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Database: UniProt/TrEMBL
Entry: Q8LKR4_TOBAC
LinkDB: Q8LKR4_TOBAC
Original site: Q8LKR4_TOBAC 
ID   Q8LKR4_TOBAC            Unreviewed;       496 AA.
AC   Q8LKR4;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   25-OCT-2017, entry version 62.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; asterids; lamiids; Solanales; Solanaceae;
OC   Nicotianoideae; Nicotianeae; Nicotiana.
OX   NCBI_TaxID=4097 {ECO:0000313|EMBL:AAM48129.1};
RN   [1] {ECO:0000313|EMBL:AAM48129.1}
RP   NUCLEOTIDE SEQUENCE.
RX   DOI=10.1023/A:1023483106582;
RA   McLean M.D., Yevtushenko D., Deschene A., Van Cauwenberghe O.R.,
RA   Makhmoudova A., Potter J.W., Bown A.W., Shelp B.J.;
RT   "Overexpression of glutamate decarboxylase in transgenic tobacco
RT   plants confers resistance to the northern root-knot nematode.";
RL   Mol. Breed. 11:277-285(2003).
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; AF506366; AAM48129.1; -; mRNA.
DR   RefSeq; NP_001312769.1; NM_001325840.1.
DR   UniGene; Nta.3619; -.
DR   ProteinModelPortal; Q8LKR4; -.
DR   GeneID; 107809522; -.
DR   KEGG; nta:107809522; -.
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   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   2: Evidence at transcript level;
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}.
FT   MOD_RES     277    277       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   496 AA;  55966 MW;  4771CF71BC478349 CRC64;
     MVLSKTASES DVSIHSTFAS RYVRTSLPRF KMPENSIPKE AAYQIINDEL MLDGNPRLNL
     ASFVTTWMEP ECNTLMMDSI NKNYVDMDEY PVTTELQNRC VNMIAHLFNA PLGDGETAVG
     VGTVGSSEAI MLAGLAFKRK WQNKMKAQGK PFDKPNIVTG ANVQVCWEKF ARYFEVELKE
     VKLSDGYYVM DPEKAVEMVD ENTICVAAIL GSTLNGEFED VKRLNDLLIE KNKETGWDTP
     IHVDAASGGF IAPFLYPELE WDFRLPLVKS INVSGHKYGL VYAGIGWAIW RNKEDLPDEL
     IFHINYLGAD QPTFTLNFSK GSSQVIAQYY QLIRLGFEGY KNVMENCQEN ARVLREGIEK
     SGRFNIISKE IGVPLVAFSL KDNSQHNEFE ISETLRRFGW IVPAYTMPPN AQHVTVLRVV
     IREDFSRTLA ERLVIDIEKV LHELDTLPAR VNAKLAVAEA NGSGVHKKTD REVQLEITTA
     WKKFVADKKK KTNGVC
//
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