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Database: UniProt/TrEMBL
Entry: X7ZRX9_MYCKA
LinkDB: X7ZRX9_MYCKA
Original site: X7ZRX9_MYCKA 
ID   X7ZRX9_MYCKA            Unreviewed;       460 AA.
AC   X7ZRX9;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 51.
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   ORFNames=I545_0106 {ECO:0000313|EMBL:EUA21463.1};
OS   Mycobacterium kansasii 662.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1299326 {ECO:0000313|EMBL:EUA21463.1, ECO:0000313|Proteomes:UP000020561};
RN   [1] {ECO:0000313|EMBL:EUA21463.1, ECO:0000313|Proteomes:UP000020561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=662 {ECO:0000313|EMBL:EUA21463.1,
RC   ECO:0000313|Proteomes:UP000020561};
RA   Brown-Elliot B., Wallace R., Lenaerts A., Ordway D., DeGroote M.A.,
RA   Parker T., Sizemore C., Tallon L.J., Sadzewicz L.K., Sengamalay N.,
RA   Fraser C.M., Hine E., Shefchek K.A., Das S.P., Tettelin H.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EUA21463.1}.
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DR   EMBL; JAOA01000001; EUA21463.1; -; Genomic_DNA.
DR   RefSeq; WP_023371123.1; NZ_JAOA01000001.1.
DR   AlphaFoldDB; X7ZRX9; -.
DR   GeneID; 29701905; -.
DR   PATRIC; fig|1299326.3.peg.104; -.
DR   Proteomes; UP000020561; Unassembled WGS sequence.
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         277
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   460 AA;  50823 MW;  25F7B2319BAABAA9 CRC64;
     MSRSHPSVPA HSIAPAYTGR MFTAPIPALR LPEESMDPEA AYQFIHDELM LDGSSRLNLA
     TFVTTWMDPE AGQLMAETFD KNMIDKDEYP ATAAIESRCV SMVADLFHAE GLRDDDPGSA
     TGVSTIGSSE AVMLGGLAMK WRWRARTKDW KGRTPNLVMG SNVQVVWEKF CRYFDVEPRY
     LPMEKGRYVI TPEQVIDAVD EDTIGVVAIL GTTYTGELEP VAEICAALDG LAARGGVDVP
     VHVDAASGGF VVPFLHPDLQ WDFRLPRVVS INVSGHKYGL TYPGVGFVVW RGPEYLPEEL
     VFRVNYLGGD MPTFTLNFSR PGNQVVGQYY NFLRLGREGY TKVMQALSQT ARWLGEQLEG
     AEHCELISDG SAIPVVAFRL AGDRGYTEFD LSHELRTCGW QVPAYTMPDN ATDISVLRIV
     VREGLSADLA RALHDDISTA VRTLDKVKPG GHYDAQHFAH
//
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