GAGT2_ARATH
ID GAGT2_ARATH Reviewed; 578 AA.
AC Q680I5; O65653;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Glutathione hydrolase 2;
DE EC=3.4.19.13;
DE AltName: Full=Gamma-glutamyltransferase 2;
DE AltName: Full=Gamma-glutamyltranspeptidase 2;
DE EC=2.3.2.2;
DE Flags: Precursor;
GN Name=GGT2; OrderedLocusNames=At4g39650; ORFNames=T19P19.40;
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;
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-578.
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION 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.
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, INDUCTION BY GLUTATHIONE, AND DISRUPTION PHENOTYPE.
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 be required for glutathione transport into developing
CC seeds. {ECO:0000305}.
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 roots, immature trichomes and pollen.
CC In developing siliques, specifically expressed in the embryo,
CC endosperm, outer integument and a small portion of the funiculus.
CC {ECO:0000269|PubMed:17316175, ECO:0000269|PubMed:17545509,
CC ECO:0000269|PubMed:20959624}.
CC -!- INDUCTION: By glutathione. {ECO:0000269|PubMed:20959624}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:17316175, ECO:0000269|PubMed:20959624}.
CC -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18751.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80628.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL022605; CAA18751.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161595; CAB80628.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE87099.1; -; Genomic_DNA.
DR EMBL; AK175882; BAD43645.1; -; mRNA.
DR EMBL; AK220806; BAD94075.1; -; mRNA.
DR EMBL; BT012661; AAT06480.1; -; mRNA.
DR PIR; T05002; T05002.
DR RefSeq; NP_195675.2; NM_120125.2.
DR AlphaFoldDB; Q680I5; -.
DR SMR; Q680I5; -.
DR STRING; 3702.AT4G39650.1; -.
DR MEROPS; T03.A03; -.
DR PaxDb; Q680I5; -.
DR PRIDE; Q680I5; -.
DR ProteomicsDB; 247357; -.
DR EnsemblPlants; AT4G39650.1; AT4G39650.1; AT4G39650.
DR GeneID; 830119; -.
DR Gramene; AT4G39650.1; AT4G39650.1; AT4G39650.
DR KEGG; ath:AT4G39650; -.
DR Araport; AT4G39650; -.
DR TAIR; locus:2135222; AT4G39650.
DR eggNOG; KOG2410; Eukaryota.
DR HOGENOM; CLU_014813_4_3_1; -.
DR InParanoid; Q680I5; -.
DR OMA; VVNSITM; -.
DR OrthoDB; 1419292at2759; -.
DR PhylomeDB; Q680I5; -.
DR BioCyc; ARA:AT4G39650-MON; -.
DR BRENDA; 2.3.2.2; 399.
DR UniPathway; UPA00204; -.
DR PRO; PR:Q680I5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q680I5; baseline and differential.
DR Genevisible; Q680I5; AT.
DR GO; GO:0048046; C:apoplast; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA: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:0034775; P:glutathione transmembrane transport; IMP: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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..578
FT /note="Glutathione hydrolase 2"
FT /id="PRO_0000420912"
FT ACT_SITE 374
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 392
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 413
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 416
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 446..447
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 467..468
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 511
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 578 AA; 61600 MW; A590038C250A7026 CRC64;
MNSFMSLVRT ATIALLLIAF LQNANAVKNL QSIVAYHGAV ATDDGRCSAI GTNVLRQGGN
AIDASVAAAL CLGVVSPASS GIGGGAFTMI KLANGTEVAY DSRETAPLSA TEDMYGDNPE
RKKKGSLSVG VPGEVAGLYT AWTQHGKLPW KQLVEPAEKL AAEGFKISKY LYMQMNATRS
DILADKGLSE LFVSNGELKK PGAICRNPKL ADTLSQIAEY GPKAFYNGTV GFNLVSDIQK
AGGIITLKDL QNYNVKVKEP LSTEILGYRL LGMPPPSSGG PAMMLILNIL AQYGIPSGVS
GPLGVHRLVE ALKHAFAVRM NLGDPDFVPE VTNVVADMLS PKFAQDLKSK INDEKTFDPK
YYGGKWGQIK DHGTSHLSII DSERNAVSMT STINGYFGAI MLSPSTGIVL NNEMDDFSIP
TKSGGDPDVP PPAPANFIRP GKRPLSSMTP TIVLKDGKVK AALGASGGMY IIAGTTQVYL
NHFFLNMDPL SSVVAPRIYH QLIPNKASYE NWTTVYSDHF EIPEEIRLVL EKKGQVLTPI
AGGTISQLIV EQSDGKSGGI SKLVAVSDPR KGGFPSGY
