SOR7_HYPJQ
ID SOR7_HYPJQ Reviewed; 358 AA.
AC G0R6S7;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Short chain dehydrogenase sor7 {ECO:0000303|PubMed:28010735};
DE EC=1.1.1.- {ECO:0000305|PubMed:28010735};
DE AltName: Full=Sorbicillinoid biosynthetic cluster protein 7 {ECO:0000303|PubMed:28010735};
GN Name=sor7 {ECO:0000303|PubMed:28010735}; ORFNames=TRIREDRAFT_102492;
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, AND FUNCTION.
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.
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: Short chain dehydrogenase; 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 -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:28010735}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; GL985056; EGR52689.1; -; Genomic_DNA.
DR RefSeq; XP_006961560.1; XM_006961498.1.
DR AlphaFoldDB; G0R6S7; -.
DR SMR; G0R6S7; -.
DR STRING; 51453.EGR52689; -.
DR EnsemblFungi; EGR52689; EGR52689; TRIREDRAFT_102492.
DR GeneID; 18480408; -.
DR KEGG; tre:TRIREDRAFT_102492; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_102492; -.
DR eggNOG; KOG1208; Eukaryota.
DR HOGENOM; CLU_010194_44_4_1; -.
DR Proteomes; UP000008984; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..358
FT /note="Short chain dehydrogenase sor7"
FT /id="PRO_0000443849"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 206
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 26..34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 53..54
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 111..113
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 206..210
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 238..240
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
SQ SEQUENCE 358 AA; 38886 MW; B7005DA21268690A CRC64;
MSSPAIGQPP IPPTPTDANI SGKTVIVTGG NSGLGYEAAR QFLTLGASRM ILACRSIARG
QEAASALRAH PTVKETNPNA VIDAFELDLD DYYSGLCFSN RVNAEVKELD ILLNNGGQVV
MGYEKSKSGH ERSMQVNCYT HLLISLELFP LLRSTSAARG VPSRITFTGS ATQIMQNTLS
KQPISSESTV LGHFDDEANF NKLYRYADSK TVVNAYVRRL AALAPSEVIV NNACPGLVQT
GIDKNLPFYL KLPMGLLRKS TGRTVEEGAR TLIYVAVVAG TETNGKFLQH NQVDPLASTY
TFAFPCYMER RPPECFSVSL EHGSKAQESL LAWNTSILRS FHGGGSAWRN TFNLALTI
