GGP2_ARATH
ID GGP2_ARATH Reviewed; 248 AA.
AC Q9M0A6;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Gamma-glutamyl peptidase 2 {ECO:0000305};
DE EC=3.4.19.16 {ECO:0000250|UniProtKB:Q9M0A7};
GN Name=GGP2 {ECO:0000305};
GN OrderedLocusNames=At4g30540 {ECO:0000312|Araport:AT4G30540};
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).
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. {ECO:0000250|UniProtKB:Q9M0A7}.
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:0000250|UniProtKB:Q9M0A7};
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:0000250|UniProtKB:Q9M0A7};
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:0000250|UniProtKB:Q9M0A7};
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:0000250|UniProtKB:Q9M0A7};
CC -!- PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9M0A7}.
CC -!- SIMILARITY: Belongs to the peptidase C26 family. {ECO:0000305}.
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DR EMBL; AL161577; CAB79772.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85778.1; -; Genomic_DNA.
DR EMBL; AY142516; AAN13059.1; -; mRNA.
DR PIR; C85357; C85357.
DR RefSeq; NP_194783.1; NM_119200.3.
DR AlphaFoldDB; Q9M0A6; -.
DR SMR; Q9M0A6; -.
DR STRING; 3702.AT4G30540.1; -.
DR MEROPS; C26.A05; -.
DR PaxDb; Q9M0A6; -.
DR PRIDE; Q9M0A6; -.
DR EnsemblPlants; AT4G30540.1; AT4G30540.1; AT4G30540.
DR GeneID; 829177; -.
DR Gramene; AT4G30540.1; AT4G30540.1; AT4G30540.
DR KEGG; ath:AT4G30540; -.
DR Araport; AT4G30540; -.
DR TAIR; locus:2118826; AT4G30540.
DR eggNOG; KOG3179; Eukaryota.
DR HOGENOM; CLU_054974_0_1_1; -.
DR InParanoid; Q9M0A6; -.
DR OMA; KEMYGGY; -.
DR OrthoDB; 1450344at2759; -.
DR PhylomeDB; Q9M0A6; -.
DR PRO; PR:Q9M0A6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M0A6; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Protease; Reference proteome.
FT CHAIN 1..248
FT /note="Gamma-glutamyl peptidase 2"
FT /id="PRO_0000435501"
FT DOMAIN 17..212
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 101
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 248 AA; 28695 MW; E7B807446D5B98EC CRC64;
MVKQIRRYAL FQATPDSEFV KEMYGGYFNV FVSAFGDEGE QWDLFRVIDG EFPRDEDLEK
YEGFVISGSL HDAFTEEDWI IELCSVCKKL DVMKKKILGI CFGHQIICRV RGGKVGRARK
GPDIGLGNIT IVQDVIKPGD YFDQIESLSI IQCHRDEVLE PPESARVIGF SDKCDVEIFS
VEDHLLCFQG HPEYNKEILL EIIDRVHKIK FVEEEILEKA KDSIKKFEPD TQRLHMLCKN
FLKGRRTH
