DHP1_CAEEL
ID DHP1_CAEEL Reviewed; 489 AA.
AC Q21773; Q9BPU2;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Dihydropyrimidinase 1;
DE EC=3.5.2.2 {ECO:0000269|PubMed:11167013};
DE AltName: Full=CeCRMP/DHP-1;
DE AltName: Full=UlipB;
GN Name=dhp-1; ORFNames=R06C7.3;
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, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11167013}.
CC -!- TISSUE SPECIFICITY: In L1-L2 larvae, expressed in body hypodermal
CC cells, hemidesmosomes and in a neuronal cell between the pharynx and
CC ring neuropil. In adults, expression is seen in body hypodermal cells
CC and pharynx. {ECO:0000269|PubMed:11167013}.
CC -!- DEVELOPMENTAL STAGE: Expressed in dorsal regions of embryos at late
CC gastrula stage, transiently expressed in the developmental process of
CC 3-fold embryo to L1-L2 larval stage. {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}.
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DR EMBL; AB040992; BAB21560.1; -; mRNA.
DR EMBL; Z71266; CAD24483.1; -; Genomic_DNA.
DR PIR; T23968; T23968.
DR RefSeq; NP_001021583.1; NM_001026412.2.
DR AlphaFoldDB; Q21773; -.
DR SMR; Q21773; -.
DR STRING; 6239.R06C7.3.1; -.
DR MEROPS; M38.973; -.
DR EPD; Q21773; -.
DR PaxDb; Q21773; -.
DR PeptideAtlas; Q21773; -.
DR EnsemblMetazoa; R06C7.3.1; R06C7.3.1; WBGene00000963.
DR EnsemblMetazoa; R06C7.3.2; R06C7.3.2; WBGene00000963.
DR GeneID; 172464; -.
DR KEGG; cel:CELE_R06C7.3; -.
DR UCSC; R06C7.3.3; c. elegans.
DR CTD; 172464; -.
DR WormBase; R06C7.3; CE30293; WBGene00000963; dhp-1.
DR eggNOG; KOG2584; Eukaryota.
DR GeneTree; ENSGT01030000234527; -.
DR HOGENOM; CLU_015572_2_2_1; -.
DR InParanoid; Q21773; -.
DR OMA; QNRIYIK; -.
DR OrthoDB; 719800at2759; -.
DR PhylomeDB; Q21773; -.
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 PRO; PR:Q21773; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000963; Expressed in larva and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; 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; Nucleus; Reference proteome; Zinc.
FT CHAIN 1..489
FT /note="Dihydropyrimidinase 1"
FT /id="PRO_0000165929"
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; 53798 MW; 314590019ACF2975 CRC64;
MSPPLVIKNG TVVNEDGMFK ADVLVRNGII VEVSPNITAL PDTEVIDATD RLVIPGGIDP
HTHMQMPYMG EVTKDDFLKG TEAAVAGGTT MIIDFCCPDH RNGESLIAGY NRWRSWADPK
VCCDYGLSVA ITMWRPETAE QMAIITSPEF GVNSFKFYMA YENTLMVRDD ELFRGMQECA
KLRALARVHC ENGSVIKEKE IDLLAKGVTG PEGHTQSRPE EIEAEATNRA CVLAAQANCP
VYIVHVMTKG AASAISHHRA QGSIVFGEPI AAGLALDGSH YYNEDWLHAA RYVMSPPLSR
DPTTPELLMK LLAAGELHLT GTDNCTYDCR QKSLGKGNFT KIPNGINGVE DRMSVVWEKG
VHSGIIDPMR YVSITSSTAA KIFNIYPRKG RIAVGSDADI VIFNPNATRT ISKDTHHHNL
DFNIFEGINC HGVAEVTISR GRIVWAHGKL QTVPGSGKFI PLLANSPFVF STHEKREQKI
QPRIVERLE
