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 03-AUG-2022, entry version 137.
DE RecName: Full=Glutamate decarboxylase 2;
DE Short=GAD 2 {ECO:0000303|PubMed:9700069, ECO:0000303|PubMed:9701597};
DE EC=4.1.1.15 {ECO:0000305|PubMed:9700069, ECO:0000305|PubMed:9701597};
GN Name=GAD2; Synonyms=GDH2; OrderedLocusNames=At1g65960; ORFNames=F12P19.12;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH
RP CALMODULIN, AND 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 by
RT 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., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., 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., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis 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 reference
RT 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., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND INDUCTION BY
RP 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 accumulation in
RT 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., Svergun D.I.,
RA Gruetter M.G., Capitani G.;
RT "A common structural basis for pH- and calmodulin-mediated regulation in
RT 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., Bouchereau A.,
RA Deleu C.;
RT "The Arabidopsis pop2-1 mutant reveals the involvement of GABA transaminase
RT in salt stress tolerance.";
RL BMC Plant Biol. 10:20-20(2010).
CC -!- FUNCTION: Catalyzes the conversion of glutamate to 4-aminobutanoate
CC (GABA). The calmodulin-binding is calcium-dependent and it is proposed
CC to directly or indirectly form a calcium regulated control of GABA
CC biosynthesis. {ECO:0000269|PubMed:9700069, ECO:0000269|PubMed:9701597}.
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 Evidence={ECO:0000305|PubMed:9700069, ECO:0000305|PubMed:9701597};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17786;
CC Evidence={ECO:0000305|PubMed:9700069, ECO:0000305|PubMed:9701597};
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, flowers,
CC siliques and leaves. {ECO:0000269|PubMed:18077464,
CC ECO:0000269|PubMed:9700069, ECO:0000269|PubMed:9701597}.
CC -!- INDUCTION: Up-regulated by salt treatment (PubMed:20122158). Up-
CC regulated by nitrogen treatments such as ammonium chloride, ammonium
CC nitrate, glutamate and glutamine but not by potassium nitrate
CC (PubMed:9701597). Down-regulated by hypoxia (PubMed:18077464).
CC {ECO:0000269|PubMed:18077464, ECO:0000269|PubMed:20122158,
CC 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=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL91148.1; Type=Frameshift; Evidence={ECO:0000305};
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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 AlphaFoldDB; Q42472; -.
DR SMR; Q42472; -.
DR STRING; 3702.AT1G65960.2; -.
DR iPTMnet; Q42472; -.
DR MetOSite; Q42472; -.
DR PaxDb; Q42472; -.
DR PRIDE; Q42472; -.
DR ProteomicsDB; 224681; -. [Q42472-1]
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 HOGENOM; CLU_019582_2_2_1; -.
DR InParanoid; Q42472; -.
DR OMA; HNEFEIA; -.
DR PhylomeDB; Q42472; -.
DR BioCyc; ARA:AT1G65960-MON; -.
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; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
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; Decarboxylase; Lyase;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..494
FT /note="Glutamate decarboxylase 2"
FT /id="PRO_0000146974"
FT REGION 463..494
FT /note="Calmodulin-binding"
FT SITE 488
FT /note="Anchoring site for calmodulin binding; modulates the
FT equilibrium between pyridoxal phosphate tautomers"
FT /evidence="ECO:0000250"
FT SITE 489
FT /note="Anchoring site for calmodulin binding; modulates the
FT equilibrium between pyridoxal phosphate tautomers"
FT /evidence="ECO:0000250"
FT MOD_RES 276
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 410
FT /note="A -> V (in Ref. 5; AAL16126)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="E -> K (in Ref. 5; AAL91148)"
FT /evidence="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
