ID   Q6FS86_CANGA            Unreviewed;       593 AA.
AC   Q6FS86;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 123.
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   OrderedLocusNames=CAGL0H02585g {ECO:0000313|CGD:CAL0131940,
GN   ECO:0000313|EMBL:CAG59841.1};
OS   Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX   NCBI_TaxID=284593 {ECO:0000313|EMBL:CAG59841.1, ECO:0000313|Proteomes:UP000002428};
RN   [1] {ECO:0000313|EMBL:CAG59841.1, ECO:0000313|Proteomes:UP000002428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC   {ECO:0000313|Proteomes:UP000002428};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR380954; CAG59841.1; -; Genomic_DNA.
DR   RefSeq; XP_446908.1; XM_446908.1.
DR   AlphaFoldDB; Q6FS86; -.
DR   STRING; 284593.Q6FS86; -.
DR   EnsemblFungi; CAGL0H02585g-T; CAGL0H02585g-T-p1; CAGL0H02585g.
DR   GeneID; 2888533; -.
DR   KEGG; cgr:CAGL0H02585g; -.
DR   CGD; CAL0131940; CAGL0H02585g.
DR   VEuPathDB; FungiDB:CAGL0H02585g; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   HOGENOM; CLU_019582_2_3_1; -.
DR   InParanoid; Q6FS86; -.
DR   OMA; KNIMQNC; -.
DR   Proteomes; UP000002428; Chromosome H.
DR   GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
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:UP000002428}.
FT   REGION          561..593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        567..587
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         322
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   593 AA;  67410 MW;  4FA82C0C253B2AB7 CRC64;
     MLHKHTDKQR LPVNIVDHHH IDPCLQDFKL LSKELQDIAS NSEKLKALGS KENKESHLLS
     MKYVIPKEGV PADQAYDMIH NELTLDGNTH LNLASFVNTS TTHEVRKLIS ENLTKNLADN
     DEYPQLIELT QRCISMLSGL WNANPEEEPI GCATTGSSEA IMLGGLAMKK MWEKKMKAAG
     RTDTSKPNII MSSACQVALE KFARYFDVEC RLVPVSRKSH HMLDPNLLWD FVDENTIGCF
     VIMGTTYTGH LENVAEVGDV LTAIEKQHPE WANKDIPIHV DGASGGFIVP FAFSREQLKA
     YGVPNWGFDH PRVVSINTSG HKFGLTTPGL GWVLWRDESH LAPELRFRLK YLGGVEETFG
     LNFSRPGFQV VHQYYNFMNL GYDGYRDTFK RSLFVARVFA HQILRSPIFN DYFEVVSSIH
     ESIDGDKVPD AANDYWENPE KYKPGVPLIA FKFSDKFQKE YPEVPQALLS HMLRTRGWII
     PNYPLPHSTD GSDKCEVLRV VFRNEMSLDL AQLLLSDIQA VLRKLQGSYS GLKTISHESD
     SDKRRDYVYK MLLALASPDA DIGEDEDEET KEKKASKKEE IKQRLKRNYR GTC
//