ID   E3GJR7_9FIRM            Unreviewed;       472 AA.
AC   E3GJR7; A0A1M7EY18;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 71.
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=ELI_0972 {ECO:0000313|EMBL:ADO35975.1};
GN   ORFNames=H0N91_19950 {ECO:0000313|EMBL:NZA40337.1},
GN   SAMN04487888_101674 {ECO:0000313|EMBL:SFO37374.1};
OS   Eubacterium callanderi.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=53442 {ECO:0000313|EMBL:ADO35975.1, ECO:0000313|Proteomes:UP000006873};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KIST612;
RA   Roh H., Ko H.-J., Kim D., Choi D.G., Park S., Kim S., Kim K.H., Chang I.S.,
RA   Choi I.-G.;
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADO35975.1, ECO:0000313|Proteomes:UP000006873}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIST612 {ECO:0000313|EMBL:ADO35975.1,
RC   ECO:0000313|Proteomes:UP000006873};
RX   PubMed=21036996; DOI=10.1128/JB.01217-10;
RA   Roh H., Ko H.J., Kim D., Choi D.G., Park S., Kim S., Chang I.S., Choi I.G.;
RT   "Complete genome sequence of a carbon monoxide-utilizing acetogen,
RT   Eubacterium limosum KIST612.";
RL   J. Bacteriol. 193:307-308(2011).
RN   [3] {ECO:0000313|EMBL:SFO37374.1, ECO:0000313|Proteomes:UP000199443}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NLAE-zl-G225 {ECO:0000313|EMBL:SFO37374.1,
RC   ECO:0000313|Proteomes:UP000199443};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:NZA40337.1, ECO:0000313|Proteomes:UP000586254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMC0717 {ECO:0000313|EMBL:NZA40337.1,
RC   ECO:0000313|Proteomes:UP000586254};
RA   Marsh A.J., Azcarate-Peril M.A.;
RT   "Organ Donor 1.";
RL   Submitted (JUL-2020) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002273; ADO35975.1; -; Genomic_DNA.
DR   EMBL; JACCKS010000045; NZA40337.1; -; Genomic_DNA.
DR   EMBL; FOWI01000001; SFO37374.1; -; Genomic_DNA.
DR   RefSeq; WP_013379297.1; NZ_JAQEYK010000002.1.
DR   AlphaFoldDB; E3GJR7; -.
DR   GeneID; 68362309; -.
DR   KEGG; elm:ELI_0972; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_019582_2_1_9; -.
DR   Proteomes; UP000006873; Chromosome.
DR   Proteomes; UP000199443; Unassembled WGS sequence.
DR   Proteomes; UP000586254; Unassembled WGS sequence.
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}.
FT   MOD_RES         280
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   472 AA;  54332 MW;  9A32576151576E1E CRC64;
     MLYSKDDQDK LKDRYLTPIF GTEASDEPLP KYKLRKDPVE PEVAYRLIKD DLLDEGSARL
     NLSTFCQTYM EPEATKIMAE TLEKNAIDKS EYPQTTELEN RCVNMIADLW HAPDDEKFLG
     TSTVGSSEAC MLGGMAMKFR WRNNAIKQGL DVKAKKPNLV ISSGYQVCWE KFCVYWDIEM
     RLVPLDEQHM SMNMDTVMDF VDEYTIGIVG IMGITYTGKF DDIKALDTLV EDYNQKNPKF
     PIYIHVDGAS GGMFAPFIEP DLEWDFRLKN VVSINTSGHK YGLVYPGIGW VLWRDEKWLP
     KELIFSVSYL GGSLPTMAIN FSRSASQIIG QYYNFLRYGY EGYKKIHERT RDVAMYISKE
     LEKTGLFEIY NDGSNLPIVC WKMKKDANKE WNLYDLADRI RMKGWQVPAY PLPENLQDDI
     IQRVVVRADL SEQLGVLLME DMNRAIKELD EAHILPHGGD QVNNKGVYGF TH
//