  W6QMT3_PENRF

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Ontology (6)   
   GO (6)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (44)   
   InterPro (23)   
   Pfam (10)   
   PROSITE (5)   
   SMART (6)   
Literature (1)   
   PubMed (1)   
All databases (52)   

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ID   W6QMT3_PENRF            Unreviewed;      2218 AA.
AC   W6QMT3;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:CDM30917.1};
GN   ORFNames=PROQFM164_S02g001067 {ECO:0000313|EMBL:CDM30917.1};
OS   Penicillium roqueforti (strain FM164).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM30917.1};
RN   [1] {ECO:0000313|EMBL:CDM30917.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FM164 {ECO:0000313|EMBL:CDM30917.1};
RX   PubMed=24407037; DOI=10.1038/ncomms3876;
RA   Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA   Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA   Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT   "Multiple recent horizontal transfers of a large genomic region in cheese
RT   making fungi.";
RL   Nat. Commun. 5:2876-2876(2014).
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DR   EMBL; HG792016; CDM30917.1; -; Genomic_DNA.
DR   STRING; 1365484.W6QMT3; -.
DR   OMA; RYPWQHG; -.
DR   OrthoDB; 5396558at2759; -.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   GO; GO:1901336; P:lactone biosynthetic process; IEA:UniProt.
DR   GO; GO:0030639; P:polyketide biosynthetic process; IEA:UniProt.
DR   CDD; cd05195; enoyl_red; 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; IPR011032; GroES-like_sf.
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; IPR032821; PKS_assoc.
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; 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; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF13; POLYKETIDE SYNTHASE 1; 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; PS50075; CARRIER; 1.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          20..445
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2134..2211
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1284..1319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1296..1317
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2218 AA;  242332 MW;  C849829E535AB77A CRC64;
     MTNMKGADSE GASYGDQGTL QPIAIIGYSC RLPGQVTSPS ELWELCTRAR SGWSPIPKDR
     FSVEAFHHPN SSKIGSFNPK GGYFLDEDIA QFDAPFFNLT VQEATAMDPQ QRLLLECAYE
     ALESAGIPKE NFARRNVSVF AGGNFADYEL NNDRDTETIP MHQATGCAAS LQSNRISYFF
     DLRGPSVTVD TACSSSLVAL HYAVQSLRSG ESKEALVAGC HLNIVPDIWV SMSMSQLFND
     EGKTFSFDER ATSGFARGEG SGVVILKPLD AALRDKDPVR AVVVHSGVNQ DGRTQGITLP
     NGQAQEELIR QVYKEANINP DECGFVEMHG TGTKAGDPIE AAAVHAALGK NRTPRNPLYI
     GSVKSNIGHL EGASGIIAII KAAMMLDREL MLPNAEFKKA NPNIPMSDWN MKVLTMTRPW
     PPRKKYLSVS NYGFGGTNAH AVLEKAPLSS KAPDRAVEDV EVDPKRKLFL ISANDKESLR
     TRIKDFGIYF EQHPEVFEKT LFGNFAYTLG NKMSQLSYRV GVSATSLDEL GIRLAQLNIN
     PSRVLGAPII SFVFTGQGAQ WAQMGVPLMH EYPVYELAIK RADQCLRDLG AEFSLVEELE
     KDATASDIDS PHLSQPACTA LQIALVNLLE SWGIRPGSVV GHSSGEISAA YAAGIYDLEG
     AMALAYWRGQ MTSLLKSSFP SLKGTMIAIG TSRETIQPIL KNLSGYATVA CVNSPTSVTV
     SGDISTISEL EKVVDNKQLF NRKLKIDVAY HSDHMKKVSK AYLAAIENIR HFSSAITPFF
     SSVFGRFAEP FELGPEYWIA NLTSPVLFSD ALGKIVADDE TRPSLLIEIG PHSTMKGPIM
     DTLKSLGPTV SKIAYTPTIL RKVNAAESIL DTAAAAYVRG ATLNMTAVNF PKTGAANRWF
     LSNLPRYPWQ HGTRYWHVAR IPQKHMVRDG ARNDVLGVLA NYSNDLEPTW RNIIRLDEVP
     YLRDHKMQGM VVYPLAGYLV MAIEAARRRA KQADIQISQF ELREVIVGSA FVLSDETDAE
     TTITLRPYAE GTRGSSDLWD EFRVCSWTSK RGWTEHCTGQ VRVRSDPKQQ AVVISSPFET
     QATYMKAQIS RIQKPATNYL DMSHMYQVLG DLGAGYGPIF QNIDNCYSSP HHSFGDLYVR
     NTRSVMPKGF ETPLTVHPSF LDGLLHFAWP LLGQGLGRMD LDTLYMPTVI KRMTVGLNVP
     TTAGEYLKGY CSGSPSLPSP EPTKFDLFAT QEGSTEPIIT IDGLVMTPLR DSDTNREETR
     KLCYKISWHP LAEAENAVEE DIQDRNGPAE SHGDTYIHGD TNTNGNTKHQ GNAHTNENPV
     KPKHDLCITY FGKSDGIADK LSIALSDESG WQVSVRNFGE VNFSQKHLVL LQTGASSLRY
     LTEDVFEGLK KALLNARTVL WVYRTDSPDA QMTVGLTRTL RSETSARIAT LGLVPDIKYP
     EKPIQAAISA LWPTDGTQPT KDLEFKAKGS ELFVQRIVED DSANSFIHNE THDMTISTQP
     FSQPGRRFKI QIGSQGSLDS LYFVDDNPLP LGDGQIELQV KANGLNFKDI VVSMGHLAQP
     YIGIECSGVV SSVGSNVKNF KVGQRVMAMP EGCFSTYARC AATSATEIPA DMSFEVAATV
     PVVFCTAYYS LFDLGHLQAG ERVLIHAGAG GVGQAAIMLA QMIGADIFTT IGSLDKKQFL
     MAQYGIPEDR IFYSRDTSFA RSIRRATGDV GVDVIVNSLA GELLRETWEC LAPFGRFVEI
     GKADITKNTR LDMQPFEHNV IFSSVDLTKV GKSKPQLMKR ILGDICRLIG DGSVHPVLPL
     SIYRISDIEK AFRTLQIGKS MGKIVVAPHE GDQVKAVAPK TSATLLRPDA SYILIGGTGG
     LGRSMAKWMS SKGAKNIVLV SRQAAINETV RTLIDTLAPL GVRIIVKACD VSSRESVKAL
     INEEMKDLPP IRGVIHGAMV LRDMLFENMS LEDFSAVACN KVEGAWNLHH ALINSPLDFF
     IALSSIAGII GNRGQAAYSA ANAFLDGFIE YRRSLGLSGT SIDLAAVSDV GYLADTDAQR
     RQEVMKNISC QTIDESEVLA LIAAALTGDL DRSCSGQCVT GLGLDSLENN FWVQDARFSV
     LYEAAKGTLG NSAQCNGPSV PLHVTLSTAP SKKEALRACY EALAAKLAQV LVLSLEDMDP
     SITVVSLGLD SLVAIEIRNW IAREANANVQ VLELLSSGSL MALAEIILNK SQAYTRTE
//

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