SORA_HYPJQ
ID SORA_HYPJQ Reviewed; 2567 AA.
AC G0R6S8;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Highly reducing polyketide synthase sor1 {ECO:0000303|PubMed:29104566};
DE Short=HR-PKS sor1 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:29104566};
DE AltName: Full=Sorbicillinoid biosynthetic cluster protein 1 {ECO:0000303|PubMed:29104566};
GN Name=sor1 {ECO:0000303|PubMed:29104566}; ORFNames=TRIREDRAFT_73618;
OS Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=431241;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QM6a;
RX PubMed=18454138; DOI=10.1038/nbt1403;
RA Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT reesei (syn. Hypocrea jecorina).";
RL Nat. Biotechnol. 26:553-560(2008).
RN [2]
RP IDENTIFICATION.
RX PubMed=28010735; DOI=10.1186/s12862-016-0834-6;
RA Druzhinina I.S., Kubicek E.M., Kubicek C.P.;
RT "Several steps of lateral gene transfer followed by events of 'birth-and-
RT death' evolution shaped a fungal sorbicillinoid biosynthetic gene
RT cluster.";
RL BMC Evol. Biol. 16:269-269(2016).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29104566; DOI=10.3389/fmicb.2017.02037;
RA Derntl C., Guzman-Chavez F., Mello-de-Sousa T.M., Busse H.J.,
RA Driessen A.J.M., Mach R.L., Mach-Aigner A.R.;
RT "In vivo study of the sorbicillinoid gene cluster in Trichoderma reesei.";
RL Front. Microbiol. 8:2037-2037(2017).
RN [4]
RP FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=28809958; DOI=10.1371/journal.pone.0182530;
RA Monroy A.A., Stappler E., Schuster A., Sulyok M., Schmoll M.;
RT "A CRE1-regulated cluster is responsible for light dependent production of
RT dihydrotrichotetronin in Trichoderma reesei.";
RL PLoS ONE 12:E0182530-E0182530(2017).
CC -!- FUNCTION: Highly reducing polyketide synthase; part of the SOR gene
CC cluster that mediates the biosynthesis of sorbicillinoids, a diverse
CC group of yellow secondary metabolites that restrict growth of competing
CC pathogenic fungi but not of bacteria (PubMed:29104566). Sorbicillinoids
CC biosynthesis requires the action of two PKSs (PubMed:28809958). The SOR
CC cluster is required for the production of trichodimerol and
CC dihydrotrichotetronin, with sor2 being sufficient for production of
CC trichodimerol, but not dihydrotrichotetronin in the light
CC (PubMed:28809958). Sor1 iteratively combines three acetyl units and the
CC growing chain is modified by the ketoacyl reductase subunit, and
CC optional by the enoyl reductase subunit in the second cycle (By
CC similarity). The polyketide is then handed over to the PKS sor2, which
CC adds three more acetyl units, and two methyl groups (By similarity).
CC Sor2 releases an aldehyde, which undergoes spontaneous cyclization
CC resulting in the formation of sorbicillin or 2',3'-dihydrosorbicillin
CC (By similarity). The monooxygenase sor5 oxidizes sorbicillin and 2',3'-
CC dihydrosorbicillin to 2',3'-dihydrosorbicillinol and sorbicillinol,
CC respectively (PubMed:29104566). The oxidoreductase sor8 further
CC converts sorbicillinol into oxosorbicillinol (PubMed:29104566).
CC Sorbicillinol is the building block for the other sorbicillinoids such
CC as disorbicillinol, bisvertinolon, dihydrobisvertinolone, and
CC dihydrotrichotetronine (PubMed:29104566, PubMed:28809958).
CC {ECO:0000250|UniProtKB:B6HNK3, ECO:0000269|PubMed:28809958,
CC ECO:0000269|PubMed:29104566}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:28809958}.
