ID   DCEC_LISIN              Reviewed;         467 AA.
AC   Q928K4;
DT   21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Probable glutamate decarboxylase gamma;
DE            Short=GAD-gamma;
DE            EC=4.1.1.15;
GN   OrderedLocusNames=lin2528;
OS   Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=272626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-680 / CLIP 11262;
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}.
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DR   EMBL; AL596172; CAC97755.1; -; Genomic_DNA.
DR   PIR; AC1748; AC1748.
DR   RefSeq; WP_010991237.1; NC_003212.1.
DR   AlphaFoldDB; Q928K4; -.
DR   SMR; Q928K4; -.
DR   STRING; 272626.lin2528; -.
DR   EnsemblBacteria; CAC97755; CAC97755; CAC97755.
DR   KEGG; lin:lin2528; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_019582_2_1_9; -.
DR   OMA; IIWRDES; -.
DR   OrthoDB; 1478871at2; -.
DR   Proteomes; UP000002513; Chromosome.
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; 3.40.640.10; -; 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   PANTHER; PTHR43321; PTHR43321; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Pyridoxal phosphate.
FT   CHAIN           1..467
FT                   /note="Probable glutamate decarboxylase gamma"
FT                   /id="PRO_0000146991"
FT   MOD_RES         278
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   467 AA;  53690 MW;  008AB18F6E274590 CRC64;
     MLYSENDKRK HESYRIPLFG SEEESTSIPK YVLKKEPMEP RIAYQLVKDQ LMDEGNARQN
     LATFCQTYME KEAEILMAET LEKNAIDKSE YPQTAELENR CVNILADLWN APKEMSYLGT
     STVGSSEACM LGGLAMKFRW RNNAEKRGLD IQAKRPNLII SSGYQVCWEK FCVYWDVDMR
     VVPMDKEHLS LDVEKVFELV DEYTIGIVGI LGITYTGKFD DIALLDEKVE AYNEANEHQL
     VIHIDGASGA MFTPFVNPEL PWDFRLKNVV SINTSGHKYG LVYPGVGWIL WKDKEYLPKE
     LIFEVSYLGG SMPTMAINFS RSASQIIGQY YNFLRYGFEG YREIHEKTKK TALYLSKTVE
     KSGYFEIIND GSNLPIVCYK LKDDLDVEWT LYDLADQLLM KGWQVPAYPL PADLSDTIIQ
     RFVCRADLGY NVAEEFAADF ADALHNLEHA RVLYHDKERN DSYGFTH