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Database: UniProt/SWISS-PROT
Entry: DCE1_ARATH
LinkDB: DCE1_ARATH
Original site: DCE1_ARATH 
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   25-APR-2018, entry version 135.
DE   RecName: Full=Glutamate decarboxylase 1;
DE            Short=GAD 1;
DE            EC=4.1.1.15;
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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
RT   the 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
RT   P1 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
RT   reference 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.,
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   [5]
RP   FUNCTION, INTERACTION WITH CLAMODULIN, 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
RT   by 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
RT   accumulation in 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.,
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).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.67 ANGSTROMS), SUBUNIT, BIOPHYSICOCHEMICAL
RP   PROPERTIES, ENZYME 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.,
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).
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: L-glutamate = 4-aminobutanoate + CO(2).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- ENZYME 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 clamodulin 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
CC       hypoxia. {ECO:0000269|PubMed:18077464,
CC       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
CC       glutamate levels and decreased GABA levels in the roots, and loss
CC       of GABA accumulation upon heat stress.
CC       {ECO:0000269|PubMed:15604684, ECO:0000269|PubMed:18077464}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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   UniGene; At.25228; -.
DR   PDB; 3HBX; X-ray; 2.67 A; A/B/C/D/E/F=1-502.
DR   PDBsum; 3HBX; -.
DR   ProteinModelPortal; Q42521; -.
DR   SMR; Q42521; -.
DR   BioGrid; 16875; 4.
DR   STRING; 3702.AT5G17330.1; -.
DR   iPTMnet; Q42521; -.
DR   PaxDb; Q42521; -.
DR   PRIDE; Q42521; -.
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; locus:2167240; AT5G17330.
DR   eggNOG; KOG1383; Eukaryota.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000070228; -.
DR   InParanoid; Q42521; -.
DR   KO; K01580; -.
DR   OMA; PVIAQYF; -.
DR   OrthoDB; EOG093607ZR; -.
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   Genevisible; Q42521; AT.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0005516; F:calmodulin binding; IDA:TAIR.
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; IEA:InterPro.
DR   GO; GO:0046686; P:response to cadmium ion; IEP: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   3D-structure; Calmodulin-binding; Complete proteome; Decarboxylase;
KW   Lyase; Phosphoprotein; Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    502       Glutamate decarboxylase 1.
FT                                /FTId=PRO_0000146973.
FT   REGION      469    502       Calmodulin-binding.
FT   SITE        496    496       Anchoring site for calmodulin binding;
FT                                modulates the equilibrium between
FT                                pyridoxal phosphate tautomers.
FT   SITE        497    497       Anchoring site for calmodulin binding;
FT                                modulates the equilibrium between
FT                                pyridoxal phosphate tautomers.
FT   MOD_RES       8      8       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9ZPS3}.
FT   MOD_RES     277    277       N6-(pyridoxal phosphate)lysine.
FT   MUTAGEN     474    475       KK->AA: No effect.
FT                                {ECO:0000269|PubMed:19580813}.
FT   MUTAGEN     489    490       KK->AA: No effect.
FT                                {ECO:0000269|PubMed:19580813}.
FT   MUTAGEN     496    496       K->A: Decreased activity. When associated
FT                                with A-497; threefold decreased activity,
FT                                but still pH-dependent.
FT                                {ECO:0000269|PubMed:19580813}.
FT   MUTAGEN     497    497       K->A: Decreased activity. When associated
FT                                with A-496; threefold decreased activity,
FT                                but still pH-dependent.
FT                                {ECO:0000269|PubMed:19580813}.
FT   MUTAGEN     502    502       C->A: No effect.
FT                                {ECO:0000269|PubMed:19580813}.
FT   CONFLICT    208    208       A -> D (in Ref. 1; AAA93132).
FT                                {ECO:0000305}.
FT   TURN         17     19       {ECO:0000244|PDB:3HBX}.
FT   HELIX        22     24       {ECO:0000244|PDB:3HBX}.
FT   STRAND       29     31       {ECO:0000244|PDB:3HBX}.
FT   HELIX        39     49       {ECO:0000244|PDB:3HBX}.
FT   HELIX        50     52       {ECO:0000244|PDB:3HBX}.
FT   HELIX        56     58       {ECO:0000244|PDB:3HBX}.
FT   HELIX        70     78       {ECO:0000244|PDB:3HBX}.
FT   TURN         79     81       {ECO:0000244|PDB:3HBX}.
FT   TURN         87     89       {ECO:0000244|PDB:3HBX}.
FT   HELIX        91    107       {ECO:0000244|PDB:3HBX}.
FT   STRAND      119    125       {ECO:0000244|PDB:3HBX}.
FT   HELIX       126    147       {ECO:0000244|PDB:3HBX}.
FT   STRAND      156    160       {ECO:0000244|PDB:3HBX}.
FT   HELIX       165    173       {ECO:0000244|PDB:3HBX}.
FT   STRAND      177    181       {ECO:0000244|PDB:3HBX}.
FT   HELIX       192    198       {ECO:0000244|PDB:3HBX}.
FT   STRAND      203    211       {ECO:0000244|PDB:3HBX}.
FT   TURN        213    215       {ECO:0000244|PDB:3HBX}.
FT   HELIX       221    235       {ECO:0000244|PDB:3HBX}.
FT   STRAND      241    244       {ECO:0000244|PDB:3HBX}.
FT   HELIX       248    250       {ECO:0000244|PDB:3HBX}.
FT   HELIX       252    255       {ECO:0000244|PDB:3HBX}.
FT   STRAND      268    274       {ECO:0000244|PDB:3HBX}.
FT   STRAND      286    292       {ECO:0000244|PDB:3HBX}.
FT   HELIX       293    295       {ECO:0000244|PDB:3HBX}.
FT   HELIX       298    300       {ECO:0000244|PDB:3HBX}.
FT   STRAND      302    304       {ECO:0000244|PDB:3HBX}.
FT   STRAND      306    309       {ECO:0000244|PDB:3HBX}.
FT   STRAND      311    313       {ECO:0000244|PDB:3HBX}.
FT   HELIX       323    359       {ECO:0000244|PDB:3HBX}.
FT   TURN        360    362       {ECO:0000244|PDB:3HBX}.
FT   STRAND      364    366       {ECO:0000244|PDB:3HBX}.
FT   STRAND      370    382       {ECO:0000244|PDB:3HBX}.
FT   HELIX       388    396       {ECO:0000244|PDB:3HBX}.
FT   TURN        397    399       {ECO:0000244|PDB:3HBX}.
FT   STRAND      404    406       {ECO:0000244|PDB:3HBX}.
FT   STRAND      415    420       {ECO:0000244|PDB:3HBX}.
FT   HELIX       427    445       {ECO:0000244|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
//
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