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Database: UniProt/SWISS-PROT
Entry: DCE2_ARATH
LinkDB: DCE2_ARATH
Original site: DCE2_ARATH 
ID   DCE2_ARATH              Reviewed;         494 AA.
AC   Q42472; Q8RXH0; Q944L6;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   16-JAN-2019, entry version 123.
DE   RecName: Full=Glutamate decarboxylase 2;
DE            Short=GAD 2;
DE            EC=4.1.1.15;
GN   Name=GAD2; Synonyms=GDH2; OrderedLocusNames=At1g65960;
GN   ORFNames=F12P19.12;
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 [MRNA], FUNCTION, INTERACTION WITH CLAMODULIN, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=9700069; DOI=10.1023/A:1006047623263;
RA   Zik M., Arazi T., Snedden W.A., Fromm H.;
RT   "Two isoforms of glutamate decarboxylase in Arabidopsis are regulated
RT   by calcium/calmodulin and differ in organ distribution.";
RL   Plant Mol. Biol. 37:967-975(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9112779; DOI=10.1104/pp.113.4.1329;
RA   Turano F.J., Thakkar S.S., Fang T., Weisemann J.M.;
RT   "Characterization and expression of NAD(H)-dependent glutamate
RT   dehydrogenase genes in Arabidopsis.";
RL   Plant Physiol. 113:1329-1341(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:816-820(2000).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [6]
RP   TISSUE SPECIFICITY, AND INDUCTION BY NITROGEN.
RX   PubMed=9701597; DOI=10.1104/pp.117.4.1411;
RA   Turano F.J., Fang T.K.;
RT   "Characterization of two glutamate decarboxylase cDNA clones from
RT   Arabidopsis.";
RL   Plant Physiol. 117:1411-1421(1998).
RN   [7]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia;
RX   PubMed=15604684; DOI=10.1007/s11103-004-0650-z;
RA   Bouche N., Fait A., Zik M., Fromm H.;
RT   "The root-specific glutamate decarboxylase (GAD1) is essential for
RT   sustaining GABA levels in Arabidopsis.";
RL   Plant Mol. Biol. 55:315-325(2004).
RN   [8]
RP   TISSUE SPECIFICITY, AND INDUCTION BY HYPOXIA.
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).
RN   [9]
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX   PubMed=19580813; DOI=10.1016/j.jmb.2009.06.080;
RA   Gut H., Dominici P., Pilati S., Astegno A., Petoukhov M.V.,
RA   Svergun D.I., Gruetter M.G., Capitani G.;
RT   "A common structural basis for pH- and calmodulin-mediated regulation
RT   in plant glutamate decarboxylase.";
RL   J. Mol. Biol. 392:334-351(2009).
RN   [10]
RP   INDUCTION BY SALT.
RX   PubMed=20122158; DOI=10.1186/1471-2229-10-20;
RA   Renault H., Roussel V., El Amrani A., Arzel M., Renault D.,
RA   Bouchereau A., Deleu C.;
RT   "The Arabidopsis pop2-1 mutant reveals the involvement of GABA
RT   transaminase in salt stress tolerance.";
RL   BMC Plant Biol. 10:20-20(2010).
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       {ECO:0000269|PubMed:9700069}.
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   -!- ACTIVITY REGULATION: Up-regulated by calmodulin binding at
CC       physiological pH. {ECO:0000269|PubMed:19580813}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.0. {ECO:0000269|PubMed:19580813};
CC   -!- SUBUNIT: Homohexamer (By similarity). Interacts with calmodulin.
CC       {ECO:0000250, ECO:0000269|PubMed:9700069}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q42472-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed in roots, inflorescence stems,
CC       flowers, siliques and leaves. {ECO:0000269|PubMed:18077464,
CC       ECO:0000269|PubMed:9700069, ECO:0000269|PubMed:9701597}.
CC   -!- INDUCTION: Up-regulated by salt or nitrogen treatments. Down-
CC       regulated by hypoxia. {ECO:0000269|PubMed:18077464,
CC       ECO:0000269|PubMed:20122158, ECO:0000269|PubMed:9701597}.
CC   -!- DOMAIN: The C-terminus (463-494) binds calmodulin in a calcium-
CC       dependent fashion.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC       {ECO:0000269|PubMed:15604684}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL91148.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=AAL91148.1; Type=Frameshift; Positions=70; Evidence={ECO:0000305};
DR   EMBL; U49937; AAC31617.1; -; mRNA.
