P28273 (OPLA_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	1286 AA.
Sequence status	Complete.
Protein existence	Evidence 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.8 Ref.9
Catalytic activity	ATP + 5-oxo-L-proline + 2 H2O = ADP + phosphate + L-glutamate.
Subunit structure	Homodimer. Ref.9
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.9 Vmax=3.5 nmol/h/µg enzyme

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glutathione metabolic process Inferred from direct assay Ref.8. Source: MGI
Cellular_component	cytoplasm Inferred from direct assay Ref.5PubMed 22842922. Source: SGD
Molecular_function	5-oxoprolinase (ATP-hydrolyzing) activity Inferred from direct assay Ref.8. Source: MGI ATP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HSP104	P31539	1	EBI-27022,EBI-8050
SSA1	P10591	1	EBI-27022,EBI-8591

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1286	1286	5-oxoprolinase		PRO_0000208582
Amino acid modifications
	Modified residue	773	1	Phosphoserine Ref.7
	Modified residue	930	1	Phosphoserine Ref.7
	Modified residue	1077	1	Phosphoserine Ref.7
Experimental info
	Mutagenesis	11	1	D → A: Impairs ATPase and 5-oxoprolinase activity. Ref.9
	Mutagenesis	324	1	D → A: Impairs ATPase and 5-oxoprolinase activity. Ref.9
	Mutagenesis	497	1	G → A: Impairs ATPase and 5-oxoprolinase activity; when associated with A-498. Ref.9
	Mutagenesis	498	1	G → A: Impairs ATPase and 5-oxoprolinase activity; when associated with A-497. Ref.9

Sequences

	Sequence		Length	Mass (Da)
	P28273 [UniParc]. Last modified June 1, 1994. Version 2. Checksum: 9A0B8C609B5D6FFF	FASTA	1,286	140,428
	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

References

	« Hide 'large scale' referencesShow '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. , 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 96604 / S288c / FY1679.
[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-773; SER-930 AND SER-1077, MASS SPECTROMETRY.
[8]	"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.
[9]	"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.
+	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.
PIR	S38058.
RefSeq	NP_012707.1. NM_001179780.1.
3D structure databases
ProteinModelPortal	P28273.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6558N.
IntAct	P28273. 3 interactions.
MINT	MINT-692651.
Proteomic databases
PaxDb	P28273.
PeptideAtlas	P28273.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YKL215C; YKL215C; YKL215C.
GeneID	853665.
KEGG	sce:YKL215C.
Organism-specific databases
CYGD	YKL215c.
SGD	S000001698. OXP1.
Phylogenomic databases
eggNOG	COG0146.
GeneTree	ENSGT00390000013463.
KO	K01469.
OMA	PLTVTDC.
OrthoDB	EOG4CJZRK.
Enzyme and pathway databases
BioCyc	YEAST:G3O-31973-MONOMER.
Gene expression databases
Genevestigator	P28273.
GermOnline	YKL215C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR008040. Hydant_A_N. IPR002821. Hydantoinase_A. IPR003692. Hydantoinase_B. [Graphical view]
Pfam	PF05378. Hydant_A_N. 1 hit. PF01968. Hydantoinase_A. 1 hit. PF02538. Hydantoinase_B. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	974599.

Entry information

Entry name

OPLA_YEAST

Accession

Primary (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:	May 29, 2013
This is version 98 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program