ID   G2ZF39_LISIP            Unreviewed;       467 AA.
AC   G2ZF39;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, 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   OrderedLocusNames=LIV_2340 {ECO:0000313|EMBL:CBW86835.1};
OS   Listeria ivanovii (strain ATCC BAA-678 / PAM 55).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=881621 {ECO:0000313|EMBL:CBW86835.1, ECO:0000313|Proteomes:UP000001286};
RN   [1] {ECO:0000313|EMBL:CBW86835.1, ECO:0000313|Proteomes:UP000001286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-678 / PAM 55 {ECO:0000313|Proteomes:UP000001286};
RX   PubMed=22072644; DOI=10.1128/JB.06120-11;
RA   Buchrieser C., Rusniok C., Garrido P., Hain T., Scortti M., Lampidis R.,
RA   Karst U., Chakraborty T., Cossart P., Kreft J., Vazquez-Boland J.A.,
RA   Goebel W., Glaser P.;
RT   "Complete genome sequence of the animal pathogen Listeria ivanovii, which
RT   provides insights into host specificities and evolution of the genus
RT   Listeria.";
RL   J. Bacteriol. 193:6787-6788(2011).
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|ARBA:ARBA00000018,
CC         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; FR687253; CBW86835.1; -; Genomic_DNA.
DR   RefSeq; WP_014093652.1; NZ_CVPH01000006.1.
DR   AlphaFoldDB; G2ZF39; -.
DR   GeneID; 57077365; -.
DR   KEGG; liv:LIV_2340; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_019582_2_1_9; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000001286; Chromosome.
DR   GO; GO:0004058; F:aromatic-L-amino-acid decarboxylase activity; IEA:UniProt.
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   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 {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}.
FT   MOD_RES         278
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   467 AA;  53684 MW;  BA4EE017138E81E7 CRC64;
     MLYSENDKRK HESYRIPLFG SEEESTSIPK YVLKKEPMEP RIAYQLVKDQ LMDEGNARQN
     LATFCQTYME EEAQLLMAET LEKNAIDKSE YPQTAELENR CVNILADLWN APKEMAYLGT
     STVGSSEACM LGGLAMKFRW RKNAEKRGLD IQAKRPNLII SSGYQVCWEK FCVYWDIDMR
     VIPMDKEHLS LDVDRVFDFV DDYTIGIVGI LGITYTGKFD DIALLDEKVE AYNEANEHQL
     VIHVDGASGA MFTPFVNPEL PWDFRLKNVV SINTSGHKYG LVYPGVGWIL WKDKEYLPEE
     LIFEVSYLGG SMPTMAINFS RSASQIIGQY YNFLRFGFEG YREIHEKTKK TALYLAKTVE
     KSGYFEIIND GSNLPIVCYK MKEDLDVEWT LYDLADQLLM KGWQVPAYPL PTDLSDTIIQ
     RFVCRADLGH NVAEEFASDF HAAIKNLEHA RVLYHDKGRN DSYGFTH
//