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Database: UniProt/TrEMBL
Entry: A0A0U3LE17_STRGL
LinkDB: A0A0U3LE17_STRGL
Original site: A0A0U3LE17_STRGL 
ID   A0A0U3LE17_STRGL        Unreviewed;       475 AA.
AC   A0A0U3LE17;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   25-OCT-2017, entry version 14.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=WQO_15215 {ECO:0000313|EMBL:ALU94572.1};
OS   Streptomyces globisporus C-1027.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1172567 {ECO:0000313|EMBL:ALU94572.1};
RN   [1] {ECO:0000313|EMBL:ALU94572.1, ECO:0000313|Proteomes:UP000064183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C-1027 {ECO:0000313|EMBL:ALU94572.1,
RC   ECO:0000313|Proteomes:UP000064183};
RX   PubMed=22815456; DOI=10.1128/JB.00797-12;
RA   Wang L., Wang S., He Q., Yu T., Li Q., Hong B.;
RT   "Draft genome sequence of Streptomyces globisporus C-1027, which
RT   produces an antitumor antibiotic consisting of a nine-membered
RT   enediyne with a chromoprotein.";
RL   J. Bacteriol. 194:4144-4144(2012).
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; CP013738; ALU94572.1; -; Genomic_DNA.
DR   RefSeq; WP_058953995.1; NZ_CP013738.1.
DR   EnsemblBacteria; ALU94572; ALU94572; WQO_15215.
DR   KEGG; sgb:WQO_15215; -.
DR   KO; K01580; -.
DR   Proteomes; UP000064183; 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:UP000064183};
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     288    288       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   475 AA;  52853 MW;  D7011EB5A2C16700 CRC64;
     MPLHRGAHPD QDEPSDERRR LALNPFFGEA DPTAAMNTAP PRHRLPDGPL PPLTAYRLVH
     DELMLDGNSR LNLATFVTTW MEPQAGVLMG ECRDKNMIDK DEYPRTAELE KRCVAMLADL
     WNAPDPSAAV GCSTTGSSEA CMLAGLALKR RWAKRNADRY PATARPNLVM GVNVQVCWEK
     FCNFWEVEAR QVPMEGGRFH IDPQAAAELC DENTIGVVGI LGSTFDGSYE PIADLCAALD
     ALQERTGLDV PVHVDGASGA MVAPFLDPDL VWDFRLPRVA SVNTSGHKYG LVYPGVGWAL
     WRTADELPEE LVFRVNYLGG DMPTFALNFS RPGAQVVAQY YTFLRLGRDG YRAVQQASRD
     VACSLARAVE DLGDFRLLTR GDELPVFAFT TTAEVHAYDV FDVSRRLRER GWLVPAYTFP
     ANRQDLSVLR VVCRNGFSSD LAELLVEDLK QFLPELRAQK HPVSHDRKAV TAFHH
//
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