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Protein

Uricase

Gene

uaZ

Organism
Aspergillus flavus
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.

Catalytic activityi

Urate + O2 + H2O = 5-hydroxyisourate + H2O2.

Pathwayi: urate degradation

This protein is involved in step 1 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. Uricase (uaZ)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
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)DescriptionActionsGraphical viewLength
Active sitei177Charge relay system1
Binding sitei177SubstrateBy similarity1
Active sitei229Charge relay system1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Purine metabolism

Enzyme and pathway databases

BRENDAi1.7.3.3. 506.
UniPathwayiUPA00394; UER00650.

Names & Taxonomyi

Protein namesi
Recommended name:
Uricase (EC:1.7.3.3)
Alternative name(s):
Urate oxidase
Gene namesi
Name:uaZ
Synonyms:uox
OrganismiAspergillus flavus
Taxonomic identifieri5059 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00001659952 – 302UricaseAdd BLAST301

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiQ00511.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi5059.CADAFLAP00005736.

Structurei

Secondary structure

1302
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 21Combined sources13
Turni23 – 25Combined sources3
Beta strandi28 – 42Combined sources15
Helixi44 – 48Combined sources5
Helixi52 – 54Combined sources3
Helixi58 – 71Combined sources14
Helixi77 – 91Combined sources15
Beta strandi95 – 105Combined sources11
Beta strandi108 – 112Combined sources5
Beta strandi115 – 122Combined sources8
Beta strandi128 – 136Combined sources9
Turni137 – 139Combined sources3
Beta strandi140 – 158Combined sources19
Beta strandi174 – 176Combined sources3
Beta strandi179 – 189Combined sources11
Beta strandi192 – 194Combined sources3
Helixi195 – 200Combined sources6
Helixi202 – 222Combined sources21
Helixi228 – 242Combined sources15
Beta strandi246 – 255Combined sources10
Beta strandi258 – 260Combined sources3
Turni264 – 268Combined sources5
Helixi273 – 275Combined sources3
Beta strandi279 – 281Combined sources3
Beta strandi287 – 294Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1R4SX-ray1.80A2-302[»]
1R4UX-ray1.65A2-302[»]
1R51X-ray1.75A2-302[»]
1R56X-ray2.30A/B/C/D/E/F/G/H2-302[»]
1WRRX-ray1.64A2-302[»]
1WS2X-ray2.70A/B/C/D2-302[»]
1WS3X-ray3.20A/B/C/D2-302[»]
1XT4X-ray2.01A2-302[»]
1XXJX-ray2.80A/B/C/D2-302[»]
1XY3X-ray3.20A/B/C/D/E/F/G/H2-302[»]
2FUBX-ray2.30A2-302[»]
2FXLX-ray1.76A2-302[»]
2IBAX-ray1.50A2-302[»]
2IC0X-ray1.78A2-302[»]
2ICQX-ray1.75A2-302[»]
2PESX-ray1.60A2-296[»]
2ZKAX-ray1.61A2-302[»]
2ZKBX-ray1.61A2-302[»]
3BJPX-ray1.80A2-302[»]
3BK8X-ray1.60A2-302[»]
3CKSX-ray1.70A2-302[»]
3CKUX-ray1.70A2-302[»]
3F2MX-ray1.80A2-302[»]
3GKOX-ray1.60A2-302[»]
3L8WX-ray1.00A2-296[»]
3L9GX-ray1.75A2-296[»]
3LBGX-ray1.50A2-296[»]
3LD4X-ray1.35A2-296[»]
3OBPX-ray1.50A2-302[»]
3P9FX-ray1.70A2-302[»]
3P9OX-ray1.45A2-302[»]
3PJKX-ray1.70A2-302[»]
3PK3X-ray1.65A2-302[»]
3PK4X-ray1.85A2-302[»]
3PK5X-ray1.75A2-302[»]
3PK6X-ray1.80A2-302[»]
3PK8X-ray1.65A2-302[»]
3PKFX-ray1.65A2-302[»]
3PKGX-ray1.60A2-302[»]
3PKHX-ray1.71A2-302[»]
3PKKX-ray1.73A2-302[»]
3PKLX-ray1.75A2-302[»]
3PKSX-ray1.75A2-302[»]
3PKTX-ray1.75A2-302[»]
3PKUX-ray1.75A2-302[»]
3PLEX-ray1.60A2-302[»]
3PLGX-ray1.60A2-302[»]
3PLHX-ray1.80A2-302[»]
3PLIX-ray1.68A2-302[»]
3PLJX-ray1.73A2-302[»]
3PLMX-ray1.62A2-302[»]
4CW0X-ray1.50A2-302[»]
4CW2X-ray1.32A2-302[»]
4CW3X-ray1.34A2-302[»]
4CW6X-ray1.28A2-302[»]
4D12X-ray1.40A1-302[»]
4D13X-ray1.30A1-302[»]
4D17X-ray1.30A1-302[»]
4D19X-ray1.35A1-302[»]
4FSKX-ray1.98A2-302[»]
4N3MOther1.90A2-302[»]
4N9MOther2.30A2-302[»]
4N9SX-ray1.06A2-302[»]
4N9VX-ray1.10A2-302[»]
4OP6X-ray1.65A2-302[»]
4OP9X-ray1.58A2-302[»]
4OQCX-ray1.30A2-302[»]
4POEX-ray1.07A2-302[»]
4PR8X-ray1.16A2-296[»]
4PUVX-ray1.30A2-302[»]
ProteinModelPortaliQ00511.
SMRiQ00511.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00511.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni58 – 59Substrate bindingBy similarity2
Regioni228 – 229Substrate bindingBy similarity2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi300 – 302Microbody targeting signalSequence analysis3

