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Q00511

- URIC_ASPFL

UniProt

Q00511 - URIC_ASPFL

Protein

Uricase

Gene

uaZ

Organism
Aspergillus flavus
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    • Comment

    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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei177 – 1771Charge relay system
    Binding sitei177 – 1771SubstrateBy similarity
    Active sitei229 – 2291Charge relay system

    GO - Molecular functioni

    1. urate oxidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. purine nucleobase metabolic process Source: UniProtKB-KW
    2. urate catabolic process Source: UniProtKB-UniPathway

    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

    1. peroxisome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Peroxisome

    Pathology & Biotechi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 302301UricasePRO_0000165995Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiQ00511.

    Interactioni

    Subunit structurei

    Homotetramer.

    Structurei

    Secondary structure

    1
    302
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 2113
    Turni23 – 253
    Beta strandi28 – 4215
    Helixi44 – 485
    Helixi52 – 543
    Helixi58 – 7114
    Helixi77 – 9115
    Beta strandi95 – 10511
    Beta strandi108 – 1125
    Beta strandi115 – 1228
    Beta strandi128 – 1369
    Turni137 – 1393
    Beta strandi140 – 15819
    Beta strandi174 – 1763
    Beta strandi179 – 18911
    Beta strandi192 – 1943
    Helixi195 – 2006
    Helixi202 – 22221
    Helixi228 – 24215
    Beta strandi246 – 25510
    Beta strandi258 – 2603
    Turni264 – 2685
    Helixi273 – 2753
    Beta strandi279 – 2813
    Beta strandi287 – 2948

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    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[»]
    ProteinModelPortaliQ00511.
    SMRiQ00511. Positions 3-300.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ00511.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni58 – 592Substrate bindingBy similarity
    Regioni228 – 2292Substrate bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi300 – 3023Microbody targeting signalSequence Analysis

    Sequence similaritiesi

    Belongs to the uricase family.Curated

    Phylogenomic databases

    eggNOGiCOG3648.
    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

    MSAVKAARYG KDNVRVYKVH KDEKTGVQTV YEMTVCVLLE GEIETSYTKA    50
    DNSVIVATDS IKNTIYITAK QNPVTPPELF GSILGTHFIE KYNHIHAAHV 100
    NIVCHRWTRM DIDGKPHPHS FIRDSEEKRN VQVDVVEGKG IDIKSSLSGL 150
    TVLKSTNSQF WGFLRDEYTT LKETWDRILS TDVDATWQWK NFSGLQEVRS 200
    HVPKFDATWA TAREVTLKTF AEDNSASVQA TMYKMAEQIL ARQQLIETVE 250
    YSLPNKHYFE IDLSWHKGLQ NTGKNAEVFA PQSDPNGLIK CTVGRSSLKS 300
    KL 302
    Length:302
    Mass (Da):34,241
    Last modified:January 23, 2007 - v3
    Checksum:iB4FAD4ED4EC121AE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X61766 mRNA. Translation: CAA43896.1.
    X61765 Genomic DNA. Translation: CAA43895.1.
    PIRiA38097.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X61766 mRNA. Translation: CAA43896.1 .
    X61765 Genomic DNA. Translation: CAA43895.1 .
    PIRi A38097.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1R4S X-ray 1.80 A 2-302 [» ]
    1R4U X-ray 1.65 A 2-302 [» ]
    1R51 X-ray 1.75 A 2-302 [» ]
    1R56 X-ray 2.30 A/B/C/D/E/F/G/H 2-302 [» ]
    1WRR X-ray 1.64 A 2-302 [» ]
    1WS2 X-ray 2.70 A/B/C/D 2-302 [» ]
    1WS3 X-ray 3.20 A/B/C/D 2-302 [» ]
    1XT4 X-ray 2.01 A 2-302 [» ]
    1XXJ X-ray 2.80 A/B/C/D 2-302 [» ]
    1XY3 X-ray 3.20 A/B/C/D/E/F/G/H 2-302 [» ]
    2FUB X-ray 2.30 A 2-302 [» ]
    2FXL X-ray 1.76 A 2-302 [» ]
    2IBA X-ray 1.50 A 2-302 [» ]
    2IC0 X-ray 1.78 A 2-302 [» ]
    2ICQ X-ray 1.75 A 2-302 [» ]
    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 [» ]
    3F2M X-ray 1.80 A 2-302 [» ]
    3GKO X-ray 1.60 A 2-302 [» ]
    3L8W X-ray 1.00 A 2-296 [» ]
    3L9G X-ray 1.75 A 2-296 [» ]
    3LBG X-ray 1.50 A 2-296 [» ]
    3LD4 X-ray 1.35 A 2-296 [» ]
    3OBP X-ray 1.50 A 2-302 [» ]
    3P9F X-ray 1.70 A 2-302 [» ]
    3P9O X-ray 1.45 A 2-302 [» ]
    3PJK X-ray 1.70 A 2-302 [» ]
    3PK3 X-ray 1.65 A 2-302 [» ]
    3PK4 X-ray 1.85 A 2-302 [» ]
    3PK5 X-ray 1.75 A 2-302 [» ]
    3PK6 X-ray 1.80 A 2-302 [» ]
    3PK8 X-ray 1.65 A 2-302 [» ]
    3PKF X-ray 1.65 A 2-302 [» ]
    3PKG X-ray 1.60 A 2-302 [» ]
    3PKH X-ray 1.71 A 2-302 [» ]
    3PKK X-ray 1.73 A 2-302 [» ]
    3PKL X-ray 1.75 A 2-302 [» ]
    3PKS X-ray 1.75 A 2-302 [» ]
    3PKT X-ray 1.75 A 2-302 [» ]
    3PKU X-ray 1.75 A 2-302 [» ]
    3PLE X-ray 1.60 A 2-302 [» ]
    3PLG X-ray 1.60 A 2-302 [» ]
    3PLH X-ray 1.80 A 2-302 [» ]
    3PLI X-ray 1.68 A 2-302 [» ]
    3PLJ X-ray 1.73 A 2-302 [» ]
    3PLM X-ray 1.62 A 2-302 [» ]
    4FSK X-ray 1.98 A 2-302 [» ]
    4N3M Other 1.90 A 2-302 [» ]
    4N9M Other 2.30 A 2-302 [» ]
    4N9S X-ray 1.06 A 2-302 [» ]
    4N9V X-ray 1.10 A 2-302 [» ]
    4OP6 X-ray 1.65 A 2-302 [» ]
    4OP9 X-ray 1.58 A 2-302 [» ]
    ProteinModelPortali Q00511.
    SMRi Q00511. Positions 3-300.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    DrugBanki DB00049. Rasburicase.

    Proteomic databases

    PRIDEi Q00511.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG3648.
    HOGENOMi HOG000250659.

    Enzyme and pathway databases

    UniPathwayi UPA00394 ; UER00650 .
    BRENDAi 1.7.3.3. 506.

    Miscellaneous databases

    EvolutionaryTracei Q00511.

    Family and domain databases

    InterProi IPR002042. Uricase.
    IPR019842. Uricase_CS.
    [Graphical view ]
    Pfami PF01014. Uricase. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF000241. Urate_oxidase. 1 hit.
    PRINTSi PR00093. URICASE.
    TIGRFAMsi TIGR03383. urate_oxi. 1 hit.
    PROSITEi PS00366. URICASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

    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: October 1, 2014
    This is version 108 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

    External Data

    Dasty 3