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Database: UniProt/TrEMBL
Entry: A0A191V1B9_9ACTN
LinkDB: A0A191V1B9_9ACTN
Original site: A0A191V1B9_9ACTN 
ID   A0A191V1B9_9ACTN        Unreviewed;       473 AA.
AC   A0A191V1B9;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   25-OCT-2017, entry version 12.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=Spa2297_18130 {ECO:0000313|EMBL:ANJ08727.1};
OS   Streptomyces parvulus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=146923 {ECO:0000313|EMBL:ANJ08727.1, ECO:0000313|Proteomes:UP000078468};
RN   [1] {ECO:0000313|EMBL:ANJ08727.1, ECO:0000313|Proteomes:UP000078468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2297 {ECO:0000313|EMBL:ANJ08727.1,
RC   ECO:0000313|Proteomes:UP000078468};
RA   Nishizawa T., Miura T., Harada C., Guo Y., Narisawa K., Ohta H.,
RA   Takahashi H., Shirai M.;
RT   "Non-Contiguous Finished Genome Sequence of Streptomyces parvulus 2297
RT   Integrated Site-Specifically with Actinophage R4.";
RL   Submitted (MAY-2016) 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}.
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DR   EMBL; CP015866; ANJ08727.1; -; Genomic_DNA.
DR   RefSeq; WP_064729091.1; NZ_CP015866.1.
DR   EnsemblBacteria; ANJ08727; ANJ08727; Spa2297_18130.
DR   KEGG; spav:Spa2297_18130; -.
DR   KO; K01580; -.
DR   Proteomes; UP000078468; 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:UP000078468};
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     286    286       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   473 AA;  52591 MW;  51679DA09F42F492 CRC64;
     MSLHKGPRPS RDDDRDRRRL AVNPFHAAAN PLGGMTEAPP AHRLPDSPLP PESAYRLVHD
     ELMLDGNARL NLATFVTTWM EPQAGVLMSE CRDKNMIDKD EYPRTAELER RCVAMLADLW
     HAPDPETAVG CSTTGSSEAC MLAGMALKRR WALRNADRYP GARPNLVMGV NVQVCWEKFC
     NFWEVEARQV PMEGDRFHLD PQAAAELCDE NTIGVVGILG STFDGSYEPV ADLCAALDAL
     QERTGLDVPV HVDGASGAMV APFLDEDLVW DFRLPRVASI NTSGHKYGLV YPGVGWALWR
     DAEALPEELV FRVNYLGGDM PTFALNFSRP GAQVVAQYYT FLRLGREGYR AVQLSARDIA
     RGLAERVEAL GDFRLLTRGD QLPVFAFTTA DDVTAYDVFD VSRRLREGGW LVPAYTFPPH
     REDLSVLRVV CRNGFSTDMA DLLLADLERL LPELRRQPGP LIRDKGAATG FHH
//
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