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Database: UniProt/TrEMBL
Entry: F9X855_ZYMTI
LinkDB: F9X855_ZYMTI
Original site: F9X855_ZYMTI 
ID   F9X855_ZYMTI            Unreviewed;       548 AA.
AC   F9X855;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   05-JUL-2017, entry version 34.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=MYCGRDRAFT_70646 {ECO:0000313|EMBL:EGP88556.1};
OS   Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf
OS   blotch fungus) (Septoria tritici).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetidae; Capnodiales; Mycosphaerellaceae;
OC   Zymoseptoria.
OX   NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP88556.1, ECO:0000313|Proteomes:UP000008062};
RN   [1] {ECO:0000313|EMBL:EGP88556.1, 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.,
RA   Crane C.F., Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J.,
RA   Aerts A., Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J.,
RA   van der Burgt A., Canto-Canche B., Churchill A.C.L., Conde-Ferraez L.,
RA   Cools H.J., Coutinho P.M., Csukai M., Dehal P., De Wit P.,
RA   Donzelli B., van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E.,
RA   Henrissat B., Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y.,
RA   Kuzniar A., Lindquist E., Lombard V., Maliepaard C., Martins N.,
RA   Mehrabi R., Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A.,
RA   Schmutz J., Schouten H.J., Shapiro H., Stergiopoulos I.,
RA   Torriani S.F.F., Tu H., de Vries R.P., Waalwijk C., Ware S.B.,
RA   Wiebenga A., Zwiers L.-H., Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT   "Finished genome of the fungal wheat pathogen Mycosphaerella
RT   graminicola reveals dispensome structure, chromosome plasticity, and
RT   stealth pathogenesis.";
RL   PLoS Genet. 7:E1002070-E1002070(2011).
CC   -!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
CC       {ECO:0000256|RuleBase:RU361171}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC         ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; CM001199; EGP88556.1; -; Genomic_DNA.
DR   RefSeq; XP_003853580.1; XM_003853532.1.
DR   EnsemblFungi; Mycgr3T70646; Mycgr3P70646; Mycgr3G70646.
DR   GeneID; 13400852; -.
DR   KEGG; ztr:MYCGRDRAFT_70646; -.
DR   InParanoid; F9X855; -.
DR   KO; K01580; -.
DR   OrthoDB; EOG092C1P0W; -.
DR   Proteomes; UP000008062; Chromosome 4.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:EnsemblFungi.
DR   GO; GO:0006538; P:glutamate catabolic process; IEA:EnsemblFungi.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR010107; Glutamate_decarboxylase.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   PANTHER; PTHR43321; PTHR43321; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 2.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000008062};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008062}.
FT   MOD_RES     299    299       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   548 AA;  60984 MW;  98BF5B7335E77A34 CRC64;
     MALASHVDPD ELMAQLHKSP HHQHGRGSSA VSHITPYSSR YNAQSELSKF KIPHDGAPAD
     AVHQMLKDEL DLDGRPNLNL ASFVGTYMER EAEQLMVENL SKNMSDADEY PAMMQMHARC
     VSIIAHMWNV QKGEKAIGSA TTGSSEAIHL GGLAMKRRWQ EKRQAAGKDT SKPNIIMGAN
     AQVALEKFAR YFEVEARILP VSAKSNYRLD PELVKQNIDE NTIGIFVILG STYTGHYEPV
     EEISNILDAY EKETGVDIPI HVDAASGGFI APFTNAKAGG PKWDFALPRV KSINVSGHKF
     GLVYAGVGWI IWRDESYLPK HLVFELHYLG GTEESYTLNF SRPGAQIIAQ YFNLIHLGFT
     GYRAIMENAL SNARLLSKSL ESTGWYKCVS DIHRPKGQHE YQKGVIAPTK EGETSADYNA
     GLPVVAFALT DEFKQKYPHV KQVSVSNLLR AKQYIIPNYP LPPNEEKLEI LRVVVRESMS
     LDLLDRLITD ICEVTENIMN TDAVDMQVYQ PASSNTTTEK KHSSRGLGAH EKHAAKRPMS
     EGVHRTVC
//
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