Reviewed, UniProtKB/Swiss-Prot Q61YQ1 (DHP2_CAEBR)

Names and origin

Protein names

Recommended name:
    Dihydropyrimidinase 2
    EC=3.5.2.2

Gene names

Name:	dhp-2
ORF Names:	CBG03443

Organism

Caenorhabditis briggsae [Complete proteome]

Taxonomic identifier

6238 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	518 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	5,6-dihydrouracil + H2O = 3-ureidopropanoate.
Cofactor	Binds 2 zinc ions per subunit By similarity.
Subunit structure	Homotetramer By similarity.
Post-translational modification	Carbamylation allows a single lysine to coordinate two zinc ions By similarity.
Sequence similarities	Belongs to the DHOase family. Hydantoinase/dihydropyrimidinase subfamily.

Ontologies

Keywords
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Molecular function	dihydropyrimidinase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 518	518	Dihydropyrimidinase 2		PRO_0000165930
Sites
	Metal binding	59	1	Zinc 1 By similarity
	Metal binding	61	1	Zinc 1 By similarity
	Metal binding	152	1	Zinc 1; via carbamate group By similarity
	Metal binding	152	1	Zinc 2; via carbamate group By similarity
	Metal binding	185	1	Zinc 2 By similarity
	Metal binding	241	1	Zinc 2 By similarity
	Metal binding	319	1	Zinc 1 By similarity
	Binding site	157	1	Substrate By similarity
	Binding site	291	1	Substrate; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	340	1	Substrate; via carbonyl oxygen By similarity
Amino acid modifications
	Modified residue	152	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q61YQ1-1 [UniParc]. Last modified November 23, 2004. Version 1. Checksum: 1AD30CE4492892AD	FASTA	518	56,215
	10 20 30 40 50 60 MSLLIKNGTI VNDDAMFKSD VLVHDGKIVE IAPSIDPTPG LEVVDATDRF VIPGGIDPHT 70 80 90 100 110 120 HMQLPFMGEV AKDDFHRGTE AAVAGGTTMI IDFVIPTKGE SLLVAYDRWR GWADPKVVCD 130 140 150 160 170 180 YGLSMAITSW GQEIAKEMEM VTKADYGINS FKFFLAYAGV FMVRDEEFYQ GMLQCAKLRA 190 200 210 220 230 240 LARVHAENGA VIAERCEHLL SSGITGPEGH TQSRPEELEA EATFRACTMA SQANCPLYVV 250 260 270 280 290 300 HVMSKGAAAA IAHHRKKGAV VFGEPIAAGL ATDGSHYYNE DWLHAARYIM SPPLSRDPST 310 320 330 340 350 360 PNALMKLLAA GELHLTATDN CTFDCHQKSL GKDDFTKIPN GVNGVEDRMS VVWDKGVHAG 370 380 390 400 410 420 IIDPMKFVAV TSTMAAKIFN CYPRKGRIAV GSDADIVVWN ANATRTISKD THHHAIDFNI 430 440 450 460 470 480 FEGMQVHGVP ETTICRGRIV WADGQLRTVQ GAGRFVPLPP DSQIVFSAVD NRGKALEPVK 490 500 510 VERAPYVATT LEAPDANANI VVKTRSAVPP GGISSIQF

References

[1]

"The genome sequence of Caenorhabditis briggsae: a platform for comparative genomics." Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N., Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P., Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W., Hillier L.W. , Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A., Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., Durbin R.M., Waterston R.H. PLoS Biol. 1:166-192(2003) [PubMed: 14624247] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AF16.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CAAC02000451 Genomic DNA. Translation: CAP24340.1.
3D structure databases
ModBase	Search...
Organism-specific databases
WormBase	WBGene00026309. Cbr-dhp-2.
Phylogenomic databases
OMA	Q61YQ1. AAFSRCK.
Enzyme and pathway databases
BRENDA	3.5.2.2. 261794.
Family and domain databases
InterPro	IPR006680. Amidohydro_1. IPR011778. D-hydantoinase. [Graphical view]
Pfam	PF01979. Amidohydro_1. 1 hit. [Graphical view]
ProDom	PD000518. DHOase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR02033. D-hydantoinase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

DHP2_CAEBR

Accession

Primary (citable) accession number: Q61YQ1
Secondary accession number(s): A8WV29

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 4, 2005
Last sequence update:	November 23, 2004
Last modified:	June 16, 2009
This is version 26 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project