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Database: UniProt/TrEMBL
Entry: A0A142KUD9_9LACO
LinkDB: A0A142KUD9_9LACO
Original site: A0A142KUD9_9LACO 
ID   A0A142KUD9_9LACO        Unreviewed;       467 AA.
AC   A0A142KUD9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   25-APR-2018, entry version 15.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=AYI71_13875 {ECO:0000313|EMBL:AMS09727.1};
OS   Lactobacillus oris.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1632 {ECO:0000313|EMBL:AMS09727.1};
RN   [1] {ECO:0000313|EMBL:AMS09727.1, ECO:0000313|Proteomes:UP000075226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J-1 {ECO:0000313|EMBL:AMS09727.1,
RC   ECO:0000313|Proteomes:UP000075226};
RA   Jia F., Su F.;
RT   "Genome sequence of Lactobacillus oris J-1.";
RL   Submitted (FEB-2016) 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; CP014787; AMS09727.1; -; Genomic_DNA.
DR   EnsemblBacteria; AMS09727; AMS09727; AYI71_13875.
DR   KEGG; lor:AYI71_13875; -.
DR   KO; K01580; -.
DR   Proteomes; UP000075226; 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:UP000075226};
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     278    278       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   467 AA;  54004 MW;  1EF5FF26AED4B972 CRC64;
     MSLYGKHDRE ERNTLDPIFG SFSEDHPLPK YKLNERPVEP RIAYQVVKDQ LLDEGNARLN
     LATFCQTYME PEAVKLMSET FDKNAIDKSE YPRTAEIENR CVNIIANLWH APKDEEFMGT
     STVGSSEACM LGGMAMKFSW KQRAAKLGLD VKAKRPNLVI SSGYQVCWEK FCTYWDVEMR
     TVPIDWEHQS LDLNHVLDYV DEYTIGIVGI MGITYTGRYD DIEALDKLVE EYNQHTDYKV
     YIHVDAASGG FYTPFMEPDL KWDFRLKNVI SINASGHKYG LVYPGIGWVL WRDQKCVPEK
     LIFRVSYLGG EMPTMAINFS RGASQIIGQY YNFIRYGFEG YHDIHKRTHD VAVYLAQEIE
     KLGLFEIVND GSRLPIVCYR HKEDKDHEWT LYDLADRLAM KGWQVPAYPL PKDLDQIEVQ
     RIVVRADFGM GMAHDFVEDM KDAIKELNGA HLVFHEKSSL KKYGFTH
//
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