GenomeNet

Database: UniProt/TrEMBL
Entry: A0A076M470_STRLI
LinkDB: A0A076M470_STRLI
Original site: A0A076M470_STRLI 
ID   A0A076M470_STRLI        Unreviewed;       475 AA.
AC   A0A076M470;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   25-OCT-2017, entry version 18.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=SLIV_20690 {ECO:0000313|EMBL:AIJ15081.1};
OS   Streptomyces lividans TK24.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=457428 {ECO:0000313|EMBL:AIJ15081.1, ECO:0000313|Proteomes:UP000028682};
RN   [1] {ECO:0000313|EMBL:AIJ15081.1, ECO:0000313|Proteomes:UP000028682}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TK24 {ECO:0000313|EMBL:AIJ15081.1,
RC   ECO:0000313|Proteomes:UP000028682};
RG   StrepSynth;
RA   Ruckert C., Fridjonson O.H., Lambert C., van Wezel G.P., Bernaerts K.,
RA   Anne J., Economou A., Kalinowski J.;
RT   "Complete genome sequence of Streptomyces lividans TK24.";
RL   Submitted (AUG-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:RU361171};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU361171}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP009124; AIJ15081.1; -; Genomic_DNA.
DR   RefSeq; WP_011028961.1; NZ_GG657756.1.
DR   ProteinModelPortal; A0A076M470; -.
DR   EnsemblBacteria; AIJ15081; AIJ15081; SLIV_20690.
DR   GeneID; 29658342; -.
DR   KEGG; slv:SLIV_20690; -.
DR   PATRIC; fig|457428.16.peg.4275; -.
DR   KO; K01580; -.
DR   Proteomes; UP000028682; 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:UP000028682};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171, ECO:0000313|EMBL:AIJ15081.1};
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;  52651 MW;  9A5D7017FF8281AA CRC64;
     MSLHQGPRPS RDSDRDRRRL AVNPFHAAAN PLGGMTEAPP AHRLPDSPLP PESAYRLVHD
     ELMLDGNARL NLATFVTTWM EPQAGVLMSE CRDKNMIDKD EYPRTAELER RCVAMLADLW
     HAPDPSTAVG CSTTGSSEAC MLAGMALKRR WALRNADRYP AKDVRPNLVM GVNVQVCWDK
     FCNFWEVEAR QVPMEGDRFH LDPQAAAELC DENTIGVVGI LGSTFDGSYE PVADLCAALD
     ALQERTGLDV PVHVDGASGA MVAPFLDEDL VWDFRLPRVA SINTSGHKYG LVYPGVGWAL
     WRDAEALPEE LVFRVNYLGG DMPTFALNFS RPGAQVVAQY YNFLRLGREG YRAVQQSARD
     IAGSLAERVA ALGDFRLLTR GDQLPVFAFT TADDVTAYDV FDVSRRLREG GWLVPAYTFP
     PHREDLSVLR VVCRNGFSAD MADLLLADLE RLLPELRRQP GPLTRDKGAA TGFHH
//
DBGET integrated database retrieval system