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Database: UniProt/TrEMBL
Entry: C7LHI0_BRUMC
LinkDB: C7LHI0_BRUMC
Original site: C7LHI0_BRUMC 
ID   C7LHI0_BRUMC            Unreviewed;       472 AA.
AC   C7LHI0;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   25-OCT-2017, entry version 49.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   Name=gadB {ECO:0000313|EMBL:ACU49468.1};
GN   OrderedLocusNames=BMI_II334 {ECO:0000313|EMBL:ACU49468.1};
OS   Brucella microti (strain CCM 4915).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=568815 {ECO:0000313|EMBL:ACU49468.1, ECO:0000313|Proteomes:UP000002188};
RN   [1] {ECO:0000313|EMBL:ACU49468.1, ECO:0000313|Proteomes:UP000002188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCM 4915 {ECO:0000313|EMBL:ACU49468.1,
RC   ECO:0000313|Proteomes:UP000002188};
RX   PubMed=19653890; DOI=10.1186/1471-2164-10-352;
RA   Audic S., Lescot M., Claverie J.-M., Scholz H.C.;
RT   "Brucella microti: the genome sequence of an emerging pathogen.";
RL   BMC Genomics 10:352-352(2009).
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; CP001579; ACU49468.1; -; Genomic_DNA.
DR   EnsemblBacteria; ACU49468; ACU49468; BMI_II334.
DR   KEGG; bmr:BMI_II334; -.
DR   HOGENOM; HOG000070228; -.
DR   KO; K01580; -.
DR   OMA; FTTSVYG; -.
DR   Proteomes; UP000002188; Chromosome 2.
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   InterPro; IPR021115; Pyridoxal-P_BS.
DR   PANTHER; PTHR43321; PTHR43321; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000002188};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171, ECO:0000313|EMBL:ACU49468.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171}.
FT   MOD_RES     281    281       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   472 AA;  53112 MW;  366F30DCCA81D455 CRC64;
     MKITLEVIMT GSNYPARDLI ASVFGTEALQ EIAASRGFPE KEMQANAVYQ IIHDELFLDG
     NARQNLATFC QTWDDDYVHK LMDLSINKNW IDKEEYPQSA AIDLRCVNMV ADLWNAPKFA
     DNATGTNTIG SSEACMLGGM AMKWRWRKKM QEMGKPTDKP NFVCGPVQVC WHKFARYWDV
     EIREIPMEPG RLFMGPEQML EAVDENTIGV VPTFGVTYTG NYEFPEPLQD ALDKLQKTKG
     LDIDIHVDAA SGGFLAPFCA PDIPWDFRLP RVKSISASGH KYGLAPLGCG WVVWRDKEAL
     PEELIFNVDY LGGQVGTFAI NFSRPAGQVI SQYYEFMRLG REGYTKVQQA AYRVAQYIAR
     EIEPLGPYEF ICAGEEKGGI PAVCFRIREG EDPGYSLYDL SERLRLTGWQ VPAFALSGKA
     SDITVMRVMC RRGFEMDLAA LFIRDFKAGI EFFKSHPSPK ITPSMGTGFH HT
//
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