CC -!- INDUCTION: The promoter contains putative CRE1 binding motifs 5'-
CC SYGGRG-3' and expression is differentially regulated in light and
CC darkness by CRE1 (PubMed:28809958). Photoreceptors BLR1 and BLR2
CC negatively regulate the expression, while ENV1 exerts positive
CC regulation (PubMed:28809958). Moreover the SOR biosynthetic genes show
CC a mechanism of positive feedback on each other in darkness
CC (PubMed:28809958). {ECO:0000269|PubMed:28809958}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of sorbicillinol
CC (PubMed:29104566). Abolishes production of trichodimerol and
CC dihydrotrichotetronin in darkness, while trichodimerol stays still
CC detectable in light (PubMed:28809958). Also impacts production of
CC paracelsin in a light dependent manner, with decreased paracelsin
CC levels in light, but likely in an indirect way (PubMed:28809958).
CC {ECO:0000269|PubMed:28809958, ECO:0000269|PubMed:29104566}.
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DR EMBL; GL985056; EGR52690.1; -; Genomic_DNA.
DR RefSeq; XP_006961561.1; XM_006961499.1.
DR AlphaFoldDB; G0R6S8; -.
DR SMR; G0R6S8; -.
DR STRING; 51453.EGR52690; -.
DR EnsemblFungi; EGR52690; EGR52690; TRIREDRAFT_73618.
DR GeneID; 18488219; -.
DR KEGG; tre:TRIREDRAFT_73618; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_73618; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR Proteomes; UP000008984; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.150; -; 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; 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; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
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; 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; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 2.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Methyltransferase; Multifunctional enzyme; NADP;
KW Oxidoreductase; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..2567
FT /note="Highly reducing polyketide synthase sor1"
FT /id="PRO_0000443835"
FT DOMAIN 2481..2558
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 17..439
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 550..841
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 939..1249
FT /note="Dehydrogenase (DH) domain"
FT /evidence="ECO:0000255"
FT REGION 1426..1534
FT /note="Methyltransferase (CMet) domain"
FT /evidence="ECO:0000255"
FT REGION 1852..2163
FT /note="Enoyl reductase (ER) domain"
FT /evidence="ECO:0000255"
FT REGION 2187..2369
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000255"
FT ACT_SITE 187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2518
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2567 AA; 277294 MW; 50557224F2541D9F CRC64;
MGSLGPDSQS RWASEPIAII GMSSKFAGDA TNTDKLWQML AEGRSGWTEF PASRFRSEGV
