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Database: UniProt/TrEMBL
Entry: X8K5B2_9FIRM
LinkDB: X8K5B2_9FIRM
Original site: X8K5B2_9FIRM 
ID   X8K5B2_9FIRM            Unreviewed;       470 AA.
AC   X8K5B2;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   20-DEC-2017, entry version 24.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=HMPREF9092_0250 {ECO:0000313|EMBL:EUC78743.1};
OS   Eubacterium sulci ATCC 35585.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales;
OC   Clostridiales Family XIII. Incertae Sedis.
OX   NCBI_TaxID=888727 {ECO:0000313|EMBL:EUC78743.1, ECO:0000313|Proteomes:UP000020233};
RN   [1] {ECO:0000313|EMBL:EUC78743.1, ECO:0000313|Proteomes:UP000020233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35585 {ECO:0000313|EMBL:EUC78743.1,
RC   ECO:0000313|Proteomes:UP000020233};
RA   Durkin A.S., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA   Methe B., Sutton G., Nelson K.E.;
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
CC       {ECO:0000256|RuleBase:RU361171}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC         ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EUC78743.1}.
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DR   EMBL; JATQ01000002; EUC78743.1; -; Genomic_DNA.
DR   RefSeq; WP_050330494.1; NZ_JATQ01000002.1.
DR   EnsemblBacteria; EUC78743; EUC78743; HMPREF9092_0250.
DR   KEGG; euu:ADJ67_02320; -.
DR   PATRIC; fig|888727.3.peg.51; -.
DR   KO; K01580; -.
DR   Proteomes; UP000020233; 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   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   PANTHER; PTHR43321; PTHR43321; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000020233};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU000382, ECO:0000313|EMBL:EUC78743.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES     276    276       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   470 AA;  53867 MW;  D3303F434E7AD37E CRC64;
     MLESMNRGEK YLTPIFGTEA SNIEMPNKKI NMDPVPPQLA AEMIRGYLKT EGNATQNLAT
     FCQTYMDPVA AELMAENFEK NAIDKDEYPM TADLENRCVE IIGNLWNVNQ NEEPIGTSTV
     GSSEACMLGG LAMLFRWKKL ADKAGIDRCK RRPNLVISAG YQVCWEKFCR YWDIEMRTVP
     IDMEHLSLNM DTVMDYIDDY TIGVVAILGI TYTGKYDDVK ALDKLVEEYN QNHKNLPIRI
     HVDGASGGMV TPFIEPELEW DFRLKNVWSI STSGHKYGLV YPGVGWIIWR GKEALPEELI
     FWVSYLGGEE ATIAINFSRS ASQIVGQYYM LMRNGFSGYR EIHQRTINVA RYMAEEIEKM
     GIFEVIEDAK QIPIVCWKLK DEACVDWNLY DLEDRLRMHG WMIPAYPMPE NIEDIDVQRL
     VIRQDFGMQL AVLCISEMKK QIEILNGSRI VIRDDTDEGK PGKCFDHSGR
//
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