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Database: UniProt
Entry: L2GBM7_COLFN
LinkDB: L2GBM7_COLFN
Original site: L2GBM7_COLFN 
ID   L2GBM7_COLFN            Unreviewed;      2319 AA.
AC   L2GBM7;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Pksn polyketide synthase for alternapyrone biosynthesis {ECO:0000313|EMBL:ELA36002.1};
GN   ORFNames=CGGC5_4358 {ECO:0000313|EMBL:ELA36002.1};
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:ELA36002.1};
RN   [1] {ECO:0000313|EMBL:ELA36002.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Nara gc5 {ECO:0000313|EMBL:ELA36002.1};
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; KB020535; ELA36002.1; -; Genomic_DNA.
DR   RefSeq; XP_007274880.1; XM_007274818.1.
DR   STRING; 1213859.L2GBM7; -.
DR   EnsemblFungi; ELA36002; ELA36002; CGGC5_4358.
DR   HOGENOM; CLU_000022_31_0_1; -.
DR   OrthoDB; 2440513at2759; -.
DR   GO; GO:0016746; F:acyltransferase 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:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
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   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; 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; 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; 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; 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; 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; 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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..211
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2232..2309
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2319 AA;  254441 MW;  F03FD511385F216B CRC64;
     MVSPDGISHS FDSSANGYGR GEGMAGVVVK RLSTAIADGD VIRAVIRATG VNSDGKTPGI
     TVPSEEAQAD LIREVYERSG LDMAQTSYFE AHGTGTPKGD PIEIRAIGST IGAARRASGM
     GRLDVGSVKP NIGHTEGCAG LAGLIKTVLC LEAGLIPPIA GLQQINPEIA AENHLINFPM
     ATKSWPGSGL RRASVNSFGF GGANAHLVLD DARSYLKEMR IKGRHITKKA GYRNQDSTDQ
     SFDTSENMRQ LLFAISSFDR QGLGRTAQSL GEFLSQKKPV QFESLAHTLN VRRTSHLFRS
     FVTAKSQEEL VSTLLSVNKE KAQPLKIRSS RSRRLVFLFT GQGAQRPGMA KELVRECPTF
     RNSIATSQTY LSNLGCRWDL IDLLKNGDAE TISDPEFSQP MCTAVQIALV HVLWYWGVTA
     AAVVGHSSGE MVAAYAAGAV SHEEAMRVAY YRGLLSTQVS RRLGRPGAML AVGLSEKSCR
     EFLQRHDFAN TVTVACINSP QGVTLSGDAQ SISRVEASLK DAGHFARLLR TGGVAYHSPD
     MQIVGEDFLK ALGPLKLRHR PLSVAMFSSV TESLILDAAE LNANYWYTNM TSSVRFSGAL
     HNLLLHEGQD GLSPSIHNTT VLEIGPSKTL AGPVGQIMAA AFDSKITTGL SYLSILSAGE
     DSRDTSLAAA GMLWAMGQAV DLDKVNNLSS RCDKLKLNEL PILPSYPWNH SRSYWHKTSP
     NSTALGALTV PRADLLGVPT APQNPFEPSW QNVLRQDELP WLEDHAVMGA VLFPAAGYLV
     IAMEALRTLA RKKNYPLYGV ELLDVQFETG LTLEDHESAL ESTNRGQGIR LTLKPRAMDE
     WEYDFTIYAT SSSPEEWRRL VRGTVVGIRN TNVLRQKEDD FETSSRKVEW HSVKRPQLLE
     VQRSSIDVVD PANFYTNLSA IGLKYGPTFQ GLNVIRCTPA TTACRVGKAY GELMVPDTQS
     TMPGAYECEY LIHPATLDGI FQLVFAALKA ICPGGMKDAA VPVSLRRAFI ASSMPRNVHS
     KLIGVADAEY DGDAKASQSA PREIIGSLVF SDGTLEEPAV MIDGIVLREL PVGSGYEAVM
     DSKSDARENR IERTAQFLWK EDIDQDFDLW KDLILSKTTR LDRCSFFLDR FYHKRPNANA
     VCIGSTELHE RLLQPAVNYS GTRRTHPLNR CTLVTSLEKW SAVIGVSSSS TLENPTTEKF
     DLILLDENML AEEDLHDDPQ RSSDWFFKTL SKGCAAGAWF VLLGGDEKSV LPMSQIMSGV
     GTRSKIKGIR ISEASVDIYC IGDELVSIHP RIKALQEQAL QADDVVKEGF RHTDIIILEQ
     DYSRNTRAAC NITAPLLNRL ASTGFRISRA TLRQAIALRD QFKDKMIISL LELGQPFVYD
     WGHQDFADFQ QLVDSASHIL WLTTGGLLCP YSERSLLYSP TVGLLRALRA EYPQLVLVHL
     DVSEATCSDT PEAIVEVISE TLRLSRVSEE TSYSLETHFE IYESEYIEQS GCLLIPRIMA
     HTEADNYVLS ETSSQDGNPL LPTFRGSFNH LESVRLQSPH LWSQTIAESR LGYWVLPERA
     TENTRENSPL MGLQKRTSAI IRASHFTVKP GTCPRLQMEN GFEVPMAFHT LGVITGLNEV
     HSSRTDYRTG DWVLNTTPQP IQPESMHDVR KLVKLPKSVA KAPAAAAYWL GPISTAYQVL
     SVIGSVSQGD YVVIDVGESQ TLERAFAMVA HHLRARKALI IGRGRLTEQV DKDAHSDGPE
     DVIISRISCL NRATIRYLQS LANGVKAVVS TTRTKETLDM LISTLSSDGC LIQLDPRGQE
     DCLDNRCPKS SQIFKFDLQL WDHSASEEYR MAISRVSTWV ETGTLTLPDA LRQASTSNAN
     DLAMIFESTT HGTEQEDAKI AVSLGHSDEV LMHRKMPASP PGKIDNATML DSNATYIISG
     GLGSLGLHMA NMLYELGARH LMLLSRSGKA NSSDIMAALM NLERNGCNVD VVACDITSME
     DMKRLGSKFS EESRPRLKGI IQSAMVLADS TFANMTFENW QKATAPKIQG SWNLHNLQRF
     MTEGSSSSEN DVEDLDFFIL LSSVSGVIGN SAQGNYCAGN TFEDVLAHHR RANGMAAVSL
     NIGLVSDSNH FGTGTMSSFK NIDEYLRVFG HLAPVVVSTA EVLASVKMAI AASNKQNTAL
     TSCPLQIPPQ LVVGISSRIR RSRELLNYWS LDRKFDHRAA WGDDAGWEGD LAPKASLLRA
     NEALPLAQDL SSGRLVVEDL LKAKLAQAMT LDVEGVDEEK SLGSYGIDSL KATEMRNWIN
     REFHVDLSIF EILAPTPIAK LAMRILKACD LVNHDALGS
//
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