CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005664
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 5-oxoprolinase 
Protein Synonyms/Alias
 5-oxo-L-prolinase; 5-OPase; Pyroglutamase 
Gene Name
 OXP1 
Gene Synonyms/Alias
 YKL215C 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
12NIRIAIDKGGTFTDCubiquitination[1]
562KRFLELSKNSIKNLLubiquitination[1]
Reference
 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301
Functional Description
 Catalyzes the cleavage of 5-oxo-L-proline to form L- glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate. 
Sequence Annotation
 MOD_RES 930 930 Phosphoserine.
 MOD_RES 1077 1077 Phosphoserine.  
Keyword
 ATP-binding; Complete proteome; Cytoplasm; Hydrolase; Nucleotide-binding; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1286 AA 
Protein Sequence
MQKGNIRIAI DKGGTFTDCV GNIGTGKQEH DTVIKLLSVD PKNYPDAPLE GIRRLLEVLE 60
HKTIPRGIPL DISNVRSLRM GTTLATNCAL ERNGERCAFI TTKGFKDSLL IGDQTRPDIF 120
NLNIKKVVPL YDTVVEIDER VTLEDFSEDP YFTKSSPNEQ EGILEGNSGE MVRVIKKPDE 180
SSVRSILKVL YASGIKSIAI AFLHSYTFPD HERIVGNIAR EIGFSHVSLS SEVSPMIKFL 240
PRAHSSVADA YLTPVIKKYL NSISAGLSHA EDTHIQFMQS DGGLVDGGKF SGLKSILSGP 300
AGGVIGYSST CYDKNNNIPL IGFDMGGTST DVSRYGDGRL EHVFETVTAG IIIQSPQLDI 360
HTVAAGGSSI LSWKNGLFRV GPDSAAADPG PAAYRKGGPL TITDANLFLG RLVPEFFPKI 420
FGPNEDESLD LETTTLKFRE LTDVINKDLN SNLTMEEVAY GFIKVANECM ARPVRAITEA 480
KGHVVSQHRL VSFGGAGGQH AIAVADSLGI DTVLIHRYSS ILSAYGIFLA DVIEENQEPC 540
SFILGEPETI LKVKKRFLEL SKNSIKNLLS QSFSREDIVL ERYLNLRYEG TETSLMILQK 600
YDDQWNFREW FSEAHKKEFG FSFDDKRIII DDIRIRAIGK SGVRKEKTVD EQLIEISHFK 660
KADVSKDASF TQKAYFDNKW VDTAVFKIDD LPAGTIIEGP AILADGTQTN IILPNSQATI 720
LNSHIFIKIN QKAAKTLSKS GYELDIDPIL LSIFSHRFMD IALQMGTQLR KTSVSTNVKE 780
RLDFSCALFD SKGNLVANAP HVPVHLGSMS TCISAQAKLW EGKLKPGDVL ITNHPDIGGT 840
HLPDITVITP SFSSTGELIF YVASRAHHAD IGGILPGSVP PNSKELYEEG TAIYSELVVK 900
EGIFQEELIY KLFVEDPGKY PGCSGSRRFS DNISDLKAQV AANTKGIQLI GSLTKEYDLA 960
TILKYMAAIQ TNASESIKKM LAKMVEHFGT TKFSGEDRLD DGSLIKLQVI IRPEKEEYIF 1020
NFDGTSPQVY GNLNAPEAIT NSAILYCLRC LVGEDIPLNQ GCLKPLTIKI PAGSLLSPRS 1080
GAAVVGGNVL TSQRVTDVIL KTFNVMADSQ GDCNNFTFGT GGNSGNKTDK QIKGFGYYET 1140
ICGGSGAGAD SWRGSGWNGS DAVHTNMTNT RMTDTEVFER RYPVLLKEFS IRRGSGGKGK 1200
YTGGNGVVRD VQFRKAVTAS ILSERRVIGP HGIKGGQDGS RGENLWVRHS TGALINVGGK 1260
NTIYAQPGDR FIIKTPGGGG FGQYKD 1286 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0017168; F:5-oxoprolinase (ATP-hydrolyzing) activity; IDA:MGI.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0006749; P:glutathione metabolic process; IDA:MGI. 
Interpro
 IPR008040; Hydant_A_N.
 IPR002821; Hydantoinase_A.
 IPR003692; Hydantoinase_B. 
Pfam
 PF05378; Hydant_A_N
 PF01968; Hydantoinase_A
 PF02538; Hydantoinase_B 
SMART
  
PROSITE
  
PRINTS