Reviewed, UniProtKB/Swiss-Prot Q00511 (URIC_ASPFL)

Names and origin

Protein names

Recommended name:
    Uricase
    EC=1.7.3.3
Alternative name(s):
    Urate oxidase

Gene names

Name:	uaZ
Synonyms:	uox

Organism

Aspergillus flavus

Taxonomic identifier

5059 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	302 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which spontaneously decomposes to form allantoin.
Catalytic activity	Urate + O2 + H2O = 5-hydroxyisourate + H2O2.
Pathway	Purine metabolism; uric acid degradation; (S)-allantoin from uric acid: step 1/3.
Subunit structure	Homotetramer.
Subcellular location	Peroxisome.
Sequence similarities	Belongs to the uricase family.

Ontologies

Keywords
Biological process	Purine metabolism
Cellular component	Peroxisome
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW purine base metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	urate oxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 302

301

Uricase

PRO_0000165995

Regions

Region

228 – 229

2

Substrate binding By similarity

Motif

300 – 302

3

Microbody targeting signal Potential

Sites

Active site

177

1

Charge relay system

Active site

229

1

Charge relay system

Binding site

58

1

Substrate By similarity

Binding site

177

1

Substrate By similarity

Amino acid modifications

Modified residue

2

1

N-acetylserine

Secondary structure

1

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302

Helix Strand Turn

Details...

Beta strand

3 – 21

19

Turn

23 – 25

3

Beta strand

28 – 42

15

Helix

44 – 48

5

Helix

52 – 54

3

Helix

58 – 71

14

Helix

77 – 91

15

Beta strand

95 – 105

11

Beta strand

108 – 122

15

Beta strand

128 – 136

9

Turn

137 – 139

3

Beta strand

140 – 158

19

Beta strand

174 – 176

3

Beta strand

179 – 189

11

Beta strand

192 – 194

3

Helix

195 – 200

6

Helix

201 – 203

3

Helix

204 – 222

19

Helix

228 – 242

15

Beta strand

246 – 255

10

Beta strand

258 – 260

3

Turn

264 – 268

5

Helix

273 – 275

3

Beta strand

278 – 281

4

Beta strand

286 – 294

9

Sequences

	Sequence		Length	Mass (Da)
	Q00511-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: B4FAD4ED4EC121AE	FASTA	302	34,241
	10 20 30 40 50 60 MSAVKAARYG KDNVRVYKVH KDEKTGVQTV YEMTVCVLLE GEIETSYTKA DNSVIVATDS 70 80 90 100 110 120 IKNTIYITAK QNPVTPPELF GSILGTHFIE KYNHIHAAHV NIVCHRWTRM DIDGKPHPHS 130 140 150 160 170 180 FIRDSEEKRN VQVDVVEGKG IDIKSSLSGL TVLKSTNSQF WGFLRDEYTT LKETWDRILS 190 200 210 220 230 240 TDVDATWQWK NFSGLQEVRS HVPKFDATWA TAREVTLKTF AEDNSASVQA TMYKMAEQIL 250 260 270 280 290 300 ARQQLIETVE YSLPNKHYFE IDLSWHKGLQ NTGKNAEVFA PQSDPNGLIK CTVGRSSLKS KL

References

[1]	"Cloning and expression in Escherichia coli of the gene encoding Aspergillus flavus urate oxidase." Legoux R., Delpech B., Dumont X., Guillemot J.-C., Ramond P., Shire D., Caput D., Ferrara P., Loison G. J. Biol. Chem. 267:8565-8570(1992) [PubMed: 1339455] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PARTIAL PROTEIN SEQUENCE. Strain: ATCC 20047.
[2]	"Crystal structure of the protein drug urate oxidase-inhibitor complex at 2.05-A resolution." Colloc'h N., el Hajji M., Bachet B., L'Hermite G., Schiltz M., Prange T., Castro B., Mornon J.-P. Nat. Struct. Biol. 4:947-952(1997) [PubMed: 9360612] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X61766 mRNA. Translation: CAA43896.1.
X61765 Genomic DNA. Translation: CAA43895.1.

PIR

A38097.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1R4S	X-ray	1.80	A	2-301	[»]
1R4U	X-ray	1.65	A	2-301	[»]
1R51	X-ray	1.75	A	2-301	[»]
1R56	X-ray	2.30	A/B/C/D/E/F/G/H	2-301	[»]
1WRR	X-ray	1.64	A	2-301	[»]
1WS2	X-ray	2.70	A/B/C/D	2-301	[»]
1WS3	X-ray	3.20	A/B/C/D	2-301	[»]
1XT4	X-ray	2.01	A	2-301	[»]
1XXJ	X-ray	2.80	A/B/C/D	2-301	[»]
1XY3	X-ray	3.20	A/B/C/D/E/F/G/H	2-301	[»]
2FUB	X-ray	2.30	A	2-301	[»]
2FXL	X-ray	1.76	A	2-301	[»]
2IBA	X-ray	1.50	A	2-301	[»]
2IC0	X-ray	1.78	A	2-301	[»]
2ICQ	X-ray	1.75	A	2-301	[»]
2PES	X-ray	1.60	A	2-296	[»]
2ZKA	X-ray	1.61	A	2-302	[»]
2ZKB	X-ray	1.61	A	2-302	[»]
3BJP	X-ray	1.80	A	2-302	[»]
3BK8	X-ray	1.60	A	2-302	[»]
3CKS	X-ray	1.70	A	2-302	[»]
3CKU	X-ray	1.70	A	2-302	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.7.3.3. 2238.

Family and domain databases

InterPro

IPR002042. Uricase.
IPR019842. Uricase_CS.
[Graphical view]

Gene3D

G3DSA:3.10.270.10. Uricase. 1 hit.

PANTHER

PTHR10395:SF1. Uricase. 1 hit.

Pfam

PF01014. Uricase. 2 hits.
[Graphical view]

PRINTS

PR00093. URICASE.

ProDom

PD003367. Uricase. 2 hits.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR03383. urate_oxi. 1 hit.

PROSITE

PS00366. URICASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00049. Rasburicase.

Entry information

Entry name

URIC_ASPFL

Accession

Primary (citable) accession number: Q00511

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 71 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)