GAGT1_ARATH
ID GAGT1_ARATH Reviewed; 572 AA.
AC Q8VYW6; B9DI67; O65652;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Glutathione hydrolase 1;
DE EC=3.4.19.13;
DE AltName: Full=Gamma-glutamyltransferase 1;
DE AltName: Full=Gamma-glutamyltranspeptidase 1;
DE EC=2.3.2.2;
DE Flags: Precursor;
GN Name=GGT1; OrderedLocusNames=At4g39640; ORFNames=T19P19.30;
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].
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].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17316175; DOI=10.1111/j.1365-313x.2006.03004.x;
RA Ohkama-Ohtsu N., Radwan S., Peterson A., Zhao P., Badr A.F., Xiang C.,
RA Oliver D.J.;
RT "Characterization of the extracellular gamma-glutamyl transpeptidases, GGT1
RT and GGT2, in Arabidopsis.";
RL Plant J. 49:865-877(2007).
RN [6]
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 [7]
RP TISSUE SPECIFICITY, AND INDUCTION BY GLUTATHIONE.
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 preventing oxidative stress by
CC metabolizing extracellular oxidized glutathione (GSSG).
CC {ECO:0000269|PubMed:17316175}.
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: Secreted, extracellular space, apoplast
CC {ECO:0000269|PubMed:17316175}. Note=Associated with the plasma membrane
CC and cell wall.
CC -!- TISSUE SPECIFICITY: Expressed in embryo, roots and leaves. In mature
CC plants, expression is restricted to vascular tissues of roots, leaves,
CC flowers and siliques. {ECO:0000269|PubMed:17316175,
CC ECO:0000269|PubMed:17545509, ECO:0000269|PubMed:20959624}.
CC -!- INDUCTION: By glutathione. {ECO:0000269|PubMed:20959624}.
CC -!- DISRUPTION PHENOTYPE: Slight reduction in size, early flowering and
CC increased chlorosis in older leaves. Accumulation of GSSG in the
CC apoplastic space. {ECO:0000269|PubMed:17316175,
CC ECO:0000269|PubMed:17545509}.
CC -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18750.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80627.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL022605; CAA18750.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161595; CAB80627.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE87097.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE87098.1; -; Genomic_DNA.
DR EMBL; AY069872; AAL47428.1; -; mRNA.
DR EMBL; BT000495; AAN18064.1; -; mRNA.
DR EMBL; AK317779; BAH20434.1; -; mRNA.
DR PIR; T05001; T05001.
DR RefSeq; NP_195674.2; NM_120124.6.
DR RefSeq; NP_974717.1; NM_202988.4.
DR AlphaFoldDB; Q8VYW6; -.
DR SMR; Q8VYW6; -.
DR STRING; 3702.AT4G39640.1; -.
DR MEROPS; T03.008; -.
DR MetOSite; Q8VYW6; -.
DR PaxDb; Q8VYW6; -.
DR PRIDE; Q8VYW6; -.
DR ProteomicsDB; 230473; -.
DR EnsemblPlants; AT4G39640.1; AT4G39640.1; AT4G39640.
DR EnsemblPlants; AT4G39640.2; AT4G39640.2; AT4G39640.
DR GeneID; 830118; -.
DR Gramene; AT4G39640.1; AT4G39640.1; AT4G39640.
DR Gramene; AT4G39640.2; AT4G39640.2; AT4G39640.
DR KEGG; ath:AT4G39640; -.
DR Araport; AT4G39640; -.
DR TAIR; locus:2135212; AT4G39640.
DR eggNOG; KOG2410; Eukaryota.
DR HOGENOM; CLU_014813_4_3_1; -.
DR InParanoid; Q8VYW6; -.
DR OMA; KATKNMF; -.
DR OrthoDB; 1419292at2759; -.
DR PhylomeDB; Q8VYW6; -.
DR BioCyc; ARA:AT4G39640-MON; -.
DR BRENDA; 2.3.2.2; 399.
DR UniPathway; UPA00204; -.
DR PRO; PR:Q8VYW6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8VYW6; baseline and differential.
DR Genevisible; Q8VYW6; AT.
DR GO; GO:0048046; C:apoplast; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0016756; F:glutathione gamma-glutamylcysteinyltransferase activity; IDA:TAIR.
DR GO; GO:0036374; F:glutathione hydrolase activity; IBA:GO_Central.
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:0006979; P:response to oxidative stress; IDA: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; Apoplast; Glycoprotein; Hydrolase; Reference proteome;
KW Secreted; Signal; Transferase.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..572
FT /note="Glutathione hydrolase 1"
FT /id="PRO_0000420911"
FT REGION 552..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 368
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 386
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 388
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 407
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 410
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 440..441
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 461..462
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 505
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 70
FT /note="V -> A (in Ref. 4; BAH20434)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 572 AA; 61190 MW; 67E3848EDCC2795F CRC64;
MSLVRTVTIV LFIIAFLQNA AAQKRQQSIV KSRGAVATDD GRCSVIGMRV LREGGNAIDA
SVAAALCLGV VSPASSGIGG GAFTVVKIAG GKEIAYDSRE TAPLRATENM YGGNVDLKKK
GALSVGVPGE VAGLFTAWKQ HGKLPWKRLV TPAEKLAEGF KISKYLYMQM NATRSDILAD
KGLSDLFVSN GELKKPGTIC HNPKLALTLK LIGEYGPKAF YNGTVGVNLA RDIKKSGGII
TLKDLQSYRV KIKEPLSADI LGYRVLGMPP PSSGGAAMML VLNILSQYGI PSGVSGPLGV
HRLIEALKHA FAVRMNLGDP DFTDVTKVVS DMLSPKFAKD LKSKINDQKT FDPKYYGGMW
NQIDDHGTSH LSIIDRERNA VSMTSTINGY FGALMLSPST GIVLNNEMDD FSIPMKSNGN
LDVPPPAPAN FIRPGKRPLS SMSPTIVLKD GKVKAAVGAS GGANIIAGTT EVYLNHFFLK
MDPLSSVLAP RIYHQLIPNR ASYENWTTVF NDHFEIPKAT RVVLEKKGHV LSPIAGGTIA
QFIVQESGEN SGGRSELVAV SDPRKGGFPS GY
