SORC_HYPJQ
ID SORC_HYPJQ Reviewed; 456 AA.
AC G0R6T0;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=FAD-dependent monooxygenase sor5 {ECO:0000303|PubMed:28010735};
DE EC=1.-.-.- {ECO:0000305|PubMed:29104566};
DE AltName: Full=Sorbicillinoid biosynthetic cluster protein 5 {ECO:0000303|PubMed:28010735};
GN Name=sor5 {ECO:0000303|PubMed:28010735};
GN Synonyms=sor3 {ECO:0000303|PubMed:29104566}; ORFNames=TRIREDRAFT_73623;
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: FAD-dependent monooxygenase; part of the SOR gene cluster
CC that mediates the biosynthesis of sorbicillinoids, a diverse group of
CC 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=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:28809958}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
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: Leads to the production of only traces of
CC sorbicillinol, probably resulting of chemical conversions and not of
CC enzymatic activity (PubMed:29104566). Abolishes production of
CC trichodimerol and dihydrotrichotetronin in darkness (PubMed:28809958).
CC Also impacts production of paracelsin in a light dependent manner, with
CC decreased paracelsin levels in light, but likely in an indirect way
CC (PubMed:28809958). {ECO:0000269|PubMed:28809958,
CC ECO:0000269|PubMed:29104566}.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; GL985056; EGR52183.1; -; Genomic_DNA.
DR RefSeq; XP_006961157.1; XM_006961095.1.
DR AlphaFoldDB; G0R6T0; -.
DR SMR; G0R6T0; -.
DR STRING; 51453.EGR52183; -.
DR EnsemblFungi; EGR52183; EGR52183; TRIREDRAFT_73623.
DR GeneID; 18488221; -.
DR KEGG; tre:TRIREDRAFT_73623; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_73623; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_009665_6_3_1; -.
DR Proteomes; UP000008984; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; Glycoprotein; Membrane; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..456
FT /note="FAD-dependent monooxygenase sor5"
FT /id="PRO_0000443846"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 48..49
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 241..243
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 331
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 341..345
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 456 AA; 49461 MW; 9078D3FB396E5F13 CRC64;
MEPNNHHDGL NGQKADNPLE VAIVGGGLTG LALALGLLRR NVNFTIYERA ASFGELGVGI
HFTPNAERAM KALDPRILQS YVDVATHAEG GFLSFVDGLH DDDLLFQLRM GEGYKAARRC
DIVSQLVKHI PQERVQLLKW LQSVEEDAEG RAVLTFRDGS TAKADVVVGC DGIRSQVRSA
MFGSGPSAPR AQYAHQLAFR GLVPMAKVAA TLGPEKTSRA IGYLGPGGFV LSVPLAGINM
MHLEVFVMDP LPWSDDTTGS KPDKDKDEDD VKRYVLPSTR AEAEKAFTEF NPTVRSLISL
LPEELGKWAI FDMLDSPAPS YALGRMCLAG DAAHASTPNQ GGGAGAGMED SLVLAEILAA
LADRAKSGAR VGSWEISEGL KIYSDARYER AQWLVQSSRR VAQLFTRKKG AGQGGEEEEP
ISREILERSH QLWDYDVDAA VEEALGKLRA KVLEKH
