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Database: UniProt/TrEMBL
Entry: A0A127CQ98_9RHIZ
LinkDB: A0A127CQ98_9RHIZ
Original site: A0A127CQ98_9RHIZ 
ID   A0A127CQ98_9RHIZ        Unreviewed;       464 AA.
AC   A0A127CQ98;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   05-JUL-2017, entry version 12.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=AZF01_20795 {ECO:0000313|EMBL:AMM87032.1};
OS   Martelella sp. AD-3.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Aurantimonadaceae; Martelella.
OX   NCBI_TaxID=686597 {ECO:0000313|EMBL:AMM87032.1, ECO:0000313|Proteomes:UP000070688};
RN   [1] {ECO:0000313|EMBL:AMM87032.1, ECO:0000313|Proteomes:UP000070688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AD-3 {ECO:0000313|EMBL:AMM87032.1,
RC   ECO:0000313|Proteomes:UP000070688};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-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:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; CP014275; AMM87032.1; -; Genomic_DNA.
DR   RefSeq; WP_024706762.1; NZ_CP014275.1.
DR   EnsemblBacteria; AMM87032; AMM87032; AZF01_20795.
DR   KEGG; maad:AZF01_20795; -.
DR   KO; K01580; -.
DR   Proteomes; UP000070688; 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:UP000070688};
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:UP000070688}.
FT   MOD_RES     273    273       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   464 AA;  52133 MW;  014430D2F7AAB52C CRC64;
     MAEEREQDGL FDPNDETYGA ADLSAILPKS GFPEKERAPR LAYAAIHDEL LLDGNARQNL
     ATFCQTWEEP EIHKLMDDCI DKNMIDKDEY PQTAEIEARC VRMLGDLWHA PEGPVTGTST
     TGSSEAAMLG GLAMKRRWEA RRKAEGKPTD KPNLITGPVQ ICWHKFTRYW DVEHREIPME
     NGRLLMTPEE VLELCDENTI GVVPTLGVTY TGEYEPVKAV SDALDDLQAR TGLDIPIHVD
     GASGGFLAPF CAPELEWDFR LPRVKSINAS GHKFGLSPLG VGWVLWREDK DLPEEMVFWV
     NYLGGNMRDI ALNFSRPGGQ VICQYYNFLR LGRQGYRKVH EACYRSAAFL AEELEKTGLV
     DIVFDGDMKK GIPAVSWKLK DGLKTNYTLF DLADRLRTRG WQVPAYTLPA NCQDQAIQRI
     LVRNGVSIDL CSLLIEDIKA AVDYFKAHPI STPLTEDEAS GFHH
//
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