ID   F9X855_ZYMTI            Unreviewed;       548 AA.
AC   F9X855;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|ARBA:ARBA00012421, ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|ARBA:ARBA00012421, ECO:0000256|RuleBase:RU361171};
GN   ORFNames=MYCGRDRAFT_70646 {ECO:0000313|EMBL:EGP88556.1};
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: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., 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-glutamate = 4-aminobutanoate + CO2;
CC         Xref=Rhea:RHEA:17785, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:59888; EC=4.1.1.15;
CC         Evidence={ECO:0000256|RuleBase:RU361171};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50, 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   AlphaFoldDB; F9X855; -.
DR   STRING; 336722.F9X855; -.
DR   EnsemblFungi; Mycgr3T70646; Mycgr3P70646; Mycgr3G70646.
DR   GeneID; 13400852; -.
DR   KEGG; ztr:MYCGRDRAFT_70646; -.
DR   VEuPathDB; FungiDB:ZTRI_4.77; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   HOGENOM; CLU_019582_2_3_1; -.
DR   InParanoid; F9X855; -.
DR   OMA; KNIMQNC; -.
DR   OrthoDB; 2783360at2759; -.
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; 3.90.1150.160; -; 1.
DR   Gene3D; 4.10.280.50; -; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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.
DR   NCBIfam; TIGR01788; Glu-decarb-GAD; 1.
DR   PANTHER; PTHR43321; GLUTAMATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43321:SF3; GLUTAMATE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, 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   REGION          511..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        523..540
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         299
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="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
//