ID   K7RXC8_ACIA4            Unreviewed;       468 AA.
AC   K7RXC8;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 56.
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   OrderedLocusNames=PACID_18390 {ECO:0000313|EMBL:AFV89643.1};
OS   Acidipropionibacterium acidipropionici (strain ATCC 4875 / DSM 20272 / JCM
OS   6432 / NBRC 12425 / NCIMB 8070 / 4) (Propionibacterium acidipropionici).
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Acidipropionibacterium.
OX   NCBI_TaxID=1171373 {ECO:0000313|EMBL:AFV89643.1, ECO:0000313|Proteomes:UP000000214};
RN   [1] {ECO:0000313|EMBL:AFV89643.1, ECO:0000313|Proteomes:UP000000214}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 4875 / DSM 20272 / JCM 6432 / NBRC 12425 / NCIMB 8070
RC   {ECO:0000313|Proteomes:UP000000214};
RX   PubMed=23083487; DOI=10.1186/1471-2164-13-562;
RA   Parizzi L.P., Grassi M.C., Llerena L.A., Carazzolle M.F., Queiroz V.L.,
RA   Lunardi I., Zeidler A.F., Teixeira P.J., Mieczkowski P., Rincones J.,
RA   Pereira G.A.;
RT   "The genome sequence of Propionibacterium acidipropionici provides insights
RT   into its biotechnological and industrial potential.";
RL   BMC Genomics 13:562-562(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; CP003493; AFV89643.1; -; Genomic_DNA.
DR   RefSeq; WP_015070547.1; NC_019395.1.
DR   AlphaFoldDB; K7RXC8; -.
DR   STRING; 1171373.PACID_18390; -.
DR   KEGG; pbo:PACID_18390; -.
DR   PATRIC; fig|1171373.8.peg.1818; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_019582_2_2_11; -.
DR   Proteomes; UP000000214; 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}.
FT   MOD_RES         281
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   468 AA;  52772 MW;  557D991E128D3668 CRC64;
     MTPHRISGQQ RHRKASPVEL NPVFVRPGES SEVPKMRIPR DESLPETAYQ IVHDEAMLDG
     NARLNLATFV GTWMEDEANR LYLEAADKNM IDKDEYPRTA EIESRCATML ADLWHAPDPE
     RAVGTSTIGS SEACMLAGLA LKRRWQHARR AAGKPADRPN LVMSSAVQVC WEKFCNYWDV
     EMRQVPVSME HKVLDGDGLD GYVDENTIGV VAILGVTYTG MYEPVARIAE ALDRIQARTG
     LDVKIHVDGA SGAMVAPFIQ PELEWDFRVD RVVSINTSGH KYGLVYPGLG WIVWREAQCL
     PEDLVFRVSY LGGDMPTFAL NFSRPGAQVL LQYYLFLRLG FTGYRRVQQT CSDVATYLAR
     EIGSMPAFDL WNDGSDIPVF AWRLHRGHTE NWTLHHLGDR LRMRGWLVPA YPMPADLEEI
     TVQRVVVRNG FSRDMADAFL ADLREEVGYL DSLDSPMPGT GHPQAFHH
//