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Database: UniProt/TrEMBL
Entry: A0A0U1HNM3_YERRO
LinkDB: A0A0U1HNM3_YERRO
Original site: A0A0U1HNM3_YERRO 
ID   A0A0U1HNM3_YERRO        Unreviewed;       466 AA.
AC   A0A0U1HNM3;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   20-JUN-2018, entry version 19.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   Name=gadA_1 {ECO:0000313|EMBL:CQI88159.1};
GN   ORFNames=ERS008555_00492 {ECO:0000313|EMBL:CQI88159.1};
OS   Yersinia rohdei.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=29485 {ECO:0000313|EMBL:CQI88159.1, ECO:0000313|Proteomes:UP000042054};
RN   [1] {ECO:0000313|EMBL:CQI88159.1, ECO:0000313|Proteomes:UP000042054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=68/02 {ECO:0000313|EMBL:CQI88159.1,
RC   ECO:0000313|Proteomes:UP000042054};
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:RU361171};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU361171}.
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DR   EMBL; CTKE01000002; CQI88159.1; -; Genomic_DNA.
DR   RefSeq; WP_004716586.1; NZ_CTKU01000013.1.
DR   EnsemblBacteria; CQI88159; CQI88159; ERS008555_00492.
DR   KEGG; yro:CH64_2125; -.
DR   KO; K01580; -.
DR   Proteomes; UP000042054; 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   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   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:UP000042054};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171, ECO:0000313|EMBL:CQI88159.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171}.
FT   MOD_RES     276    276       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   466 AA;  52476 MW;  3E9A1884A05294BD CRC64;
     MTRKSLDEYR STLLDSRFGS EAIRNMTEDK HFPKEEMRED IAFQIISDEL FLDGNARQNL
     ATFCQTWDDE NVHKLMDLSI NKNWIDKEEY PQSAAIDMRC VNMMADLWNA PKSKDGQGVG
     TNTIGSSEAC MLGGMAMKWR WRKKMEAAGK PTNKPNFVCG PVQVCWHKFA RYWDVEMREI
     PMAPGQLFMD PQRMVEACDE NTIGVVPTFG VTYTGNYEFP KPLHDALDKL QKEKGLDIDM
     HIDAASGGFL APFVAPDIEW DFRLPRVKSI SSSGHKFGLA PLGCGWVIWR DAAALPEELI
     FNVDYLGGQV GTFAINFSRP AGQVISQYYE FIRLGREGYT KVQSACYQVA EFLAKEIAPL
     GPYEFYCSGG PEEGIPAICF RVKEGANPGY TLYDLSERLR LRGWQVPAFA LSGGMSDVVV
     MRIMCRRGFE MDFAGLLLDD FKSSLKYLSE HPSLGGEASQ NSFSHT
//
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