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Database: UniProt/TrEMBL
Entry: A0A0T9PMU3_YERKR
LinkDB: A0A0T9PMU3_YERKR
Original site: A0A0T9PMU3_YERKR 
ID   A0A0T9PMU3_YERKR        Unreviewed;       466 AA.
AC   A0A0T9PMU3;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   20-DEC-2017, entry version 16.
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:CNH73104.1};
GN   ORFNames=ERS008500_02999 {ECO:0000313|EMBL:CNH73104.1};
OS   Yersinia kristensenii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=28152 {ECO:0000313|EMBL:CNH73104.1, ECO:0000313|Proteomes:UP000044230};
RN   [1] {ECO:0000313|EMBL:CNH73104.1, ECO:0000313|Proteomes:UP000044230}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FE80982 {ECO:0000313|EMBL:CNH73104.1,
RC   ECO:0000313|Proteomes:UP000044230};
RA   Murphy D.;
RL   Submitted (MAR-2015) 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; CQAQ01000007; CNH73104.1; -; Genomic_DNA.
DR   RefSeq; WP_038638890.1; NZ_CWJK01000008.1.
DR   EnsemblBacteria; CNH73104; CNH73104; ERS008500_02999.
DR   KEGG; ykr:CH54_3092; -.
DR   PATRIC; fig|28152.8.peg.3163; -.
DR   KO; K01580; -.
DR   Proteomes; UP000044230; 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   InterPro; IPR021115; Pyridoxal-P_BS.
DR   PANTHER; PTHR43321; PTHR43321; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000044230};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU000382, ECO:0000313|EMBL:CNH73104.1};
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   466 AA;  52535 MW;  E32B55135FD36BB3 CRC64;
     MTKKSLDDYR STLLDSRFGS QAIRHISENK NFPKEEMRED IAFQIISDEL FLDGNARQNL
     ATFCQTWDDD NVHKLMDLSI NKNWIDKEEY PQSAAIDMRC VNMMADLWNA PTPKGEQGVG
     TNTIGSSEAC MLGGMAMKWR WRKKREAAGK PTNKPNFVCG PVQVCWHKFA RYWDVEIREI
     PMVPGQLFMD PQRMIEACDE NTIGVVPTFG VTYTGNYEFP KPLHDALDKL QKDTGLDIDM
     HIDAASGGFL APFVAPDIEW DFRLPRVKSI STSGHKFGLA PLGCGWVIWR DAAALPEELI
     FNVDYLGGQV GTFAINFSRP AGQVISQYYE FIRLGREGYT KVQSACYQVA EFLAKEIAPL
     GPYEFYCSGG PDEGIPAICF RIKEGAKTGY TLYDLSERLR LRGWQVPAFT LSGKMSDVVV
     MRIMCRRGFE MDFAGLLLDD FKSSLKYLSE HPSLGGLASQ NSFNHT
//
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