UniProt: F8QWT2

Database: UniProt
Entry: F8QWT2_9LECA

LinkDB:  F8QWT2_9LECA 
Original site:  F8QWT2_9LECA

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Ontology (5)   
   GO (5)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (42)   
   InterPro (23)   
   Pfam (9)   
   PROSITE (4)   
   SMART (6)   
All databases (48)   

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ID   F8QWT2_9LECA            Unreviewed;      2599 AA.
AC   F8QWT2;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Reducing type I polyketide synthase {ECO:0000313|EMBL:AEE65376.1};
GN   Name=PKS8 {ECO:0000313|EMBL:AEE65376.1};
OS   Peltigera membranacea.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC   OSLEUM clade; Lecanoromycetidae; Peltigerales; Peltigerineae;
OC   Peltigeraceae; Peltigera.
OX   NCBI_TaxID=161997 {ECO:0000313|EMBL:AEE65376.1};
RN   [1] {ECO:0000313|EMBL:AEE65376.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Gagunashvili A.N., Andresson O.S.;
RT   "Diversity of type I polyketide synthase genes in the lichen Peltigera
RT   membranacea.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; HM180411; AEE65376.1; -; Genomic_DNA.
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:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd05195; enoyl_red; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 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   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; 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; IPR013217; Methyltransf_12.
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; 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; IPR029063; SAM-dependent_MTases_sf.
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; PF13602; ADH_zinc_N_2; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF08242; Methyltransf_12; 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; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          27..452
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2516..2590
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2599 AA;  285826 MW;  9615142F395AF1C6 CRC64;
     MASNFMGIRS GSTYDSTCEL EKYPDALPSV AVVGLSIRFP DEATSLDSFW DMLIQARCAS
     REFPPDRINI DAFYHPNGEI SGSLPLRGGH FLSDDISTFD APFFSITPAE AEAMDPLQRK
     LLETAYTAFE NAGIGLEAAR GSNTSVHIGC FNIDYTSNHS RDPEQMHKYT GTGGAPSMLS
     NRLSWFFDLR GPSLTLDTAC SSSMVALDLA CQTLQSGQSD MGLVGGCNLI YSVDMTMALS
     KLGFLSHNSR CYSFDHRADG YARGEGFGVL ILKRVEDAIR DGDTIRGVIR STSSNQDGHT
     PGITMPSRDA QASLIRKTYQ QAGLDMQMTG YFEAHGTGTP VGDPIEASAI GSAFQYKRPG
     KGPLYVGAVK ANIGHLEGAS GIAGVIKTIL VLEKGVIPAN ANFEQTNPRI DSKSLNIEFP
