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Database: UniProt/TrEMBL
Entry: Q3Z1N6_SHISS
LinkDB: Q3Z1N6_SHISS
Original site: Q3Z1N6_SHISS 
ID   Q3Z1N6_SHISS            Unreviewed;       466 AA.
AC   Q3Z1N6;
DT   27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2005, sequence version 1.
DT   25-OCT-2017, entry version 81.
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:AAZ88326.1};
GN   OrderedLocusNames=SSON_1631 {ECO:0000313|EMBL:AAZ88326.1};
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269 {ECO:0000313|EMBL:AAZ88326.1, ECO:0000313|Proteomes:UP000002529};
RN   [1] {ECO:0000313|EMBL:AAZ88326.1, ECO:0000313|Proteomes:UP000002529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046 {ECO:0000313|EMBL:AAZ88326.1,
RC   ECO:0000313|Proteomes:UP000002529};
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ88326.1; -; Genomic_DNA.
DR   RefSeq; WP_000358922.1; NC_007384.1.
DR   ProteinModelPortal; Q3Z1N6; -.
DR   EnsemblBacteria; AAZ88326; AAZ88326; SSON_1631.
DR   KEGG; ssn:SSON_1631; -.
DR   HOGENOM; HOG000070228; -.
DR   KO; K01580; -.
DR   OMA; RPNLVMG; -.
DR   Proteomes; UP000002529; 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:UP000002529};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171}.
FT   MOD_RES     276    276       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   466 AA;  52652 MW;  2E742F416502B52B CRC64;
     MDKKQVTDLR SELLDSRFGA KSISTIAESK RFPLHEMRDD VAFQIINDEL YLDGNARQNL
     ATFCQTWDDE NVHKLMDLSI NKNWIDKEEY PQSAAIDLRC VNMVADLWHA PAPKNGQAVG
     TNTIGSSEAC MLGGMAMKWR WRKRMEAAGK PTDKPNLVCG PVQICWHKFA RYWDVELREI
     PMRPGQLFMD PKRMIEACDE NTIGVVPTFG VTYTGNYEFP QPLHDALDKF QADTGIDIDM
     HIDAASGGFL APFVAPDIVW DFRLPRVKSI SASGHKFGLA PLGCGWVIWR DEEALPQELV
     FNVDYLGGQI GTFAINFSRP AGQVIAQYYE FLRLGREGYT KVQNASYQVA AYLADEIAKL
     GPYEFICAGR PDEGIPAVCF KLKEGEDPGY TLYDLSERLR LRGWQVPAFT LGGEATDIVV
     MRIMCRRGFE MDFAELLLED YKASLKYLSD HPKLQGIAQQ NSFKHT
//
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