Sequence similaritiesi

Belongs to the uricase family.Curated

Phylogenomic databases

eggNOGiKOG1599. Eukaryota.
COG3648. LUCA.
HOGENOMiHOG000250659.

Family and domain databases

InterProiIPR002042. Uricase.
IPR019842. Uricase_CS.
[Graphical view]
PfamiPF01014. Uricase. 2 hits.
[Graphical view]
PIRSFiPIRSF000241. Urate_oxidase. 1 hit.
PRINTSiPR00093. URICASE.
TIGRFAMsiTIGR03383. urate_oxi. 1 hit.
PROSITEiPS00366. URICASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q00511-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAVKAARYG KDNVRVYKVH KDEKTGVQTV YEMTVCVLLE GEIETSYTKA
60 70 80 90 100
DNSVIVATDS IKNTIYITAK QNPVTPPELF GSILGTHFIE KYNHIHAAHV
110 120 130 140 150
NIVCHRWTRM DIDGKPHPHS FIRDSEEKRN VQVDVVEGKG IDIKSSLSGL
160 170 180 190 200
TVLKSTNSQF WGFLRDEYTT LKETWDRILS TDVDATWQWK NFSGLQEVRS
210 220 230 240 250
HVPKFDATWA TAREVTLKTF AEDNSASVQA TMYKMAEQIL ARQQLIETVE
260 270 280 290 300
YSLPNKHYFE IDLSWHKGLQ NTGKNAEVFA PQSDPNGLIK CTVGRSSLKS

