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Database: UniProt/TrEMBL
Entry: A0A0G3UTC5_9ACTN
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ID   A0A0G3UTC5_9ACTN        Unreviewed;       463 AA.
AC   A0A0G3UTC5;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   20-DEC-2017, entry version 17.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=M444_30780 {ECO:0000313|EMBL:AKL69083.1};
OS   Streptomyces sp. Mg1.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=465541 {ECO:0000313|EMBL:AKL69083.1, ECO:0000313|Proteomes:UP000035653};
RN   [1] {ECO:0000313|EMBL:AKL69083.1, ECO:0000313|Proteomes:UP000035653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mg1 {ECO:0000313|EMBL:AKL69083.1,
RC   ECO:0000313|Proteomes:UP000035653};
RX   PubMed=23908282;
RA   Hoefler B.C., Konganti K., Straight P.D.;
RT   "De Novo Assembly of the Streptomyces sp. Strain Mg1 Genome Using
RT   PacBio Single-Molecule Sequencing.";
RL   Genome Announc. 1:e00535-13(2013).
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; CP011664; AKL69083.1; -; Genomic_DNA.
DR   RefSeq; WP_037798780.1; NZ_CP011664.1.
DR   EnsemblBacteria; AKL69083; AKL69083; M444_30780.
DR   KEGG; strm:M444_30780; -.
DR   PATRIC; fig|465541.12.peg.6504; -.
DR   KO; K01580; -.
DR   Proteomes; UP000035653; 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   InterPro; IPR017756; TM_Gly-Cys-Arg_CS.
DR   PANTHER; PTHR43321; PTHR43321; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR03382; GC_trans_RRR; 1.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000035653};
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:UP000035653}.
FT   MOD_RES     275    275       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   463 AA;  51017 MW;  4F9FFFC3F04F72F4 CRC64;
     MALHETKDVP AQDADTDVFT SALSGEILPK YRMPEDHSPS EVVYELLHNE LLLDGNAAQN
     LATFCTTWSD DGVRRLMAEC LDKNMIDKDE YPQTAEIESR CVNILADLWN APSGGAATGC
     STTGSSEAAM LGGLALKWRW RERRRAAGLP VDRPNLICGP VQICWDKFAR YFDVELRQIP
     LEPGATGLRP HQLAQYVDEN TIGVVAILGV TYSCDYEPVA EICAELDRIQ AEHGWDVPVH
     VDAASGGFVA PFLHPDVVWD FRLPRVASVN TSGHKYGLAP LGVGWIVWRT ADLLPADLVF
     NVDYLGGDMP TFALNFSRPG GEVIAQYYLF LRLGRGGYRR VQLACAETAQ YLAQEIAAMG
     PFTLLYDGRG GLPAVSYTLA DPEGSPFTLY DLSDRLRMRG WQVPSYALPA DRDDTVIQRV
     LIRHGVTRDQ IALLASDLRK AVEHLTATPP PVPATEPRSG FHH
//
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