ID N4V3N5_COLOR Unreviewed; 2321 AA.
AC N4V3N5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Reducing polyketide synthase FUB1 {ECO:0000313|EMBL:TDZ22788.1};
GN Name=FUB1-1 {ECO:0000313|EMBL:TDZ22788.1};
GN ORFNames=Cob_v004449 {ECO:0000313|EMBL:TDZ22788.1};
OS Colletotrichum orbiculare (strain 104-T / ATCC 96160 / CBS 514.97 / LARS
OS 414 / MAFF 240422) (Cucumber anthracnose fungus) (Colletotrichum
OS lagenarium).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum orbiculare species complex.
OX NCBI_TaxID=1213857 {ECO:0000313|EMBL:TDZ22788.1, ECO:0000313|Proteomes:UP000014480};
RN [1] {ECO:0000313|Proteomes:UP000014480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC {ECO:0000313|Proteomes:UP000014480};
RX PubMed=23252678; DOI=10.1111/nph.12085;
RA Gan P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA Takano Y., Kubo Y., Shirasu K.;
RT "Comparative genomic and transcriptomic analyses reveal the hemibiotrophic
RT stage shift of Colletotrichum fungi.";
RL New Phytol. 197:1236-1249(2013).
RN [2] {ECO:0000313|Proteomes:UP000014480}
RP GENOME REANNOTATION.
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC {ECO:0000313|Proteomes:UP000014480};
RX PubMed=30893003; DOI=10.1094/MPMI-12-18-0352-A;
RA Gan P., Tsushima A., Narusaka M., Narusaka Y., Takano Y., Kubo Y.,
RA Shirasu K.;
RT "Genome sequence resources for four phytopathogenic fungi from the
RT Colletotrichum orbiculare species complex.";
RL Mol. Plant Microbe Interact. 32:1088-1090(2019).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TDZ22788.1}.
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DR EMBL; AMCV02000009; TDZ22788.1; -; Genomic_DNA.
DR STRING; 1213857.N4V3N5; -.
DR EnsemblFungi; ENH76955; ENH76955; Cob_01763.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000014480; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 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; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
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; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; 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; 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 SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000014480}.
FT DOMAIN 1..426
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 2321 AA; 252752 MW; 2EF7C040F562117A CRC64;
MEAIAVIGMA CRFPGSAISP EKLWKMMVNK ESAWTEFPKD RLNINGYYHP SGDRQGSISF
KGAHFLRQDV AAFDASFFSV MAEDAKAMDP QQRLLLEVSY EALENAGLPI EGLRGTPTAV
