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P28273 (OPLA_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
5-oxoprolinase

EC=3.5.2.9
Alternative name(s):
5-oxo-L-prolinase
Short name=5-OPase
Pyroglutamase
Gene names
Name:OXP1
Ordered Locus Names:YKL215C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1286 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the cleavage of 5-oxo-L-proline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate. Ref.9 Ref.10

Catalytic activity

ATP + 5-oxo-L-proline + 2 H2O = ADP + phosphate + L-glutamate.

Subunit structure

Homodimer. Ref.10

Subcellular location

Cytoplasm Ref.5.

Miscellaneous

Present with 3180 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the oxoprolinase family.

Biophysicochemical properties

Kinetic parameters:

KM=159 µM for 5-oxoproline Ref.10

Vmax=3.5 nmol/h/µg enzyme

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglutathione metabolic process

Inferred from mutant phenotype Ref.9. Source: SGD

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function5-oxoprolinase (ATP-hydrolyzing) activity

Inferred from direct assay Ref.10. Source: SGD

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HSP104P315391EBI-27022,EBI-8050
SSA1P105911EBI-27022,EBI-8591

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 128612865-oxoprolinase
PRO_0000208582

Amino acid modifications

Modified residue9301Phosphoserine Ref.8
Modified residue10771Phosphoserine Ref.7

Experimental info

Mutagenesis111D → A: Impairs ATPase and 5-oxoprolinase activity. Ref.10
Mutagenesis3241D → A: Impairs ATPase and 5-oxoprolinase activity. Ref.10
Mutagenesis4971G → A: Impairs ATPase and 5-oxoprolinase activity; when associated with A-498. Ref.10
Mutagenesis4981G → A: Impairs ATPase and 5-oxoprolinase activity; when associated with A-497. Ref.10

Sequences

Sequence LengthMass (Da)Tools
P28273 [UniParc].

Last modified June 1, 1994. Version 2.
Checksum: 9A0B8C609B5D6FFF

FASTA1,286140,428
        10         20         30         40         50         60 
MQKGNIRIAI DKGGTFTDCV GNIGTGKQEH DTVIKLLSVD PKNYPDAPLE GIRRLLEVLE 

        70         80         90        100        110        120 
HKTIPRGIPL DISNVRSLRM GTTLATNCAL ERNGERCAFI TTKGFKDSLL IGDQTRPDIF 

       130        140        150        160        170        180 
NLNIKKVVPL YDTVVEIDER VTLEDFSEDP YFTKSSPNEQ EGILEGNSGE MVRVIKKPDE 

       190        200        210        220        230        240 
SSVRSILKVL YASGIKSIAI AFLHSYTFPD HERIVGNIAR EIGFSHVSLS SEVSPMIKFL 

       250        260        270        280        290        300 
PRAHSSVADA YLTPVIKKYL NSISAGLSHA EDTHIQFMQS DGGLVDGGKF SGLKSILSGP 

       310        320        330        340        350        360 
AGGVIGYSST CYDKNNNIPL IGFDMGGTST DVSRYGDGRL EHVFETVTAG IIIQSPQLDI 

       370        380        390        400        410        420 
HTVAAGGSSI LSWKNGLFRV GPDSAAADPG PAAYRKGGPL TITDANLFLG RLVPEFFPKI 

       430        440        450        460        470        480 
FGPNEDESLD LETTTLKFRE LTDVINKDLN SNLTMEEVAY GFIKVANECM ARPVRAITEA 

       490        500        510        520        530        540 
KGHVVSQHRL VSFGGAGGQH AIAVADSLGI DTVLIHRYSS ILSAYGIFLA DVIEENQEPC 

       550        560        570        580        590        600 
SFILGEPETI LKVKKRFLEL SKNSIKNLLS QSFSREDIVL ERYLNLRYEG TETSLMILQK 

       610        620        630        640        650        660 
YDDQWNFREW FSEAHKKEFG FSFDDKRIII DDIRIRAIGK SGVRKEKTVD EQLIEISHFK 

       670        680        690        700        710        720 
KADVSKDASF TQKAYFDNKW VDTAVFKIDD LPAGTIIEGP AILADGTQTN IILPNSQATI 

       730        740        750        760        770        780 
LNSHIFIKIN QKAAKTLSKS GYELDIDPIL LSIFSHRFMD IALQMGTQLR KTSVSTNVKE 

       790        800        810        820        830        840 
RLDFSCALFD SKGNLVANAP HVPVHLGSMS TCISAQAKLW EGKLKPGDVL ITNHPDIGGT 

