OPLA_YEAST
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 03-AUG-2022, entry version 163.
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; 63.
DR DIP; DIP-6558N; -.
DR IntAct; P28273; 5.
DR MINT; P28273; -.
DR STRING; 4932.YKL215C; -.
DR iPTMnet; P28273; -.
DR MaxQB; P28273; -.
DR PaxDb; P28273; -.
DR PRIDE; P28273; -.
DR EnsemblFungi; YKL215C_mRNA; YKL215C; YKL215C.
DR GeneID; 853665; -.
DR KEGG; sce:YKL215C; -.
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; RDIEFRT; -.
DR BioCyc; YEAST:G3O-31973-MON; -.
DR BRENDA; 3.5.2.9; 984.
DR Reactome; R-SCE-174403; Glutathione synthesis and recycling.
DR SABIO-RK; P28273; -.
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:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006749; P:glutathione metabolic process; IDA:MGI.
DR InterPro; IPR008040; Hydant_A_N.
DR InterPro; IPR002821; Hydantoinase_A.
DR InterPro; IPR003692; Hydantoinase_B.
DR InterPro; IPR045079; Oxoprolinase_fam.
DR PANTHER; PTHR11365; PTHR11365; 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
