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Database: UniProt/TrEMBL
Entry: A0A1U9R338_STRNV
LinkDB: A0A1U9R338_STRNV
Original site: A0A1U9R338_STRNV 
ID   A0A1U9R338_STRNV        Unreviewed;       472 AA.
AC   A0A1U9R338;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   25-OCT-2017, entry version 5.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=BBN63_14295 {ECO:0000313|EMBL:AQU70906.1};
OS   Streptomyces niveus (Streptomyces spheroides).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=193462 {ECO:0000313|EMBL:AQU70906.1, ECO:0000313|Proteomes:UP000189677};
RN   [1] {ECO:0000313|EMBL:AQU70906.1, ECO:0000313|Proteomes:UP000189677}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCSIO 3406 {ECO:0000313|EMBL:AQU70906.1,
RC   ECO:0000313|Proteomes:UP000189677};
RA   Zhu Q., Cheng W., Song Y., Li Q., Ju J.;
RT   "Complete genome sequence of Streptomyces niveus SCSIO 3406.";
RL   Submitted (NOV-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:RU361171};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU361171}.
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DR   EMBL; CP018047; AQU70906.1; -; Genomic_DNA.
DR   KEGG; snw:BBN63_14295; -.
DR   KO; K01580; -.
DR   Proteomes; UP000189677; 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:UP000189677};
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}.
FT   MOD_RES     285    285       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   472 AA;  52740 MW;  3EB2AFD450AACE5F CRC64;
     MRGPADNPAD NHSERLRLSL NPFFGEADPI GSMTSAPPTH RLPDGPMPPS TAYQLVHDEL
     MLDGNSRLNL ATFVTTWMER QAGVLMAECR DKNMIDKDEY PRTAELERRC VTMLADLWNA
     PDPSAAVGCS TTGSSEACML AGLALKRRWT TKNRDRYPGS ARPNLVMGVN VQVCWEKFCN
     FWEVEARLVP MEGDRFHLDP QAAADLCDEN TIGVVAVLGS TFDGSYEPVA ELCATLDALQ
     ERRGWDIPVH VDGASGAMVA PFLDEDLVWD FRLPRVSSIN TSGHKYGLVY PGVGWALWRT
     SAELPEELVF RVNYLGGEMP TFALNFSRPG AQVVAQYYTF LRLGRDGYRA VQQTARDVAR
     GLADEIGAMD DFRLLTHGNE LPVFAFTTAP HVKNFDVFDV SRRLREHGWL MPAYTFPANR
     EDLSVLRVVC RNGFSADLAA MLLADLRLLL PELRRQPHPL DRDKSRATAF HH
//
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