ID   DCEC_LISMO              Reviewed;         467 AA.
AC   Q8Y4K4;
DT   21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2002, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=Probable glutamate decarboxylase gamma;
DE            Short=GAD-gamma;
DE            EC=4.1.1.15;
GN   OrderedLocusNames=lmo2434;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL591983; CAD00512.1; -; Genomic_DNA.
DR   PIR; AB1379; AB1379.
DR   RefSeq; NP_465957.1; NC_003210.1.
DR   RefSeq; WP_010989992.1; NZ_CP023861.1.
DR   AlphaFoldDB; Q8Y4K4; -.
DR   SMR; Q8Y4K4; -.
DR   STRING; 169963.gene:17595144; -.
DR   PaxDb; 169963-lmo2434; -.
DR   DNASU; 987419; -.
DR   EnsemblBacteria; CAD00512; CAD00512; CAD00512.
DR   GeneID; 987419; -.
DR   KEGG; lmo:lmo2434; -.
DR   PATRIC; fig|169963.11.peg.2492; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_019582_2_1_9; -.
DR   OrthoDB; 9803665at2; -.
DR   PhylomeDB; Q8Y4K4; -.
DR   BioCyc; LMON169963:LMO2434-MONOMER; -.
DR   Proteomes; UP000000817; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004058; F:aromatic-L-amino-acid decarboxylase activity; IEA:UniProt.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006538; P:glutamate catabolic process; IBA:GO_Central.
DR   CDD; cd06450; DOPA_deC_like; 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:SF3; GLUTAMATE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..467
FT                   /note="Probable glutamate decarboxylase gamma"
FT                   /id="PRO_0000146992"
FT   MOD_RES         278
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   467 AA;  53640 MW;  64A8CB6FDC82B8CF CRC64;
     MLYSEDDKRK QESYRIPLFG SEEESTSIPK YVLKKEPMEP RIAYQLVKDQ LMDEGNARQN
     LATFCQTYME KEAEILMAET LEKNAIDKSE YPQTAELENR CVNILADLWN APKDMSYLGT
     STVGSSEACM LGGLAMKFRW RNNAEKRGLD IQAKRPNLII SSGYQVCWEK FCVYWDVDMR
     VVPMDKNHLS LDVDKVFDLV DEYTIGVVGI LGITYTGKFD DIQLLDEKVE AYNETNEHQL
     VIHIDGASGA MFTPFVNPEL PWDFRLKNVV SINTSGHKYG LVYPGVGWIL WKDKEYLPKE
     LIFEVSYLGG SMPTMAINFS RSASQIIGQY YNFLRYGFEG YREIHEKTKK TAIYLAKTVE
     KSGYFEIIND GANLPIVCYK MKEGLDVEWT LYDLADQLLM KGWQVPAYPL PADLSDTIIQ
     RFVCRADLGY NVAEEFAADF ADAIHNLEHA RVLYHDKERN DSYGFTH
//