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Database: UniProt/TrEMBL
Entry: A0A1P8XWP0_9ACTN
LinkDB: A0A1P8XWP0_9ACTN
Original site: A0A1P8XWP0_9ACTN 
ID   A0A1P8XWP0_9ACTN        Unreviewed;       469 AA.
AC   A0A1P8XWP0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   30-AUG-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=BV401_21425 {ECO:0000313|EMBL:AQA12624.1};
OS   Streptomyces autolyticus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=75293 {ECO:0000313|EMBL:AQA12624.1, ECO:0000313|Proteomes:UP000187851};
RN   [1] {ECO:0000313|Proteomes:UP000187851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC0516 {ECO:0000313|Proteomes:UP000187851};
RA   Yin M., Jiang M., Lu T.;
RT   "Streptomyces autolyticus CGMCC0516 complete genome sequence.";
RL   Submitted (JAN-2017) 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; CP019458; AQA12624.1; -; Genomic_DNA.
DR   Proteomes; UP000187851; 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:UP000187851};
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}.
FT   MOD_RES     285    285       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   469 AA;  51891 MW;  30AB69956C75B19F CRC64;
     MALHKGTPGP RRDERSEFST NPVYDEANPV SGMTGKPPRH CLPDGPMAPT TAYQFVHDEL
     MLDGNARQNL ATFVTTWMEP QAGKLMSDCL AKNMIDKDEY PRTAELERRC VAMLGHLWHA
     PDPDGVVGCS TTGSSEACML AGMAFKRRWA KRNPVSYPAT ARPNLVMGTN VQVCWEKFCD
     FWEVEARQVP MEGNRFHLDP QAAAELCDEN TIGVVAVLGS TFDGSYEPVA EVCRALDDLQ
     ERTGLDIPVH VDGASGAMIA PFLDPDLRWD FQLPRVASIN TSGHKYGLVY PGVGWALWRT
     AEVLPEDLVF RVDYLGGDMP TFSLNFSRPG SQVAAQYYTF VRLGRAGYRA VQQEARDVAC
     SLAERIEAFG DFTLLSRGDQ LPVFAFTTAE GVGAFDVYDV SRRLRERGWL VPAYAFPPNR
     QDLSVLRVVC RNGFSEDLAD LFLADLGSLL PELRSQPAPT GKTVTAFHH
//
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