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Database: UniProt/TrEMBL
Entry: A0A0U3Q255_9ACTN
LinkDB: A0A0U3Q255_9ACTN
Original site: A0A0U3Q255_9ACTN 
ID   A0A0U3Q255_9ACTN        Unreviewed;       469 AA.
AC   A0A0U3Q255;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-SEP-2017, entry version 15.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=ASR50_14935 {ECO:0000313|EMBL:ALV50579.1};
OS   Streptomyces sp. 4F.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1751294 {ECO:0000313|EMBL:ALV50579.1, ECO:0000313|Proteomes:UP000056717};
RN   [1] {ECO:0000313|EMBL:ALV50579.1, ECO:0000313|Proteomes:UP000056717}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4F {ECO:0000313|EMBL:ALV50579.1,
RC   ECO:0000313|Proteomes:UP000056717};
RA   Jing X.;
RT   "The complete genome sequence of a mosephilic streptomyces 4F.";
RL   Submitted (NOV-2015) 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; CP013142; ALV50579.1; -; Genomic_DNA.
DR   RefSeq; WP_033274913.1; NZ_CP013142.1.
DR   EnsemblBacteria; ALV50579; ALV50579; ASR50_14935.
DR   KEGG; strf:ASR50_14935; -.
DR   KO; K01580; -.
DR   Proteomes; UP000056717; 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:UP000056717};
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:UP000056717}.
FT   MOD_RES     282    282       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   469 AA;  51784 MW;  2D2E786AEF049D48 CRC64;
     MPLHPGRPAG ERPMSVNPFL GPANPVGGMT QAPPRHRLPD GPMAPSTAYQ LVHDELMLDG
     NARLNLATFV TTWMEPEAGV LMMECRDKNM IDKDEYPRTA ELERRCVAML ADLWHAPDPS
     KAVGCSTTGS SEACMLAGLA MKRRWALRNA GRYPSREARP NLVMGINVQV CWDKFCTFFE
     VEPRQVPMEG DRFHLDPAAA AELCDENTIG VVGILGSTFD GSYEPVAELC AALDDLQERT
     GLDVPVHVDG ASGAMVAPFL DEDLVWDFRL DRVASVNTSG HKYGLVYPGV GWVLWRDAAA
     LPEELVFRVN YLGGDMPTFA LNFSRPGAQV VAQYYSFLRL GRDGYRAVQQ AARDVATGLS
     ARIEALGDFR LLTRGDELPV FAFTTAPDVT AFDVFDVARR LRETGWLVPA YTFPANRQDL
     AVLRVVCRNG FSEDLADLFA EDLTRLLPDL RSQSHPLTRD RNAATGFHH
//
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