GAGT3_ARATH
ID GAGT3_ARATH Reviewed; 637 AA.
AC Q9M0G0; F4JMW7;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Glutathione hydrolase 3;
DE EC=3.4.19.13;
DE AltName: Full=Gamma-glutamyltransferase 3;
DE AltName: Full=Gamma-glutamyltranspeptidase 3;
DE EC=2.3.2.2;
DE AltName: Full=Gamma-glutamyltranspeptidase 4;
GN Name=GGT3; Synonyms=GGT4; OrderedLocusNames=At4g29210; ORFNames=F17A13.30;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY AUXIN.
RX PubMed=17316176; DOI=10.1111/j.1365-313x.2006.03005.x;
RA Ohkama-Ohtsu N., Zhao P., Xiang C., Oliver D.J.;
RT "Glutathione conjugates in the vacuole are degraded by gamma-glutamyl
RT transpeptidase GGT3 in Arabidopsis.";
RL Plant J. 49:878-888(2007).
RN [7]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17545509; DOI=10.1104/pp.106.094409;
RA Martin M.N., Saladores P.H., Lambert E., Hudson A.O., Leustek T.;
RT "Localization of members of the gamma-glutamyl transpeptidase family
RT identifies sites of glutathione and glutathione S-conjugate hydrolysis.";
RL Plant Physiol. 144:1715-1732(2007).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=20959624; DOI=10.1093/jxb/erq316;
RA Destro T., Prasad D., Martignago D., Bernet I.L., Trentin A.R., Renu I.K.,
RA Ferretti M., Masi A.;
RT "Compensatory expression and substrate inducibility of gamma-glutamyl
RT transferase GGT2 isoform in Arabidopsis thaliana.";
RL J. Exp. Bot. 62:805-814(2011).
CC -!- FUNCTION: May play a role in protecting plants from some xenobiotic
CC chemicals by degrading vacuolar glutathione conjugates into cysteine
CC conjugates. {ECO:0000269|PubMed:17316176}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-amino acid + an N-terminal (5-L-glutamyl)-[peptide] =
CC 5-L-glutamyl amino acid + N-terminal L-alpha-aminoacyl-[peptide];
CC Xref=Rhea:RHEA:23904, Rhea:RHEA-COMP:9780, Rhea:RHEA-COMP:9795,
CC ChEBI:CHEBI:77644, ChEBI:CHEBI:78597, ChEBI:CHEBI:78599,
CC ChEBI:CHEBI:78608; EC=2.3.2.2;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + H2O = L-cysteinylglycine + L-glutamate;
CC Xref=Rhea:RHEA:28807, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:61694; EC=3.4.19.13;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted glutathione + H2O = an S-substituted L-
CC cysteinylglycine + L-glutamate; Xref=Rhea:RHEA:59468,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:90779,
CC ChEBI:CHEBI:143103; EC=3.4.19.13;
CC -!- PATHWAY: Sulfur metabolism; glutathione metabolism.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000305|PubMed:17316176};
CC Single-pass membrane protein {ECO:0000305|PubMed:17316176}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9M0G0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9M0G0-2; Sequence=VSP_044955, VSP_044956;
CC -!- TISSUE SPECIFICITY: Expressed in roots, cotyledons, leaves, flowers and
CC siliques. {ECO:0000269|PubMed:17316176, ECO:0000269|PubMed:17545509,
CC ECO:0000269|PubMed:20959624}.
CC -!- INDUCTION: By auxin. {ECO:0000269|PubMed:17316176}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:17545509}.
CC -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AL161574; CAB79679.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85602.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85603.1; -; Genomic_DNA.
DR EMBL; BT005754; AAO64159.1; -; mRNA.
DR EMBL; BX828052; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK228574; BAF00492.1; -; mRNA.
DR PIR; T13432; T13432.
DR RefSeq; NP_194650.1; NM_119065.3. [Q9M0G0-1]
DR RefSeq; NP_974636.1; NM_202907.2. [Q9M0G0-2]
DR AlphaFoldDB; Q9M0G0; -.
DR SMR; Q9M0G0; -.
DR STRING; 3702.AT4G29210.1; -.
DR MEROPS; T03.A01; -.
DR PaxDb; Q9M0G0; -.
DR PRIDE; Q9M0G0; -.