YVGSFVKDYE QICLRDMDWQ PQYAATGTGN AIMSNRISYT YDFKGPSMTI DTGCSGSLVA
VHLAAQALRS GDCSLALAAG AGMILTPNTM MPMTALNFLS PDGKCFAFDS RANGYGRGEG
IGFVVLKRLS DAVKDNDTIR AVIRGTHVNQ DGSTPGITLP SKEAQVANIR HLYSKHGLDM
HRTAFVECHG TGTQAGDTRE LKAISETLSV GRHCDNPVLV GSVKTNIGHL EGAAGIAGLI
KGVLIIEKGE IPPNINFEKG NPDIKFEDWG VKVPTDLTQW PLEGPRRVSI NCFGFGGTNA
HVVIDELSSH LSDHRNPRLQ EPDLLGDTSG WDAPERRPQL FLFSSHERNG VSRVMKAHLN
HINDRPDFLK TGIDDYAYTL ACRRSVLEWR GFAVARDADG LKSSLEAAVS ASLLRSNVRR
EPKVAFVFCG QGAQWVRMGH ELMCFQPFKN SLESAANYIR TLGGGFDLVR EIMEPESTSR
IQDPVISQPA TTAIQMALVD LLRCCKVTPS STIGHSSGEI AAAYASGCIN SETALTLAYY
RGQSASLLSN SGSRFQGGMC AVKLSLDEAR QYLRLAGDEK DLQIACINSP TSVTISGSVQ
DIIAMRDEMK TSNILCKILD VQLAYHSRHM NLIKEKYEGL IAGIISVDSP TGIRFFSTVC
GGELRGRSLG PSYWTQNLVS PVQFWGAVEA LIDSENRPDV FVEISPQVVL ESAITEIVSS
VPAGPTSRYT ALMRRGRSSV VTFLETVGHL WSSGYQVDMI QVLSRGHTKK SFSTLVDLPS
YPWNHSNTFW HESHTCTEHR FRNHGRQDLI GSPSPDATTF EPRWRGFFRI SENPWIQDHR
VQQTIVYPAA GMVAMAIEAA SQMAENMSDI LGFQVINLHI ERAMVIAPTS HGLEYSLNLK
QVPSRPQEEP EWDFSLYSKQ EGGAWLRHAD GQVKIRKSTE AHALHAARHS DKYSELEALC
GKTLLARQLY ETLDVVGLNY GPCFQNVSSV STHGTSCISK IRIPDTKSKM PANFEYPHVI
HPATLDSMFH PLFAIDAKPM VPSTIESVFV SAGIPKGAGH EFVGYALARR RGICDATASI
YMAPGPEDLG SPSVVIEGLQ LSALSASPMD DGKFLPNHRN LCSEIIWKED YVTSKTDDLS
QLLSLMAHKY PLLAILQCGG SEQLARYILE ILSAGGPPRL ARYTVTDDQT LSAIQTSFTT
SPVLNLLEKR EWPTTSKQAF PRYNLIIIAQ DSGNNSRDAC QYLLREGLVL EEISLPTAVG
RLQRPSNAFR QNTSHSRAIA ASYRLQSENM ANDCVSEQHF EGHMFSDHLD MTSAPEVCVI
VPTTTISALD NLCSSLINIL SKQGFSVSVE TFATAEPSNK ACVSLVEVCD NFVSNWTEEQ
FQSFRNLQNE ARSVLWVTRA ANRRPSDPRN APIIALARTI LSEDSRKTIV TLDVDANTPL
ESALLPDVIF EVLAATLSGS HETELAEEGG KLYIPRLMPL DELNRLVESE SSLEIHQQPV
CHVDNAETYY EMVLSKPGLA DDCFHFCATP FSGELGSHEV EIRTSTAVLR EEDLKTALGL
NAEGRLGLDI CGFVTNVGSQ VEDFRPGDQV CAIVPGAFKT VHRIDLGFVK HSKPAQRHQY
TPSIFITAFY AMCHAGYLSR NKKVLIHAGA SSYGQAAVRI AGVLEAEVFA TVLGDATGTQ
RKQLVEVCGL PRDHILDADS DMFFADLIAI GKFDVIFNIT KDHAVTSSKC VKASGRIIQL
VDKTNRASII PTSAMTCVKL DIGLLLEEDP ELVKALFTAV DEFVSTFLRS DSDLQCEPVH
NFALSSLSAA YKHLRRHPHF GLVVMTVDQE TRVPVARELS LNPLAGVIDP LGTYILAGGL
GGLGRSIASL LAVNGARRLV FLSRSRGGPN AEAFLDGLRA EGVDARAVCV DITDREALHP
HRLSLGKISG VVQCAAVIKD ALFETMTYSE WTTVFGPKAI GAINLVEVFG SRSAGPATCA
DDADDADSKV LAGPWFIFLS SASGVIGNRG QANYAAGNAV QDALARSTPR ACSLDLGPVL
EAGMLAQNDE TLNKLRGAGF YGIRHQDFLK MVSYAIAGEI GPGIPLPAQI ISGVGTGGLI
RQNNPGDPFW SRTSLYSYMN IVDVPVTAPD LEAITRPGQE NNRVKEMLAV CTGPDEAANV
ICAGLVQLMA KAMTLLPEEI DPGRRPSAYG VDSLVAVGVR N
//
