DHP2_CAEBR
ID DHP2_CAEBR Reviewed; 518 AA.
AC Q61YQ1; A8WV29;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Dihydropyrimidinase 2;
DE EC=3.5.2.2 {ECO:0000250|UniProtKB:Q55DL0};
GN Name=dhp-2; ORFNames=CBG03443;
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 -!- 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; HE601244; CAP24340.1; -; Genomic_DNA.
DR RefSeq; XP_002633756.1; XM_002633710.1.
DR AlphaFoldDB; Q61YQ1; -.
DR SMR; Q61YQ1; -.
DR STRING; 6238.CBG03443; -.
DR EnsemblMetazoa; CBG03443.1; CBG03443.1; WBGene00026309.
DR GeneID; 8575752; -.
DR KEGG; cbr:CBG_03443; -.
DR CTD; 8575752; -.
DR WormBase; CBG03443; CBP00929; WBGene00026309; Cbr-dhp-2.
DR eggNOG; KOG2584; Eukaryota.
DR HOGENOM; CLU_015572_2_2_1; -.
DR InParanoid; Q61YQ1; -.
DR OMA; SAETHHM; -.
DR OrthoDB; 719800at2759; -.
DR Proteomes; UP000008549; Chromosome IV.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblMetazoa.
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; Reference proteome; Zinc.
FT CHAIN 1..518
FT /note="Dihydropyrimidinase 2"
FT /id="PRO_0000165930"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
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 152
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 152
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 157
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 291
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 340
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT MOD_RES 152
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
SQ SEQUENCE 518 AA; 56215 MW; 1AD30CE4492892AD CRC64;
MSLLIKNGTI VNDDAMFKSD VLVHDGKIVE IAPSIDPTPG LEVVDATDRF VIPGGIDPHT
HMQLPFMGEV AKDDFHRGTE AAVAGGTTMI IDFVIPTKGE SLLVAYDRWR GWADPKVVCD
YGLSMAITSW GQEIAKEMEM VTKADYGINS FKFFLAYAGV FMVRDEEFYQ GMLQCAKLRA
LARVHAENGA VIAERCEHLL SSGITGPEGH TQSRPEELEA EATFRACTMA SQANCPLYVV
HVMSKGAAAA IAHHRKKGAV VFGEPIAAGL ATDGSHYYNE DWLHAARYIM SPPLSRDPST
PNALMKLLAA GELHLTATDN CTFDCHQKSL GKDDFTKIPN GVNGVEDRMS VVWDKGVHAG
IIDPMKFVAV TSTMAAKIFN CYPRKGRIAV GSDADIVVWN ANATRTISKD THHHAIDFNI
FEGMQVHGVP ETTICRGRIV WADGQLRTVQ GAGRFVPLPP DSQIVFSAVD NRGKALEPVK
VERAPYVATT LEAPDANANI VVKTRSAVPP GGISSIQF
