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Database: UniProt/TrEMBL
Entry: D5DSQ6_BACMQ
LinkDB: D5DSQ6_BACMQ
Original site: D5DSQ6_BACMQ 
ID   D5DSQ6_BACMQ            Unreviewed;       467 AA.
AC   D5DSQ6;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   25-OCT-2017, entry version 46.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   OrderedLocusNames=BMQ_2467 {ECO:0000313|EMBL:ADE69489.1};
OS   Bacillus megaterium (strain ATCC 12872 / QMB1551).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=545693 {ECO:0000313|EMBL:ADE69489.1, ECO:0000313|Proteomes:UP000000935};
RN   [1] {ECO:0000313|Proteomes:UP000000935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12872 / QMB1551 {ECO:0000313|Proteomes:UP000000935};
RA   Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K.,
RA   Riley D.R., Creasy H.H., Koenig S.S.K., Galens K., Orvis J.,
RA   Creasy T., Biedendieck R., Braun C., Grayburn S., Jahn D., Ravel J.,
RA   Vary P.S.;
RT   "Genome sequences of the industrial vitamin B12-producers B.
RT   megaterium QM B1551 and DSM319 reveal new insights into the Bacillus
RT   genome evolution and pan-genome structure.";
RL   Submitted (FEB-2010) 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; CP001983; ADE69489.1; -; Genomic_DNA.
DR   RefSeq; WP_013057164.1; NC_014019.1.
DR   STRING; 545693.BMQ_2467; -.
DR   EnsemblBacteria; ADE69489; ADE69489; BMQ_2467.
DR   KEGG; bmq:BMQ_2467; -.
DR   eggNOG; ENOG4105CVK; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000070228; -.
DR   KO; K01580; -.
DR   OMA; RPNLVMG; -.
DR   OrthoDB; POG091H06F5; -.
DR   Proteomes; UP000000935; 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:UP000000935};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171, ECO:0000313|EMBL:ADE69489.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000935}.
FT   MOD_RES     279    279       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   467 AA;  53195 MW;  A89983593B08F004 CRC64;
     MPQWHPHREQ KNLPDEFPVN PLFSRQGEVT IPRLRIGDQG MLPETAYQII HDEIALDGNA
     RLNLATFVTT WMEPDAKRLY GESFDKNMID KDEYPQTAAI EERCVRILAD LWNSPNPDTT
     MGVSTTGSSE ACMLGGLALK RRWQKLRKSK GLSTDRPNIV FSSSVQVVWE KFANYWDVEP
     RYVNINPDHP YLDAEGVINA VDENTIGVVP ILGVTYTGVY EPIAAIAKAL DELQEKTGLD
     IPIHVDAASG GFIAPFLQPD LIWDFRLPRV KSINVSGHKY GLVYPGLGWV IWREKEDLPE
     DLIFRVSYLG GNMPTFALNF SRPGAQVLLQ YYNFLRLGKD GYYAVQKTSQ ENALFLSKEI
     GEMDAFEILA DGSDIPVLAW KLKEDYTPNW TLYDLSRQLR TYGWQVPAYP LPADMEEITI
     MRIVVRNGFS RDLAHLFMVN FKQAVEFLNS LDRPVLKDTK YDNGFHH
//
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