Q59699 (HYDA_PSEPU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
D-hydantoinase/dihydropyrimidinase
Short name=DHPase
EC=3.5.2.2

Gene names

Name:

dht

Organism

Pseudomonas putida (Arthrobacter siderocapsulatus)

Taxonomic identifier

303 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	495 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the hydrolysis of dihydropyrimidines and of the structurally related DL-5-mono-substituted hydantoins, to produce N-carbamoyl-D-amino acids.
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.
Sequence caution	The sequence AAA21752.1 differs from that shown. Reason: Frameshift at positions 144, 184, 200, 308, 338, 389, 426 and 444.

Ontologies

Keywords
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	pyrimidine base catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	dihydropyrimidinase activity Inferred from electronic annotation. Source: EC metal 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 – 495	495	D-hydantoinase/dihydropyrimidinase		PRO_0000165935
Sites
	Metal binding	59	1	Zinc 1 By similarity
	Metal binding	61	1	Zinc 1 By similarity
	Metal binding	150	1	Zinc 1; via carbamate group By similarity
	Metal binding	150	1	Zinc 2; via carbamate group By similarity
	Metal binding	183	1	Zinc 2 By similarity
	Metal binding	239	1	Zinc 2 By similarity
	Metal binding	316	1	Zinc 1 By similarity
	Binding site	155	1	Substrate By similarity
	Binding site	289	1	Substrate; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	337	1	Substrate; via carbonyl oxygen By similarity
Amino acid modifications
	Modified residue	150	1	N6-carboxylysine By similarity
Experimental info
	Sequence conflict	304	1	G → R in AAA21752. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q59699 [UniParc]. Last modified July 15, 1998. Version 2. Checksum: FBC65F6DFA62F972	FASTA	495	53,507
	10 20 30 40 50 60 MSLLIRGATV VTHEESYPAD VLCVDGLIRA IGPNLEPPTD CEILDGSGQY LMPGGIDPHT 70 80 90 100 110 120 HMQLPFMGTV ASEDFFSGTA AGLAGGTTSI IDFVIPNPQQ SLLEAFHTWR GWAQKSASDY 130 140 150 160 170 180 GFHVAITWWS EQVAEEMGEL VAKHGVNSFK HFMAYKNAIM AADDTLVASF ERCLQLGAVP 190 200 210 220 230 240 TVHAENGELV YHLQKKLLAQ GMTGPEAHPL SRPSQVEGEA ASRAIRIAET IGTPLYVVHI 250 260 270 280 290 300 SSREALDEIT YARAKGQPVY GEVLPGHLLL DDSVYRDPDW ATAAGYVMSP PFRPREHQEA 310 320 330 340 350 360 LWRGLQSGNL HTTATDHCCF CAEQKAMGRD DFSRIPNGTA GIEDRMAVLW DAGVNSGRLS 370 380 390 400 410 420 MHEFVALTST NTAKIFNLFP RKGAIRVGAD ADLVLWDPQG TRTLSAQTHH QRVDFNIFEG 430 440 450 460 470 480 RTVRGVPSHT ISQGKVLWAD GDLRRRGRGG AVCGTAGVSV GVRGAGATRR TAAPDARSAL 490 RPLGLLRSPS PASQI

References

[1]	"Identification of the open reading frame for the Pseudomonas putida D-hydantoinase gene and expression of the gene in Escherichia coli." Chien H.R., Jih Y.L., Yang W.Y., Hsu W.H. Biochim. Biophys. Acta 1395:68-77(1998) [PubMed: 9434154] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: CCRC 12857.
[2]	"Cloning, sequencing, and expression in Escherichia coli of the D-hydantoinase gene from Pseudomonas putida and distribution of homologous genes in other microorganisms." Lapointe G., Viau S., Leblanc D., Robert N., Morin A. Appl. Environ. Microbiol. 60:888-895(1994) [PubMed: 8161181] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DSM 84.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U84197 Genomic DNA. Translation: AAC00209.1. L24157 Genomic DNA. Translation: AAA21752.1. Frameshift.
3D structure databases
ProteinModelPortal	Q59699.
SMR	Q59699. Positions 2-444.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BRENDA	3.5.2.2. 5163.
Family and domain databases
InterPro	IPR006680. Amidohydro_1. IPR011778. Hydantoinase/dihydroPyrase. IPR011059. Metal-dep_hydrolase_composite. [Graphical view]
Pfam	PF01979. Amidohydro_1. 1 hit. [Graphical view]
SUPFAM	SSF51338. Metalo_hydrolase. 1 hit.
TIGRFAMs	TIGR02033. D-hydantoinase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HYDA_PSEPU

Accession

Primary (citable) accession number: Q59699
Secondary accession number(s): O54406

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 15, 1998
Last modified:	June 28, 2011
This is version 60 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program