ID   OPLA_ARATH              Reviewed;        1266 AA.
AC   Q9FIZ7; Q0WQ06;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=5-oxoprolinase 1 {ECO:0000303|PubMed:18768907};
DE            EC=3.5.2.9 {ECO:0000269|PubMed:18768907};
DE   AltName: Full=5-oxo-L-prolinase {ECO:0000303|PubMed:18768907};
DE            Short=5-OPase {ECO:0000303|PubMed:18768907};
DE   AltName: Full=Protein OXOPROLINASE 1 {ECO:0000303|PubMed:18768907};
DE   AltName: Full=Pyroglutamase {ECO:0000303|PubMed:18768907};
GN   Name=OXP1 {ECO:0000303|PubMed:18768907};
GN   OrderedLocusNames=At5g37830 {ECO:0000312|Araport:AT5G37830};
GN   ORFNames=K22F20.70 {ECO:0000312|EMBL:BAB10362.1};
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=9872454; DOI=10.1093/dnares/5.5.297;
RA   Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT   features of the regions of 1,013,767 bp covered by sixteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:297-308(1998).
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] OF 1-963.
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA   Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT   "Multidimensional protein identification technology (MudPIT) analysis of
RT   ubiquitinated proteins in plants.";
RL   Mol. Cell. Proteomics 6:601-610(2007).
RN   [6]
RP   FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX   PubMed=18768907; DOI=10.1104/pp.108.125716;
RA   Ohkama-Ohtsu N., Oikawa A., Zhao P., Xiang C., Saito K., Oliver D.J.;
RT   "A gamma-glutamyl transpeptidase-independent pathway of glutathione
RT   catabolism to glutamate via 5-oxoproline in Arabidopsis.";
RL   Plant Physiol. 148:1603-1613(2008).
CC   -!- FUNCTION: Catalyzes the cleavage of 5-oxo-L-proline to form L-glutamate
CC       coupled to the hydrolysis of ATP to ADP and inorganic phosphate. Acts
CC       in the glutathione degradation pathway. {ECO:0000269|PubMed:18768907}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate +
CC         phosphate; Xref=Rhea:RHEA:10348, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58402, ChEBI:CHEBI:456216; EC=3.5.2.9;
CC         Evidence={ECO:0000269|PubMed:18768907};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:18768907}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers and
CC       siliques. {ECO:0000269|PubMed:18768907}.
CC   -!- DISRUPTION PHENOTYPE: No morphological phenotype, but high accumulation
CC       of 5-oxoproline and decreased concentration of glutamate.
CC       {ECO:0000269|PubMed:18768907}.
CC   -!- SIMILARITY: Belongs to the oxoprolinase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB016873; BAB10362.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94237.1; -; Genomic_DNA.
DR   EMBL; AY102096; AAM26666.1; -; mRNA.
DR   EMBL; BT004510; AAO42756.1; -; mRNA.
DR   EMBL; AK228904; BAF00793.1; -; mRNA.
DR   RefSeq; NP_198599.1; NM_123142.5.
DR   AlphaFoldDB; Q9FIZ7; -.
DR   SMR; Q9FIZ7; -.
DR   BioGRID; 19012; 2.
DR   STRING; 3702.Q9FIZ7; -.
DR   iPTMnet; Q9FIZ7; -.
DR   PaxDb; 3702-AT5G37830-1; -.
DR   ProteomicsDB; 249367; -.
DR   EnsemblPlants; AT5G37830.1; AT5G37830.1; AT5G37830.
DR   GeneID; 833761; -.
DR   Gramene; AT5G37830.1; AT5G37830.1; AT5G37830.
DR   KEGG; ath:AT5G37830; -.
DR   Araport; AT5G37830; -.
DR   TAIR; AT5G37830; OXP1.
DR   eggNOG; KOG1939; Eukaryota.
DR   HOGENOM; CLU_002157_0_1_1; -.
DR   InParanoid; Q9FIZ7; -.
DR   OMA; TDCNVML; -.
DR   OrthoDB; 674at2759; -.
DR   PhylomeDB; Q9FIZ7; -.
DR   BioCyc; ARA:AT5G37830-MONOMER; -.
DR   BRENDA; 3.5.2.9; 399.
