ID   A0A2T2NUF0_CORCC        Unreviewed;       546 AA.
AC   A0A2T2NUF0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
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=BS50DRAFT_632863 {ECO:0000313|EMBL:PSN69047.1};
OS   Corynespora cassiicola Philippines.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Corynesporascaceae; Corynespora.
OX   NCBI_TaxID=1448308 {ECO:0000313|EMBL:PSN69047.1, ECO:0000313|Proteomes:UP000240883};
RN   [1] {ECO:0000313|EMBL:PSN69047.1, ECO:0000313|Proteomes:UP000240883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Philippines {ECO:0000313|EMBL:PSN69047.1,
RC   ECO:0000313|Proteomes:UP000240883};
RX   PubMed=29551995; DOI=10.3389/fmicb.2018.00276;
RA   Lopez D., Ribeiro S., Label P., Fumanal B., Venisse J.S., Kohler A.,
RA   de Oliveira R.R., Labutti K., Lipzen A., Lail K., Bauer D., Ohm R.A.,
RA   Barry K.W., Spatafora J., Grigoriev I.V., Martin F.M., Pujade-Renaud V.;
RT   "Genome-Wide Analysis of Corynespora cassiicola Leaf Fall Disease Putative
RT   Effectors.";
RL   Front. Microbiol. 9:276-276(2018).
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; KZ678133; PSN69047.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T2NUF0; -.
DR   STRING; 1448308.A0A2T2NUF0; -.
DR   Proteomes; UP000240883; Unassembled WGS sequence.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006536; P:glutamate metabolic process; IEA:InterPro.
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:UP000240883}.
FT   REGION          511..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         300
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   546 AA;  61303 MW;  E18B5057D25C47CE CRC64;
     MAGLARHVDP DELVETLRDH PVHKAGRHSS RAVSHTTPYS TRYASATELS KFRIPHDGAP
     AETVHQLLKD ELDLDGRPSL NLASFVGTYM EKEAEQLMVE NLSKNMSDAD EYPAMMDMHA
     RCVSIISHLW GVQKGEKAIG SATTGSSEAI HLGGLAMKRR WQEKRMAEGK DTSKPNIIMG
     ANAQVALEKF ARYFEVEARI LPVSEKSSFR LDPGLVKDNI DENTIGIFVI LGSTYTGHYE
     PVEEISNILD EYQKKTGVDI PIHVDAASGG FIAPFTHAKA GTKWNFELPR VKSINTSGHK
     FGLVYAGVGW IIWRDESYLP KHLIFELHYL GGTEESYTLN FSRPGAQIIA QYYNLIHLGF
     TGYQNIMENT LANARLLSRA LETTGWYRCV SDIHRKKGIH RYEKDAKQYD ESQSSADYNA
     GLPVVAFTLS DEFKRDFPHV KQAAVSNLLR AKQYIIPNYP LPPSEEKTEI LRVVVRETLS
     LDMIDRLITD ICSVTEMLMK SDTLDLAAWQ PTSPSVEKQH SSHGLEAKNK HKARRPMHEG
     VHRSVC
//