ID   E6U2L0_ETHHY            Unreviewed;       465 AA.
AC   E6U2L0;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 69.
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=Ethha_0732 {ECO:0000313|EMBL:ADU26301.1};
OS   Ethanoligenens harbinense (strain DSM 18485 / JCM 12961 / CGMCC 1.5033 /
OS   YUAN-3).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ethanoligenens.
OX   NCBI_TaxID=663278 {ECO:0000313|EMBL:ADU26301.1, ECO:0000313|Proteomes:UP000001551};
RN   [1] {ECO:0000313|EMBL:ADU26301.1, ECO:0000313|Proteomes:UP000001551}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18485 / JCM 12961 / CGMCC 1.5033 / YUAN-3
RC   {ECO:0000313|Proteomes:UP000001551};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Misra M., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., Wang A.,
RA   Mouttaki H., He Z., Zhou J., Hemme C.L., Woyke T.;
RT   "Complete sequence of Ethanoligenens harbinense YUAN-3.";
RL   Submitted (DEC-2010) 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; CP002400; ADU26301.1; -; Genomic_DNA.
DR   RefSeq; WP_013484671.1; NZ_CP025286.1.
DR   AlphaFoldDB; E6U2L0; -.
DR   STRING; 663278.Ethha_0732; -.
DR   KEGG; eha:Ethha_0732; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_019582_2_1_9; -.
DR   Proteomes; UP000001551; 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:UP000001551}.
FT   MOD_RES         277
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   465 AA;  52801 MW;  63A6B55839100641 CRC64;
     MLHQNKNNEK LQKIHPANTL SLYDDVDIPK YTLRKQPIEP DVACRLIKNE LLDEGNARLN
     LATFCSTFME DEAIRLMADT LEKNAIDKSE YPSTIELENR CVNIIADLWH APENQFIGTS
     TVGSSEACML AGLAMKFRWR NRAQRLGLDI CEKKPNLVIS SGYQVCWEKF CVYWDVELRA
     VPMDPEHLSL DVNAAIRAVD AYTIGIVGIL GQTYTGKFDD IRLLDKAVGQ YNSQTEETVY
     IHVDAASGGL FAPFSQPELE WDFRLENVVS INTSGHKYGL VYPGIGWVVW RDKTCLPKEL
     IFEVNYLGGT MPTMAINFSR SASHIIGQYY NFLRLGYDGY CRVHRHTRKI ADYLAENLDA
     TGLFALINRG DSIPVVCFTM KEQAADWTLY DLSDQLERNG WQVPVYPLPN HAQNIIVCRL
     VCRSDMSLNL AQRLMEDIHL AIETLGRAHP RADRAKRGDI KGFTH
//