GCT21_ARATH
ID GCT21_ARATH Reviewed; 216 AA.
AC Q8GY54;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Gamma-glutamylcyclotransferase 2-1 {ECO:0000305};
DE Short=AtGGCT2;1 {ECO:0000303|PubMed:24214398};
DE EC=4.3.2.9 {ECO:0000269|PubMed:24214398};
DE AltName: Full=Gamma-glutamyl cyclotransferase 2;1 {ECO:0000303|PubMed:24214398};
GN Name=GGCT2;1 {ECO:0000303|PubMed:24214398};
GN OrderedLocusNames=At5g26220 {ECO:0000312|Araport:AT5G26220};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
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 [5]
RP INDUCTION.
RX PubMed=15708574; DOI=10.1016/j.mrfmmm.2004.10.004;
RA Kovalchuk I., Titov V., Hohn B., Kovalchuk O.;
RT "Transcriptome profiling reveals similarities and differences in plant
RT responses to cadmium and lead.";
RL Mutat. Res. 570:149-161(2005).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP INDUCTION BY ARSENITE, AND DISRUPTION PHENOTYPE.
RX PubMed=24214398; DOI=10.1105/tpc.113.111815;
RA Paulose B., Chhikara S., Coomey J., Jung H.I., Vatamaniuk O.,
RA Dhankher O.P.;
RT "A gamma-glutamyl cyclotransferase protects Arabidopsis plants from heavy
RT metal toxicity by recycling glutamate to maintain glutathione
RT homeostasis.";
RL Plant Cell 25:4580-4595(2013).
CC -!- FUNCTION: Catalyzes the formation of 5-oxoproline from gamma-glutamyl
CC dipeptides and plays a significant role in glutathione (GSH)
CC homeostasis. Converts both GSH and gamma-glutamyl-L-alanine to 5-
CC oxoproline in vitro. Plays a role in detoxification of heavy metals and
CC metalloids by recycling glutamate and maintaining GSH homeostasis.
CC {ECO:0000269|PubMed:24214398}.
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:24214398};
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24214398}.
CC -!- TISSUE SPECIFICITY: Expressed in the central vascular bundle of roots,
CC leaf veins, hydathodes, cauline leaves, shoot apex, sepal veins, flower
CC receptacles and developing seeds. {ECO:0000269|PubMed:24214398}.
CC -!- INDUCTION: By cadmium and lead (PubMed:15708574). Induced by arsenite
CC (PubMed:24214398). {ECO:0000269|PubMed:15708574,
CC ECO:0000269|PubMed:24214398}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants show increased tolerance to arsenite and
CC cadmium. {ECO:0000269|PubMed:24214398}.
CC -!- SIMILARITY: Belongs to the gamma-glutamylcyclotransferase family.
CC {ECO:0000305}.
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DR EMBL; AC005965; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93538.1; -; Genomic_DNA.
DR EMBL; AK117855; BAC42496.1; -; mRNA.
DR EMBL; BT005234; AAO63298.1; -; mRNA.
DR RefSeq; NP_197994.1; NM_122523.4.
DR AlphaFoldDB; Q8GY54; -.
DR SMR; Q8GY54; -.
DR STRING; 3702.AT5G26220.1; -.
DR PaxDb; Q8GY54; -.
DR ProteomicsDB; 247065; -.
DR DNASU; 832691; -.
DR EnsemblPlants; AT5G26220.1; AT5G26220.1; AT5G26220.
DR GeneID; 832691; -.
DR Gramene; AT5G26220.1; AT5G26220.1; AT5G26220.
DR KEGG; ath:AT5G26220; -.
DR Araport; AT5G26220; -.
DR TAIR; locus:2179714; AT5G26220.
DR eggNOG; KOG3182; Eukaryota.
DR HOGENOM; CLU_070703_2_1_1; -.
DR InParanoid; Q8GY54; -.
DR OrthoDB; 1238273at2759; -.
DR PhylomeDB; Q8GY54; -.
DR PRO; PR:Q8GY54; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8GY54; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0003839; F:gamma-glutamylcyclotransferase activity; IDA:UniProtKB.
DR GO; GO:0006751; P:glutathione catabolic process; IDA:UniProtKB.
DR GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
DR GO; GO:0010288; P:response to lead ion; IEP:TAIR.
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..216
FT /note="Gamma-glutamylcyclotransferase 2-1"
FT /id="PRO_0000436853"
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"
SQ SEQUENCE 216 AA; 24573 MW; C91054749275CCBA CRC64;
MVLWVFGYGS LIWNPGFDFD EKLIGYIKDY KRVFDLACID HRGTPEHPAR TCTLEQSTGA
ICWGAAYCVR GGPEKEKLAM EYLERRECEY DSKTLVEFYT ENDTSTPIVT GVIVFTSTPD
KVSNKYYLGP APLEEMARQI ATASGPCGNN REYLFKLEKA MFDIEHEEEY VIELANEVRK
QLDLPEEVKA LLKPIVSHVS VKSQAHVSTR QRVFAS
