DHP1_CAEBR
ID DHP1_CAEBR Reviewed; 489 AA.
AC Q60Q85; A8Y179;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Dihydropyrimidinase 1;
DE EC=3.5.2.2 {ECO:0000250|UniProtKB:Q55DL0};
GN Name=dhp-1; ORFNames=CBG21922;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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; HE600952; CAP38640.1; -; Genomic_DNA.
DR RefSeq; XP_002629885.1; XM_002629839.1.
DR AlphaFoldDB; Q60Q85; -.
DR SMR; Q60Q85; -.
DR STRING; 6238.CBG21922; -.
DR EnsemblMetazoa; CBG21922.1; CBG21922.1; WBGene00040591.
DR GeneID; 8572900; -.
DR KEGG; cbr:CBG_21922; -.
DR CTD; 8572900; -.
DR WormBase; CBG21922; CBP05205; WBGene00040591; Cbr-dhp-1.
DR eggNOG; KOG2584; Eukaryota.
DR HOGENOM; CLU_015572_2_2_1; -.
DR InParanoid; Q60Q85; -.
DR OMA; QNRIYIK; -.
DR OrthoDB; 719800at2759; -.
DR Proteomes; UP000008549; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004157; F:dihydropyrimidinase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006208; P:pyrimidine nucleobase catabolic process; IBA:GO_Central.
DR CDD; cd01314; D-HYD; 1.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR030633; Dihydropyrimidinase.
DR InterPro; IPR011778; Hydantoinase/dihydroPyrase.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11647:SF65; PTHR11647:SF65; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; SSF51338; 2.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR02033; D-hydantoinase; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Nucleus; Reference proteome; Zinc.
FT CHAIN 1..489
FT /note="Dihydropyrimidinase 1"
FT /id="PRO_0000165928"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 156
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 156
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 161
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT MOD_RES 156
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
SQ SEQUENCE 489 AA; 53528 MW; 573FBF5DC04C545A CRC64;
MSPPLVIKNG TVVNEDGMFK ADVLVKNGII VEVSPKIIAL PEMEIIDATD RLVIPGGIDP
HTHMQMPYAG EVTKDDFLRG TQAAVAGGTT MIIDFCCPDH RNGESLMAGY ARWRSWADPK
VCCDYGLSVA ITQWRPETAD QMAVITSPEF GVNSFKFYMA YEGTLMVRDD EMYRAMQECA
KLRALARVHA ENGSVIKERE IDLLAKGVTG PEGHTQSRPE EIEAEATNRA CVLAAQANCP
VYIVHVMTKG AAAAISHHRA QGSIVFGEPI AAGLALDGSH YYNEDWLHAA RYVMSPPLSR
DPTTPELLMK LLAAGELHLT GTDNCTYDGC QKSLGKGNFT KIPNGINGVE DRMSVVWEKG
VHSGIIDPMR YVSITSATAA KIFNIYPKKG RIAVGSDADI VIFNPNATRT ISAETHHHNL
DFNIFEGIKC HGVAEITISR GRIVWANGQL QTVPGSGKFV PLLANSPFVF SSHEIREKKK
EPRIVERLE
