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P28273

- OPLA_YEAST

UniProt

P28273 - OPLA_YEAST

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Protein

5-oxoprolinase

Gene

OXP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the cleavage of 5-oxo-L-proline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.2 Publications

Catalytic activityi

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

Kineticsi

  1. KM=159 µM for 5-oxoproline1 Publication

Vmax=3.5 nmol/h/µg enzyme1 Publication

GO - Molecular functioni

  1. 5-oxoprolinase (ATP-hydrolyzing) activity Source: SGD
  2. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. glutathione metabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-6163-MONOMER.
YEAST:G3O-31973-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
5-oxoprolinase (EC:3.5.2.9)
Alternative name(s):
5-oxo-L-prolinase
Short name:
5-OPase
Pyroglutamase
Gene namesi
Name:OXP1
Ordered Locus Names:YKL215C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XI

Organism-specific databases

CYGDiYKL215c.
SGDiS000001698. OXP1.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi11 – 111D → A: Impairs ATPase and 5-oxoprolinase activity. 1 Publication
Mutagenesisi324 – 3241D → A: Impairs ATPase and 5-oxoprolinase activity. 1 Publication
Mutagenesisi497 – 4971G → A: Impairs ATPase and 5-oxoprolinase activity; when associated with A-498. 1 Publication
Mutagenesisi498 – 4981G → A: Impairs ATPase and 5-oxoprolinase activity; when associated with A-497. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 128612865-oxoprolinasePRO_0000208582Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei930 – 9301Phosphoserine1 Publication
Modified residuei1077 – 10771Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP28273.
PaxDbiP28273.
PeptideAtlasiP28273.

Expressioni

Gene expression databases

GenevestigatoriP28273.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
HSP104P315391EBI-27022,EBI-8050
SSA1P105911EBI-27022,EBI-8591

Protein-protein interaction databases

BioGridi33950. 15 interactions.
DIPiDIP-6558N.
IntActiP28273. 2 interactions.
MINTiMINT-692651.

Structurei

3D structure databases

ProteinModelPortaliP28273.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the oxoprolinase family.Curated

Phylogenomic databases

eggNOGiCOG0146.
GeneTreeiENSGT00390000013463.
InParanoidiP28273.
KOiK01469.
OMAiYEGTETS.
OrthoDBiEOG7966RF.

