ID E3Q7C5_COLGM Unreviewed; 2319 AA.
AC E3Q7C5;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Beta-ketoacyl synthase domain-containing protein {ECO:0000313|EMBL:EFQ26763.1};
GN ORFNames=GLRG_02583 {ECO:0000313|EMBL:EFQ26763.1};
OS Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS anthracnose fungus) (Glomerella graminicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN [1] {ECO:0000313|Proteomes:UP000008782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG697335; EFQ26763.1; -; Genomic_DNA.
DR RefSeq; XP_008090783.1; XM_008092592.1.
DR STRING; 645133.E3Q7C5; -.
DR EnsemblFungi; EFQ26763; EFQ26763; GLRG_02583.
DR GeneID; 24407948; -.
DR VEuPathDB; FungiDB:GLRG_02583; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000008782; 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; 3.
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:UP000008782}.
FT DOMAIN 1..426
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 2319 AA; 251091 MW; 229E8452318DFB39 CRC64;
MEDIAIIGMA CRFPGNATSP EKLWQMMVQK ESAWSEFPKD RLNIDGYYHP SGDRQGSISF
RGAHFIKDDI AAFDASFFSV MAEDAKAIDP QQRFLLEVSY EALENAGLRM EDLRGSPTAV
YVGSFVKDYE QICLRDMDWQ PQYAATGTGN AIMSNRVSYT YDFKGPSMTI DTGCSGSLVA
VHLAAQALRA GDCSLALAAG AGLILTPNTM MPMTALNFLS PDGKCFAFDA RANGYGRGEG
IGFVVLKKLS DAVRDNDTIR AVIRGTHVNQ DGLTTGITLP SKEAQVANIR ALYAKHDLDM
KQTAFVECHG TGTQAGDFRE LKAISETLAE GRTTENPVFV GSVKTNIGHL EGAAGVSGLI
KGVLTTEKGR IPPNINFERG NPDIDFRNWK VKVPTDLTEW PVDGIRRVSV NCFGFGGTNA
HAVLDDAAVY LAERGMTANH NSSLDSTQSR QPGAVSEAHG PFLTPKLFVF SSNERKGVSR
LMETHLGHIT GLTDMTEIDA DNYAYTLGCR RSIMEWKSFA VARSVADLTS KLQSSDETSF
LRSGRESKPK LGFVFCGQGA QWAQMGLELM CFDAFKSSMT AASRHLKTLG SELDLVEELA
KAKTESRIQD PQISQPATTA VQVALVDLLR ACNITPSSVV GHSSGEIAAA YASTAITREA
AWALAYYRGR SASLLSTVAP YLKGAMCAAR MTNAEARQYI ESHDKDSGLQ VACVNSPNSV
TISGNRCDVL RMRDELKSRQ VLCKVLDVDV AYHSRHMRLV EGSYKDCIQT VLSNDASENI
PFFSSVRGEM LPHSLLDPSY WVQNLVSPVQ FVAAVKAMMT SDSRPDILVE LSPHATLESA
LAETISELGP GSQATYLSLI RRDKDSAVTT LQTIGEIWAR GHPVDMLKVC SKGADAQAYK
TLVNLPSYPW NHSKVFWHES HTCTEHRFRN FGRQDLIGSP SPDATTFEPR WRGFFRISEN
PWIQDHRVQK AIVYPAAGMV TMALEAASQL ACGTTDVLGF HLTGLRIERA MIIPSSAYGL
EYSLNLKQLP AKAEADPEWE FTIYSKPEDG PWIRHADGSI KIRRQSEALL TTSEHAHRYT
QIQGLCDKSL PPRQLYELLD VVGLNYGPCF QNVVSISTHE NACISKVRVP DTKSKMPAGF
EFPHVIHPAT LDAMFQTLFA IDSKPMVPSS IESIFVSAQI PHGAGHEFTG FATAERHGLR
GAVGSIVMAS DESNWGKPLV VVDGLKFTSL STPSIDDGGF IPNHGNLCSE VVWREDYTRA
VTEDFYDMLS LMAHKYPSLS VLQCGGSMQL AQTILDILPE GVAPNLSRYT ITDPDILGEA
QKAYEKSPVA TLLEHRNWPN VKDHTARYNL IIVARDAGID LGEAGNILQP EGVILNETTP
PMTPTSTDSM LEVELVFDDP TTLQMSCDAE PDNVIHCDTL DQHFEASVYV DKPKAASSPG
VLIIMPDAFG SAVEELAKSL SDLLLQRDFK VSIGTLHGCD PKGKACIALL EACDSFVYGW
TEGQFRSFHS LQEQASSLLW VTRGANRRPT NPRNAPIIAL ARTILSEDPQ KTIVTLDLDE
NTCLASCALP QTVEWVLDSM LSGSAEAEFA EEGGRLYIPR LMPLQELNKM IESDSNVEIV
QQPIFNQPIA QAEYEMTISQ PGIDNDNFHF VESSQASQLG PYEVEIQTLS AALHLNDLHT
AMGRTSGDRL GLDVLGIVKN IGSQVIDFRR GEQVLALVPG AFKTVHRVDQ GFVKPAPPPV
ECCQYTPSAL IAAYYTLCTV GRLTPRKKVL VHAGASSYGQ AAIRVAAFFG AEVFATVMGE
NSKAQHATLI DAHRIPEDHI FDATGESFVA DVSRFGKVDV LYNPTQEHTA ASFKCVKPSG
CVVQLADRTG GALSVPVSAA AYIKLDLGLL VEEDPDLVKD LFSIVDRFAF DYLRASSSLQ
CQPVHRFPMS ALEDAFKQLE RDPHHGLTIV EANQDTLVHV ARAVRTKSLA DAINPEGTYV
LAGGLGGLGR SITKLLADNG AKKLVFLSRS GGGAEANTFF ESLCGVDAKA IAVDITDRKA
LEALVPDLGK VSGVVQCAAV IKDALFEKMS HADWVTAFGP KAVGAINLTE VFGRGPSAAA
GDLVGSSDPR GPWFLFLSSA SGIIGNRGQA NYAAANAVQD ILARSLPRAV SLDLGPVLEA
GMLVEDEETL SKLRGAGFYG IRHRDFLTMV ERAITGEVAP GVATPAQIVS GVGTGGLIRQ
NNPGDPFWSR SAMYSYMNTV DMPVASPEEA TGGGGVPSEA DIKRMLAVCS GAEAAAAVVC
AGLVQLMAKA MTLLPEEIDP ERAPSAYGVD SLVAVGVRN
//
