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Database: UniProt/TrEMBL
Entry: A0A0M3UGA5_9MICC
LinkDB: A0A0M3UGA5_9MICC
Original site: A0A0M3UGA5_9MICC 
ID   A0A0M3UGA5_9MICC        Unreviewed;       455 AA.
AC   A0A0M3UGA5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   25-OCT-2017, entry version 16.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=AOC05_08970 {ECO:0000313|EMBL:ALE92419.1};
OS   Arthrobacter alpinus.
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=656366 {ECO:0000313|EMBL:ALE92419.1, ECO:0000313|Proteomes:UP000062833};
RN   [1] {ECO:0000313|Proteomes:UP000062833}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R3.8 {ECO:0000313|Proteomes:UP000062833};
RA   See-Too W.S., Chan K.G.;
RT   "Complete genome of Arthrobacter alpinus strain R3.8.";
RL   Submitted (SEP-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:RU361171};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU361171}.
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DR   EMBL; CP012677; ALE92419.1; -; Genomic_DNA.
DR   RefSeq; WP_062006939.1; NZ_CP012677.1.
DR   EnsemblBacteria; ALE92419; ALE92419; AOC05_08970.
DR   KEGG; aaq:AOC05_08970; -.
DR   PATRIC; fig|656366.3.peg.1949; -.
DR   KO; K01580; -.
DR   Proteomes; UP000062833; 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:UP000062833};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000062833}.
FT   MOD_RES     276    276       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   455 AA;  50107 MW;  249E91CB45972727 CRC64;
     MSLHKHHPQH EEKITDSAFD GGVGSIPRHR LPRHTQDADA ALRFVQDELM LDGNARQNLA
     TFVTTWMEPQ AATLIQASLE KNIIDKDEYP RSAEIERRCV NILANLWNAS TPAGGEDAIG
     CSTTGSSEAA MLAGMALKWR WRARREEAGA NASKPNLVMG ANVQVCWEKF ARYWDVEARL
     VPLDGATHLT ADQAAAACDE NTIAVVAVLG STFDGSYEPV AEIAAALDAL QASTGLDIPL
     HVDAASGGFI APFLDQELLW DFRLDRVKSI NASGHKYGLV YPGVGWVVWR SSDDLPRELI
     FSVDYLGGSM PTFALNFSRP ASQVIAQYYT LVRYGFDGYQ RIQQRARDIA TTIAQGVEKL
     GPFTLLSRGE ELPVLAFKLT TPDGWDVYDL SHELRSFGWI VPAYPMPKGM ADVDVLRVVV
     RNGFTFDLAE MFLADLAKSV ARLSGQQQAR VAFHH
//
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