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Database: UniProt/TrEMBL
Entry: A0A0A8EXY8_9ACTN
LinkDB: A0A0A8EXY8_9ACTN
Original site: A0A0A8EXY8_9ACTN 
ID   A0A0A8EXY8_9ACTN        Unreviewed;       482 AA.
AC   A0A0A8EXY8;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   25-OCT-2017, entry version 18.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=GZL_07782 {ECO:0000313|EMBL:AJC60332.1};
OS   Streptomyces sp. 769.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1262452 {ECO:0000313|EMBL:AJC60332.1, ECO:0000313|Proteomes:UP000031113};
RN   [1] {ECO:0000313|EMBL:AJC60332.1, ECO:0000313|Proteomes:UP000031113}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=769 {ECO:0000313|EMBL:AJC60332.1,
RC   ECO:0000313|Proteomes:UP000031113};
RA   Du Q., Wang Q., Li Q., Wang L., Zhang Z., Ren J., Wang J., Wang M.;
RT   "Complete Genome Sequence of Streptomyces gongzhulingensis.";
RL   Submitted (DEC-2012) 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; CP003987; AJC60332.1; -; Genomic_DNA.
DR   RefSeq; WP_039638492.1; NZ_CP003987.1.
DR   EnsemblBacteria; AJC60332; AJC60332; GZL_07782.
DR   KEGG; stre:GZL_07782; -.
DR   KO; K01580; -.
DR   Proteomes; UP000031113; 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:UP000031113};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031113}.
FT   MOD_RES     277    277       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   482 AA;  53568 MW;  82B56849A8715062 CRC64;
     MPLKRPHQHR DASRNLAVNP VFSRQPVHVP RYELPADGMD PDTAYQIVHD ELMLDGNARL
     NLATFVSTWA EPQAQRLMAE CAEKNMIDKD EYPQTAEIEA RCVHMLADLW HAPDSHAAVG
     CSTTGSSEAA MLAGLALKRR WQHRRRTEGR STERPNMVMG INVQICWEKF ANYFEVEPRY
     VPMEGDRFIL SPEQAVELCD ENTIGVVAVL GSTFDGAYEP VAEISAALDD LQERTGIDVP
     LHVDGASGAM IAPFLDPELV WDFRLPRVAS INTSGHKYGL VMPGVGWALW RDADALPEDL
     VFHVNYLGGD MPTFALNFSR PGAQVIAQYY NFLRLGFEGY RAVQQTSRDV ATRIAAEIAG
     MGPFTLLTDG SQLPVFAFRT SDDVTNFTVF DVSAALRERG WQVPAYTFPA NRTDLAALRV
     VVRNGFGHDL GDLFLEDLRR VLPRLQAQQR PHRDAADAGG FAHGAESKQA GRPVIPEQTV
     RD
//
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