OPLA_RAT
ID OPLA_RAT Reviewed; 1288 AA.
AC P97608; Q5U3Z8;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=5-oxoprolinase;
DE EC=3.5.2.9;
DE AltName: Full=5-oxo-L-prolinase;
DE Short=5-OPase;
DE AltName: Full=Pyroglutamase;
GN Name=Oplah;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX PubMed=8943290; DOI=10.1074/jbc.271.50.32293;
RA Ye G.-J., Breslow E., Meister A.;
RT "The amino acid sequence of rat kidney 5-oxo-L-prolinase determined by cDNA
RT cloning.";
RL J. Biol. Chem. 271:32293-32300(1996).
RN [2]
RP ERRATUM OF PUBMED:8943290.
RA Ye G.-J., Breslow E., Meister A.;
RL J. Biol. Chem. 272:4646-4646(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1265, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(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 -!- 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 -!- SUBUNIT: Homodimer.
CC -!- TISSUE SPECIFICITY: Well expressed in testis, kidney and liver.
CC -!- SIMILARITY: Belongs to the oxoprolinase family. {ECO:0000305}.
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DR EMBL; U70825; AAC52955.1; -; mRNA.
DR EMBL; BC085330; AAH85330.1; -; mRNA.
DR PIR; T42756; T42756.
DR RefSeq; NP_446356.1; NM_053904.1.
DR RefSeq; XP_006241836.1; XM_006241774.3.
DR RefSeq; XP_006241837.1; XM_006241775.3.
DR RefSeq; XP_017450065.1; XM_017594576.1.
DR RefSeq; XP_017450066.1; XM_017594577.1.
DR AlphaFoldDB; P97608; -.
DR SMR; P97608; -.
DR IntAct; P97608; 2.
DR STRING; 10116.ENSRNOP00000016424; -.
DR iPTMnet; P97608; -.
DR PhosphoSitePlus; P97608; -.
DR jPOST; P97608; -.
DR PaxDb; P97608; -.
DR PRIDE; P97608; -.
DR Ensembl; ENSRNOT00000077314; ENSRNOP00000074664; ENSRNOG00000011781.
DR GeneID; 116684; -.
DR KEGG; rno:116684; -.
DR CTD; 26873; -.
DR RGD; 620956; Oplah.
DR eggNOG; KOG1939; Eukaryota.
DR GeneTree; ENSGT00390000013463; -.
DR InParanoid; P97608; -.
DR OMA; TDCNVML; -.
DR OrthoDB; 62698at2759; -.
DR PhylomeDB; P97608; -.
DR TreeFam; TF300520; -.
DR BioCyc; MetaCyc:MON-10109; -.
DR BRENDA; 3.5.2.9; 5301.
DR Reactome; R-RNO-174403; Glutathione synthesis and recycling.
DR PRO; PR:P97608; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000011781; Expressed in adult mammalian kidney and 19 other tissues.
DR Genevisible; P97608; RN.
DR GO; GO:0017168; F:5-oxoprolinase (ATP-hydrolyzing) activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
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; Direct protein sequencing; Hydrolase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1288
FT /note="5-oxoprolinase"
FT /id="PRO_0000208579"
FT REGION 1248..1270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1255..1270
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 44
FT /note="A -> P (in Ref. 1; AAC52955)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1288 AA; 137720 MW; 23DA4809D60D5730 CRC64;
MGSPEGRFHF AIDRGGTFTD VFAQCPGGHV RVLKLLSEDP ANYADAPTEG IRRILEQEEG
VLLPRGRPLD TSRIASIRMG TTVATNALLE RQGERVALLV TRGFRDLLHI GTQARPDLFD
LAVPMPEVLY EEVLEVDERV VLYRGEPGAG SPVKGRTGDL LEIQQPVDLE ALRGKLEGLL
SRGIHSLAVV LMHSYTWAQH EQQVGTLARE LGFTHVSLSS EVMPMVRIVP RGHTACADAY
LTPTIQRYVQ GFRRGFQGQL KNVQVLFMRS DGGLAPMDAF SGSRAVLSGP AGGVVGYSAT
TYHLEGGQPV IGFDMGGTST DVSRYAGEFE HVFEASTAGV TLQAPQLDIN TVAAGGGSRL
FFRSGLFVVG PESAGAHPGP ACYRKGGPVT VTDANLVLGR LLPASFPCIF GPGEDQPLSP
EASRKALEAV AMEVNSFLTN GPCPASQLSL EEVAMGFVRV ANEAMCRPIR ALTQARGHDP
SAHVLACFGG AGGQHACAIA RALGMDTVHI HRHSGLLSAL GLALADVVHE AQEPCSLSYT
PETFAQLDQR LSRLEEQCVD ALQVQGFPRS QISTESFLHL RYQGTDCALM VSAHQHPATA
CSPRAGDFGA AFVERYMREF GFIIPERPVV VDDVRVRGTG RSGLQLEDTP KIQTGPPHVE
KVTQCYFEGG YQETPVYLLG ELGYGHQLQG PCLIIDNNST ILVEPGCQAE VTDTGDIRIS
VGAEGPSMAD TRLDPIQLSI FSHRFMSIAE QMGRILQRTA ISTNIKERLD FSCALFGPDG
GLVSNAPHIP VHLGAMQETV QFQIQHLGAD LHPGDVLLSN HPSAGGSHLP DLTVITPVFW
PGQTRPVFYV ASRGHHADIG GITPGSMPPH STTLQQEGAV FLSFKLVQGG VFQEEAVTEA
LRAPGKISGC SGTRNLHDNL SDLRAQVAAN QKGIQLVGEL IGQYGLDVVQ AYMGHIQANA
ELAVRDMLRA FGTSRQARGL PLEVSAEDHM DDGSPICLRV QINLSQGSAV FDFTGSGSEV
FGNLNAPRAI TLSALIYCLR CLVGRDIPLN QGCLAPVRVI IPKGSILDPS PEAAVVGGNV
LTSQRVVDVI LGAFGACSAS QGCMNNVTLG NARMGYYETV AGGAGAGPGW HGRSGVHSHM
TNTRITDPEI LESRYPVILR RFELRPGSGG RGRFRGGDGV VRELVFREEA LLSVLTERRA
FQPYGLHGGE PGARGLNLLI RKDGRTVNLG GKTSVTVYPG DVFCLHTPGG GGYGDPEDPA
PPPGSPPLFP AFPERGSVFE YRRAQEAV
