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Database: UniProt/TrEMBL
Entry: A0A068MZU5_SYNY4
LinkDB: A0A068MZU5_SYNY4
Original site: A0A068MZU5_SYNY4 
ID   A0A068MZU5_SYNY4        Unreviewed;       467 AA.
AC   A0A068MZU5;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   20-JUN-2018, entry version 22.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   Name=gad {ECO:0000313|EMBL:AIE75400.1};
GN   ORFNames=D082_28720 {ECO:0000313|EMBL:AIE75400.1};
OS   Synechocystis sp. (strain PCC 6714) (Aphanocapsa sp. (strain PCC
OS   6714)).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1147 {ECO:0000313|EMBL:AIE75400.1, ECO:0000313|Proteomes:UP000027989};
RN   [1] {ECO:0000313|EMBL:AIE75400.1, ECO:0000313|Proteomes:UP000027989}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PCC 6714 {ECO:0000313|EMBL:AIE75400.1};
RX   PubMed=24408876; DOI=10.1093/dnares/dst055;
RA   Kopf M., Klahn S., Pade N., Weingartner C., Hagemann M., Voss B.,
RA   Hess W.R.;
RT   "Comparative Genome Analysis of the Closely Related Synechocystis
RT   Strains PCC 6714 and PCC 6803.";
RL   DNA Res. 21:255-266(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:RU361171};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU361171}.
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DR   EMBL; CP007542; AIE75400.1; -; Genomic_DNA.
DR   RefSeq; WP_028947225.1; NZ_CP007542.1.
DR   EnsemblBacteria; AIE75400; AIE75400; D082_28720.
DR   KEGG; syj:D082_28720; -.
DR   KO; K01580; -.
DR   Proteomes; UP000027989; Genome.
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   InterPro; IPR010107; Glutamate_decarboxylase.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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:UP000027989};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171, ECO:0000313|EMBL:AIE75400.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171}.
FT   MOD_RES     279    279       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   467 AA;  53045 MW;  7BE04E010BB1E6D5 CRC64;
     MVHKKIDLNQ LSPLESLLTP TYAARGLVNP VSKYEMPETE MLPAIAYNLI HDELGLDGNS
     RLNLATFVTT WMEPEARQLM ADTFDKNMID KDEYPQTAEI ELRCVNILSR LWNAPENAEA
     TGCSTIGSSE AAMLGGMAMK WKWRKRRQIE GKSGDRPNLV MGINVQVCWE KFCRYWEVEP
     RFVPMEGDRY HISPDEAVKL IDENTIGVIG ILGSTFDGSY EPIEALNDAL EILNERTGWQ
     VPLHVDAASG GFIAPFLDPD LRWDFRLPWV KSINTSGHKY GLVYPGVGWI IWRDKEELPE
     ELIFHCSYLG GDLPNFALNF SRPGNQVVAQ YYNFLRLGKE GYRKIQQACR DTALYLSSKI
     AQLGPFELLT DGGDIPVFAW KLKDDVLAHS CYTLYDMADK LRERGWLAPA YPMPKNRDDL
     VVQRIVVKEG FSRDMADILL ADMERAIAYF VSQPDHKPKQ GGSHFSH
//
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