ID   J9Z8Y3_LEPFM            Unreviewed;       457 AA.
AC   J9Z8Y3;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, 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=LFML04_0731 {ECO:0000313|EMBL:AFS52965.1};
OS   Leptospirillum ferriphilum (strain ML-04).
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Leptospirillum.
OX   NCBI_TaxID=1048260 {ECO:0000313|EMBL:AFS52965.1, ECO:0000313|Proteomes:UP000006177};
RN   [1] {ECO:0000313|EMBL:AFS52965.1, ECO:0000313|Proteomes:UP000006177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ML-04 {ECO:0000313|EMBL:AFS52965.1,
RC   ECO:0000313|Proteomes:UP000006177};
RX   PubMed=22203551; DOI=10.1007/s12275-011-1099-9;
RA   Mi S., Song J., Lin J., Che Y., Zheng H., Lin J.;
RT   "Complete genome of Leptospirillum ferriphilum ML-04 provides insight into
RT   its physiology and environmental adaptation.";
RL   J. Microbiol. 49:890-901(2011).
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; CP002919; AFS52965.1; -; Genomic_DNA.
DR   RefSeq; WP_014960475.1; NC_018649.1.
DR   AlphaFoldDB; J9Z8Y3; -.
DR   STRING; 1048260.LFML04_0731; -.
DR   KEGG; lfi:LFML04_0731; -.
DR   PATRIC; fig|1048260.3.peg.790; -.
DR   HOGENOM; CLU_019582_2_2_0; -.
DR   Proteomes; UP000006177; 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         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
//