ID   Q9X8J5_STRCO            Unreviewed;       475 AA.
AC   Q9X8J5;
DT   01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 129.
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=gad {ECO:0000313|EMBL:CAB42769.1};
GN   OrderedLocusNames=SCO3416 {ECO:0000313|EMBL:CAB42769.1};
GN   ORFNames=SCE9.23 {ECO:0000313|EMBL:CAB42769.1};
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226 {ECO:0000313|EMBL:CAB42769.1, ECO:0000313|Proteomes:UP000001973};
RN   [1] {ECO:0000313|EMBL:CAB42769.1, ECO:0000313|Proteomes:UP000001973}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145
RC   {ECO:0000313|Proteomes:UP000001973};
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.H.,
RA   Kieser T., Larke L., Murphy L., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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; AL939116; CAB42769.1; -; Genomic_DNA.
DR   PIR; T36342; T36342.
DR   RefSeq; NP_627622.1; NC_003888.3.
DR   RefSeq; WP_011028961.1; NZ_VNID01000023.1.
DR   AlphaFoldDB; Q9X8J5; -.
DR   STRING; 100226.gene:17761038; -.
DR   PaxDb; 100226-SCO3416; -.
DR   PATRIC; fig|100226.15.peg.3479; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_019582_2_1_11; -.
DR   InParanoid; Q9X8J5; -.
DR   OrthoDB; 3401800at2; -.
DR   PhylomeDB; Q9X8J5; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
DR   GO; GO:0006538; P:glutamate catabolic process; IBA:GO_Central.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001973}.
FT   MOD_RES         288
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   475 AA;  52651 MW;  9A5D7017FF8281AA CRC64;
     MSLHQGPRPS RDSDRDRRRL AVNPFHAAAN PLGGMTEAPP AHRLPDSPLP PESAYRLVHD
     ELMLDGNARL NLATFVTTWM EPQAGVLMSE CRDKNMIDKD EYPRTAELER RCVAMLADLW
     HAPDPSTAVG CSTTGSSEAC MLAGMALKRR WALRNADRYP AKDVRPNLVM GVNVQVCWDK
     FCNFWEVEAR QVPMEGDRFH LDPQAAAELC DENTIGVVGI LGSTFDGSYE PVADLCAALD
     ALQERTGLDV PVHVDGASGA MVAPFLDEDL VWDFRLPRVA SINTSGHKYG LVYPGVGWAL
     WRDAEALPEE LVFRVNYLGG DMPTFALNFS RPGAQVVAQY YNFLRLGREG YRAVQQSARD
     IAGSLAERVA ALGDFRLLTR GDQLPVFAFT TADDVTAYDV FDVSRRLREG GWLVPAYTFP
     PHREDLSVLR VVCRNGFSAD MADLLLADLE RLLPELRRQP GPLTRDKGAA TGFHH
//