SORB_HYPJQ
ID SORB_HYPJQ Reviewed; 2633 AA.
AC G0R6S9;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Non-reducing polyketide synthase sor2 {ECO:0000303|PubMed:29104566};
DE Short=NR-PKS sor2 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:29104566};
DE AltName: Full=Sorbicillinoid biosynthetic cluster protein 2 {ECO:0000303|PubMed:29104566};
GN Name=sor2 {ECO:0000303|PubMed:29104566}; ORFNames=TRIREDRAFT_73621;
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.
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: Non-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 -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000255};
CC Note=Binds 1 phosphopantetheine covalently. {ECO:0000255};
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 -!- DOMAIN: Multidomain protein; including an N-terminal starter unit:ACP
CC transacylase (SAT) domain, a beta-ketoacyl synthase (KS) domain, a
CC malonyl-CoA:ACP transacylase (MAT) domain, a product template domain, a
CC acyl carrier protein (ACP) domain, a methyltransferase domain and a
CC reductive NADPH-binding domain that is required for NADPH-dependent
CC product release. {ECO:0000305|PubMed:29104566}.
CC -!- DISRUPTION PHENOTYPE: Abolishes production of trichodimerol and
CC dihydrotrichotetronin in darkness (PubMed:28809958). Also impacts
CC production of paracelsin in a light dependent manner, with decreased
CC paracelsin levels in light, but likely in an indirect way
CC (PubMed:28809958). Results also in a positive trend for cbh1 transcript
CC levels and increased specific cellulase activity (PubMed:28809958).
CC {ECO:0000269|PubMed:28809958}.
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; GL985056; EGR52182.1; -; Genomic_DNA.
DR RefSeq; XP_006961156.1; XM_006961094.1.
DR AlphaFoldDB; G0R6S9; -.
DR SMR; G0R6S9; -.
DR STRING; 51453.EGR52182; -.
DR EnsemblFungi; EGR52182; EGR52182; TRIREDRAFT_73621.
DR GeneID; 18488220; -.
DR KEGG; tre:TRIREDRAFT_73621; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_73621; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_6_2_1; -.
DR Proteomes; UP000008984; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 2.
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; IPR013120; Far_NAD-bd.
DR InterPro; IPR041068; HTH_51.
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; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF18558; HTH_51; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF16073; SAT; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Methyltransferase; Multifunctional enzyme; NADP;
KW Phosphopantetheine; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..2633
FT /note="Non-reducing polyketide synthase sor2"
FT /id="PRO_0000443837"
FT DOMAIN 1684..1758
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 67..237
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000250|UniProtKB:A0A0K0MCJ4"
FT REGION 392..817
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 928..1239
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 1338..1509
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255"
FT REGION 1762..1792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1982..2166
FT /note="Methyltransferase domain"
FT /evidence="ECO:0000255"
FT REGION 2253..2495
FT /note="NADPH-binding (R) domain"
FT /evidence="ECO:0000255"
