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Database: UniProt/TrEMBL
Entry: U5PPT5_LACLL
LinkDB: U5PPT5_LACLL
Original site: U5PPT5_LACLL 
ID   U5PPT5_LACLL            Unreviewed;       466 AA.
AC   U5PPT5;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   20-JUN-2018, entry version 31.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=P620_07300 {ECO:0000313|EMBL:AGY44310.1};
OS   Lactococcus lactis subsp. lactis KLDS 4.0325.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1399116 {ECO:0000313|EMBL:AGY44310.1, ECO:0000313|Proteomes:UP000017161};
RN   [1] {ECO:0000313|EMBL:AGY44310.1, ECO:0000313|Proteomes:UP000017161}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KLDS 4.0325 {ECO:0000313|EMBL:AGY44310.1};
RX   PubMed=24285665;
RA   Yang X., Wang Y., Huo G.;
RT   "Complete Genome Sequence of Lactococcus lactis subsp. lactis
RT   KLDS4.0325.";
RL   Genome Announc. 1:e00962-13(2013).
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:RU361171};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU361171}.
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DR   EMBL; CP006766; AGY44310.1; -; Genomic_DNA.
DR   RefSeq; WP_023164198.1; NC_022593.1.
DR   EnsemblBacteria; AGY44310; AGY44310; P620_07300.
DR   KEGG; lld:P620_07300; -.
DR   PATRIC; fig|1399116.3.peg.1433; -.
DR   KO; K01580; -.
DR   BioCyc; LLAC1399116:G1389-1428-MONOMER; -.
DR   Proteomes; UP000017161; 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; 3.40.640.10; -; 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.
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:UP000017161};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171}.
FT   MOD_RES     277    277       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   466 AA;  53913 MW;  CE5062019CD6A771 CRC64;
     MLYGKENRDE AEFLEPIFGS ESEQVDLPKY KLAQQSIEPR VAYQLVQDEM LDEGNARLNL
     ATFCQTYMEP EAVKLMSQTL EKNAIDKSEY PRTTEIENRC VNMIADLWNA SEKEKFMGTS
     TIGSSEACML GGMAMKFSWR KRAEKLGLDI NAKKPNLVIS SGYQVCWEKF CVYWDIEMRE
     VPMDKEHMSI NLDKVMDYVD EYTIGVVGIM GITYTGRYDD IKALDNLIEE YNKQTDYKVY
     IHVDAASGGL YAPFVEPELE WDFRLKNVIS INTSGHKYGL VYPGVGWVLW RDKKYLPEEL
     IFKVSYLGGE LPTMAINFSH SASQLIGQYY NFVRYGFDGY KAIHERTHKV AMFLAKEIEK
     TGMFEIMNDG SQLPIVCYKL KEDSNRGWNL YDLADRLLMK GWQVPAYPLP KNLENEIIQR
     LVIRADFGMN MAFNYVQDMQ EAIEALNKAH ILYHEEPENK TYGFTH
//
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