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Database: UniProt/TrEMBL
Entry: V7BM00_PHAVU
LinkDB: V7BM00_PHAVU
Original site: V7BM00_PHAVU 
ID   V7BM00_PHAVU            Unreviewed;       501 AA.
AC   V7BM00;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   28-FEB-2018, entry version 26.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=PHAVU_006G087600g {ECO:0000313|EMBL:ESW18987.1};
OS   Phaseolus vulgaris (Kidney bean) (French bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
OC   Phaseoleae; Phaseolus.
OX   NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW18987.1, ECO:0000313|Proteomes:UP000000226};
RN   [1] {ECO:0000313|EMBL:ESW18987.1, ECO:0000313|Proteomes:UP000000226}
RP   NUCLEOTIDE SEQUENCE.
RA   Schmutz J., McClean P., Shu S., Cregan P., Rokhsar D., Jackson S.;
RL   Submitted (APR-2013) 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}.
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DR   EMBL; CM002293; ESW18987.1; -; Genomic_DNA.
DR   RefSeq; XP_007146993.1; XM_007146931.1.
DR   EnsemblPlants; ESW18987; ESW18987; PHAVU_006G087600g.
DR   GeneID; 18628219; -.
DR   Gramene; ESW18987; ESW18987; PHAVU_006G087600g.
DR   KEGG; pvu:PHAVU_006G087600g; -.
DR   KO; K01580; -.
DR   PhylomeDB; V7BM00; -.
DR   Proteomes; UP000000226; Chromosome 6.
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:UP000000226};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000226}.
FT   MOD_RES     277    277       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   501 AA;  56973 MW;  C76ECC37A0A20E28 CRC64;
     MVLSKTASES DVSVHSTFAS RYVRTSLPRF RMPEESIPKE AAYQIINDEL MLDGNPRLNL
     ASFVTTWMEP ECDKLIMASI NKNYVDMDEY PVTTELQNRC VNMIAHLFNA PLQDSEAAVG
     VGTVGSSEAI MLAGLAFKRK WQNRRKEEGK PYDKPNIVTG ANVQVCWEKF ARYFEVELKE
     VKLRDGYYVM DPDQAVELVD ENTICVAAIL GSTLNGEFED VKRLNDLLVE KNKQTGWDTP
     IHVDAASGGF IAPFIYPELE WDFRLPLVKS INVSGHKYGL VYAGIGWIIW RSKEDLPEEL
     IFHINYLGAD QPTFTLNFSK GSSQVIAQYY QLIRLGYEGY RNVMENCRDN MLVLKEGLEK
     TGRFTIVSKD DGVPLVAFTL KDHTHFNEFQ ISDMLRRFGW IVPAYTMPPD AQHVTVLRVV
     IREDFSRTLA ERLVADVEKV VHELDALPVR VISSSSVTVN TEENGKVVKK SALETQREIT
     AIWRKFVLER KKLNDKMSGV C
//
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