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Database: UniProt/TrEMBL
Entry: Q6ARB0_DESPS
LinkDB: Q6ARB0_DESPS
Original site: Q6ARB0_DESPS 
ID   Q6ARB0_DESPS            Unreviewed;       474 AA.
AC   Q6ARB0;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   05-JUL-2017, entry version 85.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   OrderedLocusNames=DP0385 {ECO:0000313|EMBL:CAG35114.1};
OS   Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfobulbaceae; Desulfotalea.
OX   NCBI_TaxID=177439 {ECO:0000313|EMBL:CAG35114.1, ECO:0000313|Proteomes:UP000000602};
RN   [1] {ECO:0000313|Proteomes:UP000000602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LSv54 / DSM 12343 {ECO:0000313|Proteomes:UP000000602};
RX   PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA   Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M.,
RA   Bauer M., Zibat A., Lombardot T., Becker I., Amann J., Gellner K.,
RA   Teeling H., Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R.,
RA   Klenk H.-P.;
RT   "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium
RT   from permanently cold Arctic sediments.";
RL   Environ. Microbiol. 6:887-902(2004).
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; CR522870; CAG35114.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q6ARB0; -.
DR   STRING; 177439.DP0385; -.
DR   EnsemblBacteria; CAG35114; CAG35114; DP0385.
DR   KEGG; dps:DP0385; -.
DR   eggNOG; ENOG4105CVK; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000070228; -.
DR   KO; K01580; -.
DR   OMA; RPNLVMG; -.
DR   OrthoDB; POG091H06F5; -.
DR   BioCyc; DPSY177439:GJW5-389-MONOMER; -.
DR   Proteomes; UP000000602; 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:UP000000602};
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:UP000000602}.
FT   MOD_RES     284    284       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   474 AA;  54088 MW;  1F23CD853D7F0620 CRC64;
     MLRCYPRTEK EKRMPLHNKR KNNIMDDIYA SSDLSIVLPK YKMPQKELDP RHAYQMVHDE
     LMLDGNARQN LATFCQTWDD PEVHRLMDEC IDKNMIDKDE YPQTAEIESR CVHILADLWN
     APDSANSLGC STTGSSEAAM LGGLALKKRW SEKRKAAGKG TDRPNIVCGP VQICWHKFAR
     YWDVELREVP LEDQLYMTAE EAVKRCDENT IGVIPTLGVT FTCVYEPVEE ICRALDQLQK
     ETGLDIPVHV DGASGGFLAP FVDPDLKWDF RLKRVKSINA SGHKFGLAPL GVGWVLWRDK
     EELPEDLIFW VNYLGGNMPT FALNFSRPGG QIIAQYYNFL RLGHEGYRKI HQACYKTAQY
     LSSEVKKLGP FEIIYDGRGG IPAMSFSLQE GVAPGFNLFD LSDRIRSRGW QIAAYSMPAN
     REDLVVMRIL VRHGFSRDLA DLLLKDLQHC LEYFKKNPVI HQSSEEFSGS FKHS
//
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