DHP2_CAEEL
ID DHP2_CAEEL Reviewed; 520 AA.
AC Q18677;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Dihydropyrimidinase 2;
DE EC=3.5.2.2 {ECO:0000269|PubMed:11167013};
DE AltName: Full=CeCRMP/DHP-2;
DE AltName: Full=UlipA;
GN Name=dhp-2; ORFNames=C47E12.8;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Bristol N2;
RX PubMed=11167013; DOI=10.1016/s0378-1119(00)00494-7;
RA Takemoto T., Sasaki Y., Hamajima N., Goshima Y., Nonaka M., Kimura H.;
RT "Cloning and characterization of the Caenorhabditis elegans CeCRMP/DHP-1
RT and -2; common ancestors of CRMP and dihydropyrimidinase?";
RL Gene 261:259-267(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP IDENTIFICATION.
RX PubMed=9652388; DOI=10.1046/j.1432-1327.1998.2540014.x;
RA Byk T., Ozon S., Sobel A.;
RT "The Ulip family phosphoproteins -- common and specific properties.";
RL Eur. J. Biochem. 254:14-24(1998).
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:0000269|PubMed:11167013};
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 -!- TISSUE SPECIFICITY: Body wall muscles. {ECO:0000269|PubMed:11167013}.
CC -!- DEVELOPMENTAL STAGE: All developmental stages.
CC {ECO:0000269|PubMed:11167013}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB040993; BAB21561.1; -; mRNA.
DR EMBL; Z68882; CAA93104.1; -; Genomic_DNA.
DR PIR; T20007; T20007.
DR RefSeq; NP_501797.1; NM_069396.6.
DR AlphaFoldDB; Q18677; -.
DR SMR; Q18677; -.
DR BioGRID; 42955; 3.
DR STRING; 6239.C47E12.8; -.
DR iPTMnet; Q18677; -.
DR EPD; Q18677; -.
DR PaxDb; Q18677; -.
DR PeptideAtlas; Q18677; -.
DR EnsemblMetazoa; C47E12.8.1; C47E12.8.1; WBGene00000964.
DR GeneID; 177852; -.
DR KEGG; cel:CELE_C47E12.8; -.
DR UCSC; C47E12.8; c. elegans.
DR CTD; 177852; -.
DR WormBase; C47E12.8; CE05452; WBGene00000964; dhp-2.
DR eggNOG; KOG2584; Eukaryota.
DR GeneTree; ENSGT01030000234527; -.
DR HOGENOM; CLU_015572_2_2_1; -.
DR InParanoid; Q18677; -.
DR OMA; SAETHHM; -.
DR OrthoDB; 719800at2759; -.
DR PhylomeDB; Q18677; -.
DR BRENDA; 3.5.2.2; 1045.
DR Reactome; R-CEL-399956; CRMPs in Sema3A signaling.
DR Reactome; R-CEL-437239; Recycling pathway of L1.
DR Reactome; R-CEL-73621; Pyrimidine catabolism.
DR PRO; PR:Q18677; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00000964; Expressed in larva and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0004157; F:dihydropyrimidinase activity; ISS:WormBase.
DR GO; GO:0016812; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046113; P:nucleobase catabolic process; ISS:WormBase.
DR GO; GO:0006208; P:pyrimidine nucleobase catabolic process; IDA:WormBase.
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 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..520
FT /note="Dihydropyrimidinase 2"
FT /id="PRO_0000165931"
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 520 AA; 56293 MW; 4912F1635D82ECFB CRC64;
MSLLIKNGTI VNDDAIFKSD VLVLDGRIVE IAPSIQPTPG LEVVDATDRL VIPGGIDPHT
HMQLPFMGEI AKDDFHRGTE AAVAGGTTMI IDFVIPTKGE SLLVAYDRWR GWADPKVVCD
YGLSMAITSW GPEIAKEMEI VTGAEYGINS FKFFLAYAGV FMVRDEEFYQ GMIQCAKLRA
LARVHAENGS VIAERCEHLL SSGITGPEGH TQSRPEELEA EATFRACTMA SQANCPLYVV
HVMSKGAAAA IAHHRKKGAV VFGEPIAAGL ATDGSHYYNE DWLHAARYVM SPPLSRDPST
PSALMKLLAA GELHLTATDN CTFDCQQKSL GKDDFTKIPN GVNGVEDRMS VVWDKGVHAG
IIDPMRFVAV TSTMAAKIFN CYPQKGRIAV GSDADIVIWN ANATRTISKD THHHAIDFNI
FEGMQVHGVP EITISRGRTV WANGQLKTVQ GSGQFIPLAP DSQIVFSAVD NRKKAMEPVK
IDRIPYEPSA LQTPDANANI VVKAPVRAAI PPGGASSIQF
