ID   A0A059XY27_9BACT        Unreviewed;       457 AA.
AC   A0A059XY27;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 43.
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=Y981_02970 {ECO:0000313|EMBL:AIA30132.1};
OS   Leptospirillum ferriphilum YSK.
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Leptospirillum.
OX   NCBI_TaxID=1441628 {ECO:0000313|EMBL:AIA30132.1, ECO:0000313|Proteomes:UP000027059};
RN   [1] {ECO:0000313|Proteomes:UP000027059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YSK {ECO:0000313|Proteomes:UP000027059};
RA   Guo X., Yin H., Liang Y., Hu Q., Ma L., Xiao Y., Zhang X., Qiu G., Liu X.;
RT   "Complete genome sequence and comparative genomic analysis of the nitrogen-
RT   fixing bacterium Leptospirillum ferriphilum YSK.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AIA30132.1, ECO:0000313|Proteomes:UP000027059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YSK {ECO:0000313|EMBL:AIA30132.1,
RC   ECO:0000313|Proteomes:UP000027059};
RX   PubMed=26064886; DOI=10.1155/2015/203197;
RA   Jiang H., Liang Y., Yin H., Xiao Y., Guo X., Xu Y., Hu Q., Liu H., Liu X.;
RT   "Effects of Arsenite Resistance on the Growth and Functional Gene
RT   Expression of Leptospirillum ferriphilum and Acidithiobacillus thiooxidans
RT   in Pure Culture and Coculture.";
RL   Biomed. Res. Int. 2015:203197-203197(2015).
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; CP007243; AIA30132.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059XY27; -.
DR   KEGG; lfp:Y981_02970; -.
DR   HOGENOM; CLU_019582_2_2_0; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000027059; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027059}.
FT   MOD_RES         276
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   457 AA;  51800 MW;  385010175AA335DD CRC64;
     MLTRRRHSQT RDDSLSATYG NRFFTKDLKT FRMGEDSLPP ASVYQIIHDE LELDGNPSLN
     LASFVTTWME PEAEQLIREN LRKNLVDQSE YPRTGEIQHR VIHMLADLFH APDDADIAGT
     STIGSSEAIL LGLLAHKKSW QNRRKTAGKP ADRPNLVLGG EVHVVWDKFA RYFDVELRTV
     PLSPARFTLD VQEAVRRIDE NTIAVGAVVG TTFTGQIDPV EELNEAVEKK NREQGWRVPI
     HVDGASGGLI LPFLEPERRW DFRLSAVRSI NVSGHKFGLV YPGVGWLLFR DRKDLPDDLV
     FRVNYLGAEE ETYTLNFSSN AAFVIAQYYN LLRLGKKGYR SIMENCRDNA RFLAKELAAG
     KTFEPVEKKP LLPIVAFRLR GKHAGREPEI ASELRKYGWI VPAYTLPPDA ENITLLRVVV
     RENVSRQMLV ELLAHLDRCA GILENPATKR KTHPPLC
//