ID F9WWR3_ZYMTI Unreviewed; 299 AA.
AC F9WWR3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Short chain dehydrogenase/reductase {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=MYCGRDRAFT_34603 {ECO:0000313|EMBL:EGP91470.1};
OS Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS fungus) (Septoria tritici).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP91470.1, ECO:0000313|Proteomes:UP000008062};
RN [1] {ECO:0000313|EMBL:EGP91470.1, ECO:0000313|Proteomes:UP000008062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT reveals dispensome structure, chromosome plasticity, and stealth
RT pathogenesis.";
RL PLoS Genet. 7:E1002070-E1002070(2011).
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484, ECO:0000256|RuleBase:RU000363}.
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DR EMBL; CM001196; EGP91470.1; -; Genomic_DNA.
DR RefSeq; XP_003856494.1; XM_003856446.1.
DR AlphaFoldDB; F9WWR3; -.
DR EnsemblFungi; Mycgr3T34603; Mycgr3P34603; Mycgr3G34603.
DR GeneID; 13395127; -.
DR KEGG; ztr:MYCGRDRAFT_34603; -.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_12_0_1; -.
DR InParanoid; F9WWR3; -.
DR OMA; EPNGIHL; -.
DR OrthoDB; 1472673at2759; -.
DR Proteomes; UP000008062; Chromosome 1.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43618; 7-ALPHA-HYDROXYSTEROID DEHYDROGENASE; 1.
DR PANTHER; PTHR43618:SF4; SHORT CHAIN DEHYDROGENASE_REDUCTASE FAMILY (AFU_ORTHOLOGUE AFUA_7G04540); 1.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008062}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EGP91470.1"
SQ SEQUENCE 299 AA; 31853 MW; 0954162C94E82F95 CRC64;
GRADNHDLKT TDLFDVSHVT ALVTGGATGI GLMITQALVA NGAKVWITGR REETLDKTVE
KYNTGAGSLQ SITGDVSTKE GCLKLAEEMK EKEPKGIQLL VNNAGIARDD DTKFSSNGEP
DMSSAEAISK HFLRSDGQQW TDTFTTNVAA QFFMSMAFLP LLATGGQVTP GYSSSVVNVS
SISGAMKGSS MGQFSYASSK AASTHLSRML ATTFKDVKVR VNVIAPGVFP SEMTAGESGE
DNKSELDMRS YNPAGRKGMD TDMAATILFL AGKGGVFYNE QILYPDGGMH CQLCRTDSH
//