ID   A0A423WSW0_9PEZI        Unreviewed;       518 AA.
AC   A0A423WSW0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=VMCG_04299 {ECO:0000313|EMBL:ROW06518.1};
OS   Valsa malicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX   NCBI_TaxID=356882 {ECO:0000313|EMBL:ROW06518.1, ECO:0000313|Proteomes:UP000283895};
RN   [1] {ECO:0000313|EMBL:ROW06518.1, ECO:0000313|Proteomes:UP000283895}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=03-1 {ECO:0000313|EMBL:ROW06518.1,
RC   ECO:0000313|Proteomes:UP000283895};
RA   Yin Z., Huang L.;
RT   "Host preference determinants of Valsa canker pathogens revealed by
RT   comparative genomics.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ROW06518.1}.
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DR   EMBL; LKEA01000010; ROW06518.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A423WSW0; -.
DR   STRING; 356882.A0A423WSW0; -.
DR   Proteomes; UP000283895; 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:SF6; 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:UP000283895}.
FT   REGION          483..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        493..510
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         296
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   518 AA;  58555 MW;  3B30EC1D33F81531 CRC64;
     MVHLSHIPNP EEVEKHLVNE VKKVHLDLAQ NNDDDFATSV YGSKFAIEDL PRHEIPDEEM
     PRDVAYRMIR DELSLDGNPM LNLASFVTTY MEDEAEKLMA ESLSKNFIDY EEYPKTAEIQ
     NRCVSMIGRM FNAPTGEGVG AVGTSCVGSS EAIMLGVLAM KRVWKNKRKA EGKSTENPNI
     VMSSAVQVCW EKATRYFEIE EKLVYCSQDR YVIDPKETVD LVDENTIGIC CILGTTYTGE
     YEDVKAVNDL LIERGMDTPI HVDAASGGFV APFTVPDLEW DFRLPRVVSI NVSGHKYGLV
     YPGVGWVVWR GAEFLPQELV FNINYLGADQ SSFTLNFSKG ASQVIGQYYQ LIRLGKHGYK
     AIMSNLTRTS DYLADSVQAL GFVLMSKKSG EGLPLVAFRL PDDENDERSY DEFALARQLR
     VRGWVVPAYT MAPNTNNLKM LRVVVREDFT RNRCDALITD IKLCMQLLEQ MDKDSVKRLQ
     KFHTKSHHRA GKPNHNHPDY RNEKHSLQGK TGKTHAVC
//