ID L2FIN9_COLFN Unreviewed; 1796 AA.
AC L2FIN9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:ELA25891.1};
DE Flags: Fragment;
GN ORFNames=CGGC5_1818 {ECO:0000313|EMBL:ELA25891.1};
OS Colletotrichum fructicola (strain Nara gc5) (Anthracnose fungus)
OS (Colletotrichum gloeosporioides (strain Nara gc5)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1213859 {ECO:0000313|EMBL:ELA25891.1};
RN [1] {ECO:0000313|EMBL:ELA25891.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Nara gc5 {ECO:0000313|EMBL:ELA25891.1};
RA Gan P.H.P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA Takano Y., Kubo Y., Shirasu K.;
RT "Genome analysis of Colletotrichum orbiculare and Colletotrichum
RT fructicola.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KB021102; ELA25891.1; -; Genomic_DNA.
DR RefSeq; XP_007285078.1; XM_007285016.1.
DR STRING; 1213859.L2FIN9; -.
DR EnsemblFungi; ELA25891; ELA25891; CGGC5_1818.
DR HOGENOM; CLU_000022_31_1_1; -.
DR OrthoDB; 2464658at2759; -.
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; -; 2.
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; 2.
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; 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; IPR013968; PKS_KR.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF54; SYNTHASE, PUTATIVE (JCVI)-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 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; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 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}.
FT DOMAIN 1..412
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT NON_TER 1796
FT /evidence="ECO:0000313|EMBL:ELA25891.1"
SQ SEQUENCE 1796 AA; 194352 MW; BB3DECEC42EFC54F CRC64;
MGWLIGRAGA AAAAATKKGL PAATGRFDAT GFQSDTPAKN TLQALQAYLL NHVSMGDFDP
SFFPVGAKEA SRMDPMQRQL LEVAYECAEN AGAARNLFGG NTSITTTCGV GTGTKETASD
LAARKDVGVF VGVFGEDWLQ ENVMDSQLAG LYRGTGFLDF LQANRVSFAM DWQGPSIVVK
TGCSASLVAL DMACHSLRAG ECAAAVVLGV NLITSPLMTL LYTAQGLLSP SGCCKTFDAA
ANAGDPIRAV VRASATGHDG RKVGQLKPDA AAQELLIRKT YALAGIPDSQ FGDTAWIECH
GTGTAVGDPI EMRSVANVFG RDGIVVGSVK PNVGHSEGAA GLTALIKAVL SLEHGVIPPN
IFFNTPNPLI TWQAAKLRVP VDPLPWPDGR KKRVSVNSFG VGGSNAHVIV EDGRPSKSLV
PRAPTEAARV LLLSSATHPW SLQKQVLNHR NYLLERLPAS RHDLSSLLHD LAYTLGCRRH
HFPLRTYTVV RVQREPENDY EDETKAAESG LLSFGDAGHS GQVQDKTPPP RVAFVFTGQG
AQSARMGYEL LRDNNVFADS IRYLDQCLKT LPKALAPKWT LFEELSKPAP DSLVEETRYS
LPYCTAVQIG LVNMFRAWGV LPAAVVGHSS GEVASAYAAG VLSARKAIII AYLRGMPGMM
ATIGLGAMQA EKFLSPGAVV ACHNSPSNTT ISGDADAVQE TLRKVAEVDP RIRCHALRVR
TAFHSHHIGP SALRYEELLR PILDGVETGS RPLDSPPLYS SVSGSLEADA AKLVGSAQYW
RDSLEKPVMF RQALEQLVKR EHDNNPLLLL EIGPHPALKK PIGETLSALE ASSSSLSTTS
EPQASHIATL RRGERSDEAM LRTVGELFVR GALTEANMQS IFRPDGSASP APHCLTDLPP
YAWHHGTQYL DPPRVASVYK SARHLPHELL GARVPDATDI EPCXXXXXXX XXXXXXXXXG
QGVFPAAGFV AMAGEAVHRL GPGHVADKSY VMRNVSIRSP LVVPQGSTFE LFTRFSQAQH
QDQDSGDGAI EDNCPESTWY DFHIMALVPD RDGDQWTSHC RGLWYSIADS VGLSYGPSLQ
GLQDITASTS RLLASASVYD YDEDEDEAGY ALHPAVLDMG LQLNLVAMCQ GLGEKCDLLL
LPTYIEEISV EADTTRLLQN RGNSPQARDG RLKMRAEVSW VRKGRSLQGT VTATANGDES
SHNDNILPRL SMRNVKFMAK PPRARRTPQD APLATTQPHL ASVFEWAPDA ELVNMDMVDS
VVGMARLLSF KNPRVRVCVF ARDGDVALVS AVMRALETQA MSNGNVLASL TYAAATTAEL
GLAQLSLQEG EQYHVKFAPT WLDMSKILPA QLENHSGFDL VLVDGPAALT RLCSISSSYE
SPLPVNPGGW FLVDRYSGEA KTETETDRKL GQLGFTLVRR HSPSSDSTNK GFHAARALLP
GHRKYAGSRQ RRVVIILATP ALEELARSLQ SVLEESDLRS EIRVCHSGGE PLSSYDDDNE
QTVIVSMLHL EQSPAEEALT AKSFRSYIDS LLAARQPRVW LLPPLQLSST GPASLCHWPD
PAWLIGLTRT ARTENPALDF TTIELDRVNT PVRMAADAVA RIIERLTQLG PELEPEILQH
DRPDMDRELG VTPDGTVLIP RMTWSSLDDA ASSVEAETAD HSGGPGLVSF REDASYLLVG
GLGGLGRSVC RWMAARGARQ LVLXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
XRPVAPADHS APRGLAGVFH MPMVLRDRPL TDMTWDDWTA VVDPKVRGAW NLHNTL
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