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Database: UniProt/TrEMBL
Entry: A0A0A0KPY1_CUCSA
LinkDB: A0A0A0KPY1_CUCSA
Original site: A0A0A0KPY1_CUCSA 
ID   A0A0A0KPY1_CUCSA        Unreviewed;       499 AA.
AC   A0A0A0KPY1;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   25-APR-2018, entry version 20.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=Csa_5G348050 {ECO:0000313|EMBL:KGN50929.1};
OS   Cucumis sativus (Cucumber).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; fabids; Cucurbitales; Cucurbitaceae;
OC   Benincaseae; Cucumis.
OX   NCBI_TaxID=3659 {ECO:0000313|EMBL:KGN50929.1, ECO:0000313|Proteomes:UP000029981};
RN   [1] {ECO:0000313|EMBL:KGN50929.1, ECO:0000313|Proteomes:UP000029981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=19881527; DOI=10.1038/ng.475;
RA   Huang S., Li R., Zhang Z., Li L., Gu X., Fan W., Lucas W.J., Wang X.,
RA   Xie B., Ni P., Ren Y., Zhu H., Li J., Lin K., Jin W., Fei Z., Li G.,
RA   Staub J., Kilian A., van der Vossen E.A., Wu Y., Guo J., He J.,
RA   Jia Z., Ren Y., Tian G., Lu Y., Ruan J., Qian W., Wang M., Huang Q.,
RA   Li B., Xuan Z., Cao J., Asan null, Wu Z., Zhang J., Cai Q., Bai Y.,
RA   Zhao B., Han Y., Li Y., Li X., Wang S., Shi Q., Liu S., Cho W.K.,
RA   Kim J.Y., Xu Y., Heller-Uszynska K., Miao H., Cheng Z., Zhang S.,
RA   Wu J., Yang Y., Kang H., Li M., Liang H., Ren X., Shi Z., Wen M.,
RA   Jian M., Yang H., Zhang G., Yang Z., Chen R., Liu S., Li J., Ma L.,
RA   Liu H., Zhou Y., Zhao J., Fang X., Li G., Fang L., Li Y., Liu D.,
RA   Zheng H., Zhang Y., Qin N., Li Z., Yang G., Yang S., Bolund L.,
RA   Kristiansen K., Zheng H., Li S., Zhang X., Yang H., Wang J., Sun R.,
RA   Zhang B., Jiang S., Wang J., Du Y., Li S.;
RT   "The genome of the cucumber, Cucumis sativus L.";
RL   Nat. Genet. 41:1275-1281(2009).
RN   [2] {ECO:0000313|EMBL:KGN50929.1, ECO:0000313|Proteomes:UP000029981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=19495411; DOI=10.1371/journal.pone.0005795;
RA   Ren Y., Zhang Z., Liu J., Staub J.E., Han Y., Cheng Z., Li X., Lu J.,
RA   Miao H., Kang H., Xie B., Gu X., Wang X., Du Y., Jin W., Huang S.;
RT   "An integrated genetic and cytogenetic map of the cucumber genome.";
RL   PLoS ONE 4:E5795-E5795(2009).
RN   [3] {ECO:0000313|EMBL:KGN50929.1, ECO:0000313|Proteomes:UP000029981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20565788; DOI=10.1186/1471-2164-11-384;
RA   Guo S., Zheng Y., Joung J.G., Liu S., Zhang Z., Crasta O.R.,
RA   Sobral B.W., Xu Y., Huang S., Fei Z.;
RT   "Transcriptome sequencing and comparative analysis of cucumber flowers
RT   with different sex types.";
RL   BMC Genomics 11:384-384(2010).
RN   [4] {ECO:0000313|EMBL:KGN50929.1, ECO:0000313|Proteomes:UP000029981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22047402; DOI=10.1186/1471-2164-12-540;
RA   Li Z., Zhang Z., Yan P., Huang S., Fei Z., Lin K.;
RT   "RNA-Seq improves annotation of protein-coding genes in the cucumber
RT   genome.";
RL   BMC Genomics 12:540-540(2011).
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; CM002926; KGN50929.1; -; Genomic_DNA.
DR   RefSeq; XP_011655149.1; XM_011656847.1.
DR   EnsemblPlants; KGN50929; KGN50929; Csa_5G348050.
DR   GeneID; 101216119; -.
DR   Gramene; KGN50929; KGN50929; Csa_5G348050.
DR   KEGG; csv:101216119; -.
DR   KO; K01580; -.
DR   Proteomes; UP000029981; Chromosome 5.
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:UP000029981};
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:UP000029981}.
FT   MOD_RES     277    277       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   499 AA;  56596 MW;  C67A26016C6A5283 CRC64;
     MVLSKTASQS DVSVHSTFAS RYVRTSLPRF KMPENSIPKE AAFQIINDEL MLDGNPRLNL
     ASFVTTWMEP ECDKLIMASI NKNYVDMDEY PVTTELQNRC VNMIAHLFNA PLGDSETAVG
     VGTVGSSEAI MLAGLAFKRK WQNRRKAEGK PYDKPNIVTG ANVQVCWEKF ARYFEVELKE
     VKLREGYYVM DPEKAVEMVD ENTICVAAIL GSTLNGEFED VKLLNDLLVE KNKETGWDTP
     IHVDAASGGF IAPFIYPELE WDFRLPLVKS INVSGHKYGL VYAGIGWVIW RNKEDLPEEL
     IFHINYLGAD QPTFTLNFSK GSSQVIAQYY QLIRLGYEGY QNVMENCREN MIVLKEGLEK
     TGRFNIVSKD NGVPLVAFSL KDNTRHTEFE VSEMLRRFGW IVPAYTMPPD AQHITVLRVV
     IREDFSRTLA ERLVNDIEKT LHELDSLPSK ADIKTTVAGE ETQKNDVVVA KKSALETQRE
     ITTAWRKFVM EKKKTNGVC
//
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