ID   DCE3_ARATH              Reviewed;         500 AA.
AC   Q9ZPS4;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Glutamate decarboxylase 3;
DE            Short=GAD 3;
DE            EC=4.1.1.15;
GN   Name=GAD3; OrderedLocusNames=At2g02000; ORFNames=F14H20.7;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [4]
RP   IDENTIFICATION.
RX   PubMed=10529826; DOI=10.1016/s1360-1385(99)01486-7;
RA   Shelp B.J., Bown A.W., McLean M.D.;
RT   "Metabolism and functions of gamma-aminobutyric acid.";
RL   Trends Plant Sci. 4:446-452(1999).
RN   [5]
RP   TISSUE SPECIFICITY.
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).
CC   -!- FUNCTION: Catalyzes the production of GABA. The calmodulin-binding is
CC       calcium-dependent and it is proposed that this may, directly or
CC       indirectly, form a calcium regulated control of GABA biosynthesis (By
CC       similarity). {ECO:0000250}.
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         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homohexamer. Interacts with calmodulin (By similarity).
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed at low levels in siliques.
CC       {ECO:0000269|PubMed:18077464}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; AC006532; AAD20093.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC05531.1; -; Genomic_DNA.
DR   EMBL; AK118125; BAC42751.1; -; mRNA.
DR   PIR; G84431; G84431.
DR   RefSeq; NP_178309.1; NM_126261.2.
DR   AlphaFoldDB; Q9ZPS4; -.
DR   SMR; Q9ZPS4; -.
DR   STRING; 3702.AT2G02000.1; -.
DR   iPTMnet; Q9ZPS4; -.
DR   PaxDb; Q9ZPS4; -.
DR   PRIDE; Q9ZPS4; -.
DR   ProteomicsDB; 224682; -.
DR   EnsemblPlants; AT2G02000.1; AT2G02000.1; AT2G02000.
DR   GeneID; 814731; -.
DR   Gramene; AT2G02000.1; AT2G02000.1; AT2G02000.
DR   KEGG; ath:AT2G02000; -.
DR   Araport; AT2G02000; -.
DR   TAIR; locus:2041120; AT2G02000.
DR   eggNOG; KOG1383; Eukaryota.
DR   HOGENOM; CLU_019582_2_2_1; -.
DR   InParanoid; Q9ZPS4; -.
DR   OrthoDB; 521159at2759; -.
DR   PhylomeDB; Q9ZPS4; -.
DR   BioCyc; ARA:AT2G02000-MON; -.
DR   PRO; PR:Q9ZPS4; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9ZPS4; baseline and differential.
DR   Genevisible; Q9ZPS4; AT.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006538; P:glutamate catabolic process; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Calmodulin-binding; Decarboxylase; Lyase; Phosphoprotein;
KW   Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..500
FT                   /note="Glutamate decarboxylase 3"
FT                   /id="PRO_0000416954"
FT   MOD_RES         8
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZPS3"
FT   MOD_RES         277
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   500 AA;  56507 MW;  1A47C0D14C6CD3B8 CRC64;
     MVLSKTASKS DDSIHSTFAS RYVRNSISRF EIPKNSIPKE AAYQIINDEL KFDGNPRLNL
     ASFVTTWMEP ECDKLMMESI NKNNVEMDQY PVTTDLQNRC VNMIARLFNA PLGDGEAAIG
     VGTVGSSEAV MLAGLAFKRQ WQNKRKALGL PYDRPNIVTG ANIQVCLEKF ARYFEVELKE
     VKLREGYYVM DPDKAVEMVD ENTICVVAIL GSTLTGEFED VKLLNDLLVE KNKKTGWDTP
     IHVDAASGGF IAPFLYPDLE WDFRLPLVKS INVSGHKYGL VYAGIGWVVW RTKTDLPDEL
     IFHINYLGAD QPTFTLNFSK GSSQVIAQYY QLIRLGFEGY RNVMDNCREN MMVLRQGLEK
     TGRFNIVSKE NGVPLVAFSL KDSSRHNEFE VAEMLRRFGW IVPAYTMPAD AQHVTVLRVV
     IREDFSRTLA ERLVADFEKV LHELDTLPAR VHAKMASGKV NGVKKTPEET QREVTAYWKK
     FVDTKTDKNG VPLVASITNQ