ID   E3J4E6_PSEI1            Unreviewed;       470 AA.
AC   E3J4E6;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 66.
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=FraEuI1c_5076 {ECO:0000313|EMBL:ADP83065.1};
OS   Pseudofrankia inefficax (strain DSM 45817 / CECT 9037 / DDB 130130 / EuI1c)
OS   (Frankia inefficax).
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae;
OC   Pseudofrankia.
OX   NCBI_TaxID=298654 {ECO:0000313|EMBL:ADP83065.1, ECO:0000313|Proteomes:UP000002484};
RN   [1] {ECO:0000313|EMBL:ADP83065.1, ECO:0000313|Proteomes:UP000002484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45817 / CECT 9037 / EuI1c
RC   {ECO:0000313|Proteomes:UP000002484};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., Beauchemin N., Sen A.,
RA   Sur S.A., Gtari M., Wall L., Tisa L., Woyke T.;
RT   "Complete sequence of Frankia sp. EuI1c.";
RL   Submitted (OCT-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; CP002299; ADP83065.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3J4E6; -.
DR   STRING; 298654.FraEuI1c_5076; -.
DR   KEGG; fri:FraEuI1c_5076; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_019582_2_2_11; -.
DR   InParanoid; E3J4E6; -.
DR   Proteomes; UP000002484; 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:UP000002484}.
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         280
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   470 AA;  50934 MW;  210F47F28CC8A1E8 CRC64;
     MGDQANARLA VRPQFRWPAG QARPGEETGG ELPRYRIPAG PTDPETAYQL VHDELMLDGN
     ARLNLATFVT TWMDPHADRL MAECAAKNMI DKDEYPQTAE LEARCVSMLA DLWHAADAAD
     AVGCSTTGSS EAGMLAGLAM TRRWRAARRA AGLPADRPNL VMGANVQVCW EKFARYWDVE
     ARLVPLAPGR THLTADEAVR HCDENTVGVV AILGSTFDGT YEPVAEIAAA LDRLAAGGGP
     DVPVHVDAAS GGFVAPFCDP DLLWDFRLDR VVSINASGHK FGLVYPGVGW VLWRDREHLP
     EELVFHVDYL GGTMPTFALN FSRPGAQVVA QYYSLLRHGR EGYRQVIQGC RDVATRLSGE
     IAEMGPFALV SDGAGGGIPA FAFTLRDADA AGFSVFDVSE LLRTRGWQVP AYRFPPALQE
     LAVLRVVVRN GFGPDLADLL VADLRRVVDR LTDAGRPGPP PAEATAAFHH
//