       850        860        870        880        890        900 
HLPDITVITP SFSSTGELIF YVASRAHHAD IGGILPGSVP PNSKELYEEG TAIYSELVVK 

       910        920        930        940        950        960 
EGIFQEELIY KLFVEDPGKY PGCSGSRRFS DNISDLKAQV AANTKGIQLI GSLTKEYDLA 

       970        980        990       1000       1010       1020 
TILKYMAAIQ TNASESIKKM LAKMVEHFGT TKFSGEDRLD DGSLIKLQVI IRPEKEEYIF 

      1030       1040       1050       1060       1070       1080 
NFDGTSPQVY GNLNAPEAIT NSAILYCLRC LVGEDIPLNQ GCLKPLTIKI PAGSLLSPRS 

      1090       1100       1110       1120       1130       1140 
GAAVVGGNVL TSQRVTDVIL KTFNVMADSQ GDCNNFTFGT GGNSGNKTDK QIKGFGYYET 

      1150       1160       1170       1180       1190       1200 
ICGGSGAGAD SWRGSGWNGS DAVHTNMTNT RMTDTEVFER RYPVLLKEFS IRRGSGGKGK 

      1210       1220       1230       1240       1250       1260 
YTGGNGVVRD VQFRKAVTAS ILSERRVIGP HGIKGGQDGS RGENLWVRHS TGALINVGGK 

      1270       1280 
NTIYAQPGDR FIIKTPGGGG FGQYKD 

« Hide

References

« Hide 'large scale' references
[1]"The complete sequencing of a 24.6 kb segment of yeast chromosome XI identified the known loci URA1, SAC1 and TRP3, and revealed 6 new open reading frames including homologues to the threonine dehydratases, membrane transporters, hydantoinases and the phospholipase A2-activating protein."
Tzermia M., Horaitis O., Alexandraki D.
Yeast 10:663-679(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"Complete DNA sequence of yeast chromosome XI."
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. expand/collapse author list , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Nucleotide sequence of the URA1 gene of Saccharomyces cerevisiae."
Roy A.
Gene 118:149-150(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1003-1285.
Strain: ATCC 28383 / FL100 / VTT C-80102.
[5]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1077, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-930, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Metabolomic analysis via reversed-phase ion-pairing liquid chromatography coupled to a stand alone orbitrap mass spectrometer."
Lu W., Clasquin M.F., Melamud E., Amador-Noguez D., Caudy A.A., Rabinowitz J.D.
Anal. Chem. 82:3212-3221(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"OXP1/YKL215c encodes an ATP-dependent 5-oxoprolinase in Saccharomyces cerevisiae: functional characterization, domain structure and identification of actin-like ATP-binding motifs in eukaryotic 5-oxoprolinases."
Kumar A., Bachhawat A.K.
FEMS Yeast Res. 10:394-401(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-11; ASP-324; GLY-497 AND GLY-498.
[11]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X75951 Genomic DNA. Translation: CAA53558.1.
Z28215 Genomic DNA. Translation: CAA82060.1.
X59371 Genomic DNA. Translation: CAA42015.1.
M83295 Genomic DNA. Translation: AAA34567.1.
BK006944 Genomic DNA. Translation: DAA08954.1.
PIRS38058.
RefSeqNP_012707.1. NM_001179780.1.

3D structure databases

ProteinModelPortalP28273.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33950. 14 interactions.
DIPDIP-6558N.
IntActP28273. 2 interactions.
MINTMINT-692651.

Proteomic databases

PaxDbP28273.
PeptideAtlasP28273.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYKL215C; YKL215C; YKL215C.
GeneID853665.
KEGGsce:YKL215C.

Organism-specific databases

CYGDYKL215c.
SGDS000001698. OXP1.

Phylogenomic databases

eggNOGCOG0146.
GeneTreeENSGT00390000013463.
KOK01469.
OMAPNSKELY.
OrthoDBEOG7966RF.

Enzyme and pathway databases

BioCycYEAST:G3O-31973-MONOMER.

Gene expression databases

GenevestigatorP28273.

Family and domain databases

InterProIPR008040. Hydant_A_N.
IPR002821. Hydantoinase_A.
IPR003692. Hydantoinase_B.
[Graphical view]
PfamPF05378. Hydant_A_N. 1 hit.
PF01968. Hydantoinase_A. 1 hit.
PF02538. Hydantoinase_B. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio974599.
PROP28273.

Entry information

Entry nameOPLA_YEAST
AccessionPrimary (citable) accession number: P28273
Secondary accession number(s): D6VWY8, O60212
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: June 1, 1994
Last modified: March 19, 2014
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XI

Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families