ID   Q0SRB9_CLOPS            Unreviewed;       466 AA.
AC   Q0SRB9;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 104.
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=CPR_2029 {ECO:0000313|EMBL:ABG85385.1};
OS   Clostridium perfringens (strain SM101 / Type A).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=289380 {ECO:0000313|EMBL:ABG85385.1, ECO:0000313|Proteomes:UP000001824};
RN   [1] {ECO:0000313|EMBL:ABG85385.1, ECO:0000313|Proteomes:UP000001824}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM101 / Type A {ECO:0000313|Proteomes:UP000001824};
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., Deboy R.T.,
RA   Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA   Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA   Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA   Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA   Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA   Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT   Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(2006).
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; CP000312; ABG85385.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0SRB9; -.
DR   KEGG; cpr:CPR_2029; -.
DR   BioCyc; CPER289380:GI76-2040-MONOMER; -.
DR   Proteomes; UP000001824; 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         276
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   466 AA;  53200 MW;  141317A798F66613 CRC64;
     MLFGKNELGS QFETPIFGTV ESNEPIPKYK LAKKSIAPQV AYRLIKDDLL DEGNARQNLA
     TFCQTYMDDE AVKLMSETLE KNAIDKSEYP QTTDMENRCV NILADLWHAP KELNYMGTST
     VGSSEACMLG GMAMKFRWRN RAKALGMDVT SKKPNLVISS GYQVCWEKFC VYWDIEMRLV
     PMDEQHMSIN VDKVLDYVDD YTIGVVGILG ITYTGKYDDI KALDKKLEEY NKTAKITVPI
     HVDGASGAMF APFIEPDLKW DFQLKNVVSI STSGHKYGLV YPGIGWVLWK DKEYLPQELV
     FEVSYLGGKM PTMAINFSRS ASQILGQYYN FLRYGFEGYR QIHQRTKDVA MYLSSELEKT
     GLFEIYNNGE NLPIVCYKLK DDVKVNWTLY DLADRLLMKG WQVPAYPLPE DLQNVIIQRF
     VCRADLSRNL ADLLMRDLKA AIEDLNNARI LSKTQVDNKG VQGFTH
//