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Database: UniProt/TrEMBL
Entry: V9SJB6_MALDO
LinkDB: V9SJB6_MALDO
Original site: V9SJB6_MALDO 
ID   V9SJB6_MALDO            Unreviewed;       501 AA.
AC   V9SJB6;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   23-MAY-2018, entry version 23.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   Name=GAD2 {ECO:0000313|EMBL:AHC56661.1};
OS   Malus domestica (Apple) (Pyrus malus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; fabids; Rosales; Rosaceae; Amygdaloideae;
OC   Maleae; Malus.
OX   NCBI_TaxID=3750 {ECO:0000313|EMBL:AHC56661.1};
RN   [1] {ECO:0000313|EMBL:AHC56661.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mature fruit {ECO:0000313|EMBL:AHC56661.1};
RX   PubMed=24074460; DOI=10.1186/1471-2229-13-144;
RA   Trobacher C.P., Zarei A., Liu J., Clark S.M., Bozzo G.G., Shelp B.J.;
RT   "Calmodulin-dependent and calmodulin-independent glutamate
RT   decarboxylases in apple fruit.";
RL   BMC Plant Biol. 13:144-144(2013).
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; KC812243; AHC56661.1; -; mRNA.
DR   RefSeq; NP_001280764.1; NM_001293835.1.
DR   GeneID; 103444237; -.
DR   KEGG; mdm:103444237; -.
DR   KO; K01580; -.
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   2: Evidence at transcript level;
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU000382, ECO:0000313|EMBL:AHC56661.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES     277    277       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   501 AA;  56932 MW;  62B57214DFA569DF CRC64;
     MALSRTASES DVSVHSTFAS RYVRTSLPRF KMAENSIPKE AAYQIINDEL MLDGNPRLNL
     ASFVTTWMEP ECDKLMMASI NKNYVDMDEY PVTTELQNRC VNMIAHLFNA PLGDSEAAIG
     VGTVGSSEAI MLAGLAFKRK WQNKRRAEGK PVDKPNIVTG ANVQVCWEKF ARYFEVELKE
     VKLRDGYYVM DPEKAVEMVD ENTICVAAIL GSTLNGEFED VKLLNDLLIE KNKETGWDTT
     IHVDAASGGF IAPFLYPELE WDFRLPLVKS INVSGHKYGL VYAGIGWVIW RNKEDLPEEL
     IFHINYLGAD QPTFTLNFSK GSSQVIAQYY QLIRLGFEGY RNVMENCREN MVVLKEGLEK
     TGRFNIVSKD EGVPLVAFSL KDNHRHDEFE ISDLLRRFGW IVPAYTMPPD AQHITVLRVV
     IREDFSRTLA ERLVNDIKKV LRELDTLPSK LSSNVKAADE EGEKPGTTLE SKKSDLEKTR
     EITIVWRKFV MARKQKMNVV C
//
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