KL
Length:302
Mass (Da):34,241
Last modified:January 23, 2007 - v3
Checksum:iB4FAD4ED4EC121AE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61766 mRNA. Translation: CAA43896.1.
X61765 Genomic DNA. Translation: CAA43895.1.
PIRiA38097.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61766 mRNA. Translation: CAA43896.1.
X61765 Genomic DNA. Translation: CAA43895.1.
PIRiA38097.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1R4SX-ray1.80A2-302[»]
1R4UX-ray1.65A2-302[»]
1R51X-ray1.75A2-302[»]
1R56X-ray2.30A/B/C/D/E/F/G/H2-302[»]
1WRRX-ray1.64A2-302[»]
1WS2X-ray2.70A/B/C/D2-302[»]
1WS3X-ray3.20A/B/C/D2-302[»]
1XT4X-ray2.01A2-302[»]
1XXJX-ray2.80A/B/C/D2-302[»]
1XY3X-ray3.20A/B/C/D/E/F/G/H2-302[»]
2FUBX-ray2.30A2-302[»]
2FXLX-ray1.76A2-302[»]
2IBAX-ray1.50A2-302[»]
2IC0X-ray1.78A2-302[»]
2ICQX-ray1.75A2-302[»]
2PESX-ray1.60A2-296[»]
2ZKAX-ray1.61A2-302[»]
2ZKBX-ray1.61A2-302[»]
3BJPX-ray1.80A2-302[»]
3BK8X-ray1.60A2-302[»]
3CKSX-ray1.70A2-302[»]
3CKUX-ray1.70A2-302[»]
3F2MX-ray1.80A2-302[»]
3GKOX-ray1.60A2-302[»]
3L8WX-ray1.00A2-296[»]
3L9GX-ray1.75A2-296[»]
3LBGX-ray1.50A2-296[»]
3LD4X-ray1.35A2-296[»]
3OBPX-ray1.50A2-302[»]
3P9FX-ray1.70A2-302[»]
3P9OX-ray1.45A2-302[»]
3PJKX-ray1.70A2-302[»]
3PK3X-ray1.65A2-302[»]
3PK4X-ray1.85A2-302[»]
3PK5X-ray1.75A2-302[»]
3PK6X-ray1.80A2-302[»]
3PK8X-ray1.65A2-302[»]
3PKFX-ray1.65A2-302[»]
3PKGX-ray1.60A2-302[»]
3PKHX-ray1.71A2-302[»]
3PKKX-ray1.73A2-302[»]
3PKLX-ray1.75A2-302[»]
3PKSX-ray1.75A2-302[»]
3PKTX-ray1.75A2-302[»]
3PKUX-ray1.75A2-302[»]
3PLEX-ray1.60A2-302[»]
3PLGX-ray1.60A2-302[»]
3PLHX-ray1.80A2-302[»]
3PLIX-ray1.68A2-302[»]
3PLJX-ray1.73A2-302[»]
3PLMX-ray1.62A2-302[»]
4CW0X-ray1.50A2-302[»]
4CW2X-ray1.32A2-302[»]
4CW3X-ray1.34A2-302[»]
4CW6X-ray1.28A2-302[»]
4D12X-ray1.40A1-302[»]
4D13X-ray1.30A1-302[»]
4D17X-ray1.30A1-302[»]
4D19X-ray1.35A1-302[»]
4FSKX-ray1.98A2-302[»]
4N3MOther1.90A2-302[»]
4N9MOther2.30A2-302[»]
4N9SX-ray1.06A2-302[»]
4N9VX-ray1.10A2-302[»]
4OP6X-ray1.65A2-302[»]
4OP9X-ray1.58A2-302[»]
4OQCX-ray1.30A2-302[»]
4POEX-ray1.07A2-302[»]
4PR8X-ray1.16A2-296[»]
4PUVX-ray1.30A2-302[»]
ProteinModelPortaliQ00511.
SMRiQ00511.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5059.CADAFLAP00005736.

Proteomic databases

PRIDEiQ00511.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1599. Eukaryota.
COG3648. LUCA.
HOGENOMiHOG000250659.

Enzyme and pathway databases

UniPathwayiUPA00394; UER00650.
BRENDAi1.7.3.3. 506.

Miscellaneous databases

EvolutionaryTraceiQ00511.

Family and domain databases

InterProiIPR002042. Uricase.
IPR019842. Uricase_CS.
[Graphical view]
PfamiPF01014. Uricase. 2 hits.
[Graphical view]
PIRSFiPIRSF000241. Urate_oxidase. 1 hit.
PRINTSiPR00093. URICASE.
TIGRFAMsiTIGR03383. urate_oxi. 1 hit.
PROSITEiPS00366. URICASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiURIC_ASPFL
AccessioniPrimary (citable) accession number: Q00511
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 118 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.