Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A6NGE7 (URAD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase

Short name=OHCU decarboxylase
EC=4.1.1.97
Alternative name(s):
Parahox neighbor
Ureidoimidazoline (2-oxo-4-hydroxy-4-carboxy-5-) decarboxylase
Gene names
Name:URAD
Synonyms:PRHOXNB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length173 AA.
Sequence statusComplete.
Protein existenceUncertain

General annotation (Comments)

Function

Catalyzes the stereoselective decarboxylation of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) to (S)-allantoin Potential.

Catalytic activity

5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate = (S)-allantoin + CO2.

Pathway

Purine metabolism; urate degradation; (S)-allantoin from urate: step 3/3.

Subcellular location

Peroxisome Potential.

Tissue specificity

Apparently not expressed. Ref.2

Sequence similarities

Belongs to the OHCU decarboxylase family.

Caution

Could be the product of a pseudogene. In primates the genes coding for the enzymes for the degradation of uric acid were inactivated and converted to pseudogenes (Ref.2).

Ontologies

Keywords
   Biological processPurine metabolism
   Cellular componentPeroxisome
   Coding sequence diversityPolymorphism
   Molecular functionDecarboxylase
Lyase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processallantoin biosynthetic process

Inferred from electronic annotation. Source: InterPro

purine nucleobase metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

urate catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncarboxy-lyase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 173173Putative 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase
PRO_0000315240

Regions

Region84 – 885Substrate binding Potential
Region119 – 1235Substrate binding Potential
Motif171 – 1733Microbody targeting signal Potential

Sites

Active site671Proton donor Potential
Binding site681Substrate; via carbonyl oxygen Potential

Natural variations

Natural variant571Q → P.
Corresponds to variant rs3897926 [ dbSNP | Ensembl ].
VAR_053987

Sequences

Sequence LengthMass (Da)Tools
A6NGE7 [UniParc].

Last modified January 15, 2008. Version 2.
Checksum: 521C44BEF163077C

FASTA17319,130
        10         20         30         40         50         60 
MDIEKVNSMD LGEFVDVFGN ATERCPLIAA AVWSQRPFSD LEDLEKHFFA FIDALAQSGQ 

        70         80         90        100        110        120 
EGILRCHPDL AGSELQRGTL TAESQREQSG AGLRSLGADE RLRLAELNAQ YRARFGFPFV 

       130        140        150        160        170 
LAARFSDRTA VPRELARRLL CPSAQELRTA LGEVKKIGSL RLADLLRADP AKL 

« Hide

References

« Hide 'large scale' references
[1]"The DNA sequence and analysis of human chromosome 13."
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Completing the uric acid degradation pathway through phylogenetic comparison of whole genomes."
Ramazzina I., Folli C., Secchi A., Berni R., Percudani R.
Nat. Chem. Biol. 2:144-148(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: LACK OF TISSUE SPECIFICITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL591024 Genomic DNA. No translation available.
RefSeqNP_001099047.1. NM_001105577.1.
UniGeneHs.705356.

3D structure databases

ProteinModelPortalA6NGE7.
SMRA6NGE7. Positions 2-162.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000333490.

PTM databases

PhosphoSiteA6NGE7.

Proteomic databases

PaxDbA6NGE7.
PRIDEA6NGE7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000332715; ENSP00000333490; ENSG00000183463.
GeneID646625.
KEGGhsa:646625.
UCSCuc010aan.1. human.

Organism-specific databases

CTD646625.
GeneCardsGC13M028555.
HGNCHGNC:17785. URAD.
HPAHPA038972.
neXtProtNX_A6NGE7.
PharmGKBPA142671135.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3195.
HOGENOMHOG000251764.
HOVERGENHBG108651.
InParanoidA6NGE7.
KOK13485.
OMAKEGILRC.
OrthoDBEOG7GFB6D.
PhylomeDBA6NGE7.
TreeFamTF323276.

Enzyme and pathway databases

UniPathwayUPA00394; UER00652.

Gene expression databases

CleanExHS_PRHOXNB.
GenevestigatorA6NGE7.

Family and domain databases

Gene3D1.10.3330.10. 1 hit.
InterProIPR018020. OHCU_decarboxylase.
IPR017580. OHCU_decarboxylase-1.
[Graphical view]
PfamPF09349. OHCU_decarbox. 1 hit.
[Graphical view]
TIGRFAMsTIGR03164. UHCUDC. 1 hit.
ProtoNetSearch...

Other

NextBio119115.
PROA6NGE7.

Entry information

Entry nameURAD_HUMAN
AccessionPrimary (citable) accession number: A6NGE7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: April 16, 2014
This is version 57 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM