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Database: UniProt/TrEMBL
Entry: A0A1B1MEZ6_STRLN
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Original site: A0A1B1MEZ6_STRLN 
ID   A0A1B1MEZ6_STRLN        Unreviewed;       470 AA.
AC   A0A1B1MEZ6;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   25-APR-2018, entry version 14.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=SLINC_4748 {ECO:0000313|EMBL:ANS66972.1};
OS   Streptomyces lincolnensis.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1915 {ECO:0000313|EMBL:ANS66972.1, ECO:0000313|Proteomes:UP000092598};
RN   [1] {ECO:0000313|EMBL:ANS66972.1, ECO:0000313|Proteomes:UP000092598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 2936 {ECO:0000313|EMBL:ANS66972.1,
RC   ECO:0000313|Proteomes:UP000092598};
RA   Meng S.C.;
RT   "Enhancement of antibiotic productionsby engineered nitrateutilization
RT   in actinobacteria.";
RL   Submitted (JUL-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; CP016438; ANS66972.1; -; Genomic_DNA.
DR   RefSeq; WP_067437445.1; NZ_CP016438.1.
DR   EnsemblBacteria; ANS66972; ANS66972; SLINC_4748.
DR   KEGG; sls:SLINC_4748; -.
DR   PATRIC; fig|1915.4.peg.5281; -.
DR   KO; K01580; -.
DR   Proteomes; UP000092598; 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:UP000092598};
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:UP000092598}.
FT   MOD_RES     283    283       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   470 AA;  52363 MW;  5A4153FC40D58282 CRC64;
     MPLHQGPEQP DERPLSVNPF YGEADPVGGM AEAPPKHRLP AAPLPPSTAY QLVHDELMLD
     GNSRLNLATF VTTWMEPQAG VLMDECRDKN MIDKDEYPRT AELERRCVAM LADLWHAPDP
     SAAVGCSTTG SSEACMLAGM ALKRRWARRN ADRYPSRDVR PNLVMGVNVQ VCWEKFCTFW
     EVEARQVPME GDRFHLDAQA AAELCDENTI GVVGILGSTF DGSYEPVAEL CAALDALQER
     TGLDIPVHVD GASGAMVAPF LDEDLVWDFR LPRVASINTS GHKYGLVYPG VGWALWRDQE
     ALPEELVFRV NYLGGDMPTF ALNFSRPGAQ VVAQYYTFLR LGREGYRAVQ QSTRDVARGL
     AARVEALGDF RLLTRGDELP VFAFTTAPGV EAYDVFDVSR RMRERGWLVP AYTFPPNRED
     LSVLRVVCRN GFSADLAELF VEDLGRLVPE LRRQPHPLTR DKEAATGFHH
//
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