ID   G2ZEY7_LISIP            Unreviewed;       464 AA.
AC   G2ZEY7;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 69.
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_2275 {ECO:0000313|EMBL:CBW86770.1};
OS   Listeria ivanovii (strain ATCC BAA-678 / PAM 55).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=881621 {ECO:0000313|EMBL:CBW86770.1, ECO:0000313|Proteomes:UP000001286};
RN   [1] {ECO:0000313|EMBL:CBW86770.1, 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; CBW86770.1; -; Genomic_DNA.
DR   RefSeq; WP_014093602.1; NZ_CVPH01000006.1.
DR   AlphaFoldDB; G2ZEY7; -.
DR   GeneID; 57077283; -.
DR   KEGG; liv:LIV_2275; -.
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         275
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   464 AA;  53503 MW;  2FF58EF5F2A1520A CRC64;
     MLYSKENQES YLEPIFGSSA EDCDIPKYTL GKEPLEPRIA YRLVKDELLD EGSARQNLAT
     FCQTYMEDEA TKLMSETLEK NAIDKSEYPR TAELENRCVN IIADLWHAPK EQKFMGTSTI
     GSSEACMLGG MAMKFAWRNR AEKLGLDIHA KKPNLVISSG YQVCWEKFCV YWDIDMRVVP
     MDRDHMQLNT DQVLDYIDEY TIGVVGILGI TYTGRYDDIY ALNEKIEQYN SQTDYKVYIH
     VDAASGGFFT PFVEPDIIWD FRLKNVISIN TSGHKYGLVY PGIGWVLWKD ESYLPKELIF
     KVSYLGGEMP TMQINFSRSA SHIIGQYYNF LRYGFEGYRT IHQKTSDVAQ YLANAVEATG
     YFDIYNDGSH LPIVCYKLKE DANVDWTLYD LADRLQMRGW QVPAYPLPKN LENIIIQRYV
     CRADLGFNMA EEFIQDFNAS IHELNNAHIL FHNKQQSGVH GFTH
//