DPYS_RAT
ID DPYS_RAT Reviewed; 519 AA.
AC Q63150; Q642F0;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Dihydropyrimidinase;
DE Short=DHP;
DE Short=DHPase;
DE EC=3.5.2.2 {ECO:0000250|UniProtKB:Q55DL0};
DE AltName: Full=Dihydropyrimidine amidohydrolase;
DE AltName: Full=Hydantoinase;
GN Name=Dpys;
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 TISSUE=Liver;
RX PubMed=8679696; DOI=10.1016/0167-4781(96)00056-5;
RA Matsuda K., Sakata S., Kaneko M., Hamajima N., Nonaka M., Sasaki M.,
RA Tamaki N.;
RT "Molecular cloning and sequencing of a cDNA encoding dihydropyrimidinase
RT from the rat liver.";
RL Biochim. Biophys. Acta 1307:140-144(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway; TISSUE=Kidney;
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).
CC -!- FUNCTION: Catalyzes the second step of the reductive pyrimidine
CC degradation, the reversible hydrolytic ring opening of
CC dihydropyrimidines. Can catalyze the ring opening of 5,6-dihydrouracil
CC to N-carbamyl-alanine and of 5,6-dihydrothymine to N-carbamyl-amino
CC isobutyrate.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouracil + H2O = 3-(carbamoylamino)propanoate + H(+);
CC Xref=Rhea:RHEA:16121, ChEBI:CHEBI:11892, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15901; EC=3.5.2.2;
CC Evidence={ECO:0000250|UniProtKB:Q55DL0};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q55DL0};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q55DL0};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q55DL0}.
CC -!- PTM: Carboxylation allows a single lysine to coordinate two zinc ions.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Hydantoinase/dihydropyrimidinase family. {ECO:0000305}.
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DR EMBL; D63704; BAA09833.1; -; mRNA.
DR EMBL; BC081768; AAH81768.1; -; mRNA.
DR PIR; S70581; S70581.
DR RefSeq; NP_113893.1; NM_031705.1.
DR AlphaFoldDB; Q63150; -.
DR SMR; Q63150; -.
DR STRING; 10116.ENSRNOP00000006004; -.
DR MEROPS; M38.973; -.
DR iPTMnet; Q63150; -.
DR PhosphoSitePlus; Q63150; -.
DR jPOST; Q63150; -.
DR PaxDb; Q63150; -.
DR PRIDE; Q63150; -.
DR Ensembl; ENSRNOT00000006004; ENSRNOP00000006004; ENSRNOG00000004298.
DR GeneID; 65135; -.
DR KEGG; rno:65135; -.
DR UCSC; RGD:68376; rat.
DR CTD; 1807; -.
DR RGD; 68376; Dpys.
DR eggNOG; KOG2584; Eukaryota.
DR GeneTree; ENSGT01030000234527; -.
DR HOGENOM; CLU_015572_2_2_1; -.
DR InParanoid; Q63150; -.
DR OMA; SAETHHM; -.
DR OrthoDB; 719800at2759; -.
DR PhylomeDB; Q63150; -.
DR TreeFam; TF314706; -.
DR BioCyc; MetaCyc:MON-15404; -.
DR Reactome; R-RNO-73621; Pyrimidine catabolism.
DR SABIO-RK; Q63150; -.
DR PRO; PR:Q63150; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000004298; Expressed in liver and 4 other tissues.
DR Genevisible; Q63150; RN.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0016597; F:amino acid binding; IDA:RGD.
DR GO; GO:0004157; F:dihydropyrimidinase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0051219; F:phosphoprotein binding; ISO:RGD.
DR GO; GO:0002059; F:thymine binding; IDA:RGD.
DR GO; GO:0002058; F:uracil binding; IDA:RGD.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0019482; P:beta-alanine metabolic process; IDA:RGD.
DR GO; GO:0006248; P:CMP catabolic process; ISO:RGD.
DR GO; GO:0006249; P:dCMP catabolic process; ISO:RGD.
DR GO; GO:0046079; P:dUMP catabolic process; ISO:RGD.
DR GO; GO:0006208; P:pyrimidine nucleobase catabolic process; ISO:RGD.
DR GO; GO:0006210; P:thymine catabolic process; IDA:UniProtKB.
DR GO; GO:0046050; P:UMP catabolic process; ISO:RGD.
DR GO; GO:0006212; P:uracil catabolic process; IDA:UniProtKB.
DR GO; GO:0019860; P:uracil metabolic process; IDA:RGD.
DR CDD; cd01314; D-HYD; 1.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011778; Hydantoinase/dihydroPyrase.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; SSF51338; 2.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR02033; D-hydantoinase; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Metal-binding; Phosphoprotein;
KW Reference proteome; Zinc.
FT CHAIN 1..519
FT /note="Dihydropyrimidinase"
FT /id="PRO_0000165908"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /note="via carbamate group"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 347
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14117"
FT MOD_RES 159
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT MOD_RES 256
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQF5"
FT MOD_RES 510
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQF6"
FT CONFLICT 403
FT /note="I -> M (in Ref. 1; BAA09833)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 519 AA; 56815 MW; 9A4CEB468303B990 CRC64;
MAPQERLLIR GGRVVNDDFS QVADVLVEDG VVRALGRDLL PPGDTSRGLR ILDAAGKLVL
PGGIDTHTHM QFPFMGSQSV DDFHQGTKAA LAGGTTMIID FAIPQKGSSL IEAFETWRNW
ADPKVCCDYS LHVAVTWWSD KVKEEMKTLA QDKGVNSFKM FMAYKDLYMV QDQQMYAAFS
QCKEIGAIAQ VHAENGDLIA EGAKKMLALG ITGPEGHELC RPEAVEAEAT LRAITIASAV
NCPLYIVHVM SKSAAKVIAD AKREGKVVYG EPIAAGLGTD GTQYWNKEWR HAAHHVMGPP
LRPDPSTPGF LMNLLANGDL TTTGSDNCTF NTCQKALGKD DFTKIPNGVN GVEDRMSVIW
EKGVHSGKMD ENRFVAVTST NAAKIFNLYP KKGRIAVGSD ADIVIWDPEA TRTISAKTHH
QAVNFNIFEG MVCHGVPLVT ISRGRVVYEA GVFDVTAGHG KFIPRQPFAE FIYKRVKQRD
QTCTPIPVKR APYKGEVITL KPRETKEDDT AGTRMQGHS
