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Database: UniProt/TrEMBL
Entry: A0A089XI81_9LACT
LinkDB: A0A089XI81_9LACT
Original site: A0A089XI81_9LACT 
ID   A0A089XI81_9LACT        Unreviewed;       466 AA.
AC   A0A089XI81;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   20-DEC-2017, entry version 21.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   Name=gadA {ECO:0000313|EMBL:AIS03708.1};
GN   ORFNames=LG36_1111 {ECO:0000313|EMBL:AIS03708.1};
OS   Lactococcus lactis.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1358 {ECO:0000313|EMBL:AIS03708.1, ECO:0000313|Proteomes:UP000029483};
RN   [1] {ECO:0000313|EMBL:AIS03708.1, ECO:0000313|Proteomes:UP000029483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AI06 {ECO:0000313|EMBL:AIS03708.1,
RC   ECO:0000313|Proteomes:UP000029483};
RA   McCulloch J.A., Oliveira V.M., Pina A.A., Perez-Chaparro P.J.,
RA   Vasconcelos J.M., Almeida L.M., Oliveira L.F., Silva D.A., Rogez H.G.,
RA   Cretenet M., Mamizuka E.M., Nunes M.T.;
RL   Submitted (SEP-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}.
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DR   EMBL; CP009472; AIS03708.1; -; Genomic_DNA.
DR   RefSeq; WP_021722858.1; NZ_LDEK01000020.1.
DR   EnsemblBacteria; AIS03708; AIS03708; LG36_1111.
DR   KEGG; llj:LG36_1111; -.
DR   PATRIC; fig|1358.58.peg.902; -.
DR   eggNOG; ENOG4105CVK; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   KO; K01580; -.
DR   Proteomes; UP000029483; 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   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:UP000029483};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES     277    277       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   466 AA;  53913 MW;  4289D3BFCB982107 CRC64;
     MLYGKENRDE AEFLEPIFGS ESEQVDLPKY KLAQKSIEPR 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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