GCT22_ARATH
ID GCT22_ARATH Reviewed; 227 AA.
AC Q84MC1; O49579; Q8LAB4;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Gamma-glutamylcyclotransferase 2-2 {ECO:0000305};
DE Short=AtGGCT2;2 {ECO:0000303|PubMed:25716890};
DE EC=4.3.2.9 {ECO:0000269|PubMed:25716890};
DE AltName: Full=Gamma-glutamyl cyclotransferase 2;2 {ECO:0000303|PubMed:25716890};
GN Name=GGCT2;2 {ECO:0000303|PubMed:25716890};
GN OrderedLocusNames=At4g31290 {ECO:0000312|Araport:AT4G31290};
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;
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=25716890; DOI=10.1042/bj20141154;
RA Kumar S., Kaur A., Chattopadhyay B., Bachhawat A.K.;
RT "Defining the cytosolic pathway of glutathione degradation in Arabidopsis
RT thaliana: role of the ChaC/GCG family of gamma-glutamyl cyclotransferases
RT as glutathione-degrading enzymes and AtLAP1 as the Cys-Gly peptidase.";
RL Biochem. J. 468:73-85(2015).
CC -!- FUNCTION: Catalyzes the formation of 5-oxoproline from gamma-glutamyl
CC dipeptides and plays a significant role in glutathione (GSH)
CC homeostasis. Converts GSH to 5-oxoproline and cysteine-glycine (Cys-
CC Gly) dipeptide in vitro. Possesses low activity towards gamma-glutamyl-
CC L-alanine. Has no activity towards gamma-glutamyl-L-cysteine.
CC {ECO:0000269|PubMed:25716890}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-(gamma-L-glutamyl)-L-amino acid = 5-oxo-L-proline +
CC an L-alpha-amino acid; Xref=Rhea:RHEA:20505, ChEBI:CHEBI:58402,
CC ChEBI:CHEBI:59869, ChEBI:CHEBI:71304; EC=4.3.2.9;
CC Evidence={ECO:0000269|PubMed:25716890};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P30184};
CC Note=Binds 2 Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:P30184};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.7 mM for glutathione {ECO:0000269|PubMed:25716890};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8GY54}.
CC -!- SIMILARITY: Belongs to the gamma-glutamylcyclotransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA16532.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79847.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL021633; CAA16532.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161578; CAB79847.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85886.1; -; Genomic_DNA.
DR EMBL; BT006411; AAP21219.1; -; mRNA.
DR EMBL; AK227743; BAE99727.1; -; mRNA.
DR EMBL; AY087934; AAM65482.1; -; mRNA.
DR PIR; T04496; T04496.
DR RefSeq; NP_567871.1; NM_119278.6.
DR AlphaFoldDB; Q84MC1; -.
DR SMR; Q84MC1; -.
DR STRING; 3702.AT4G31290.1; -.
DR PaxDb; Q84MC1; -.
DR PRIDE; Q84MC1; -.
DR ProteomicsDB; 247066; -.
DR EnsemblPlants; AT4G31290.1; AT4G31290.1; AT4G31290.
DR GeneID; 829256; -.
DR Gramene; AT4G31290.1; AT4G31290.1; AT4G31290.
DR KEGG; ath:AT4G31290; -.
DR Araport; AT4G31290; -.
DR TAIR; locus:2128096; AT4G31290.
DR eggNOG; KOG3182; Eukaryota.
DR HOGENOM; CLU_070703_2_1_1; -.
DR InParanoid; Q84MC1; -.
DR OMA; RPECTAV; -.
DR OrthoDB; 1238273at2759; -.
DR PhylomeDB; Q84MC1; -.
DR SABIO-RK; Q84MC1; -.
DR PRO; PR:Q84MC1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q84MC1; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0003839; F:gamma-glutamylcyclotransferase activity; IDA:UniProtKB.
DR GO; GO:0006751; P:glutathione catabolic process; IDA:UniProtKB.
DR CDD; cd06661; GGCT_like; 1.
DR InterPro; IPR006840; ChaC.
DR InterPro; IPR013024; GGCT-like.
DR PANTHER; PTHR12192; PTHR12192; 1.
DR Pfam; PF04752; ChaC; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lyase; Reference proteome.
FT CHAIN 1..227
FT /note="Gamma-glutamylcyclotransferase 2-2"
FT /id="PRO_0000436854"
FT ACT_SITE 87
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O75223"
FT BINDING 5..10
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O75223"
FT CONFLICT 103
FT /note="D -> Y (in Ref. 5; AAM65482)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 227 AA; 25607 MW; A8E7E35800487933 CRC64;
MVMWVFGYGS LVWNPGFHYD EKVLGFIKGY KRVFDLACID HRGTPEHPAR TCTLEKAEEA
ICWGTAFCVR GGPEKERLAM EYLERRECEY DLKTSVDFYK EDDPLKPAVT GVIVFTSTPD
KVSNKYYLGP APLEDMARQI ATANGPCGNN RDYLFLLEKA MHDIGHEEDY VIELANEVRK
VLAESSTKKV TPVKESRASR VANKSKNNVP TAHQILPHHP EAVATTI
