ID   D7GH26_PROFC            Unreviewed;       470 AA.
AC   D7GH26;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 67.
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:CBL57837.1};
GN   OrderedLocusNames=PFREUD_23230 {ECO:0000313|EMBL:CBL57837.1};
OS   Propionibacterium freudenreichii subsp. shermanii (strain ATCC 9614 / DSM
OS   4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1).
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Propionibacterium.
OX   NCBI_TaxID=754252 {ECO:0000313|EMBL:CBL57837.1, ECO:0000313|Proteomes:UP000000936};
RN   [1] {ECO:0000313|EMBL:CBL57837.1, ECO:0000313|Proteomes:UP000000936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9614 / DSM 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1
RC   {ECO:0000313|Proteomes:UP000000936};
RX   PubMed=20668525; DOI=10.1371/journal.pone.0011748;
RA   Falentin H., Deutsch S.M., Jan G., Loux V., Thierry A., Parayre S.,
RA   Maillard M.B., Dherbecourt J., Cousin F.J., Jardin J., Siguier P.,
RA   Couloux A., Barbe V., Vacherie B., Wincker P., Gibrat J.F., Gaillardin C.,
RA   Lortal S.;
RT   "The complete genome of Propionibacterium freudenreichii CIRM-BIA1, a hardy
RT   actinobacterium with food and probiotic applications.";
RL   PLoS ONE 5:E11748-E11748(2010).
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; FN806773; CBL57837.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7GH26; -.
DR   STRING; 754252.PFREUD_23230; -.
DR   KEGG; pfr:PFREUD_23230; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_019582_2_2_11; -.
DR   Proteomes; UP000000936; 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   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:UP000000936}.
FT   MOD_RES         283
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   470 AA;  52989 MW;  E04DC3333C758069 CRC64;
     MNDPTRHPAY SIDRSQLGAV EINPVFARPA EATEFSKFRL PASESLPETA YQVVHDEAML
     DGNARLNLAT FVGTWMDDYA NRLYAESADK NMIDKDEYPK TAEIETRCWM MLADLWHAPD
     PDNTIGTSTI GSSEACMLGG LALKRRWQHA RKAAGKPTDH PNMVMSSAVQ VCWEKFCNYW
     DIEPRYVPIS EDHKVLDGAN LADYVDENTI GVVAIMGVTY TGMYEPVKQI AAALDEIQER
     TGLDVKIHVD AASGGMIAPF IQPDLEWDFR IERVASINTS GHKYGLVYPG LGWVVWRSVD
     DLPEDLIFKV SYLGGDMPTF ALNFSRPGAQ VLLQYYMFLR LGMDGFRRVQ ANSHDVAKFL
     SSQIGAMDDF ELWNDGSDIP VFAWRLKDRP NRKWDLYDLS ERLRTRGWLV PAYPMPADLT
     DVTVQRIVVR NGLSHDLADA FLESMRAEVA YLDALPAPMP SQHKQSGFHH
//