SRDB_NEUCR
ID SRDB_NEUCR Reviewed; 196 AA.
AC Q7SHI5;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Cupin-domain-containing oxidoreductase srdB {ECO:0000303|PubMed:30908040};
DE EC=1.-.-.- {ECO:0000305|PubMed:30908040};
DE AltName: Full=Sordarial biosynthesis cluster protein srdB {ECO:0000303|PubMed:30908040};
GN Name=srdB {ECO:0000303|PubMed:30908040}; ORFNames=NCU02919;
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: Cupin-domain-containing oxidoreductase; part of the gene
CC cluster that mediates the biosynthesis of sordarial, a salicylic
CC aldehyde structurally related to the phytotoxin pyriculol
CC (PubMed:19277664, PubMed:28485098, PubMed:30908040). The most
CC interesting aspect of this pathway is formation of an aromatic product
CC from the highly reducing polyketide synthase srdA (PubMed:30908040).
CC SrdA synthesizes a reduced polyketide chain from one molecule of
CC acetyl-CoA and five molecules of malonyl-CoA (PubMed:30908040). The
CC polyketide chain is then reductively released as an aldehyde
CC (PubMed:30908040). The oxidoreductases srdC, srdD and srdE then oxidize
CC one of the hydroxy groups to facilitate the intramolecular aldol
CC condensation, followed by dehydration to yield a salicylic aldehyde
CC (PubMed:30908040). This aldehyde can undergo facile reduction by
CC endogenous reductases to yield the alcohol 1-hydroxy-2-hydroxymethyl-3-
CC pent-1,3-dienylbenzene (PubMed:30908040). The flavin-dependent srdI
CC counteract against the propensity of the aldehydes to be reduced under
CC physiological conditions and is responsible for reoxidizing 1-hydroxy-
CC 2-hydroxymethyl-3-pent-1,3-dienylbenzene back to the salicylic aldehyde
CC (PubMed:30908040). This salicylic aldehyde is then selectively
CC epoxidized by the cupin-domain-containing oxidoreductase srdB to yield
CC the epoxide, which can be hydrolyzed stereoselectively by the hydrolase
CC srdG to give the final product sordarial (PubMed:30908040).
CC {ECO:0000269|PubMed:19277664, ECO:0000269|PubMed:28485098,
CC 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 virC family. {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; EAA36365.1; -; Genomic_DNA.
DR RefSeq; XP_965601.1; XM_960508.2.
DR AlphaFoldDB; Q7SHI5; -.
DR SMR; Q7SHI5; -.
DR STRING; 5141.EFNCRP00000002373; -.
DR EnsemblFungi; EAA36365; EAA36365; NCU02919.
DR GeneID; 3881726; -.
DR KEGG; ncr:NCU02919; -.
DR VEuPathDB; FungiDB:NCU02919; -.
DR HOGENOM; CLU_096188_0_2_1; -.
DR InParanoid; Q7SHI5; -.
DR OMA; FRYITGH; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR013096; Cupin_2.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR Pfam; PF07883; Cupin_2; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
PE 2: Evidence at transcript level;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..196
FT /note="Cupin-domain-containing oxidoreductase srdB"
FT /id="PRO_0000449330"
FT REGION 92..156
FT /note="Cupin-like domain"
FT /evidence="ECO:0000255"
SQ SEQUENCE 196 AA; 21418 MW; 9A21E3F536E9C855 CRC64;
MSTSGPITEF PAPGLRDPFR YITGHDAEGN AVFVQTDNGD HRAVMLGGAA AQNIIYSAGS
NPIELTGNVD LEFAKNRPSL HIPNGVCVRM IDFAPGCKSN MHRALCMGIG TVCEGEVELT
LGSGEKRILR PGDVSINRGA MHQWRNTSDE KPARMLYTLL DIKPLIVNGK QLDFDMGYLM
KEYAEYDEGE GDKKAE