DR   PRO; PR:Q9FIZ7; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FIZ7; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; NAS:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0017168; F:5-oxoprolinase (ATP-hydrolyzing) activity; IMP:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006751; P:glutathione catabolic process; IMP:TAIR.
DR   InterPro; IPR049517; ACX-like_C.
DR   InterPro; IPR008040; Hydant_A_N.
DR   InterPro; IPR002821; Hydantoinase_A.
DR   InterPro; IPR003692; Hydantoinase_B.
DR   InterPro; IPR045079; Oxoprolinase_fam.
DR   PANTHER; PTHR11365:SF2; 5-OXOPROLINASE; 1.
DR   PANTHER; PTHR11365; 5-OXOPROLINASE RELATED; 1.
DR   Pfam; PF19278; Hydant_A_C; 1.
DR   Pfam; PF05378; Hydant_A_N; 1.
DR   Pfam; PF01968; Hydantoinase_A; 1.
DR   Pfam; PF02538; Hydantoinase_B; 1.
DR   Genevisible; Q9FIZ7; AT.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..1266
FT                   /note="5-oxoprolinase 1"
FT                   /id="PRO_0000380674"
SQ   SEQUENCE   1266 AA;  137531 MW;  77E862B3E4EB7395 CRC64;
     MGTVIEGKLR FCIDRGGTFT DVYAEIPGHS DGHVLKLLSV DPSNYDDAPV EGIRRILEEY
     TGKKIPRTSK IPTDKIQWIR MGTTVATNAL LERKGERIAL CVTKGFKDLL QIGNQARPDI
     FDLTVAKPSN LYEEVIEVDE RVVLALEDDD DDEGSLIKGV SGEFLRVVKP FDGEGLKPLL
     KGLLDKGISC LAVVLMHSYT YPKHEMDVEK LALEMGFRHV SLSSALTPMV RAVPRGLTAT
     VDAYLTPVIK EYLSGFISKF DDDLGKVNVL FMQSDGGLAP ESRFSGHKAV LSGPAGGVVG
     YSQTLFGLET EKPLIGFDMG GTSTDVSRYD GSYEQVIETQ IAGTIIQAPQ LDINTVAAGG
     GSKLKFQFGA FRVGPDSVGA HPGPVCYRKG GELAVTDANL VLGFVIPDYF PSIFGPNEDQ
     PLDVAATREA FEKLAGQINI YRKSQDPSAK DMSVEEIAMG FVSVANETMC RPIRQLTEMK
     GHETKNHALA CFGGAGPQHA CAIARSLGMK EVLVHRYCGI LSAYGMGLAD VIEDAQEPYS
     AVYGPESLSE VFRRETVLLR EVREKLQEQG FGDGNISTET YLNLRYDGTD TAIMVKGKKT
     GDGSAFDYAA EFLKLFEQEY GFKLQNRNLL ICDVRVRGIG VTSILKPRAV EAAPVTPKVE
     RHYKVYFEGG WHDTPLFKLE NLGFGHEILG PAIIMNGNST VIVEPQCKAI ITKYGNIKIE
     VEPATSSVKL AENVADVVQL SIFNHRFMGI AEQMGRTLQR TSISTNIKER LDFSCALFSP
     DGGLVANAPH VPVHLGAMSS TVRWQLKHWG ENLNEGDVLV TNHPCAGGSH LPDITVITPV
     FDKGKLVFFV ASRGHHAEVG GITPGSMPPF SKAIWEEGAA IKAFKVVEKG VFQEEGIVKL
     LQFPSSDETT TKIPGTRRIQ DNLSDLQAQI AANQRGISLI KELIEQYGLG TVQAYMKYVQ
     LNAEEAVREM LKSVANRVSS ETPNSRVGNS VTIEEEDYMD DGSIIHLKLT IDADKGEASF
     DFTGTSPEVY GNWNAPEAVT SAAVIYCLRC LVNVDIPLNQ GCLAPVEIRI PAGSFLSPSE
     KAAVVGGNVL TSQRVTDVVL TAFQACACSQ GCMNNLTFGD DTFGYYETIG GGCGAGPTWN
     GTSGVQCHMT NTRMTDPEIF EQRYPVLLHR FGLRENSGGN GLHKGGDGLV REIEFRKPVV
     VSILSERRVH SPRGLNGGQN GLRGANYLIT KDKRRIYLGG KNTVHVEAGE ILQILTPGGG
     GFGSNI
//