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Protein

Putative 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase

Gene

URAD

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein uncertaini

Functioni

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

Catalytic activityi

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

Pathway: urate degradation

This protein is involved in step 3 of the subpathway that synthesizes (S)-allantoin from urate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. no protein annotated in this organism
  3. Putative 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase (URAD)
This subpathway is part of the pathway urate degradation, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-allantoin from urate, the pathway urate degradation and in Purine metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei67 – 671Proton donorSequence Analysis
Binding sitei68 – 681Substrate; via carbonyl oxygenSequence Analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Purine metabolism

Enzyme and pathway databases

UniPathwayiUPA00394; UER00652.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase (EC:4.1.1.97)
Short name:
OHCU decarboxylase
Alternative name(s):
Parahox neighbor
Ureidoimidazoline (2-oxo-4-hydroxy-4-carboxy-5-) decarboxylase
Gene namesi
Name:URAD
Synonyms:PRHOXNB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:17785. URAD.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671135.

Polymorphism and mutation databases

BioMutaiURAD.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 173173Putative 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylasePRO_0000315240Add
BLAST

Proteomic databases

PaxDbiA6NGE7.
PRIDEiA6NGE7.

PTM databases

PhosphoSiteiA6NGE7.

Expressioni

Tissue specificityi

Apparently not expressed.

Gene expression databases

CleanExiHS_PRHOXNB.

Organism-specific databases

HPAiHPA038972.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000333490.

Structurei

3D structure databases

ProteinModelPortaliA6NGE7.
SMRiA6NGE7. Positions 2-162.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni84 – 885Substrate bindingSequence Analysis
Regioni119 – 1235Substrate bindingSequence Analysis

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi171 – 1733Microbody targeting signalSequence Analysis

Sequence similaritiesi

Belongs to the OHCU decarboxylase family.Curated

Phylogenomic databases

eggNOGiCOG3195.
GeneTreeiENSGT00390000002395.
HOGENOMiHOG000251764.
HOVERGENiHBG108651.
InParanoidiA6NGE7.
KOiK13485.
OMAiKICHLRL.
OrthoDBiEOG7GFB6D.
PhylomeDBiA6NGE7.
TreeFamiTF323276.

Family and domain databases

Gene3Di1.10.3330.10. 1 hit.
InterProiIPR018020. OHCU_decarboxylase.
IPR017580. OHCU_decarboxylase-1.
[Graphical view]
PfamiPF09349. OHCU_decarbox. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03164. UHCUDC. 1 hit.

Sequencei

Sequence statusi: Complete.

A6NGE7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDIEKVNSMD LGEFVDVFGN ATERCPLIAA AVWSQRPFSD LEDLEKHFFA
60 70 80 90 100
FIDALAQSGQ EGILRCHPDL AGSELQRGTL TAESQREQSG AGLRSLGADE
110 120 130 140 150
RLRLAELNAQ YRARFGFPFV LAARFSDRTA VPRELARRLL CPSAQELRTA
160 170
LGEVKKIGSL RLADLLRADP AKL
Length:173
Mass (Da):19,130
Last modified:January 15, 2008 - v2
Checksum:i521C44BEF163077C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti57 – 571Q → P.
Corresponds to variant rs3897926 [ dbSNP | Ensembl ].
VAR_053987

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL591024 Genomic DNA. No translation available.
CCDSiCCDS45020.1.
RefSeqiNP_001099047.1. NM_001105577.1.
UniGeneiHs.705356.

Genome annotation databases

EnsembliENST00000332715; ENSP00000333490; ENSG00000183463.
GeneIDi646625.
KEGGihsa:646625.
UCSCiuc010aan.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL591024 Genomic DNA. No translation available.
CCDSiCCDS45020.1.
RefSeqiNP_001099047.1. NM_001105577.1.
UniGeneiHs.705356.

3D structure databases

ProteinModelPortaliA6NGE7.
SMRiA6NGE7. Positions 2-162.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000333490.

PTM databases

PhosphoSiteiA6NGE7.

Polymorphism and mutation databases

BioMutaiURAD.

Proteomic databases

PaxDbiA6NGE7.
PRIDEiA6NGE7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000332715; ENSP00000333490; ENSG00000183463.
GeneIDi646625.
KEGGihsa:646625.
UCSCiuc010aan.1. human.

Organism-specific databases

CTDi646625.
GeneCardsiGC13M028555.
HGNCiHGNC:17785. URAD.
HPAiHPA038972.
MIMi615804. gene.
neXtProtiNX_A6NGE7.
PharmGKBiPA142671135.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG3195.
GeneTreeiENSGT00390000002395.
HOGENOMiHOG000251764.
HOVERGENiHBG108651.
InParanoidiA6NGE7.
KOiK13485.
OMAiKICHLRL.
OrthoDBiEOG7GFB6D.
PhylomeDBiA6NGE7.
TreeFamiTF323276.

Enzyme and pathway databases

UniPathwayiUPA00394; UER00652.

Miscellaneous databases

GenomeRNAii646625.
NextBioi119115.
PROiA6NGE7.
SOURCEiSearch...

Gene expression databases

CleanExiHS_PRHOXNB.

Family and domain databases

Gene3Di1.10.3330.10. 1 hit.
InterProiIPR018020. OHCU_decarboxylase.
IPR017580. OHCU_decarboxylase-1.
[Graphical view]
PfamiPF09349. OHCU_decarbox. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03164. UHCUDC. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiURAD_HUMAN
AccessioniPrimary (citable) accession number: A6NGE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: June 24, 2015
This is version 64 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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 (PubMed:16462750).1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.