GenomeNet

Database: UniProt/TrEMBL
Entry: A0A097R8A8_HAFAL
LinkDB: A0A097R8A8_HAFAL
Original site: A0A097R8A8_HAFAL 
ID   A0A097R8A8_HAFAL        Unreviewed;       426 AA.
AC   A0A097R8A8;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   05-JUL-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=AT03_19075 {ECO:0000313|EMBL:AIU74973.1};
OS   Hafnia alvei FB1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Hafnia.
OX   NCBI_TaxID=1453496 {ECO:0000313|EMBL:AIU74973.1, ECO:0000313|Proteomes:UP000029986};
RN   [1] {ECO:0000313|EMBL:AIU74973.1, ECO:0000313|Proteomes:UP000029986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FB1 {ECO:0000313|EMBL:AIU74973.1,
RC   ECO:0000313|Proteomes:UP000029986};
RX   PubMed=25075225; DOI=10.1186/1757-4749-6-29;
RA   Tan J.Y., Yin W.F., Chan K.G.;
RT   "Gene clusters of Hafnia alvei strain FB1 important in survival and
RT   pathogenesis: a draft genome perspective.";
RL   Gut Pathog 6:29-29(2014).
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP009706; AIU74973.1; -; Genomic_DNA.
DR   EnsemblBacteria; AIU74973; AIU74973; AT03_19075.
DR   KEGG; hav:AT03_19075; -.
DR   PATRIC; fig|1453496.5.peg.3924; -.
DR   KO; K01580; -.
DR   Proteomes; UP000029986; 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:UP000029986};
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:UP000029986}.
FT   MOD_RES     233    233       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   426 AA;  47906 MW;  AC7508930655A8A1 CRC64;
     MFNAVRDELM LDGNSRQNLA TFCQTWVDEE IRDLMDLSID KNMIDKDEYP QTAEIETRCV
     HMLADLWNSP TPETTLGCST IGSSEAAMLG GLALKWQWRK KRAALGLSTD KPNLICGPVQ
     ICWHKFARYF DVELREIPLQ GDRLIMSPEE VLKRVDENTI GVVPTLGVTF TCQYEPVKQV
     HDALDQLQKE TGLDIPMHID GASGGFLAPF CAPDLEWDFR LPRVKSINAS GHKFGLAPLG
     TGWVIWREAA DLPQELIFNV NYLGGDMPTF ALNFSRPGGQ IIAQYYNFLR LGREGYAKIH
     NACYSTAQYL AQEIEKLGPF EMIFDGDCEK GIPALAWKLK DNASTNGYTL YDLADRLRSR
     GWQVPAYSMP AEREDLVVQR ILVRHGVSRD LGSLLIDDMK RALDYFEKHP VSHALSAKEA
     GGFNHG
//
DBGET integrated database retrieval system