GenomeNet

Database: UniProt/TrEMBL
Entry: A0A182AMV7_9CYAN
LinkDB: A0A182AMV7_9CYAN
Original site: A0A182AMV7_9CYAN 
ID   A0A182AMV7_9CYAN        Unreviewed;       462 AA.
AC   A0A182AMV7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   25-OCT-2017, entry version 11.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   Name=gadA {ECO:0000313|EMBL:SBO42884.1};
GN   ORFNames=CBM981_1173 {ECO:0000313|EMBL:SBO42884.1};
OS   Cyanobium sp. NIES-981.
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Cyanobium.
OX   NCBI_TaxID=1851505 {ECO:0000313|EMBL:SBO42884.1, ECO:0000313|Proteomes:UP000196310};
RN   [1] {ECO:0000313|EMBL:SBO42884.1, ECO:0000313|Proteomes:UP000196310}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-981 {ECO:0000313|EMBL:SBO42884.1,
RC   ECO:0000313|Proteomes:UP000196310};
RA   Lavstsen T., Jespersen J.S.;
RL   Submitted (MAY-2016) 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:RU361171};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU361171}.
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; LT578417; SBO42884.1; -; Genomic_DNA.
DR   KEGG; cyi:CBM981_1173; -.
DR   KO; K01580; -.
DR   Proteomes; UP000196310; Chromosome i.
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:UP000196310};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171, ECO:0000313|EMBL:SBO42884.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171}.
FT   MOD_RES     270    270       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   462 AA;  51029 MW;  6966F99E5599CBE1 CRC64;
     MALHLTRPTR ADAVLHSEEF TRPLPRDRFP QHGQEAAATA EILSDELLLD GNSKQNLATF
     CQTTEGPQVH ALMDLAMDKN LIDKDEYPQT AELERRCVAL LADLWHAPAG AIGCSTIGSS
     EAAMLGGMAA KWRWRARQQA AGRPTDKPNM VCGSVQICWH KFARYWDIEL REITMEPGRL
     CLTAEDVLSR VDENTILVVP TLGVTYHGLY EDVASLSAAL DGLQQRSGLD IPIHVDAASG
     GFLAPFTAPH LPPWDFRLER VKSINASGHK FGLGPLGVGW VLWRQASDLP SELVFKVSYL
     GGDMPTFQIN FSRPAGQVIA QYYTFVQLGR EGYRRIHAVS HAVAQVVAAA LQAMPLFEVL
     HDGNPHRGIP AVVWRLAPGQ DPGFSLYDLA DRLRVRGWQV PAYPLTGSLA STPFQRILVK
     RGFTREMADL LVEDIRQAVD HLHNHPRAVP LSAEEAASYN HL
//
DBGET integrated database retrieval system