ID W0P1N8_LACPN Unreviewed; 469 AA.
AC W0P1N8;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
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 Name=gadB {ECO:0000313|EMBL:AHG59384.1};
OS Lactiplantibacillus plantarum (Lactobacillus plantarum).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=1590 {ECO:0000313|EMBL:AHG59384.1};
RN [1] {ECO:0000313|EMBL:AHG59384.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Taj-Apis362 {ECO:0000313|EMBL:AHG59384.1};
RX PubMed=25757029; DOI=10.1111/1751-7915.12254;
RA Tajabadi N., Baradaran A., Ebrahimpour A., Rahim R.A., Bakar F.A.,
RA Manap M.Y., Mohammed A.S., Saari N.;
RT "Overexpression and optimization of glutamate decarboxylase in
RT Lactobacillus plantarum?Taj-Apis362 for high gamma-aminobutyric acid
RT production.";
RL Microb. Biotechnol. 8:623-632(2015).
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; KF770955; AHG59384.1; -; Genomic_DNA.
DR AlphaFoldDB; W0P1N8; -.
DR SMR; W0P1N8; -.
DR BRENDA; 4.1.1.15; 2849.
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 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 280
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 469 AA; 53590 MW; E24F43A974B7D292 CRC64;
MAMLYGKHNH EAEEYLEPVF GAPSEQHDLP KYRLPKHSLS PREADRLVRD ELLDEGNSRL
NLATFCQTYM EPEAVELMKD TLAKNAIDKS EYPRTAEIEN RCVYIIANLW HAPDDEHFTG
TSTIGSSEAC MLGGLAMKFA WRKRAQAAGL DLNAHRPNLV ISAGYQVCWE KFCIYWDVDM
HVVPMDEQHM ALDVNHVLDY VDEYTIGIVG IMGITYTGQH DDLAALDKVV THYNHQHPKL
PVYIHVDAAS GGFYTPFIEP QLIWDFRLAN VVSINASGHK YGLVYPGVGW VVWRDRQFLP
PELVFKVSYL GGELPTMAIN FSHSAAQLIG QYYNFIRFGM DGYREIQTKT HDVARYLAAA
LDKVGEFKMI NNGHQLPLIC YQLAPREDRE WTLYDLSDRL LMNGWQVPTY PLPANLEQQV
IQRIVVRADF GVNMAHDFMD DLTEAVHDLN HAHIVYHHDA APKKYGFTH
//
