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Database: UniProt/TrEMBL
Entry: A0A0F7HHJ5_SERFO
LinkDB: A0A0F7HHJ5_SERFO
Original site: A0A0F7HHJ5_SERFO 
ID   A0A0F7HHJ5_SERFO        Unreviewed;       466 AA.
AC   A0A0F7HHJ5;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   05-JUL-2017, entry version 18.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=WN53_24805 {ECO:0000313|EMBL:AKG72082.1};
OS   Serratia fonticola.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=47917 {ECO:0000313|EMBL:AKG72082.1, ECO:0000313|Proteomes:UP000034699};
RN   [1] {ECO:0000313|EMBL:AKG72082.1, ECO:0000313|Proteomes:UP000034699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4576 {ECO:0000313|EMBL:AKG72082.1,
RC   ECO:0000313|Proteomes:UP000034699};
RA   Chan K.-G., Ee R.;
RT   "Complete Genome Sequencing of Serratia Fonticola DSM-4576.";
RL   Submitted (APR-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:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; CP011254; AKG72082.1; -; Genomic_DNA.
DR   RefSeq; WP_024485171.1; NZ_CP011254.1.
DR   EnsemblBacteria; AKG72082; AKG72082; WN53_24805.
DR   KEGG; sfw:WN53_24805; -.
DR   PATRIC; fig|47917.8.peg.5190; -.
DR   KO; K01580; -.
DR   OMA; RPNLVMG; -.
DR   Proteomes; UP000034699; 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   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:UP000034699};
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:UP000034699}.
FT   MOD_RES     273    273       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   466 AA;  51828 MW;  ECC0CF043E108CB6 CRC64;
     MSNSNQKNNS NVNDDVYSSI DLAISLPKSG FPDAERNPRH VFSAIRDELM LDGNSRQNLA
     TFCQTWVDEE IRDLMDLSID KNMIDKDEYP QTAEIEARCV RMLADLWKSP SPGTTLGCST
     IGSSEAAMLG GLALKWQWRK KRAAQGLTTD KPNMICGPVQ ICWHKFARYF DVELREIPLE
     GDRLIMSPEE VLKRVDENTI GVVPTLGVTF TCQYEPVKAV SDALDKLQQD TGLDIPIHVD
     GASGGFLAPF CAPDLEWDFR LPRVKSINTS GHKFGLAPLG AGWVVWREAA DLPEELIFNV
     NYLGGNMPTF ALNFSRPGGQ IIAQYYNFLR LGREGYAKVH NACYATAQYL ADEIGKLGPF
     EILFDGDSGK GIPALAWKLK EDANIGGYTL YDLADKLRSR GWQVPAYSMP ANREDLVIQR
     ILVRHGVSFD LGSLLLDDLK RALEHFESHP VVNPLTEDEA AGFNHG
//
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