A6NGE7 (URAD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase
Short name=OHCU decarboxylase
EC=4.1.1.n1

Alternative name(s):
Parahox neighbor

Gene names

Name:

PRHOXNB

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	173 AA.
Sequence status	Complete.
Protein existence	Uncertain

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.
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.

Ontologies

Keywords
Biological process	Purine metabolism
Cellular component	Peroxisome
Coding sequence diversity	Polymorphism
Molecular function	Decarboxylase Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	allantoin biosynthetic process Inferred from electronic annotation. Source: InterPro purine base metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	carboxy-lyase activity 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 – 173	173	Putative 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase		PRO_0000315240
Regions
	Region	84 – 88	5	Substrate binding Potential
	Region	119 – 123	5	Substrate binding Potential
	Motif	171 – 173	3	Microbody targeting signal Potential
Sites
	Active site	67	1	Proton donor Potential
	Binding site	68	1	Substrate; via carbonyl oxygen Potential
Natural variations
	Natural variant	57	1	Q → P. Corresponds to variant rs3897926 [ dbSNP | Ensembl ].		VAR_053987

Sequences

	Sequence		Length	Mass (Da)
	A6NGE7 [UniParc]. Last modified January 15, 2008. Version 2. Checksum: 521C44BEF163077C	FASTA	173	19,130
	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

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. , 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: 15057823] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL591024 Genomic DNA. No translation available.
IPI	IPI00161055.
RefSeq	NP_001099047.1. NM_001105577.1.
UniGene	Hs.705356.
3D structure databases
ProteinModelPortal	A6NGE7.
SMR	A6NGE7. Positions 1-168.
ModBase	Search...
Protein-protein interaction databases
STRING	A6NGE7.
PTM databases
PhosphoSite	A6NGE7.
Proteomic databases
PRIDE	A6NGE7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000332715; ENSP00000333490; ENSG00000183463.
GeneID	646625.
KEGG	hsa:646625.
UCSC	uc010aan.1. human.
Organism-specific databases
CTD	646625.
GeneCards	GC13M028552.
HGNC	HGNC:17785. PRHOXNB.
HPA	HPA038972.
neXtProt	NX_A6NGE7.
PharmGKB	PA142671135.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG04218.
GeneTree	ENSGT00390000002395.
HOGENOM	HBG696689.
HOVERGEN	HBG108651.
InParanoid	A6NGE7.
OMA	VICAREA.
OrthoDB	EOG4H19X0.
PhylomeDB	A6NGE7.
Gene expression databases
CleanEx	HS_PRHOXNB.
Genevestigator	A6NGE7.
Family and domain databases
InterPro	IPR018020. OHCU_decarboxylase. IPR017580. OHCU_decarboxylase-1. [Graphical view]
Gene3D	G3DSA:1.10.3330.10. G3DSA:1.10.3330.10. 1 hit.
KO	K13485.
Pfam	PF09349. OHCU_decarbox. 1 hit. [Graphical view]
TIGRFAMs	TIGR03164. UHCUDC. 1 hit.
ProtoNet	Search...
Other
NextBio	119115.

Entry information

Entry name

URAD_HUMAN

Accession

Primary (citable) accession number: A6NGE7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	January 15, 2008
Last modified:	January 25, 2012
This is version 39 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.