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Database: UniProt
Entry: A0A172Q5N5_9STRE
LinkDB: A0A172Q5N5_9STRE
Original site: A0A172Q5N5_9STRE 
ID   A0A172Q5N5_9STRE        Unreviewed;       467 AA.
AC   A0A172Q5N5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 39.
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=A0O21_01275 {ECO:0000313|EMBL:AND78757.1};
OS   Streptococcus pantholopis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1811193 {ECO:0000313|EMBL:AND78757.1, ECO:0000313|Proteomes:UP000077317};
RN   [1] {ECO:0000313|EMBL:AND78757.1, ECO:0000313|Proteomes:UP000077317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TA 26 {ECO:0000313|EMBL:AND78757.1,
RC   ECO:0000313|Proteomes:UP000077317};
RX   PubMed=27226124; DOI=10.1099/ijsem.0.001189;
RA   Bai X., Xiong Y., Lu S., Jin D., Lai X., Yang J., Niu L., Hu S., Meng X.,
RA   Pu J., Ye C., Xu J.;
RT   "Streptococcuspantholopis sp. nov., isolated from faeces of the Tibetan
RT   antelope (Pantholops hodgsonii).";
RL   Int. J. Syst. Evol. Microbiol. 66:3281-3286(2016).
RN   [2] {ECO:0000313|Proteomes:UP000077317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TA 26 {ECO:0000313|Proteomes:UP000077317};
RA   Bai X.;
RT   "Streptococcus antelopensis sp. nov., isolated from the feces of the
RT   Tibetan antelope (Pantholops hodgsonii) in Hoh Xil National Nature Reserve,
RT   Qinghai, China.";
RL   Submitted (MAR-2016) 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}.
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DR   EMBL; CP014699; AND78757.1; -; Genomic_DNA.
DR   RefSeq; WP_067060278.1; NZ_CP014699.1.
DR   AlphaFoldDB; A0A172Q5N5; -.
DR   STRING; 1811193.A0O21_01275; -.
DR   KEGG; spat:A0O21_01275; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000077317; Chromosome.
DR   GO; GO:0004058; F:aromatic-L-amino-acid decarboxylase activity; IEA:UniProt.
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:UP000077317}.
FT   MOD_RES         278
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   467 AA;  53587 MW;  8F5771234F1E8D47 CRC64;
     MALYGKHNQE KHDVLSPIFG SVSEDHDLPK YKLNQTPVEP RIAYQVIKDQ LLDEGNARLN
     LATFCQTYME PEAIQLMSET LEKNAIDKSE YPRTAEIENR CVNMMADLWH AQPEEEFLGT
     STVGSSEACM LGGLAMKFAW RKRAESLGLD TSAQKPNLVI STGYQVCWEK FCTYWDIELR
     TVPMDKEHQS LNMETVMDYV DPYTIGIVGI MGITYTGRYD NIKQLNDLVE AYNSHTDFKV
     YIHVDAASGG FYAPFMEPEI AWDFRLKNVI SINTSGHKYG LVYPGIGWIL WRDKAFLPEE
     LIFRVSYLGG EIPTMAINFS RSASQIIGQY YNFIRYGYDG YRAIHQRTHD VALYLAKEIK
     ALDCFEMVND GAHLPIICYK QKDAKQQEWT LYDLADRLAM KGWQVPAYPL PADLDQTEVQ
     RLVVRADFGM GMAHDYIEDM KAAIADLDRA HILFHEKKEI KNYGFTH
//
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