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
//