GCT23_ARATH
ID GCT23_ARATH Reviewed; 199 AA.
AC Q84QC1; Q9FPD4; Q9LPF2;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Gamma-glutamylcyclotransferase 2-3 {ECO:0000305};
DE Short=AtGGCT2;3 {ECO:0000303|PubMed:25716890};
DE EC=4.3.2.9 {ECO:0000269|PubMed:25716890};
DE AltName: Full=Gamma-glutamyl cyclotransferase 2;3 {ECO:0000303|PubMed:25716890};
GN Name=GGCT2;3 {ECO:0000303|PubMed:25716890};
GN OrderedLocusNames=At1g44790 {ECO:0000312|Araport:AT1G44790};
GN ORFNames=T12C22.6 {ECO:0000312|EMBL:AAF78262.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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=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 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=4.9 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=AAF78262.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC020576; AAF78262.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32052.1; -; Genomic_DNA.
DR EMBL; AF332442; AAG48805.1; -; mRNA.
DR EMBL; BT006192; AAP06821.1; -; mRNA.
DR EMBL; AK228371; BAF00310.1; -; mRNA.
DR PIR; H96506; H96506.
DR RefSeq; NP_564490.1; NM_103560.3.
DR AlphaFoldDB; Q84QC1; -.
DR SMR; Q84QC1; -.
DR STRING; 3702.AT1G44790.1; -.
DR PaxDb; Q84QC1; -.
DR PRIDE; Q84QC1; -.
DR ProteomicsDB; 247067; -.
DR DNASU; 841043; -.
DR EnsemblPlants; AT1G44790.1; AT1G44790.1; AT1G44790.
DR GeneID; 841043; -.
DR Gramene; AT1G44790.1; AT1G44790.1; AT1G44790.
DR KEGG; ath:AT1G44790; -.
DR Araport; AT1G44790; -.
DR TAIR; locus:2194854; AT1G44790.
DR eggNOG; KOG3182; Eukaryota.
DR HOGENOM; CLU_070703_2_2_1; -.
DR InParanoid; Q84QC1; -.
DR OMA; LLWYTDF; -.
DR OrthoDB; 1238273at2759; -.
DR PhylomeDB; Q84QC1; -.
DR SABIO-RK; Q84QC1; -.
DR PRO; PR:Q84QC1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q84QC1; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
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 InterPro; IPR036568; GGCT-like_sf.
DR PANTHER; PTHR12192; PTHR12192; 1.
DR Pfam; PF04752; ChaC; 1.
DR SUPFAM; SSF110857; SSF110857; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lyase; Reference proteome.
FT CHAIN 1..199
FT /note="Gamma-glutamylcyclotransferase 2-3"
FT /id="PRO_0000436855"
FT ACT_SITE 86
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 199 AA; 22229 MW; D56097DAF3507102 CRC64;
MAMWVFGYGS LIWKTGFPFD ESLPGFIKGY RRVFHQGSTD HRGTPDFPGR TVTLEAAHEE
VCCGVAYKIT KEEDKRDALL HLEVREKQYD QKEYLDFFTD SNASEPAVAG VMVYIASPDK
KSNNNYLGPA PLEDIAKQIV KAKGPSGPNR DYLFNLEEAL AQLGFKDKHV TDLANQVRHI
LSESEELDID ATAATANNV
