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Entry: Q5LI66_BACFN
LinkDB: Q5LI66_BACFN
Original site: Q5LI66_BACFN 
ID   Q5LI66_BACFN            Unreviewed;       480 AA.
AC   Q5LI66;
DT   21-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   21-JUN-2005, sequence version 1.
DT   24-JAN-2024, entry version 107.
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   Name=gadB {ECO:0000313|EMBL:CAH06161.1};
GN   ORFNames=BF9343_0382 {ECO:0000313|EMBL:CAH06161.1}, NCTC9343_02030
GN   {ECO:0000313|EMBL:SUV38133.1};
OS   Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS   / NCTC 9343 / Onslow).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=272559 {ECO:0000313|EMBL:CAH06161.1, ECO:0000313|Proteomes:UP000006731};
RN   [1] {ECO:0000313|EMBL:CAH06161.1, ECO:0000313|Proteomes:UP000006731}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 /
RC   Onslow {ECO:0000313|Proteomes:UP000006731};
RX   PubMed=15746427; DOI=10.1126/science.1107008;
RA   Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA   Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA   Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA   Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA   Barrell B.G., Parkhill J.;
RT   "Extensive DNA inversions in the B. fragilis genome control variable gene
RT   expression.";
RL   Science 307:1463-1465(2005).
RN   [2] {ECO:0000313|EMBL:SUV38133.1, ECO:0000313|Proteomes:UP000255401}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC9343 {ECO:0000313|EMBL:SUV38133.1,
RC   ECO:0000313|Proteomes:UP000255401};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) 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; CR626927; CAH06161.1; -; Genomic_DNA.
DR   EMBL; UFTH01000001; SUV38133.1; -; Genomic_DNA.
DR   RefSeq; WP_005784276.1; NZ_UFTH01000001.1.
DR   PaxDb; 272559-BF9343_0382; -.
DR   GeneID; 66330502; -.
DR   KEGG; bfs:BF9343_0382; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_019582_2_2_10; -.
DR   OMA; ECRDKNM; -.
DR   BioCyc; BFRA272559:G1GHZ-411-MONOMER; -.
DR   Proteomes; UP000006731; Chromosome.
DR   Proteomes; UP000255401; Unassembled WGS sequence.
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         274
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   480 AA;  54594 MW;  2D028490E1BA5B09 CRC64;
     MEDLNFRKGD AKTEAFGSNR MLQPSPVEKI PDGPTTPEIA YQMVKDETFA QTQPRLNLAT
     FVTTYMDDYA TKLMNEAINI NYIDETEYPR IAVMNGKCIN IVANLWNSPE KDTWKTGALA
     IGSSEACMLG GVAAWLRWRK KRQAQGKPFD KPNFVISTGF QVVWEKFAQL WQIEMRQVPL
     TLDKTTLDPE EALKMCDENT ICVVPIQGVT WTGLNDDVEA LDKALDAYNA KTGYDIPIHV
     DAASGGFILP FLYPDTKWDF RLKWVLSISV SGHKFGLVYP GLGWVVWKGK EYLPEEMAFS
     VNYLGANITQ VGLNFSRPAA QILGQYYQFI RLGFQGYKEV QYNSLQIAKY IHSQIAKMTP
     FVNYSEDVVN PLFIWYMKPE YAKNAKWTLY DLQDKLAQHG WMVPAYTLPA KLQDYVVMRV
     VVRQGFSRDM ADMLLGDIKN AIAELEKLEY PTSTRIAQEK NLPVEAKVFN HTGKPQAAKK
//
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