SRDE_NEUCR
ID SRDE_NEUCR Reviewed; 290 AA.
AC Q7SHI2;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Short-chain dehydrogenase srdE {ECO:0000303|PubMed:30908040};
DE EC=1.1.1.- {ECO:0000305|PubMed:30908040};
DE AltName: Full=Sordarial biosynthesis cluster protein srdE {ECO:0000303|PubMed:30908040};
GN Name=srdE {ECO:0000303|PubMed:30908040}; ORFNames=NCU02922;
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: Short-chain dehydrogenase; part of the gene cluster that
CC mediates the biosynthesis of sordarial, a salicylic aldehyde
CC structurally related to the phytotoxin pyriculol (PubMed:19277664,
CC PubMed:28485098, PubMed:30908040). The most interesting aspect of this
CC pathway is formation of an aromatic product from the highly reducing
CC polyketide synthase srdA (PubMed:30908040). SrdA synthesizes a reduced
CC polyketide chain from one molecule of acetyl-CoA and five molecules of
CC malonyl-CoA (PubMed:30908040). The polyketide chain is then reductively
CC released as an aldehyde (PubMed:30908040). The oxidoreductases srdC,
CC srdD and srdE then oxidize one of the hydroxy groups to facilitate the
CC intramolecular aldol condensation, followed by dehydration to yield a
CC salicylic aldehyde (PubMed:30908040). This aldehyde can undergo facile
CC reduction 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
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 short-chain dehydrogenases/reductases (SDR)
CC 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; EAA36368.1; -; Genomic_DNA.
DR RefSeq; XP_965604.1; XM_960511.1.
DR AlphaFoldDB; Q7SHI2; -.
DR SMR; Q7SHI2; -.
DR STRING; 5141.EFNCRP00000002422; -.
DR EnsemblFungi; EAA36368; EAA36368; NCU02922.
DR GeneID; 3881729; -.
DR KEGG; ncr:NCU02922; -.
DR VEuPathDB; FungiDB:NCU02922; -.
DR HOGENOM; CLU_010194_2_9_1; -.
DR InParanoid; Q7SHI2; -.
DR OMA; GPMRMVH; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; IBA:GO_Central.
DR GO; GO:0000140; F:acylglycerone-phosphate reductase activity; IBA:GO_Central.
DR GO; GO:0004806; F:triglyceride lipase activity; IBA:GO_Central.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0019433; P:triglyceride catabolic process; IBA:GO_Central.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Membrane; NAD; NADP; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..290
FT /note="Short-chain dehydrogenase srdE"
FT /id="PRO_0000449334"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 150
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 10..19
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 38..39
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 57..59
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 150..154
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 183..185
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 290 AA; 32040 MW; 005F8AF1ABA0147D CRC64;
MAPQSTKFAL ITGCGAGGIG EALILEYLRR GIHPIATLLP FESSEHLDKA GITWFKLDVT
NEESVVQLKK DVSELTKGRL DFLVNNAGIC YTMTAIDTDV KSVQRMFDVN LFGPMRMVHH
FHDMLIASSG IIVNIGSIGG VVPFVYGSSY NASKAALAHW GNSLRVELAP LGVRVLVIIS
GEVGTNILKN DHGRTLPEGS YYSPMAEEFK NHVHRTPDAA TDRFVYAKNV VGESLKKSPT
TWFWTGSYSG VIRFLHTFFP KTVFDRWFSS LFNLAKLKEA HDAAMKKKVA
