ID   A0A250VG79_STROL        Unreviewed;       468 AA.
AC   A0A250VG79;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=SO3561_04735 {ECO:0000313|EMBL:GAX53208.1};
OS   Streptomyces olivochromogenes.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1963 {ECO:0000313|EMBL:GAX53208.1, ECO:0000313|Proteomes:UP000217446};
RN   [1] {ECO:0000313|Proteomes:UP000217446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 3561 {ECO:0000313|Proteomes:UP000217446};
RA   Dohra H., Kodani S.;
RT   "Streptomyces olivochromogenes NBRC 3561 whole genome shotgun sequence.";
RL   Submitted (MAY-2017) 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:GAX53208.1}.
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DR   EMBL; BDQI01000009; GAX53208.1; -; Genomic_DNA.
DR   RefSeq; WP_067373740.1; NZ_KQ948460.1.
DR   AlphaFoldDB; A0A250VG79; -.
DR   STRING; 1963.AQJ27_26140; -.
DR   Proteomes; UP000217446; 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:0009058; P:biosynthetic process; IEA:UniProt.
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:UP000217446}.
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         281
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   468 AA;  52287 MW;  9D268A525D03B23B CRC64;
     MPLHQGPEKP DERPVSVNPF FGEANPVGGM TEAPPKHRLP DGPLPPNTAY QVVHDDLMLD
     GNARLNLATF VTTWMEPQAG LLMGECRDKN MIDKDEYPRT AELERRCVAI LADLWNAPDP
     ASTVGCSTTG SSEACMLAGM ALKRRWMRRN ADRYPGARPN LVMGVNVQVC WEKFCNFWEV
     EARQVPMEGD RFHLDPQAAA ELCDENTIGV VGILGSTFDG SYEPIAELCA ALDQLQERTG
     LDIPVHVDGA SGAMIAPFLD PDLVWDFRLP RVSSINTSGH KYGLVYPGVG WALWRTEAEL
     PEELVFRVNY LGGNMPTFAL NFSRPGAQVV AQYYTFLRLG REGFRTVQQT TRDLARGLAE
     RIEALEDFRL LTRGDELPVF AFTTAPHVTA YDVFDVSRRM RESGWLVPAY TFPANREDLS
     VLRVVCRNGF SVDLADLFIE DLSRLVPQLR RLPHPLTLDK EAATGFHH
//