SRDJ_NEUCR
ID SRDJ_NEUCR Reviewed; 233 AA.
AC Q7SHI7;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 2.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Methyltransferase srdJ {ECO:0000303|PubMed:30908040};
DE EC=2.1.1.- {ECO:0000305|PubMed:30908040};
DE AltName: Full=Sordarial biosynthesis cluster protein srdJ {ECO:0000303|PubMed:30908040};
GN Name=srdJ {ECO:0000303|PubMed:30908040}; ORFNames=NCU02917;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [2]
RP FUNCTION, AND INDUCTION.
RX PubMed=19277664; DOI=10.1007/s00294-009-0236-z;
RA Nowrousian M.;
RT "A novel polyketide biosynthesis gene cluster is involved in fruiting body
RT morphogenesis in the filamentous fungi Sordaria macrospora and Neurospora
RT crassa.";
RL Curr. Genet. 55:185-198(2009).
RN [3]
RP FUNCTION, AND INDUCTION.
RX PubMed=28485098; DOI=10.1111/1462-2920.13791;
RA Zhao Y., Ding J., Yuan W., Huang J., Huang W., Wang Y., Zheng W.;
RT "Production of a fungal furocoumarin by a polyketide synthase gene cluster
RT confers the chemo-resistance of Neurospora crassa to the predation by
RT fungivorous arthropods.";
RL Environ. Microbiol. 19:3920-3929(2017).
RN [4]
RP FUNCTION, AND PATHWAY.
RX PubMed=30908040; DOI=10.1021/acs.jnatprod.8b00983;
RA Zhao Z., Ying Y., Hung Y.S., Tang Y.;
RT "Genome mining reveals Neurospora crassa can produce the salicylaldehyde
RT sordarial.";
RL J. Nat. Prod. 82:1029-1033(2019).
CC -!- FUNCTION: Methyltransferase; part of the gene cluster that mediates the
CC biosynthesis of sordarial, a salicylic aldehyde structurally related to
CC the phytotoxin pyriculol (PubMed:19277664, PubMed:28485098,
CC PubMed:30908040). The most interesting aspect of this pathway is
CC formation of an aromatic product from the highly reducing polyketide
CC synthase srdA (PubMed:30908040). SrdA synthesizes a reduced polyketide
CC chain from one molecule of acetyl-CoA and five molecules of malonyl-CoA
CC (PubMed:30908040). The polyketide chain is then reductively released as
CC an aldehyde (PubMed:30908040). The oxidoreductases srdC, srdD and srdE
CC then oxidize one of the hydroxy groups to facilitate the intramolecular
CC aldol condensation, followed by dehydration to yield a salicylic
CC aldehyde (PubMed:30908040). This aldehyde can undergo facile reduction
CC by endogenous reductases to yield the alcohol 1-hydroxy-2-
CC hydroxymethyl-3-pent-1,3-dienylbenzene (PubMed:30908040). The flavin-
CC dependent srdI counteract against the propensity of the aldehydes to be
CC reduced under physiological conditions and is responsible for
CC reoxidizing 1-hydroxy-2-hydroxymethyl-3-pent-1,3-dienylbenzene back to
CC the salicylic aldehyde (PubMed:30908040). This salicylic aldehyde is
CC then selectively epoxidized by the cupin-domain-containing
CC oxidoreductase srdB to yield the epoxide, which can be hydrolyzed
CC stereoselectively by the hydrolase srdG to give the final product
CC sordarial (PubMed:30908040). {ECO:0000269|PubMed:19277664,
CC ECO:0000269|PubMed:28485098, ECO:0000269|PubMed:30908040}.
CC -!- INDUCTION: Expression is up-reglated during sexual development
CC (PubMed:19277664). Expression is also up-reglated during confrontation
CC with the arthropod fungivore Drosophila melanogaster (PubMed:28485098).
CC {ECO:0000269|PubMed:19277664, ECO:0000269|PubMed:28485098}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
CC -!- CAUTION: A recent genetics report associated srdA and its cluster with
CC the biosynthesis of furanocoumarin neurosporin A, a metabolite produced
CC by N.crassa for chemoresistance against predation by arthropod
CC fungivores (PubMed:28485098). However, based on the gene cluster
CC organization and predicted gene functions, this cluster is unlikely to
CC be involved in neurosporin A biosynthesis, but instead produces
CC compounds similar to pyriculol (PubMed:30908040).
CC {ECO:0000269|PubMed:28485098, ECO:0000269|PubMed:30908040}.
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DR EMBL; CM002236; EAA36363.2; -; Genomic_DNA.
DR RefSeq; XP_965599.2; XM_960506.2.
DR AlphaFoldDB; Q7SHI7; -.
DR SMR; Q7SHI7; -.
DR STRING; 5141.EFNCRP00000002245; -.
DR EnsemblFungi; EAA36363; EAA36363; NCU02917.
DR GeneID; 3881724; -.
DR KEGG; ncr:NCU02917; -.
DR VEuPathDB; FungiDB:NCU02917; -.
DR HOGENOM; CLU_1360269_0_0_1; -.
DR InParanoid; Q7SHI7; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 2: Evidence at transcript level;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..233
FT /note="Methyltransferase srdJ"
FT /id="PRO_0000449338"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 140..146
FT /note="Required for methyltransferase activity"
FT /evidence="ECO:0000250|UniProtKB:P0DPD7"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 40
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0DPD7"
FT BINDING 52
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0DPD7"
FT BINDING 81
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0DPD7"
SQ SEQUENCE 233 AA; 25774 MW; 134F13AA835B9272 CRC64;
MFQVQTAGTR TGTSSPDTTT SEAGLGSTPP MPDFDKQSYW HQRFESETAF EWLIPSSTFM
PLLEAFLNKL PGSDARILHL GFGTSDLQVQ LRTRGFVNIT NVDYEPLAIE RGRHLEMTAF
GDVTMQYITA DATNLASVPE ISSQKYHLVV DKSTADAISC AGDDAVLAMA QGIHRSLADD
GVWISVSYSA FRYDSPQLPF DVEVIARIPT AKARATDPDI YHYCYLLRPK PKV
