ID   H6MZ78_GORPV            Unreviewed;       469 AA.
AC   H6MZ78;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 66.
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:AFA74414.1};
GN   OrderedLocusNames=GPOL_c34020 {ECO:0000313|EMBL:AFA74414.1};
OS   Gordonia polyisoprenivorans (strain DSM 44266 / VH2).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1112204 {ECO:0000313|EMBL:AFA74414.1, ECO:0000313|Proteomes:UP000009154};
RN   [1] {ECO:0000313|EMBL:AFA74414.1, ECO:0000313|Proteomes:UP000009154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44266 / VH2 {ECO:0000313|Proteomes:UP000009154};
RX   PubMed=22327575; DOI=10.1128/AEM.07969-11;
RA   Hiessl S., Schuldes J., Thurmer A., Halbsguth T., Broker D., Angelov A.,
RA   Liebl W., Daniel R., Steinbuchel A.;
RT   "Involvement of two latex-clearing proteins during rubber degradation and
RT   insights into the subsequent degradation pathway revealed by the genome
RT   sequence of Gordonia polyisoprenivorans strain VH2.";
RL   Appl. Environ. Microbiol. 78:2874-2887(2012).
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; CP003119; AFA74414.1; -; Genomic_DNA.
DR   RefSeq; WP_006368665.1; NC_016906.1.
DR   AlphaFoldDB; H6MZ78; -.
DR   STRING; 1112204.GPOL_c34020; -.
DR   KEGG; gpo:GPOL_c34020; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_019582_2_1_11; -.
DR   Proteomes; UP000009154; Chromosome.
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:UP000009154}.
FT   MOD_RES         282
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   469 AA;  52747 MW;  8DC00C09F3DC7A29 CRC64;
     MTKRKHTNAR ATTNLNDSLT VNPVFVRPGE ATEYPKFAIP ESMSLPETAY QIVHDEAMLD
     GNARLNLATF VSTWMDDEAR RLYAETYDKN MIDKDEYPQT AAIEDRCWKI IADLWHVPDV
     DKSIGTSTIG SSEAAMLGGL ALKRHWQARR KAEGKSIEKP NLVLSTAVQV CWEKFLNYFE
     VEPRWVPVSQ EHFVFDGHEL ETYVDENTIG VVAILGVTYN GLYEPVQQIS AKLDEIEKNT
     GLDVKIHVDG ASGAMVAPFC QPDLEWDFRV SRVVSINTSG HKYGLVYPGL GWIVWRDSEA
     LPESMVFHCS YLGGDMPTLA LNFSRPGAQV LLQYYNFLRL GREGYRLIQQ GSIDVATYLS
     SAIAEMGPFE LVSKGDTIPV FAWKLKDGYT DKWSLYDLSD RLRLKGWLVP AYPMADGLAD
     WTLQRIVVRA GLSHDLATAL LTDLESEVAF LDQLESPMPR EGTGSHFHH
//