ID   D4DEM9_TRIVH            Unreviewed;       505 AA.
AC   D4DEM9;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   02-SEP-2026, entry version 73.
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=TRV_05598 {ECO:0000313|EMBL:EFE39704.1};
OS   Trichophyton verrucosum (strain HKI 0517).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663202 {ECO:0000313|EMBL:EFE39704.1, ECO:0000313|Proteomes:UP000008383};
RN   [1] {ECO:0000313|Proteomes:UP000008383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HKI 0517 {ECO:0000313|Proteomes:UP000008383};
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamate + H(+) = 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|ARBA:ARBA00009533, 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:EFE39704.1}.
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DR   EMBL; ACYE01000301; EFE39704.1; -; Genomic_DNA.
DR   RefSeq; XP_003020322.1; XM_003020276.1.
DR   AlphaFoldDB; D4DEM9; -.
DR   GeneID; 9584061; -.
DR   KEGG; tve:TRV_05598; -.
DR   HOGENOM; CLU_019582_2_2_1; -.
DR   OrthoDB; 287at34384; -.
DR   Proteomes; UP000008383; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006538; P:L-glutamate catabolic process; IEA:TreeGrafter.
DR   FunFam; 3.40.640.10:FF:000017; Glutamate decarboxylase; 1.
DR   FunFam; 3.90.1150.160:FF:000004; Glutamate decarboxylase; 1.
DR   FunFam; 4.10.280.50:FF:000001; Glutamate decarboxylase; 1.
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|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR602129-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008383}.
FT   DOMAIN          119..426
FT                   /note="Pyridoxal phosphate-dependent decarboxylase major"
FT                   /evidence="ECO:0000259|Pfam:PF00282"
FT   MOD_RES         322
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   505 AA;  57665 MW;  FA2E0BBA707A6A21 CRC64;
     MVHISRVRKD SVAFPPKLLN RVDTLDLEEP QDHDFYSSVY GSRFAAEDLP TDEMPEKEMP
     KEVAYRMIKD ELSLDGNPML KYVLAVVILF IYRVILADLD HVYSLASFVT TYMEDEAEKL
     MTESFSKNFI DYEEYPQSAD IQNRCVNMIA RLFHAPVGEG EHEHDHAMGT SCIGSSEAIM
     LGTLAMKKRW QNRRKAEGKD CSRPNIIMSS AVQVCWEKAA RYFDIEEKFV YCTNERYVLD
     PEEAVNLIDK NTIGICVILG TTYTGQYEDI KAVNDLLVEK KIDCPIHVDA ASGGFVAPFV
     NPSLEWDFRL EKVVSINVSG HKYGLVYPGV GWIVWRSTEY LPQELVFNIN YLGANQASFT
     LNFSKGASQV IGQYYQMIRL GKRGYRAIML NLTRTADYLA ASLKELGFII MSDGKGRGLP
     LVAFRLPPET AEKYDEFAIA HQLRERGWVV PAYTMAPHSE KLKLMRIVVR EDFSRSRCDS
     LVNDFKLALA QLEEMDKKAL EKYRE
//