FT COMPBIAS 1768..1792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 140
FT /note="Nucleophile; for transacylase activity"
FT /evidence="ECO:0000250|UniProtKB:A0A0K0MCJ4"
FT ACT_SITE 258
FT /note="Proton donor/acceptor; for transacylase activity"
FT /evidence="ECO:0000250|UniProtKB:A0A0K0MCJ4"
FT ACT_SITE 561
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 1718
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2633 AA; 288715 MW; 47908285506032DA CRC64;
MAASSTRTLL MFGPGAMSLN ETYFASILSF ISTDSASQWA LSAVRDIESH WPSLCEAIPK
LQHTSGVSNA QKLAEWLRTG TLAPGSTIAS LPNAILGPLV VIAQLVEYLR HVDSLSESGL
RGGEGFQVPS APDAETVGCC LGTFSALVVS SSSSWAQFCH NASAVVRIVF VLGALSDAQD
ATDASGPSVS LIAFWRGGQS LSDLKKALEK FPEAYISVLY DENRVTVTTS TRTVAALKNH
LQTVGITTNE TEFHGRFHAA QLYQTELEAF LAYCRRFPTF QLPDSSCIVV PTRVNSENVV
TSQESLLEIS CRAFLVSQFD WIKTFRAAVS STLQNRASRI IEFGPERCVP PTLLRRLNSQ
VTHFDFEESI KRAKASLSHD QELPAGVAEN DIAVIGMACK VAGADDVNEY WELLLQGKSQ
HRELIPNDRF VMETPFRPFE AGDDKKKWFG NFIGDHDAFD YKFFKKSPRE ALHMDPQQRL
MLQAAYQAVA QSGYYNANLN VHGPTKVGCY IGVVANDYEN NISHTTPIAF SATGALRSYI
AGKVSHFFGW TGPAMTVDTA CSASTVALDL ACKAILSGEC SAALVGGTNF FSTPMFFQNL
AAGSFLSTTG QCKPFDAKAD GYCRGEAVGT VFLKKLSQAI ADGDQVLGVI SATAINQNRN
ETPIFVPNSP SLTNVFRTAI EKSGLDAKDI SVVEAHGTGT PVGDPVEYDS IRQVFGGAVR
AGQDALQVGS VKGLVGHTEG ASGVVALVKI LLMLQRGQIP PQASFETINP SIKYSPSDNL
EITKTPLPWN QEFKAALINN YGAAGSNASV IIKQGPAQLL RRLPPVVDSE TEALLSKVGA
DDAQKAPFFI SGLDEKAILA YAQKLRQFIY SHSNLDIQDL AFSVNRQSNW SLGRGAVFSA
GSIAELDEKL ASIETFPVPS SQPPVILCFG GQVSTFVGLD YQLFAKSAIL RRHLDQCDAA
CKSIGAGSIY PRIFQSDPID DPSVLQPLLF SLQYSCAMSW IDCGIVPAKL VGHSFGELTA
LCISGVVSLQ DGLKLVYGRS KIIKESWGAE RGAMLAVEAD LEELESLLTT VNSSLQEGRA
TIACFNGPRS FTVAGSSAAI DAVQQAISNT QPVLKHKRLN VTNAFHSVLV ERLKPDLEAL
GRQLTFALPQ IPLERATRSR EDHGLSPSYV ANHMREPVYF HHAVERIAKE YPEAIWLEAG
SNSTITTMAS KALGLPKAST FQPVNVTNNS KASSQLSDVT MNLWKAGLRI TFWPHSRAQT
YEYKHIILPP YQFEKHRQWL EFKPPQALQV VVQTDSSTDA RNGTTEPQPV GLYTLLDRGQ
DKYRFRVNTA AGQFVDAMSD HAIGKAQTLP AMFGVDLAIE ALLSIHPELG DTSRFDPQIY
NVVNQEYIHD SSRALFVLFE RLGQDENSWA FELTSKGKDG AESLHMSGQL HFQASDDARS
RLEFSRLDRF ITHDRCLQVL ESSGRSDEVI QGQTIYSVLS SSDVNYGQRL RGLQRLVGRS
NESAGRLVRR RSGKLFVDFA LGEVFTQVGS IWANCMAQHQ RNTRNKGIYM ATGLEQWSKS
PKVLQKFNQG LYDNDPEIEW HVLAQHKRNT SDDSFTTDIF VFDAASGDLE EVILGIKYAP
VSLDQLFSGS AIATATTPVA NGYVPLTTPF VPVPTTTKQA AVPQPQHVAK KAAPRAAPKR
DIKEELWLRL RPVLADISGL EPEEIQPTDA LADIGIDSLM GMEMAREVET TFNCTVEQSE
LLSIVDVPGI LKFLQSTLGD EDVHDSSETM STVSSDGNVH SPPTSGSEMA SPNLKVSYGS
AYGSSDLPIS AVLEAFGESS AKTDQFLKTY GCAGYLDGVS QKQTRLCLVL TSAAFKQLGC
DLEAAKPGEV LQPVPFVERH RRFHQYLYSM LEETRIINID GDVITRTAIP LPSQSADAIL
QDLMRRHADN GSSHQLAYNV GSRMADVLSG KADGPQLIFG DAKNRELVAN FYGELPFNKL
YFELMADFLT RLANKLKLSS SRSGTPTLKI LEMGAGTGGT TKVLLPILAK LGIPLEYTFT
DLSPSLVAQA KRRFKEYPFM KFAVHDIEQP PSDPELVGSQ HVVIASNAVH ATHSLRDSAR
NIHKFLRPDG FLMLLEMMRT LHWVDVVWGT LEGWWLFDDG RTHAIVNEQR WEKELLASGF
KHVRWTDGKL PEVHVQRVII ALAGDGDGDV SDIPALTSPA LKDEEDHGSK LDGEERKRVA
NAYVESTIRD FAIPSYTGPI LSTAPGAGAC VLVTGATGSL GSHLVAHIAG LPSVDTIYCL
NRPRPGKKGQ EDQSRDPLSR LTEVLASKSI QLSEAEISKL RVIETDLPLP QFGLDEIQYE
QLLNNVTHIV HSAFPVNGLR SLKQNEPQFT LMRNLVDLAA GVSARRPTEF KFTFQFISSL
SAVGMYPKVH GEKRVPEQQW DVDSALPNGY GEAKVICERV LLETLGQHPD RFRAMTVRLG
QLSGSMKTGY WNHMEMLSFL FKSAQTLRAL PDVDGDVSWL HLEDASASLA DLLLRDAPTC
HAVYHLDNPR PRDWKDVIPV LADALDIPSS HIVPFEEWLR RVRAYPGEDP WDNPSAKAMD
FFEHKFKHMS CGGVTMATDH ALEHSETLRA VQPVSDELVR KYIQAWKDSG FLR
