GGP3_ARATH
ID GGP3_ARATH Reviewed; 249 AA.
AC Q9M0A5; Q8LBZ3; Q8VZH8;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Gamma-glutamyl peptidase 3 {ECO:0000305};
DE EC=3.4.19.16 {ECO:0000269|PubMed:21712415};
GN Name=GGP3 {ECO:0000303|PubMed:21712415};
GN OrderedLocusNames=At4g30550 {ECO:0000312|Araport:AT4G30550};
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=21712415; DOI=10.1105/tpc.111.083998;
RA Geu-Flores F., Moeldrup M.E., Boettcher C., Olsen C.E., Scheel D.,
RA Halkier B.A.;
RT "Cytosolic gamma-glutamyl peptidases process glutathione conjugates in the
RT biosynthesis of glucosinolates and camalexin in Arabidopsis.";
RL Plant Cell 23:2456-2469(2011).
CC -!- FUNCTION: Involved in glucosinolate biosynthesis. Hydrolyzes the gamma-
CC glutamyl peptide bond of several glutathione (GSH) conjugates to
CC produce Cys-Gly conjugates related to glucosinolates. The gamma-Glu-
CC Cys-Gly-GSH conjugates are the sulfur-donating molecule in
CC glucosinolate biosynthesis. Can use the GSH conjugate of the camalexin
CC intermediate IAN (GS-IAN) as substrate. Required for the biosynthesis
CC of camalexin, a pathogen-inducible phytoalexin with antibacterial and
CC antifungal properties. {ECO:0000269|PubMed:21712415}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-[(1E)-1-(hydroxyimino)-omega-(methylsulfanyl)alkyl]-L-
CC glutathione + H2O = an S-[(1E)-1-(hydroxyimino)-omega-
CC (methylsulfanyl)alkyl]-L-cysteinylglycine + L-glutamate;
CC Xref=Rhea:RHEA:52756, Rhea:RHEA-COMP:13138, Rhea:RHEA-COMP:13355,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:136061,
CC ChEBI:CHEBI:136825; EC=3.4.19.16;
CC Evidence={ECO:0000269|PubMed:21712415};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-1-(glutathione-S-yl)-2-(1H-indol-3-yl)acetohydroximate +
CC H2O = (E)-1-(glycyl-L-cystein-S-yl)-2-(1H-indol-3-yl)acetohydroximate
CC + L-glutamate; Xref=Rhea:RHEA:52764, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:136444, ChEBI:CHEBI:136831;
CC EC=3.4.19.16; Evidence={ECO:0000269|PubMed:21712415};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(glutathion-S-yl)-2-(1H-indol-3-yl)acetonitrile + H2O = 2-
CC (glycyl-L-cystein-S-yl)-2-(1H-indol-3-yl)acetonitrile + L-glutamate;
CC Xref=Rhea:RHEA:52768, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:64981, ChEBI:CHEBI:136832; EC=3.4.19.16;
CC Evidence={ECO:0000269|PubMed:21712415};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(Z)-1-(glutathione-S-yl)-2-phenylacetohydroximate + H2O = (Z)-
CC 1-(glycyl-L-cystein-S-yl)-2-phenylacetohydroximate + L-glutamate;
CC Xref=Rhea:RHEA:52760, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:136447, ChEBI:CHEBI:136830; EC=3.4.19.16;
CC Evidence={ECO:0000269|PubMed:21712415};
CC -!- PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21712415}.
CC -!- SIMILARITY: Belongs to the peptidase C26 family. {ECO:0000305}.
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DR EMBL; AL161577; CAB79773.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85779.1; -; Genomic_DNA.
DR EMBL; AY064159; AAL36065.1; -; mRNA.
DR EMBL; AY143831; AAN28770.1; -; mRNA.
DR EMBL; AY086910; AAM63954.1; -; mRNA.
DR PIR; D85357; D85357.
DR RefSeq; NP_194784.1; NM_119201.3.
DR AlphaFoldDB; Q9M0A5; -.
DR SMR; Q9M0A5; -.
DR STRING; 3702.AT4G30550.1; -.
DR MEROPS; C26.A05; -.
DR PaxDb; Q9M0A5; -.
DR PRIDE; Q9M0A5; -.
DR ProteomicsDB; 221840; -.
DR EnsemblPlants; AT4G30550.1; AT4G30550.1; AT4G30550.
DR GeneID; 829178; -.
DR Gramene; AT4G30550.1; AT4G30550.1; AT4G30550.
DR KEGG; ath:AT4G30550; -.
DR Araport; AT4G30550; -.
DR TAIR; locus:2118831; AT4G30550.
DR eggNOG; KOG3179; Eukaryota.
DR HOGENOM; CLU_054974_0_1_1; -.
DR InParanoid; Q9M0A5; -.
DR OMA; RWILRLC; -.
DR OrthoDB; 1450344at2759; -.
DR PhylomeDB; Q9M0A5; -.
DR BioCyc; ARA:AT4G30550-MON; -.
DR BioCyc; MetaCyc:GQT-2803-MON; -.
DR BRENDA; 3.4.19.16; 399.
DR PRO; PR:Q9M0A5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M0A5; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0008233; F:peptidase activity; IDA:TAIR.
DR GO; GO:0019760; P:glucosinolate metabolic process; IMP:TAIR.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01741; GATase1_1; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR044992; ChyE-like.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR PANTHER; PTHR42695; PTHR42695; 1.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Protease; Reference proteome.
FT CHAIN 1..249
FT /note="Gamma-glutamyl peptidase 3"
FT /id="PRO_0000435502"
FT DOMAIN 19..217
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 103
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT CONFLICT 44
FT /note="W -> S (in Ref. 4; AAM63954)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="S -> Y (in Ref. 3; AAL36065/AAN28770)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 249 AA; 28225 MW; 5957C5886E71F33E CRC64;
MVVIEQKKRF ALFLATCDSE FVKKTYGGYF NVFVSTFGEE GEQWDLFRVI DGQFPDENDL
DKYDGFVISG SPHDAFGDAD WIVKLCEVCQ KLDHMKKKVL GICFGHQIIT RVKGGKIGRA
LKGADMGLRS ITIAKDNEKL RGYFGDVEVP ASLAIIKCHQ DEVLELPESA TLLASSEVCN
VEMFSIGDHF FCIQGHPEYN KEILFEIVDR VLNMKLMEQE FADKAKSTME TAQPDRILWQ
KLCKNFLKG