DR ProteomicsDB; 248569; -. [Q9M0G0-1]
DR EnsemblPlants; AT4G29210.1; AT4G29210.1; AT4G29210. [Q9M0G0-1]
DR EnsemblPlants; AT4G29210.2; AT4G29210.2; AT4G29210. [Q9M0G0-2]
DR GeneID; 829042; -.
DR Gramene; AT4G29210.1; AT4G29210.1; AT4G29210. [Q9M0G0-1]
DR Gramene; AT4G29210.2; AT4G29210.2; AT4G29210. [Q9M0G0-2]
DR KEGG; ath:AT4G29210; -.
DR Araport; AT4G29210; -.
DR TAIR; locus:2118229; AT4G29210.
DR eggNOG; KOG2410; Eukaryota.
DR InParanoid; Q9M0G0; -.
DR OMA; VCGMGPP; -.
DR PhylomeDB; Q9M0G0; -.
DR BioCyc; ARA:AT4G29210-MON; -.
DR BioCyc; MetaCyc:AT4G29210-MON; -.
DR BRENDA; 2.3.2.2; 399.
DR BRENDA; 3.4.19.13; 399.
DR UniPathway; UPA00204; -.
DR PRO; PR:Q9M0G0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M0G0; baseline and differential.
DR Genevisible; Q9M0G0; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; IDA:TAIR.
DR GO; GO:0016756; F:glutathione gamma-glutamylcysteinyltransferase activity; IDA:TAIR.
DR GO; GO:0036374; F:glutathione hydrolase activity; IMP:TAIR.
DR GO; GO:0102953; F:hypoglycin A gamma-glutamyl transpeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0103068; F:leukotriene C4 gamma-glutamyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006751; P:glutathione catabolic process; IDA:TAIR.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR GO; GO:0006805; P:xenobiotic metabolic process; IEP:TAIR.
DR Gene3D; 1.10.246.130; -; 1.
DR Gene3D; 3.60.20.40; -; 1.
DR InterPro; IPR043138; GGT_lsub_C.
DR InterPro; IPR000101; GGT_peptidase.
DR InterPro; IPR043137; GGT_ssub.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR PANTHER; PTHR11686; PTHR11686; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR00066; g_glut_trans; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Alternative splicing; Detoxification; Glycoprotein;
KW Hydrolase; Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Vacuole.
FT CHAIN 1..637
FT /note="Glutathione hydrolase 3"
FT /id="PRO_0000420913"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 418
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 436
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 438
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 457
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 460
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 488..489
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 509..510
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 553
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 498..512
FT /note="DGEFVAALGGAGGMH -> VHNQYISTFPVIYNS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_044955"
FT VAR_SEQ 513..637
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_044956"
SQ SEQUENCE 637 AA; 69148 MW; 87E3B7A210EF8323 CRC64;
MRDAIIADPL LAIDHETVAE KKKQSKNLKI SLLLLLILLA TSGYYSFSDN ITTVFLSRQA
IDDDHSLSLG TISDVVESEN GVVAADDARC SEIGASVLRS GGHAVDAAVA ITLCVGVVNP
MSSGIGGGSF LIVSSQKDSK AEAFDMRETA PLAASKDMYK NDASAKSLGA LSMGVPGEIA
GLYEAWKRYG RLPWKPLFEP AIKLARDGFV VYPYLGKAIS TKVAMILKDP GMRSVFSRNG
QVLKTGETCY NPELAQSLET ISEQGPGAFY NGTVGEKLVK DVKKAGGIIT MDDLRSYKVR
VTDAMSVDVM GYTVHGMPPP SGGTVGFSMV MNILDSYSNL YTASGRELGL HRLIEAMKHM
FAARMDLGDP EFVNVTNSMN QMLSKAHAEE IQKRIFDNTT FPPEYYMNRW SQLRDQGTSH
FCVVDADRNS VSMTSTVNYR FGAGVLSPST GIVLNNEMDD FSTPTEITPD MLPPAPTNFI
EPNKRPLSSM TPLVITKDGE FVAALGGAGG MHIIPAVLQV FLNCFVLNMK PKEAVESARI
YHRLIPNVVS YENFTTINGD HIGVSEDTKM FLAERGHELK ELSGGAIVQL IVQSFKEEKE
EEMIIEIGRK IGKKSKPLKG LLTAVSDPRK DGKPAAV
