DCEC_LISMO
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 03-AUG-2022, entry version 100.
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; Firmicutes; 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}.
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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.lmo2434; -.
DR PaxDb; Q8Y4K4; -.
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 OMA; IIWRDES; -.
DR PhylomeDB; Q8Y4K4; -.
DR BioCyc; LMON169963:LMO2434-MON; -.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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 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; 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