ID   L7KGD4_9ACTN            Unreviewed;       468 AA.
AC   L7KGD4;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 46.
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=GOACH_04_00800 {ECO:0000313|EMBL:GAC47684.1};
OS   Gordonia aichiensis NBRC 108223.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1220583 {ECO:0000313|EMBL:GAC47684.1, ECO:0000313|Proteomes:UP000010988};
RN   [1] {ECO:0000313|EMBL:GAC47684.1, ECO:0000313|Proteomes:UP000010988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 108223 {ECO:0000313|EMBL:GAC47684.1,
RC   ECO:0000313|Proteomes:UP000010988};
RA   Isaki-Nakamura S., Hosoyama A., Tsuchikane K., Ando Y., Baba S., Ohji S.,
RA   Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT   "Whole genome shotgun sequence of Gordonia aichiensis NBRC 108223.";
RL   Submitted (DEC-2012) 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:GAC47684.1}.
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DR   EMBL; BANR01000004; GAC47684.1; -; Genomic_DNA.
DR   RefSeq; WP_005171521.1; NZ_BANR01000004.1.
DR   AlphaFoldDB; L7KGD4; -.
DR   STRING; 1220583.GOACH_04_00800; -.
DR   eggNOG; COG0076; Bacteria.
DR   OrthoDB; 3401800at2; -.
DR   Proteomes; UP000010988; 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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010988}.
FT   MOD_RES         281
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   468 AA;  52501 MW;  D31F848137605822 CRC64;
     MFQTHHTHSR FKTNINDSLA LPVFSRDGEA TTISKFAIPA EPMLPETAYQ IVHDEAILDG
     NARLNLATFV TTWMDDHANR IYAETYDKNS IDKDEYPATA AIEERCWKIM ADLWHAPDPT
     NTIGTSTVGS SDACMFGGLA LKRKWQERRK AEGKPTDKPN LVLSAAVQVC WEKFCNYWDV
     EARFVPCTPE HVLFDGTDLE KYVDENTIGV VAIMGVTYNG LYEPVKKIAA KLDEIEKDTG
     LDIKIHVDGA SGGFIAPFCQ PELEWDFRVP RVVSINTSGH KFGLVYPGIG WVVWRDKEAL
     PESLVFHVSY LGGDMPTLAL PFSRPGAQIL LQYYNFLRLG FEGYRQVQQG SLDVAQYLSK
     HIGEMAPFEL ISKGDTIPVF AWKLKDGYTD KWTLYDLADR LRLSGWLVPA YPMADNMSDL
     TLQRIVVKNG MSHDLATALL TEITTQVAFL DDLTGPLPKE GQHPGFSH
//