Family and domain databases

InterProiIPR008040. Hydant_A_N.
IPR002821. Hydantoinase_A.
IPR003692. Hydantoinase_B.
[Graphical view]
PfamiPF05378. Hydant_A_N. 1 hit.
PF01968. Hydantoinase_A. 1 hit.
PF02538. Hydantoinase_B. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P28273-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQKGNIRIAI DKGGTFTDCV GNIGTGKQEH DTVIKLLSVD PKNYPDAPLE
60 70 80 90 100
GIRRLLEVLE HKTIPRGIPL DISNVRSLRM GTTLATNCAL ERNGERCAFI
110 120 130 140 150
TTKGFKDSLL IGDQTRPDIF NLNIKKVVPL YDTVVEIDER VTLEDFSEDP
160 170 180 190 200
YFTKSSPNEQ EGILEGNSGE MVRVIKKPDE SSVRSILKVL YASGIKSIAI
210 220 230 240 250
AFLHSYTFPD HERIVGNIAR EIGFSHVSLS SEVSPMIKFL PRAHSSVADA
260 270 280 290 300
YLTPVIKKYL NSISAGLSHA EDTHIQFMQS DGGLVDGGKF SGLKSILSGP
310 320 330 340 350
AGGVIGYSST CYDKNNNIPL IGFDMGGTST DVSRYGDGRL EHVFETVTAG
360 370 380 390 400
IIIQSPQLDI HTVAAGGSSI LSWKNGLFRV GPDSAAADPG PAAYRKGGPL
410 420 430 440 450
TITDANLFLG RLVPEFFPKI FGPNEDESLD LETTTLKFRE LTDVINKDLN
460 470 480 490 500
SNLTMEEVAY GFIKVANECM ARPVRAITEA KGHVVSQHRL VSFGGAGGQH
510 520 530 540 550
AIAVADSLGI DTVLIHRYSS ILSAYGIFLA DVIEENQEPC SFILGEPETI
560 570 580 590 600
LKVKKRFLEL SKNSIKNLLS QSFSREDIVL ERYLNLRYEG TETSLMILQK
610 620 630 640 650
YDDQWNFREW FSEAHKKEFG FSFDDKRIII DDIRIRAIGK SGVRKEKTVD
660 670 680 690 700
EQLIEISHFK KADVSKDASF TQKAYFDNKW VDTAVFKIDD LPAGTIIEGP
710 720 730 740 750
AILADGTQTN IILPNSQATI LNSHIFIKIN QKAAKTLSKS GYELDIDPIL
760 770 780 790 800
LSIFSHRFMD IALQMGTQLR KTSVSTNVKE RLDFSCALFD SKGNLVANAP
810 820 830 840 850
HVPVHLGSMS TCISAQAKLW EGKLKPGDVL ITNHPDIGGT HLPDITVITP
860 870 880 890 900
SFSSTGELIF YVASRAHHAD IGGILPGSVP PNSKELYEEG TAIYSELVVK
910 920 930 940 950
EGIFQEELIY KLFVEDPGKY PGCSGSRRFS DNISDLKAQV AANTKGIQLI
960 970 980 990 1000
GSLTKEYDLA TILKYMAAIQ TNASESIKKM LAKMVEHFGT TKFSGEDRLD
1010 1020 1030 1040 1050
DGSLIKLQVI IRPEKEEYIF NFDGTSPQVY GNLNAPEAIT NSAILYCLRC
1060 1070 1080 1090 1100
LVGEDIPLNQ GCLKPLTIKI PAGSLLSPRS GAAVVGGNVL TSQRVTDVIL
1110 1120 1130 1140 1150
KTFNVMADSQ GDCNNFTFGT GGNSGNKTDK QIKGFGYYET ICGGSGAGAD
1160 1170 1180 1190 1200
SWRGSGWNGS DAVHTNMTNT RMTDTEVFER RYPVLLKEFS IRRGSGGKGK
1210 1220 1230 1240 1250
YTGGNGVVRD VQFRKAVTAS ILSERRVIGP HGIKGGQDGS RGENLWVRHS
1260 1270 1280
TGALINVGGK NTIYAQPGDR FIIKTPGGGG FGQYKD
Length:1,286
Mass (Da):140,428
Last modified:June 1, 1994 - v2
Checksum:i9A0B8C609B5D6FFF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiS38058.
RefSeqiNP_012707.1. NM_001179780.1.

Genome annotation databases

EnsemblFungiiYKL215C; YKL215C; YKL215C.
GeneIDi853665.
KEGGisce:YKL215C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi S38058.
RefSeqi NP_012707.1. NM_001179780.1.

3D structure databases

ProteinModelPortali P28273.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33950. 15 interactions.
DIPi DIP-6558N.
IntActi P28273. 2 interactions.
MINTi MINT-692651.

Proteomic databases

MaxQBi P28273.
PaxDbi P28273.
PeptideAtlasi P28273.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YKL215C ; YKL215C ; YKL215C .
GeneIDi 853665.
KEGGi sce:YKL215C.

Organism-specific databases

CYGDi YKL215c.
SGDi S000001698. OXP1.

Phylogenomic databases

eggNOGi COG0146.
GeneTreei ENSGT00390000013463.
InParanoidi P28273.
KOi K01469.
OMAi YEGTETS.
OrthoDBi EOG7966RF.

Enzyme and pathway databases

BioCyci RETL1328306-WGS:GSTH-6163-MONOMER.
YEAST:G3O-31973-MONOMER.

Miscellaneous databases

NextBioi 974599.
PROi P28273.

Gene expression databases

Genevestigatori P28273.

Family and domain databases

InterProi IPR008040. Hydant_A_N.
IPR002821. Hydantoinase_A.
IPR003692. Hydantoinase_B.
[Graphical view ]
Pfami PF05378. Hydant_A_N. 1 hit.
PF01968. Hydantoinase_A. 1 hit.
PF02538. Hydantoinase_B. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiOPLA_YEAST
AccessioniPrimary (citable) accession number: P28273
Secondary accession number(s): D6VWY8, O60212
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: June 1, 1994
Last modified: October 29, 2014
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 3180 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

External Data

Dasty 3