ID   DCE4_ARATH              Reviewed;         493 AA.
AC   Q9ZPS3;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   24-JAN-2024, entry version 136.
DE   RecName: Full=Glutamate decarboxylase 4;
DE            Short=GAD 4;
DE            EC=4.1.1.15;
GN   Name=GAD4; OrderedLocusNames=At2g02010; ORFNames=F14H20.8;
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=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   [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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Root;
RX   PubMed=18433157; DOI=10.1021/pr8000173;
RA   de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA   Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA   Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT   "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT   spectrometry and peptide chip analysis.";
RL   J. Proteome Res. 7:2458-2470(2008).
RN   [6]
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   [7]
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 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 in flowers and shoots. Detected at low
CC       levels in siliques, stems, leaves and roots.
CC       {ECO:0000269|PubMed:18077464}.
CC   -!- INDUCTION: Up-regulated by salt treatment and hypoxia.
CC       {ECO:0000269|PubMed:18077464, ECO:0000269|PubMed:20122158}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; AC006532; AAD20099.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC05532.1; -; Genomic_DNA.
DR   EMBL; AF361836; AAK32848.1; -; mRNA.
DR   EMBL; AY124860; AAM70569.1; -; mRNA.
DR   PIR; H84431; H84431.
DR   RefSeq; NP_178310.1; NM_126262.2.
DR   AlphaFoldDB; Q9ZPS3; -.
DR   SMR; Q9ZPS3; -.
DR   STRING; 3702.Q9ZPS3; -.
DR   iPTMnet; Q9ZPS3; -.
DR   PaxDb; 3702-AT2G02010-1; -.
DR   ProteomicsDB; 223984; -.
DR   DNASU; 814732; -.
DR   EnsemblPlants; AT2G02010.1; AT2G02010.1; AT2G02010.
DR   GeneID; 814732; -.
DR   Gramene; AT2G02010.1; AT2G02010.1; AT2G02010.
DR   KEGG; ath:AT2G02010; -.
DR   Araport; AT2G02010; -.
DR   TAIR; AT2G02010; GAD4.
DR   eggNOG; KOG1383; Eukaryota.
DR   HOGENOM; CLU_019582_2_2_1; -.
DR   InParanoid; Q9ZPS3; -.
DR   PhylomeDB; Q9ZPS3; -.
DR   PRO; PR:Q9ZPS3; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9ZPS3; baseline and differential.
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; IEA:UniProtKB-EC.
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   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:SF38; GLUTAMATE DECARBOXYLASE 3-RELATED; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   Genevisible; Q9ZPS3; AT.
PE   1: Evidence at protein level;
KW   Calmodulin-binding; Decarboxylase; Lyase; Phosphoprotein;
KW   Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..493
FT                   /note="Glutamate decarboxylase 4"
FT                   /id="PRO_0000416955"
FT   MOD_RES         8
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18433157"
FT   MOD_RES         277
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   493 AA;  56005 MW;  36B3FC93F2978168 CRC64;
     MVLSKTVSES DVSIHSTFAS RYVRNSLPRF EMPENSIPKE AAYQIINDEL MLDGNPRLNL
     ASFVTTWMEP ECDKLMMESI NKNYVDMDEY PVTTELQNRC VNMIARLFNA PLGDGEAAVG
     VGTVGSSEAI MLAGLAFKRQ WQNKRKAQGL PYDKPNIVTG ANVQVCWEKF ARYFEVELKE
     VNLREDYYVM DPVKAVEMVD ENTICVAAIL GSTLTGEFED VKLLNDLLVE KNKQTGWDTP
     IHVDAASGGF IAPFLYPELE WDFRLPLVKS INVSGHKYGL VYAGIGWVVW RTKTDLPDEL
     IFHINYLGAD QPTFTLNFSK GSSQVIAQYY QLIRLGFEGY RNVMDNCREN MMVLRQGLEK
     TGRFKIVSKE NGVPLVAFSL KDSSRHNEFE VAHTLRRFGW IVPAYTMPAD AQHVTVLRVV
     IREDFSRTLA ERLVADFEKV LHELDTLPAR VHAKMANGKV NGVKKTPEET QREVTAYWKK
     LLETKKTNKN TIC
//