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Database: UniProt
Entry: F9XMQ4_ZYMTI
LinkDB: F9XMQ4_ZYMTI
Original site: F9XMQ4_ZYMTI 
ID   F9XMQ4_ZYMTI            Unreviewed;       487 AA.
AC   F9XMQ4;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=3-dehydroquinate synthase {ECO:0000313|EMBL:EGP83658.1};
GN   Name=MgCET1 {ECO:0000313|EMBL:EGP83658.1};
GN   ORFNames=MYCGRDRAFT_76728 {ECO:0000313|EMBL:EGP83658.1};
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:EGP83658.1, ECO:0000313|Proteomes:UP000008062};
RN   [1] {ECO:0000313|EMBL:EGP83658.1, 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   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|ARBA:ARBA00001911};
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DR   EMBL; CM001206; EGP83658.1; -; Genomic_DNA.
DR   RefSeq; XP_003848682.1; XM_003848634.1.
DR   AlphaFoldDB; F9XMQ4; -.
DR   STRING; 336722.F9XMQ4; -.
DR   EnsemblFungi; Mycgr3T76728; Mycgr3P76728; Mycgr3G76728.
DR   GeneID; 13396317; -.
DR   KEGG; ztr:MYCGRDRAFT_76728; -.
DR   VEuPathDB; FungiDB:ZTRI_11.123; -.
DR   eggNOG; KOG0692; Eukaryota.
DR   HOGENOM; CLU_001201_0_4_1; -.
DR   InParanoid; F9XMQ4; -.
DR   OMA; HIRIPTT; -.
DR   OrthoDB; 453at2759; -.
DR   Proteomes; UP000008062; Chromosome 11.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
DR   CDD; cd08199; EEVS; 1.
DR   Gene3D; 3.40.50.1970; -; 1.
DR   Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR   InterPro; IPR030960; DHQS/DOIS.
DR   InterPro; IPR035872; EEVS-like.
DR   PANTHER; PTHR43622; 3-DEHYDROQUINATE SYNTHASE; 1.
DR   PANTHER; PTHR43622:SF1; 3-DEHYDROQUINATE SYNTHASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01761; DHQ_synthase; 1.
DR   SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008062}.
FT   DOMAIN          86..341
FT                   /note="3-dehydroquinate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01761"
FT   REGION          433..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        451..469
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   487 AA;  53699 MW;  3262E90B88DF8B2B CRC64;
     MSDMSATVAE TPKGFHVEGY EKIEYDFTFL DYVFDVKKDD LAKCYERWGR VLAVMDANIF
     EQYGEDLQQY CDHYKLDLSI HKTMIGEKAK SIDTFLSIVD SMTKFGIYRK EPVLVIGGGL
     VTDVAGFACA AYRRNTNFIR IPTTVIGLID ASVSIKVGVN YGNYKNRLGA YHAPIHTFLD
     FTFLRSLPTA QIRNGFAELI KISSCAHLPT FDLLDKYCEE IIKTGFGRTD DATAEVKEAC
     DKINRAGIHE MLKLETPNLH EIGLDRVIAY GHTWSPLHEL VPKVPLRHGH AISIDMAFSA
     TLAHQRGNLP QADYERLLKL FSRCGLSMDH PDFNEEILAQ ATAAILKTRD GKLRAAVPSP
     LGSCEFFNDV TEKEMNDALR KHKEVCKTYP RNGEGLEAFV DASDTGYTKN KAPVEKKLSN
     GLKKLNVLND DVSNGTNGFS PEKAEGLANG ALNGSTKSIN GNGHANGHAN GNGHANGHAN
     GDHGDCC
//
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