SORD_HYPJQ
ID SORD_HYPJQ Reviewed; 574 AA.
AC G0R6T3;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=FAD-linked oxidoreductase sor8 {ECO:0000303|PubMed:28010735};
DE EC=1.-.-.- {ECO:0000305|PubMed:29104566};
DE AltName: Full=Sorbicillinoid biosynthetic cluster protein 8 {ECO:0000303|PubMed:29104566};
DE Flags: Precursor;
GN Name=sor8 {ECO:0000303|PubMed:28010735};
GN Synonyms=sor4 {ECO:0000303|PubMed:29104566}; ORFNames=TRIREDRAFT_73631;
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.
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: FAD-linked oxidoreductase; part of the SOR gene cluster that
CC mediates the biosynthesis of sorbicillinoids, a diverse group of yellow
CC secondary metabolites that restrict growth of competing pathogenic
CC 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=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:29104566}.
CC -!- DISRUPTION PHENOTYPE: Leads to the accumulation of dihydrosorbicillinol
CC as well as to higher amounts of oxosorbicillinol (PubMed:29104566).
CC {ECO:0000269|PubMed:29104566}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; GL985056; EGR52692.1; -; Genomic_DNA.
DR RefSeq; XP_006961562.1; XM_006961500.1.
DR AlphaFoldDB; G0R6T3; -.
DR SMR; G0R6T3; -.
DR EnsemblFungi; EGR52692; EGR52692; TRIREDRAFT_73631.
DR GeneID; 18488222; -.
DR KEGG; tre:TRIREDRAFT_73631; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_73631; -.
DR eggNOG; ENOG502R8I5; Eukaryota.
DR HOGENOM; CLU_018354_4_2_1; -.
DR Proteomes; UP000008984; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.465.10; -; 2.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Reference proteome;
KW Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..574
FT /note="FAD-linked oxidoreductase sor8"
FT /evidence="ECO:0000255"
FT /id="PRO_5003408468"
FT DOMAIN 126..305
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 574 AA; 60910 MW; C42A715A9828DD06 CRC64;
MYAPPFVRAF GIAVLAVLPS FSSPATAASL KSSGSSSSCR CFPGDACWPS PADWKAFNQS
VGGRLIATVP LGSVCHGTTY DAARCADVKA AWPYADTHTD SSSSVLAPFF ANQSCDPFLP
RETPCVIGTY VQYAVNVSSV ADIQKTLAFS QKKNLRLVVR NTGHDYFGKS TGAGGLGLWM
HNLKTYDIHD YKSAAYTGKA VTMGAGIQAG ESAATAFKQG LTIVSGICPT VGLAGGYTQG
GGLGPLTTRY GLGADQVLEW HAVLANGSEI TATPTKNSDL YWALTGGGGG TYAVVYSMTV
KAHANEKTTG ANLTFPNAGS EDVFFQGVQA FHDIIPAISD AGGTAVWTVL SKALSVGPVT
GPNMTKATMD SIFQPVLQKL DALNITYSYS SGEFSSFYES NAAYDPPVVS NGLQIGGRLV
KRSDFTGNPD GFIQAIRGIA DQGGLVTGAS YQLSSSLQHP PNSVNPELRK SLISFQIGVP
WINTDWATDL HNQDLITNSF VPALAALLPS GGSAYLNQAD FREPGWQQVF YGENYEKLLE
LKDVYDPNGV FWGRTTVGSE RWAETEDKRL CRVS