DR   EMBL; U46665; AAC33485.1; -; mRNA.
DR   EMBL; AC009513; AAF06056.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE34445.1; -; Genomic_DNA.
DR   EMBL; AF428294; AAL16126.1; -; mRNA.
DR   EMBL; AF428372; AAL16302.1; -; mRNA.
DR   EMBL; AY124873; AAM70582.1; -; mRNA.
DR   EMBL; AY081259; AAL91148.1; ALT_SEQ; mRNA.
DR   PIR; H96683; H96683.
DR   RefSeq; NP_001117556.1; NM_001124084.1. [Q42472-1]
DR   UniGene; At.19149; -.
DR   UniGene; At.20543; -.
DR   UniGene; At.24993; -.
DR   UniGene; At.66846; -.
DR   ProteinModelPortal; Q42472; -.
DR   SMR; Q42472; -.
DR   STRING; 3702.AT1G65960.2; -.
DR   iPTMnet; Q42472; -.
DR   PaxDb; Q42472; -.
DR   PRIDE; Q42472; -.
DR   DNASU; 842908; -.
DR   EnsemblPlants; AT1G65960.2; AT1G65960.2; AT1G65960. [Q42472-1]
DR   GeneID; 842908; -.
DR   Gramene; AT1G65960.2; AT1G65960.2; AT1G65960. [Q42472-1]
DR   KEGG; ath:AT1G65960; -.
DR   Araport; AT1G65960; -.
DR   TAIR; locus:2009704; AT1G65960.
DR   eggNOG; KOG1383; Eukaryota.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000070228; -.
DR   InParanoid; Q42472; -.
DR   KO; K01580; -.
DR   OMA; DESVCTM; -.
DR   OrthoDB; 521159at2759; -.
DR   PhylomeDB; Q42472; -.
DR   BioCyc; ARA:AT1G65960-MONOMER; -.
DR   PRO; PR:Q42472; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q42472; baseline and differential.
DR   Genevisible; Q42472; AT.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IDA:TAIR.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006538; P:glutamate catabolic process; IBA:GO_Central.
DR   GO; GO:0006536; P:glutamate metabolic process; IDA:TAIR.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; TAS:TAIR.
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   1: Evidence at protein level;
KW   Alternative splicing; Calmodulin-binding; Complete proteome;
KW   Decarboxylase; Lyase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    494       Glutamate decarboxylase 2.
FT                                /FTId=PRO_0000146974.
FT   REGION      463    494       Calmodulin-binding.
FT   SITE        488    488       Anchoring site for calmodulin binding;
FT                                modulates the equilibrium between
FT                                pyridoxal phosphate tautomers.
FT                                {ECO:0000250}.
FT   SITE        489    489       Anchoring site for calmodulin binding;
FT                                modulates the equilibrium between
FT                                pyridoxal phosphate tautomers.
FT                                {ECO:0000250}.
FT   MOD_RES     276    276       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000250}.
FT   CONFLICT    410    410       A -> V (in Ref. 5; AAL16126).
FT                                {ECO:0000305}.
FT   CONFLICT    461    461       E -> K (in Ref. 5; AAL91148).
FT                                {ECO:0000305}.
SQ   SEQUENCE   494 AA;  56141 MW;  741E83A25DCBC48C CRC64;
     MVLTKTATND ESVCTMFGSR YVRTTLPKYE IGENSIPKDA AYQIIKDELM LDGNPRLNLA
     SFVTTWMEPE CDKLIMDSIN KNYVDMDEYP VTTELQNRCV NIIARLFNAP LEESETAVGV
     GTVGSSEAIM LAGLAFKRKW QNKRKAEGKP YDKPNIVTGA NVQVCWEKFA RYFEVELKEV
     NLSEGYYVMD PDKAAEMVDE NTICVAAILG STLNGEFEDV KRLNDLLVKK NEETGWNTPI
     HVDAASGGFI APFIYPELEW DFRLPLVKSI NVSGHKYGLV YAGIGWVVWR AAEDLPEELI
     FHINYLGADQ PTFTLNFSKG SSQIIAQYYQ LIRLGFEGYK NVMENCIENM VVLKEGIEKT
     ERFNIVSKDQ GVPVVAFSLK DHSFHNEFEI SEMLRRFGWI VPAYTMPADA QHITVLRVVI
     REDFSRTLAE RLVADISKVL HELDTLPSKI SKKMGIEGIA ENVKEKKMEK EILMEVIVGW
     RKFVKERKKM NGVC
//
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