ID A0A135UQS0_9PEZI Unreviewed; 2589 AA.
AC A0A135UQS0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Beta-ketoacyl synthase domain-containing protein {ECO:0000313|EMBL:KXH62741.1};
GN ORFNames=CNYM01_02499 {ECO:0000313|EMBL:KXH62741.1};
OS Colletotrichum nymphaeae SA-01.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1460502 {ECO:0000313|EMBL:KXH62741.1, ECO:0000313|Proteomes:UP000070054};
RN [1] {ECO:0000313|EMBL:KXH62741.1, ECO:0000313|Proteomes:UP000070054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA-01 {ECO:0000313|EMBL:KXH62741.1,
RC ECO:0000313|Proteomes:UP000070054};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum nymphaeae SA-01.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:KXH62741.1}.
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DR EMBL; JEMN01000269; KXH62741.1; -; Genomic_DNA.
DR Proteomes; UP000070054; Unassembled WGS sequence.
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; 2.
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; 3.
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; IPR013149; ADH-like_C.
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; 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; 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; PF00107; ADH_zinc_N; 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; 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; 3.
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 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 2..426
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2504..2581
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2589 AA; 282885 MW; 47C8ECE719D873EE CRC64;
MGDPIAIVGL SARLPGDGDT PERFYESLLA GRSARTEVPR ERYNAEAFWH PDADRSGATR
VRHGHFLKGS ISAFDAPFFS ITPTEARSID PQQRGMLESV YKALENAGIP LDTVAGTQTG
VYVGCFTADY NDHIAKDLDI PNKYSALGTV ASMLSNRVSW FFDFRGPSVT VDTACSSSLV
AVHEACMSLK LREVNMAVVG GCNLILTPEM TLKLDAAGVL GPDGKSYSFD HRANGYSRGE
GFGALVLKRV SDAIRDGDVI RAVIRNSSTN QDGRSPGITQ PTKRGQVALI KHVYERANLD
PSLTRFAEAH GTGTPVGDPI EASALAEIFA PHRSADEPLY VGALKSNVGH LEGAAGVAAV
IKGVLTLESG VIPGNIWFEK RNPKIQDEWN LRFPTKPTAW PQRGLRRMSV NSFGVGGSNA
HVVMDDALHF LKSFRLVGNH RTETIPKIPR QLDAPLVNGT GRVNGFHRPS DSGIHLDDFD
TEDAPRLFVL SANDQDAVSR LRDGYRDYLA TKAAQIVGES AQLRFLRDLS YTLACRRTRH
SWRTFSIASS PVQLEKSLEG NAATPIRAKT NPRLAFVFTG QGAQWATMGM DLLAYRAFQE
SLLAADRYLN DLGCNWSLTF ELSKSKTSSR INDPEFCQPI CTALQVAMVD LLSTWDVYPH
AITGHSSGEV AAAYAAGAIS RQAAWKIAYF RGKLSAKLAR SACRPSTGMA AVGLSKAATQ
EAIDRVNQQL GGEGTLEIAC MNSVDSHTVS GDAEKIDALV QLLSAEKVFA RKLNVEIAYH
SQYMRAMADE YLVAMGDLQQ GTLRSSVKPR FYSSTMGVPI LPSQLRRPEY WVKNLVSPVR
FTESVTEMLK GFETPKINGH VDGHVNGLVN GYVDGYVNGV VNGDCDEEFP FEPITDFLEI
GPHSALKGPL FSTVKQVRGN AKVDYHSLLV RQKPGIETAL ESVGTLFCHG HNVNLAQVND
ADEPHGPKPL MLTNLPSYPF DHSKEYWVQN TLSDDYRKRP VGRHELLGAP MAGFNENNAV
WRNYIRLSEN PWIEDHKVSG DILYPAAGML VMAIEASRQI ADKSKVLKGF RLRDVSFKLA
LRVPEDANGV ESQFYLRQHR ENSHSAVSTW REFQLWTLQD GAWREHCHGF VQTEYESDDQ
LALRGFEESI HDGCGTDVSV DKLYRSFADS GLNFGPTFQT LSDIRLGQDL NMVATLHPPV
DKIEKSMPHQ YVQPHLVHPA TLDGLVHANL VALVSSSKYA GATRVPTYLA DGWISAQLSQ
SHNAYSVSAE SRVKGRSEVV SDVRATHLEQ GDEMVQMSGL VFKTISSGPS KENSQAMVHP
AFNISWKPDP SFLTKQQASQ LFQLPLTQKD DPSIWMLDCE ALCLAYMRRC VESLTQESIG
KMTWYHQRYV KWFQHVARQH SDGPASESIE ELEAQVLAGN ASEGKLIIAV GQALSGILTG
DRDPLDVIFK DKLAEDVYSN GLGSKRCYAQ LCSYLDIMAH KNPNMEILEI GAGTGGATRP
AMATLTRDSG RRYGHYDFTD ISPSFFEQAK ENFKDEVGRM GFRVLNVEND PLSQGFEAGK
YDLIIAANVL HATKKIDETL VNARKLLKPG GKLLLFEITN TDILLGSFCF GTLHGWWLSE
DKDRVWGPLM SPNAWDTHLR ASGFSGLDAV FDDFALSPHQ MSSILVSSNP SSEIVACSPS
SYYILTSESP TQNELAAQVV QSIGKGGGCE IATITSLADK SLANATCVVL SELDHAALKD
MNEETFNGFK RVLTKSKNIL WVTRGGTSTA PDPDSELVTG LARVVRSERP DVNFLTLSFE
QNADEELIAA SCVQVLEAAQ DSVENSFRVI DDVVHVSRLV QADYMTDHIQ NQTGVVSIEN
KLLKDEASRS LCLQVGDVGQ LDSLRFEADA LTDTPLRDHD VEFKAMACGV STSDVSSVLG
KAEESPLGLE ASGIVTESGP ASRFQVGDKV FGLTVSGTLK THVRSTDGLL AKLPDGVSFT
DGAVLPVDYT TAYAILCEVG SIREGDSVMV HGGCSSIGKA FVQVAQLQGA EVYTIVTNQS
ERDELVKECS IPEDHVFSSR DLSMRSTLQK LVKGRGMNVL VTATDDLVDG VIDCIAPFGR
IVYIGSGAGI SNTRVPRGRN IRLESFDLTS CLAFDLTRTE TMFQHMVDTV FANWKNISRP
SPTAIYSFSQ VGDAFRRMQS EDQDTAKVVL EPRDDDMIPV VPSRKSLSSF DPDASYVIAG
GLGGLGRSVA RWMASRGAKN LVLLSRRGAV EKAAIELVAE LEAVCDHVVT PACDVTDAGA
LQTLMSELAT ALPPIKGCIQ GSMVLQDNLL ENMSLDNWKA AVQPKVQASW NLYNALGDKM
DFFVFLSSTV GVTGSPEQAN YAAGGTFQDA FAHHLVSKGV NAVSIDLPII RGVGYVAEKP
ELWDYLSSAG WTHITADELY AVLDYHCRPA KASTSQETTG AQVIPRLWLP QETAAEGYQT
QTWGEDPLFS HLRLTETDDA EKGEDANKGI NHKAHLQCAS SLEEAEKIVL DALLLKIARM
LSIDALNLET SKPLHAYGID SLTAVELRSW LMKELGAEVS VFDITNNSSI AQLAVLATKK
SSLRQRFAD
//
