ID   DCE1_ARATH              Reviewed;         502 AA.
AC   Q42521; Q9FFH9;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   27-MAR-2024, entry version 165.
DE   RecName: Full=Glutamate decarboxylase 1;
DE            Short=GAD 1 {ECO:0000303|PubMed:9700069};
DE            EC=4.1.1.15 {ECO:0000305|PubMed:9700069};
GN   Name=GAD1; Synonyms=GAD, GDH1; OrderedLocusNames=At5g17330;
GN   ORFNames=MKP11.30, MKP11_18;
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], AND INTERACTION WITH CALMODULIN.
RC   STRAIN=cv. Columbia;
RX   PubMed=7610159; DOI=10.1104/pp.108.2.551;
RA   Arazi T., Baum G., Snedden W.A., Shelp B.J., Fromm H.;
RT   "Molecular and biochemical analysis of calmodulin interactions with the
RT   calmodulin-binding domain of plant glutamate decarboxylase.";
RL   Plant Physiol. 108:551-561(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA   Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA   Miyajima N., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT   features of the 1.6 Mb regions covered by twenty physically assigned P1
RT   clones.";
RL   DNA Res. 4:215-230(1997).
RN   [3]
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   [4]
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   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CALMODULIN, AND TISSUE
RP   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   [6]
RP   TISSUE SPECIFICITY.
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   TISSUE SPECIFICITY, AND 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, INDUCTION BY HYPOXIA, AND DISRUPTION PHENOTYPE.
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   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).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.67 ANGSTROMS), SUBUNIT, BIOPHYSICOCHEMICAL
RP   PROPERTIES, ACTIVITY REGULATION, AND MUTAGENESIS OF 474-LYS-LYS-475;
RP   489-LYS-LYS-490; LYS-496; LYS-497 AND CYS-502.
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).
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}.
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};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17786;
CC         Evidence={ECO:0000305|PubMed:9700069};
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. Interacts with calmodulin with a 1:3
CC       stoichiometry. {ECO:0000269|PubMed:19580813,
CC       ECO:0000269|PubMed:7610159, ECO:0000269|PubMed:9700069}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots. Detected at low levels in
CC       shoots of young seedlings. Not detected in the root tips or in the
CC       central vascular bundle in the elongating region of mature roots.
CC       {ECO:0000269|PubMed:15604684, ECO:0000269|PubMed:18077464,
CC       ECO:0000269|PubMed:9700069, ECO:0000269|PubMed:9701597}.
CC   -!- INDUCTION: Down-regulated by salt treatment. Not induced by hypoxia.
CC       {ECO:0000269|PubMed:18077464, ECO:0000269|PubMed:20122158}.
CC   -!- DOMAIN: The N-terminus (1-57) is involved in the formation of the
CC       multimer. The C-terminus (471-502) binds calmodulin in a calcium-
CC       dependent fashion and contains probably an autoinhibitory domain.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype, but increased glutamate
CC       levels and decreased GABA levels in the roots, and loss of GABA
CC       accumulation upon heat stress. {ECO:0000269|PubMed:15604684,
CC       ECO:0000269|PubMed:18077464}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; U10034; AAA93132.1; -; mRNA.
DR   EMBL; AB005238; BAB10520.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED92414.1; -; Genomic_DNA.
DR   EMBL; AY094464; AAM19834.1; -; mRNA.
DR   EMBL; BT001047; AAN46801.1; -; mRNA.
DR   RefSeq; NP_197235.1; NM_121739.4.
DR   PDB; 3HBX; X-ray; 2.67 A; A/B/C/D/E/F=1-502.
DR   PDBsum; 3HBX; -.
DR   AlphaFoldDB; Q42521; -.
DR   SMR; Q42521; -.
DR   BioGRID; 16875; 4.
DR   STRING; 3702.Q42521; -.
DR   iPTMnet; Q42521; -.
DR   MetOSite; Q42521; -.
DR   PaxDb; 3702-AT5G17330-1; -.
DR   ProteomicsDB; 222197; -.
DR   EnsemblPlants; AT5G17330.1; AT5G17330.1; AT5G17330.
DR   GeneID; 831599; -.
DR   Gramene; AT5G17330.1; AT5G17330.1; AT5G17330.
DR   KEGG; ath:AT5G17330; -.
DR   Araport; AT5G17330; -.
DR   TAIR; AT5G17330; GAD.
DR   eggNOG; KOG1383; Eukaryota.
DR   HOGENOM; CLU_019582_2_2_1; -.
DR   InParanoid; Q42521; -.
DR   OMA; RPNLVMG; -.
DR   OrthoDB; 2783360at2759; -.
DR   PhylomeDB; Q42521; -.
DR   BioCyc; ARA:AT5G17330-MONOMER; -.
DR   BRENDA; 4.1.1.15; 399.
