ID   OPLA_YEAST              Reviewed;        1286 AA.
AC   P28273; D6VWY8; O60212;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 2.
DT   27-MAR-2024, entry version 170.
DE   RecName: Full=5-oxoprolinase;
DE            EC=3.5.2.9 {ECO:0000269|PubMed:20402795};
DE   AltName: Full=5-oxo-L-prolinase;
DE            Short=5-OPase;
DE   AltName: Full=Pyroglutamase;
GN   Name=OXP1; OrderedLocusNames=YKL215C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7941750; DOI=10.1002/yea.320100511;
RA   Tzermia M., Horaitis O., Alexandraki D.;
RT   "The complete sequencing of a 24.6 kb segment of yeast chromosome XI
RT   identified the known loci URA1, SAC1 and TRP3, and revealed 6 new open
RT   reading frames including homologues to the threonine dehydratases, membrane
RT   transporters, hydantoinases and the phospholipase A2-activating protein.";
RL   Yeast 10:663-679(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1003-1285.
RC   STRAIN=ATCC 28383 / FL100 / VTT C-80102;
RX   PubMed=1511880; DOI=10.1016/0378-1119(92)90265-q;
RA   Roy A.;
RT   "Nucleotide sequence of the URA1 gene of Saccharomyces cerevisiae.";
RL   Gene 118:149-150(1992).
RN   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1077, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-930, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [9]
RP   FUNCTION.
RX   PubMed=20349993; DOI=10.1021/ac902837x;
RA   Lu W., Clasquin M.F., Melamud E., Amador-Noguez D., Caudy A.A.,
RA   Rabinowitz J.D.;
RT   "Metabolomic analysis via reversed-phase ion-pairing liquid chromatography
RT   coupled to a stand alone orbitrap mass spectrometer.";
RL   Anal. Chem. 82:3212-3221(2010).
RN   [10]
RP   FUNCTION, SUBUNIT, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   MUTAGENESIS OF ASP-11; ASP-324; GLY-497 AND GLY-498.
RX   PubMed=20402795; DOI=10.1111/j.1567-1364.2010.00619.x;
RA   Kumar A., Bachhawat A.K.;
RT   "OXP1/YKL215c encodes an ATP-dependent 5-oxoprolinase in Saccharomyces
RT   cerevisiae: functional characterization, domain structure and
RT   identification of actin-like ATP-binding motifs in eukaryotic 5-
RT   oxoprolinases.";
RL   FEMS Yeast Res. 10:394-401(2010).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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.
CC       {ECO:0000269|PubMed:20349993, ECO:0000269|PubMed:20402795}.
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:20402795};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10349;
CC         Evidence={ECO:0000269|PubMed:20402795};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=159 uM for 5-oxoproline {ECO:0000269|PubMed:20402795};
CC         Vmax=3.5 nmol/h/ug enzyme {ECO:0000269|PubMed:20402795};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20402795}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 3180 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the oxoprolinase family. {ECO:0000305}.
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DR   EMBL; X75951; CAA53558.1; -; Genomic_DNA.
DR   EMBL; Z28215; CAA82060.1; -; Genomic_DNA.
DR   EMBL; X59371; CAA42015.1; -; Genomic_DNA.
DR   EMBL; M83295; AAA34567.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA08954.1; -; Genomic_DNA.
DR   PIR; S38058; S38058.
DR   RefSeq; NP_012707.1; NM_001179780.1.
DR   AlphaFoldDB; P28273; -.
DR   SMR; P28273; -.
DR   BioGRID; 33950; 65.
DR   DIP; DIP-6558N; -.
DR   IntAct; P28273; 5.
DR   MINT; P28273; -.
DR   STRING; 4932.YKL215C; -.
DR   iPTMnet; P28273; -.
DR   MaxQB; P28273; -.
DR   PaxDb; 4932-YKL215C; -.
DR   PeptideAtlas; P28273; -.
DR   EnsemblFungi; YKL215C_mRNA; YKL215C; YKL215C.
DR   GeneID; 853665; -.
DR   KEGG; sce:YKL215C; -.
DR   AGR; SGD:S000001698; -.
DR   SGD; S000001698; OXP1.
DR   VEuPathDB; FungiDB:YKL215C; -.
DR   eggNOG; KOG1939; Eukaryota.
DR   GeneTree; ENSGT00390000013463; -.
DR   HOGENOM; CLU_002157_0_1_1; -.
DR   InParanoid; P28273; -.
DR   OMA; QMGTQLR; -.
DR   OrthoDB; 674at2759; -.
DR   BioCyc; YEAST:G3O-31973-MONOMER; -.
