GGP1_ARATH
ID GGP1_ARATH Reviewed; 250 AA.
AC Q9M0A7; Q8LAM4;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Gamma-glutamyl peptidase 1 {ECO:0000305};
DE EC=3.4.19.16 {ECO:0000269|PubMed:21712415};
GN Name=GGP1 {ECO:0000303|PubMed:19483696};
GN OrderedLocusNames=At4g30530 {ECO:0000312|Araport:AT4G30530};
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, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19483696; DOI=10.1038/nchembio.185;
RA Geu-Flores F., Nielsen M.T., Nafisi M., Moeldrup M.E., Olsen C.E.,
RA Motawia M.S., Halkier B.A.;
RT "Glucosinolate engineering identifies a gamma-glutamyl peptidase.";
RL Nat. Chem. Biol. 5:575-577(2009).
RN [6]
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 (PubMed:19483696, PubMed:21712415). Converts
CC phenylacetohydroximoyl-GSH to benzylglucosinolate (PubMed:19483696).
CC Can use the GSH conjugate of the camalexin intermediate IAN (GS-IAN) as
CC substrate. Required for the biosynthesis of camalexin, a pathogen-
CC inducible phytoalexin with antibacterial and antifungal properties
CC (PubMed:21712415). {ECO:0000269|PubMed:19483696,
CC 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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=37 uM for phenylacetohydroximoyl-glutathione
CC {ECO:0000269|PubMed:19483696};
CC -!- PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21712415}.
CC -!- BIOTECHNOLOGY: Cancer prevention by GLSs is attributed to the formation
CC of isothiocyanates (Scheme 1a) upon hydrolysis.
CC -!- SIMILARITY: Belongs to the peptidase C26 family. {ECO:0000305}.
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DR EMBL; AL161577; CAB79771.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85777.1; -; Genomic_DNA.
DR EMBL; AF410267; AAK95253.1; -; mRNA.
DR EMBL; AY093724; AAM10348.1; -; mRNA.
DR EMBL; AY087727; AAM65264.1; -; mRNA.
DR PIR; B85357; B85357.
DR RefSeq; NP_194782.1; NM_119199.5.
DR AlphaFoldDB; Q9M0A7; -.
DR SMR; Q9M0A7; -.
DR STRING; 3702.AT4G30530.1; -.
DR MEROPS; C26.A05; -.
DR PaxDb; Q9M0A7; -.
DR PRIDE; Q9M0A7; -.
DR ProteomicsDB; 220740; -.
DR EnsemblPlants; AT4G30530.1; AT4G30530.1; AT4G30530.
DR GeneID; 829176; -.
DR Gramene; AT4G30530.1; AT4G30530.1; AT4G30530.
DR KEGG; ath:AT4G30530; -.
DR Araport; AT4G30530; -.
DR TAIR; locus:2118821; AT4G30530.
DR eggNOG; KOG3179; Eukaryota.
DR HOGENOM; CLU_054974_0_1_1; -.
DR InParanoid; Q9M0A7; -.
DR OMA; WETICKN; -.
DR OrthoDB; 1450344at2759; -.
DR PhylomeDB; Q9M0A7; -.
DR BioCyc; ARA:AT4G30530-MON; -.
DR BioCyc; MetaCyc:AT4G30530-MON; -.
DR BRENDA; 3.4.19.16; 399.
DR PRO; PR:Q9M0A7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M0A7; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0034722; F:gamma-glutamyl-peptidase activity; IDA:TAIR.
DR GO; GO:0008233; F:peptidase activity; IDA:TAIR.
DR GO; GO:0010120; P:camalexin biosynthetic process; IMP:TAIR.
DR GO; GO:0019760; P:glucosinolate metabolic process; IDA: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..250
FT /note="Gamma-glutamyl peptidase 1"
FT /id="PRO_0000435500"
FT DOMAIN 16..213
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 100
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT CONFLICT 245
FT /note="G -> V (in Ref. 4; AAM65264)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 250 AA; 28385 MW; 55BEBB778FE5C19C CRC64;
MVEQKRYALF LATLDSEFVK KTYGGYHNVF VTTFGDEGEH WDSFRVVSGE FPDEKDLEKY
DGFVISGSSH DAFENDDWIL KLCDIVKKID EMKKKILGIC FGHQIIARVR GGTVGRAKKG
PELKLGDITI VKDAITPGSY FGNEIPDSIA IIKCHQDEVL VLPETAKVLA YSKNYEVEMY
SIEDHLFCIQ GHPEYNKEIL FEIVDRVLAL GYVKQEFADA AKATMENRGA DRKLWETICK
NFLKGRVPTN
