ID   DCE5_ARATH              Reviewed;         494 AA.
AC   Q9LSH2;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Glutamate decarboxylase 5;
DE            Short=GAD 5;
DE            EC=4.1.1.15;
GN   Name=GAD5; OrderedLocusNames=At3g17760; ORFNames=MIG5.6;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(2000).
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   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   [4]
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 in flowers.
CC       {ECO:0000269|PubMed:18077464}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; AB026646; BAB02870.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE76003.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE76004.1; -; Genomic_DNA.
DR   RefSeq; NP_001154621.1; NM_001161149.1.
DR   RefSeq; NP_188403.1; NM_112657.2.
DR   AlphaFoldDB; Q9LSH2; -.
DR   SMR; Q9LSH2; -.
DR   IntAct; Q9LSH2; 1.
DR   STRING; 3702.AT3G17760.2; -.
DR   iPTMnet; Q9LSH2; -.
DR   PaxDb; Q9LSH2; -.
DR   PRIDE; Q9LSH2; -.
DR   ProteomicsDB; 222745; -.
DR   EnsemblPlants; AT3G17760.1; AT3G17760.1; AT3G17760.
DR   EnsemblPlants; AT3G17760.2; AT3G17760.2; AT3G17760.
DR   GeneID; 821044; -.
DR   Gramene; AT3G17760.1; AT3G17760.1; AT3G17760.
DR   Gramene; AT3G17760.2; AT3G17760.2; AT3G17760.
DR   KEGG; ath:AT3G17760; -.
DR   Araport; AT3G17760; -.
DR   TAIR; locus:2089779; AT3G17760.
DR   eggNOG; KOG1383; Eukaryota.
DR   HOGENOM; CLU_019582_2_2_1; -.
DR   InParanoid; Q9LSH2; -.
DR   OMA; IMENCWD; -.
DR   OrthoDB; 521159at2759; -.
DR   PhylomeDB; Q9LSH2; -.
DR   BioCyc; ARA:AT3G17760-MON; -.
DR   PRO; PR:Q9LSH2; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LSH2; baseline and differential.
DR   Genevisible; Q9LSH2; AT.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0009506; C:plasmodesma; 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; Pyridoxal phosphate;
KW   Reference proteome.
FT   CHAIN           1..494
FT                   /note="Glutamate decarboxylase 5"
FT                   /id="PRO_0000416956"
FT   MOD_RES         276
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   494 AA;  55770 MW;  7985F175E54DF262 CRC64;
     MVLATNSDSD EHLHSTFASR YVRAVVPRFK MPDHCMPKDA AYQVINDELM LDGNPRLNLA
     SFVTTWMEPE CDKLIMDSVN KNYVDMDEYP VTTELQNRCV NMIANLFHAP VGEDEAAIGC
     GTVGSSEAIM LAGLAFKRKW QHRRKAQGLP IDKPNIVTGA NVQVCWEKFA RYFEVELKEV
     KLSEDYYVMD PAKAVEMVDE NTICVAAILG STLTGEFEDV KQLNDLLAEK NAETGWETPI
     HVDAASGGFI APFLYPDLEW DFRLPWVKSI NVSGHKYGLV YAGVGWVVWR TKDDLPEELV
     FHINYLGADQ PTFTLNFSKG SSQIIAQYYQ FIRLGFEGYK NIMENCMDNA RRLREGIEMT
     GKFNIVSKDI GVPLVAFSLK DSSKHTVFEI AESLRKFGWI IPAYTMPADA QHIAVLRVVI
     REDFSRGLAD RLITHIIQVL KEIEGLPSRI AHLAAAAAVS GDDEEVKVKT AKMSLEDITK
     YWKRLVEHKR NIVC