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T4HR_ZYMTI
ID   T4HR_ZYMTI              Reviewed;         267 AA.
AC   F9XMW6;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Probable tetrahydroxynaphthalene reductase MYCGRDRAFT_87994 {ECO:0000303|PubMed:28818040};
DE            EC=1.1.1.252 {ECO:0000250|UniProtKB:Q12634};
DE   AltName: Full=Conidial pigment biosynthesis cluster 29 protein MYCGRDRAFT_87994 {ECO:0000303|PubMed:28818040};
GN   ORFNames=MYCGRDRAFT_87994;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 115943 / IPO323;
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).
RN   [2]
RP   FUNCTION, AND PATHWAY.
RX   PubMed=28818040; DOI=10.1186/s12864-017-3969-y;
RA   Cairns T., Meyer V.;
RT   "In silico prediction and characterization of secondary metabolite
RT   biosynthetic gene clusters in the wheat pathogen Zymoseptoria tritici.";
RL   BMC Genomics 18:631-631(2017).
CC   -!- FUNCTION: Probable tetrahydroxynaphthalene reductase; part of the gene
CC       cluster 29 that mediates the biosynthesis dihydroxynaphthalene (DHN)-
CC       melanin, a bluish-green pigment and a structural component of the
CC       conidial wall (PubMed:28818040). Catalyzes the NADPH-dependent
CC       reduction of 1,3,6,8-tetrahydroxynaphthalene (T4HN) into (+)-scytalone
CC       (By similarity). {ECO:0000250|UniProtKB:Q12634,
CC       ECO:0000269|PubMed:28818040}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + scytalone = H(+) + NADPH + naphthalene-1,3,6,8-
CC         tetrol; Xref=Rhea:RHEA:21908, ChEBI:CHEBI:15378, ChEBI:CHEBI:16945,
CC         ChEBI:CHEBI:18365, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.252; Evidence={ECO:0000250|UniProtKB:Q12634};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21910;
CC         Evidence={ECO:0000250|UniProtKB:Q12634};
CC   -!- PATHWAY: Pigment biosynthesis; melanin biosynthesis.
CC       {ECO:0000305|PubMed:28818040}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q12634}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; CM001206; EGP83311.1; -; Genomic_DNA.
DR   RefSeq; XP_003848335.1; XM_003848287.1.
DR   AlphaFoldDB; F9XMW6; -.
DR   SMR; F9XMW6; -.
DR   STRING; 1047171.Mycgr3P87994; -.
DR   EnsemblFungi; Mycgr3T87994; Mycgr3P87994; Mycgr3G87994.
DR   GeneID; 13396131; -.
DR   KEGG; ztr:MYCGRDRAFT_87994; -.
DR   eggNOG; KOG0725; Eukaryota.
DR   HOGENOM; CLU_010194_1_3_1; -.
DR   InParanoid; F9XMW6; -.
DR   UniPathway; UPA00785; -.
DR   Proteomes; UP000008062; Chromosome 11.
DR   GO; GO:0047039; F:tetrahydroxynaphthalene reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Melanin biosynthesis; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..267
FT                   /note="Probable tetrahydroxynaphthalene reductase
FT                   MYCGRDRAFT_87994"
FT                   /id="PRO_0000451091"
FT   ACT_SITE        163
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         18..26
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         45..46
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         71..73
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         163..167
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         196..198
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
SQ   SEQUENCE   267 AA;  28465 MW;  661F2735877984B9 CRC64;
     MAVTPYVDTS RLDGKVALVT GSGRGIGAAM AIHLANRGAK VVVNYANSVE AANKVVDEIK
     SRGGEAIALQ ADVGEVSQTT KLMDDAVAHF GQLDIVCSNS GVVSFGHLKD VTEEEYDRVF
     RINTRGQFFV AREAYKHLSV GGRIIMMGSI TGQAKGVPKH AVYSASKGAI ETFVRCMAID
     CGDKKITVNA VAPGGIKTDM YHAVCKEYIP NGENLTDEEV DEYAKTWSPM DRVGQPMDIA
     KVVGFLASED GEWINGKVIG IDGAACM
 
 
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