     KANMIWSGDG LRRASINSFG FGGTNAHAVI DDAYNYLRMR SLPGNHCTVR RVIEPRSPNN
     VLELSSDSLY SFSSSCGVDS REENALPKLV VWSAADGVIL SDLATRYHSY FEKLSLKANT
     EAAFLENLTY TLNTRRTSLL WKSFVVADSL TQLKNRTLST PVQSKLKPRL AFIFTGQGAQ
     WYAMGRELLI YPVFKCSLLK SQRCLEGLGC DWLLLNELLK DSDESDINDP RLSQPLCTAL
     QIALVDLFRS IGIIPAAVTG HSSGEIAAAY CVGALHQQAA LKVAYYRGAL ASKLSNEGQI
     QQSMMSVGLS EEQIPQFLEK VAPGLNVSCI NSRKNVTLAG DEDHINSLKL LLEKDGIFAR
     KLNVRVAYHS PQMNKIAAEY SRCIEVLDKG DSAGSGNIGF ISSVTGQSVS AADLSKADYW
     VQNMVRPVQF KTAVETLCSR PTQALQKKLD GSHRKVILVH DLLEIGPHSA LQGPIRDILK
     ELTNCEGLSY SSALVRNRSA LETFMEAAGS LYCLGYPVRL EGVNVLREKL LDHRPVVLSN
     LPEYPFNHSQ THWYESRTSK NYRFRQNPPI CLLGTQVHDW NPFEARWKNV LRVAEIPWVS
     DHQVNGSIIF PAAGMLVMAI EAAKQLSDRH KIVGYEIKDA RFYAPINLSL NPAGVETELH
     LQRLRSASDK NNAWSQFRLY VCESEKWTET CKGEIQVQYE AGSTQVDGGL EANKMREILR
     QSQTKLSGCC TKVADARYVY SRLKAHGLDY GPAFQPLRRL RYGENVEAMA DLTLPFNAKN
     VIHPTTLDGM LQLTFVGLTK GGTDVIPTTV ATRINRLWLA SSGFLATPMA ESMQAFCKAE
     VTSNRTAEAW ICALSSVGQE PKIEIDGFEA TAITGPESSM QAEANAAKQI FYNVDWKPDV
     DLLDAQQLLR YCEKGRRHSE PDSDDFFHDL DFLLFSFIYS TYRQLNGVTI PVPHLQKYVQ
     WMELQINTFE TGSLVVNNRE WERLLQQSAY LEALTKRLEG SNKQGRYYVK VGENLQELLS
     GELSLLDLVG NGLLQDFYGD LPCFDMLAVY LDALAHKNPG LKVLEVEAGV GAITALILKT
     LISHGEQESG TPRYSQYDFT DSSISIFESA QKAVGAYPRT KFNYLDIESD PGTQAFELYS
     YDLIVAATVI HTAKDISTIL RNIRMLLKPG GKLILVEIVR PKSLRAGIAF GLFPGWYLGT
     DDYQSQDRCN AENTWHNVLK KTGFSGVDVE FRDFESNACH DFSILISTAN PATTSPAGFP
     PVLIIVDPES ERQQALAKGV KVCLEESGQH SCSVINFQEA ALTSNGLRDQ CCLLLEESGR
     SILRETNEET FNKLKGVLMN SNSVLWVTEH QRLKSPDFGM VQGLSRVLRT EHTKLTISTL
     ALDLHGSIDK GVEKIEKVLS AMVLNQKDRC HEPEYIEKDG LLQISRLIEA KDLNQDIFLK
     TCPQQSRFQH FKEGPALKLS IRAPGLLDTF EFREDTSFGT PLTPGEIEVE VRAVGLNFLD
     CLAALGRVNA KSLGSECAGI VTRIGDTCQL RPGDRVSVCS FDVFGTYARV MEDCAIKIPD
     TISFVVAAAV PTTFTTVYYG LCEVARMQKG ETILIHAGAG GTGQAAIQLA QNAGLEIFTT
     VGSNEKKKLL IDRYGLEPNN ILYSRDLSFA QGIKRLTSGR GVDIILNSLA GEGLVASWEC
     IAPYGRFIEI GKKDIYSHGK LPMFPFAANV SFSAIDLAFK PQNRPPVIRR SFENAMILLN
     EGKMRPAHPL NVFGLAEIEK AFRYLQSGKH SGKIVIDYYL EDKVPMIVEP KPPYSFEAGA
     TYLISGGLGG LGRSIARWMV NRGAKNLLLL SRSGPNLDKS RILVEELRRS GARIEAPRCD
     VADAISLERV LKSCEKTMPP IRGCIQGSMV LRDATFETMS PESWNACIAP KVQGSWNLHM
     LLPKGLQFFI LLSSVSGVFG NGGQANYAAG NAYQDALARC RVAQGEKATA LDIGALLSEG
     YLAENDSALN RSIRTGILPP MSQAELFSLL DHYCDPGFKA PFSELKCQSI TGIEIPANIQ
     AMGIETPYWI HQPLFRHLHQ IRPSIGTYIS SGTTVNLRQD FESSFAAVGS LTEAGTIISE
     ALSQKLSKIL GVPVERIDPS RSMGSYGVDS LVAVELRNWF AKEVSAEVAI FEILGEPSIA
     SLAVAVAGKS QYRLPTWTG
//

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