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Database: UniProt/TrEMBL
Entry: A0A059VX09_STRA9
LinkDB: A0A059VX09_STRA9
Original site: A0A059VX09_STRA9 
ID   A0A059VX09_STRA9        Unreviewed;       482 AA.
AC   A0A059VX09;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   05-JUL-2017, entry version 19.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=DC74_1434 {ECO:0000313|EMBL:AIA01950.1};
OS   Streptomyces albulus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=68570 {ECO:0000313|EMBL:AIA01950.1, ECO:0000313|Proteomes:UP000026918};
RN   [1] {ECO:0000313|Proteomes:UP000026918}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NK660 {ECO:0000313|Proteomes:UP000026918};
RA   Gu Y., Yang C., Song C., Wang S., Wang X., Geng W., Sun Y., Feng J.,
RA   Wang Y.;
RT   "Genome Sequence of the epsilon-Poly-L-Lysine-Producing Microorganism
RT   Streptomyces albulus NK660.";
RL   Submitted (APR-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; CP007574; AIA01950.1; -; Genomic_DNA.
DR   RefSeq; WP_038517677.1; NZ_CP007574.1.
DR   EnsemblBacteria; AIA01950; AIA01950; DC74_1434.
DR   GeneID; 32396302; -.
DR   KEGG; salu:DC74_1434; -.
DR   PATRIC; fig|68570.5.peg.1580; -.
DR   KO; K01580; -.
DR   Proteomes; UP000026918; 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:UP000026918};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026918}.
FT   MOD_RES     277    277       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   482 AA;  53409 MW;  046E7799E6D3593A CRC64;
     MPLKRPHQHR DASRNLAVNP VFSQQPVHVP RYELPGDGMD PDTAYQIVHD ELMLDGNARL
     NLATFVSTWA EPQAQRLMAE CAEKNMIDKD EYPQTAEIEA RCVHMLADLW HAPDSHAAVG
     CSTTGSSEAA MLAGLALKRR WQHRRRAEGK STERPNMVMG INVQICWEKF ANYFEVEPRY
     VPMEGDRFIL SPEEAVELCD ENTIGVVAVL GSTFDGAYEP VAKISAALDA LQERTGIDVP
     LHVDGASGAM IAPFLDPELV WDFRLPRVAS INTSGHKYGL VMPGVGWALW RDADALPEDL
     VFHVNYLGGD MPTFALNFSR PGAQVIAQYY NFLRLGFEGY RAVQQTSRDV ATRVAAEIAA
     MGPFTLLTDG SQLPVFAFRM SDDVTNFTVF DVSAALRERG WQVPAYTFPA NRTDLAALRV
     VIRNGFGHDL GDLFLDDLRR VLPRLQAQQR PHRDAADAGG FAHGAETKQA GRPAIPEQAV
     RD
//
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