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Q9I676 (HYDA_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
D-hydantoinase/dihydropyrimidinase
Short name=DHPase
EC=3.5.2.2
Gene names
Name:dht
Ordered Locus Names:PA0441
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length479 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity.

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
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processpyrimidine base catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: InterPro

   Molecular functiondihydropyrimidinase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 479479D-hydantoinase/dihydropyrimidinase
PRO_0000287767

Sites

Metal binding591Zinc 1 By similarity
Metal binding611Zinc 1 By similarity
Metal binding1501Zinc 1; via carbamate group By similarity
Metal binding1501Zinc 2; via carbamate group By similarity
Metal binding1831Zinc 2 By similarity
Metal binding2391Zinc 2 By similarity
Metal binding3161Zinc 1 By similarity
Binding site1551Substrate By similarity
Binding site2891Substrate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3371Substrate; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue1501N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9I676 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 46582DFE22E38925

FASTA47952,212
        10         20         30         40         50         60 
MSLLIRGATV VTHEESYRAD VLCANGLIQA IGENLETPSG CDVLDGGGQY LMPGGIDPHT 

        70         80         90        100        110        120 
HMQLPFMGTV ASEDFFSGTA AGLAGGTTSI IDFVIPNPRQ SLLEAFHTWR GWAQKSAADY 

       130        140        150        160        170        180 
GFHVAITWWS DEVAREMGEL VAQHGVNSFK HFMAYKNAIM AADDTLVASF ERCLELGAVP 

       190        200        210        220        230        240 
TVHAENGELV FHLQQKLLAQ GLTGPEAHPL SRPPQVEGEA ASRAIRIAET LGTPLYLVHI 

       250        260        270        280        290        300 
SSREALDEIA YARAKGQPVY GEVLAGHLLL DDSVYRHPDW ATAAGYVMSP PFRPVEHQEA 

       310        320        330        340        350        360 
LWRGLQSGNL HTTATDHCCF CAEQKAMGRD DFSKIPNGTA GIEDRMALLW DAGVNSGRLS 

       370        380        390        400        410        420 
MHEFVALTST NTAKIFNLFP RKGAIRVGAD ADLVLWDPQG SRTLSAATHH QRVDFNIFEG 

       430        440        450        460        470 
RTVRGIPSHT ISQGKLLWAA GDLRAEPGAG RYVERPAYPS VYEVLGRRAE RQRPVAVER

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE004091 Genomic DNA. Translation: AAG03830.1.
PIRH83590.
RefSeqNP_249132.1. NC_002516.2.

3D structure databases

HSSPHSSP built from PDB template 2FTW based on UniProtKB Q86LT2.
ProteinModelPortalQ9I676.
SMRQ9I676. Positions 2-471.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID882285.
GenomeReviewsGene locus PA0441 in contig AE004091_GR.
KEGGpae:PA0441.
PATRIC19835126. VBIPseAer58763_0464.

Organism-specific databases

PseudoCAPPA0441.

Phylogenomic databases

HOGENOMHBG724623.
OMAKSASDYG.
ProtClustDBPRK08323.

Enzyme and pathway databases

BioCycPAER208964:PA0441-MONOMER.
BRENDA3.5.2.2. 5087.

Family and domain databases

InterProIPR006680. Amidohydro_1.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
KOK01464.
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMSSF51338. Metalo_hydrolase. 1 hit.
TIGRFAMsTIGR02033. D-hydantoinase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHYDA_PSEAE
AccessionPrimary (citable) accession number: Q9I676
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: March 1, 2001
Last modified: January 25, 2012
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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