DR   BRENDA; 3.5.2.9; 984.
DR   Reactome; R-SCE-174403; Glutathione synthesis and recycling.
DR   SABIO-RK; P28273; -.
DR   BioGRID-ORCS; 853665; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P28273; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P28273; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0017168; F:5-oxoprolinase (ATP-hydrolyzing) activity; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006749; P:glutathione metabolic process; IDA:MGI.
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.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..1286
FT                   /note="5-oxoprolinase"
FT                   /id="PRO_0000208582"
FT   MOD_RES         930
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         1077
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MUTAGEN         11
FT                   /note="D->A: Impairs ATPase and 5-oxoprolinase activity."
FT                   /evidence="ECO:0000269|PubMed:20402795"
FT   MUTAGEN         324
FT                   /note="D->A: Impairs ATPase and 5-oxoprolinase activity."
FT                   /evidence="ECO:0000269|PubMed:20402795"
FT   MUTAGEN         497
FT                   /note="G->A: Impairs ATPase and 5-oxoprolinase activity;
FT                   when associated with A-498."
FT                   /evidence="ECO:0000269|PubMed:20402795"
FT   MUTAGEN         498
FT                   /note="G->A: Impairs ATPase and 5-oxoprolinase activity;
FT                   when associated with A-497."
FT                   /evidence="ECO:0000269|PubMed:20402795"
SQ   SEQUENCE   1286 AA;  140428 MW;  9A0B8C609B5D6FFF CRC64;
     MQKGNIRIAI DKGGTFTDCV GNIGTGKQEH DTVIKLLSVD PKNYPDAPLE GIRRLLEVLE
     HKTIPRGIPL DISNVRSLRM GTTLATNCAL ERNGERCAFI TTKGFKDSLL IGDQTRPDIF
     NLNIKKVVPL YDTVVEIDER VTLEDFSEDP YFTKSSPNEQ EGILEGNSGE MVRVIKKPDE
     SSVRSILKVL YASGIKSIAI AFLHSYTFPD HERIVGNIAR EIGFSHVSLS SEVSPMIKFL
     PRAHSSVADA YLTPVIKKYL NSISAGLSHA EDTHIQFMQS DGGLVDGGKF SGLKSILSGP
     AGGVIGYSST CYDKNNNIPL IGFDMGGTST DVSRYGDGRL EHVFETVTAG IIIQSPQLDI
     HTVAAGGSSI LSWKNGLFRV GPDSAAADPG PAAYRKGGPL TITDANLFLG RLVPEFFPKI
     FGPNEDESLD LETTTLKFRE LTDVINKDLN SNLTMEEVAY GFIKVANECM ARPVRAITEA
     KGHVVSQHRL VSFGGAGGQH AIAVADSLGI DTVLIHRYSS ILSAYGIFLA DVIEENQEPC
     SFILGEPETI LKVKKRFLEL SKNSIKNLLS QSFSREDIVL ERYLNLRYEG TETSLMILQK
     YDDQWNFREW FSEAHKKEFG FSFDDKRIII DDIRIRAIGK SGVRKEKTVD EQLIEISHFK
     KADVSKDASF TQKAYFDNKW VDTAVFKIDD LPAGTIIEGP AILADGTQTN IILPNSQATI
     LNSHIFIKIN QKAAKTLSKS GYELDIDPIL LSIFSHRFMD IALQMGTQLR KTSVSTNVKE
     RLDFSCALFD SKGNLVANAP HVPVHLGSMS TCISAQAKLW EGKLKPGDVL ITNHPDIGGT
     HLPDITVITP SFSSTGELIF YVASRAHHAD IGGILPGSVP PNSKELYEEG TAIYSELVVK
     EGIFQEELIY KLFVEDPGKY PGCSGSRRFS DNISDLKAQV AANTKGIQLI GSLTKEYDLA
     TILKYMAAIQ TNASESIKKM LAKMVEHFGT TKFSGEDRLD DGSLIKLQVI IRPEKEEYIF
     NFDGTSPQVY GNLNAPEAIT NSAILYCLRC LVGEDIPLNQ GCLKPLTIKI PAGSLLSPRS
     GAAVVGGNVL TSQRVTDVIL KTFNVMADSQ GDCNNFTFGT GGNSGNKTDK QIKGFGYYET
     ICGGSGAGAD SWRGSGWNGS DAVHTNMTNT RMTDTEVFER RYPVLLKEFS IRRGSGGKGK
     YTGGNGVVRD VQFRKAVTAS ILSERRVIGP HGIKGGQDGS RGENLWVRHS TGALINVGGK
     NTIYAQPGDR FIIKTPGGGG FGQYKD
//