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Database: UniProt/SWISS-PROT
Entry: DCE5_ARATH
LinkDB: DCE5_ARATH
Original site: DCE5_ARATH 
ID   DCE5_ARATH              Reviewed;         494 AA.
AC   Q9LSH2;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   16-JAN-2019, entry version 116.
DE   RecName: Full=Glutamate decarboxylase 5;
DE            Short=GAD 5;
DE            EC=4.1.1.15;
GN   Name=GAD5; OrderedLocusNames=At3g17760; ORFNames=MIG5.6;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   IDENTIFICATION.
RX   PubMed=10529826; DOI=10.1016/S1360-1385(99)01486-7;
RA   Shelp B.J., Bown A.W., McLean M.D.;
RT   "Metabolism and functions of gamma-aminobutyric acid.";
RL   Trends Plant Sci. 4:446-452(1999).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=18077464; DOI=10.1093/pcp/pcm171;
RA   Miyashita Y., Good A.G.;
RT   "Contribution of the GABA shunt to hypoxia-induced alanine
RT   accumulation in roots of Arabidopsis thaliana.";
RL   Plant Cell Physiol. 49:92-102(2008).
CC   -!- FUNCTION: Catalyzes the production of GABA. The calmodulin-binding
CC       is calcium-dependent and it is proposed that this may, directly or
CC       indirectly, form a calcium regulated control of GABA biosynthesis
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-glutamate = 4-aminobutanoate + CO2;
CC         Xref=Rhea:RHEA:17785, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:59888; EC=4.1.1.15;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homohexamer. Interacts with clamodulin (By similarity).
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in flowers.
CC       {ECO:0000269|PubMed:18077464}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
DR   EMBL; AB026646; BAB02870.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE76003.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE76004.1; -; Genomic_DNA.
DR   RefSeq; NP_001154621.1; NM_001161149.1.
DR   RefSeq; NP_188403.1; NM_112657.2.
DR   UniGene; At.38660; -.
DR   ProteinModelPortal; Q9LSH2; -.
DR   SMR; Q9LSH2; -.
DR   IntAct; Q9LSH2; 1.
DR   STRING; 3702.AT3G17760.1; -.
DR   iPTMnet; Q9LSH2; -.
DR   PaxDb; Q9LSH2; -.
DR   PRIDE; Q9LSH2; -.
DR   EnsemblPlants; AT3G17760.1; AT3G17760.1; AT3G17760.
DR   EnsemblPlants; AT3G17760.2; AT3G17760.2; AT3G17760.
DR   GeneID; 821044; -.
DR   Gramene; AT3G17760.1; AT3G17760.1; AT3G17760.
DR   Gramene; AT3G17760.2; AT3G17760.2; AT3G17760.
DR   KEGG; ath:AT3G17760; -.
DR   Araport; AT3G17760; -.
DR   TAIR; locus:2089779; AT3G17760.
DR   eggNOG; KOG1383; Eukaryota.
DR   eggNOG; COG0076; LUCA.
DR   InParanoid; Q9LSH2; -.
DR   KO; K01580; -.
DR   OMA; NAETGWE; -.
DR   OrthoDB; 521159at2759; -.
DR   PhylomeDB; Q9LSH2; -.
DR   BioCyc; ARA:AT3G17760-MONOMER; -.
DR   PRO; PR:Q9LSH2; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LSH2; baseline and differential.
DR   Genevisible; Q9LSH2; AT.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0009506; C:plasmodesma; IDA:TAIR.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006538; P:glutamate catabolic process; IBA:GO_Central.
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   Calmodulin-binding; Complete proteome; Decarboxylase; Lyase;
KW   Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    494       Glutamate decarboxylase 5.
FT                                /FTId=PRO_0000416956.
FT   MOD_RES     276    276       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000250}.
SQ   SEQUENCE   494 AA;  55770 MW;  7985F175E54DF262 CRC64;
     MVLATNSDSD EHLHSTFASR YVRAVVPRFK MPDHCMPKDA AYQVINDELM LDGNPRLNLA
     SFVTTWMEPE CDKLIMDSVN KNYVDMDEYP VTTELQNRCV NMIANLFHAP VGEDEAAIGC
     GTVGSSEAIM LAGLAFKRKW QHRRKAQGLP IDKPNIVTGA NVQVCWEKFA RYFEVELKEV
     KLSEDYYVMD PAKAVEMVDE NTICVAAILG STLTGEFEDV KQLNDLLAEK NAETGWETPI
     HVDAASGGFI APFLYPDLEW DFRLPWVKSI NVSGHKYGLV YAGVGWVVWR TKDDLPEELV
     FHINYLGADQ PTFTLNFSKG SSQIIAQYYQ FIRLGFEGYK NIMENCMDNA RRLREGIEMT
     GKFNIVSKDI GVPLVAFSLK DSSKHTVFEI AESLRKFGWI IPAYTMPADA QHIAVLRVVI
     REDFSRGLAD RLITHIIQVL KEIEGLPSRI AHLAAAAAVS GDDEEVKVKT AKMSLEDITK
     YWKRLVEHKR NIVC
//
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