YHPNNERLNT THVKGAHFLQ EDVGLFDAAF FSYSSETASS LDPQYRLQLE SAYEALENAG
IPLTQIAGSN TSVFTGVFVH DYRDALLRDA DNLPRLMATG TGVPMMSNRI SHFFDLRGAS
MTIETACSSG MVATHQGIQS LRTGEADMSI VGGANLTLNP DMFKALGSAG FLSADGKSYA
FDSRASGYGR GEGVATIVMK RLSDALAAGD PIRAVIRSSL LNQDGKTETI TTPSLEAQID
LIRQCYARAG LDPRDTQYFE AHGTGTQAGD TVEARAIATV FSHNQDPLLI GSIKTNIGHT
EAASGLASII KTALALEKGV IPASINFEKP NPKLSLEDWH LKLVRQLQEW PAASTRRASI
NNFGYGGANA HIILEDGASW TPSPVEGTSS KEPIDTGSRV LVLSGKDEQA CRTMISNLAE
YLQRVASAED EPSRLLDSLA YTLGQRRTRF PWVAAHPVPV TEGIGAVVNT LQSPKFKPYR
SSRRPRIGMV FTGQGAQWWA MGRELRDAYP VYKASLDEAD AYIRQFGADW SLVEELSRDA
ASSRINESGL STPICVAVQI SLVRLLESWG VVPAAVTSHS SGEIAAAYTV GALSYKDAMA
YAYHRAVLAA DTSLRGPVKG GMLAIGLGRE DTEAYLKRLT TGGKAMVACV NSPSSTTVSG
DLSAVQELEE LANADGVFAR LLKVETAWHS HHMTAIANVY VEALDNIKRK NSRNESSIAY
SSPVTGGRVA NIEEVARPEH WVKSLVQPVQ FVDAFTDMVL GNPNGSANVD VVVEVGPHTA
LGGPIQQILA LPAFKGLQIP YYGCLVRKAD AKDTMQALAA NLLQQGYPLD MDAVNFPHGR
GSRVRVLTGL PSYPWNHQVK HWVEPRFNRA LRERSVPPHH LLGSLVEGTN LEEPTWRHTL
RISESPWTRD HAIQSNVVYP AAGYICLAIE ATKQLHALNH TKAGAKEVSG YRLRDVDFLQ
ALMIPDTSDG IEIQTSLRPV NDKDVAIQGW KHFEVWTVTG DNRWTQHAKG LISIEFEASA
QVYEPKLGEF TIKGYKRQIP PAQLFANLKA LGIGHGPVFQ NMSHIVQSGF DRRSVVLTTV
PDTSVPNDLP REHVLHPVTL DSFITSPYSA VPGAAGRETA AKVPRSVKSF WVSSNISHSP
EHVFKAHSHI IRDDKHGMEA DVIVANDGVD DNNVLLEMKG FSYQSLGRSV SLQHTEPWES
QLCSSIHWRP DISIKLPATV SLVKQELSSN SNSAEAGGVE ISSLCLYFIQ KALASLSDSD
FTNGSHYSKY YAWMKSAAQQ AAITDIDEEH IDQIAKAQAD GEMIRLLGKQ LVSILRGQST
PTEIMEQDKN LLSRFYSETP RAKRTSSQLS GLLRHLVHKN PRARILEIGA STGGITGSAL
GVLDTATSGG PHASLYHYTD LSDRNFDAAR EGFAAWSDIL AFDVLDIERD PADQGFTVGS
YDVVIASHAF SSTSSAIAGV LENVRSLLKP GGTLLFTEDF KPSIDVQFVK GLFPSWWSSE
RFSEQHVEPS PLLSVPLWDR SLRHAGFTGI DIELRDSDDV DASVSATIMS TLPPHPAGQS
DIDAGKVVIV TSEQAGIPPS EWLKALQHSI ASYSKAVNGA EGKVLPSVQS IESAAATAAW
YADKICIFIG EINEPILYNL DAASLEGIKA MSTGCKGLLW VTRGGAVDCE RPEVSLATGF
VRTLRNEYVG RKFITLDLSP KGSLWQESGH EAIAQVLQNA FGQSLPGHSS GPDKGPVELE
YAERDGVILI PRVYHDVAKD NAITPKTLES EEDTQGITTV EPFYQQHRPL CFLPELLVFG
DDASAAVYRD TLPPRLVEIM PRAYGAGLNP ADRTITGQEC SGIITRVGIE ASKHGYSVGD
RVVCLLQQSS FTSRAVVDWT SVVQMPSRLS FQQAASLPAA FLVAYFSLVE TARLKTSQSV
LIHNAAGSIG QAAIMVAKHI GATVFTTVAS PKQRDLLTRE HGIPSHQIFD SNNASFGTAV
TAATNGRGVD VVLNSLTGPL LQTSFNLVAP LGHFIEVGKY DSLANSNLEM LPFTRGVSFS
AVDVPSLLQH RGSDVHRCLE EVMRLFELEA LAPVSPVIEH NIGDIAQVSR LIQTEEETGK
RVLSVAQDEM VSVLPHTAPA ATLSPDASYL IVGGNGGLGQ AVAHWMVSRG AKNLVLLSRS
AGQSPKMAVL AEELRDAGCH RVLPVSCDVA KEDDLARAMD TCAREGLPPI RGVVHAAFVL
HDSFVENMTL DDYKYTIQSK VSGAWNLHNQ FNLPGDLDFF VLFSSINGIL GYASQAAYSA
AGAYEDALAH WRVKHKGLPA VSIDLSLVDG VGYVAEASAA EAMRKSLIKA GRRVINEEQV
LASLELAIVS PYDPQFILGG INSGPGPHWD VDGDLGRDMR LLALKYRQPA AADGHDDEDS
KAANGGDSLS AKIASASSRD EAISVVGSAV AAMLADMFLV SVEEVDLNDS PSQQGIDSLV
AVEVRNMLFS QAGAELSIFN IMQSPSLAQL VANVVDRSTF AKFAKSS
