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   27-MAR-2024, entry version 145.
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;
GN   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   IntAct; Q42472; 1.
DR   STRING; 3702.Q42472; -.
DR   iPTMnet; Q42472; -.
DR   MetOSite; Q42472; -.
DR   PaxDb; 3702-AT1G65960-2; -.
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; AT1G65960; GAD2.
DR   eggNOG; KOG1383; Eukaryota.
DR   HOGENOM; CLU_019582_2_2_1; -.
DR   InParanoid; Q42472; -.
DR   OMA; ESVCTMF; -.
DR   OrthoDB; 2783360at2759; -.
DR   PhylomeDB; Q42472; -.
DR   BioCyc; ARA:AT1G65960-MONOMER; -.
DR   PRO; PR:Q42472; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q42472; baseline and differential.
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:0006536; P:glutamate metabolic process; IDA:TAIR.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; TAS:TAIR.
DR   CDD; cd06450; DOPA_deC_like; 1.
DR   Gene3D; 3.90.1150.160; -; 1.
DR   Gene3D; 4.10.280.50; -; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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   NCBIfam; TIGR01788; Glu-decarb-GAD; 1.
DR   PANTHER; PTHR43321; GLUTAMATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43321:SF19; GLUTAMATE DECARBOXYLASE 2; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   Genevisible; Q42472; AT.
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
//