DR   EvolutionaryTrace; Q42521; -.
DR   PRO; PR:Q42521; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q42521; baseline and differential.
DR   GO; GO:0005516; F:calmodulin binding; IDA:TAIR.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IDA:TAIR.
DR   GO; GO:0060090; F:molecular adaptor activity; EXP:DisProt.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006536; P:glutamate metabolic process; IEA:InterPro.
DR   CDD; cd06450; DOPA_deC_like; 1.
DR   DisProt; DP02726; -.
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:SF3; GLUTAMATE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   Genevisible; Q42521; AT.
PE   1: Evidence at protein level;
KW   3D-structure; Calmodulin-binding; Decarboxylase; Lyase; Phosphoprotein;
KW   Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..502
FT                   /note="Glutamate decarboxylase 1"
FT                   /id="PRO_0000146973"
FT   REGION          469..502
FT                   /note="Calmodulin-binding"
FT   SITE            496
FT                   /note="Anchoring site for calmodulin binding; modulates the
FT                   equilibrium between pyridoxal phosphate tautomers"
FT   SITE            497
FT                   /note="Anchoring site for calmodulin binding; modulates the
FT                   equilibrium between pyridoxal phosphate tautomers"
FT   MOD_RES         8
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZPS3"
FT   MOD_RES         277
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT   MUTAGEN         474..475
FT                   /note="KK->AA: No effect."
FT                   /evidence="ECO:0000269|PubMed:19580813"
FT   MUTAGEN         489..490
FT                   /note="KK->AA: No effect."
FT                   /evidence="ECO:0000269|PubMed:19580813"
FT   MUTAGEN         496
FT                   /note="K->A: Decreased activity. When associated with
FT                   A-497; threefold decreased activity, but still
FT                   pH-dependent."
FT                   /evidence="ECO:0000269|PubMed:19580813"
FT   MUTAGEN         497
FT                   /note="K->A: Decreased activity. When associated with
FT                   A-496; threefold decreased activity, but still
FT                   pH-dependent."
FT                   /evidence="ECO:0000269|PubMed:19580813"
FT   MUTAGEN         502
FT                   /note="C->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:19580813"
FT   CONFLICT        208
FT                   /note="A -> D (in Ref. 1; AAA93132)"
FT                   /evidence="ECO:0000305"
FT   TURN            17..19
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   HELIX           22..24
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   STRAND          29..31
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   HELIX           39..49
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   HELIX           50..52
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   HELIX           56..58
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   HELIX           70..78
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   TURN            79..81
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   TURN            87..89
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   HELIX           91..107
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   STRAND          119..125
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   HELIX           126..147
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   STRAND          156..160
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   HELIX           165..173
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   STRAND          177..181
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   HELIX           192..198
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   STRAND          203..211
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   TURN            213..215
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   HELIX           221..235
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   STRAND          241..244
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   HELIX           248..250
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   HELIX           252..255
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   STRAND          268..274
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   STRAND          286..292
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   HELIX           293..295
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   HELIX           298..300
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   STRAND          302..304
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   STRAND          306..309
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   STRAND          311..313
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   HELIX           323..359
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   TURN            360..362
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   STRAND          364..366
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   STRAND          370..382
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   HELIX           388..396
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   TURN            397..399
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   STRAND          404..406
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   STRAND          415..420
FT                   /evidence="ECO:0007829|PDB:3HBX"
FT   HELIX           427..445
FT                   /evidence="ECO:0007829|PDB:3HBX"
SQ   SEQUENCE   502 AA;  57066 MW;  4E8141FF523E0E22 CRC64;
     MVLSHAVSES DVSVHSTFAS RYVRTSLPRF KMPENSIPKE AAYQIINDEL MLDGNPRLNL
     ASFVTTWMEP ECDKLIMSSI NKNYVDMDEY PVTTELQNRC VNMIAHLFNA PLEEAETAVG
     VGTVGSSEAI MLAGLAFKRK WQNKRKAEGK PVDKPNIVTG ANVQVCWEKF ARYFEVELKE
     VKLSEGYYVM DPQQAVDMVD ENTICVAAIL GSTLNGEFED VKLLNDLLVE KNKETGWDTP
     IHVDAASGGF IAPFLYPELE WDFRLPLVKS INVSGHKYGL VYAGIGWVIW RNKEDLPEEL
     IFHINYLGAD QPTFTLNFSK GSSQVIAQYY QLIRLGHEGY RNVMENCREN MIVLREGLEK
     TERFNIVSKD EGVPLVAFSL KDSSCHTEFE ISDMLRRYGW IVPAYTMPPN AQHITVLRVV
     IREDFSRTLA ERLVIDIEKV MRELDELPSR VIHKISLGQE KSESNSDNLM VTVKKSDIDK
     QRDIITGWKK FVADRKKTSG IC
//