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Protein

Uric acid degradation bifunctional protein

Gene

uao

Organism
Bacillus sp. (strain TB-90)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes two steps in the degradation of uric acid, i.e. the oxidation of uric acid to 5-hydroxyisourate (HIU) and the stereoselective decarboxylation of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) to (S)-allantoin (By similarity).By similarity

Catalytic activityi

5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate = (S)-allantoin + CO2.
Urate + O2 + H2O = 5-hydroxyisourate + H2O2.

Pathwayi: urate degradation

This protein is involved in step 1 and 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. Uric acid degradation bifunctional protein (uao)
  2. no protein annotated in this organism
  3. Uric acid degradation bifunctional protein (uao)
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 sitei68 – 681Proton donor; for OHCU decarboxylase activityBy similarity
Binding sitei69 – 691Substrate; via carbonyl oxygenBy similarity
Binding sitei243 – 2431Substrate
Active sitei371 – 3711Charge relay system; for urate oxidase activityBy similarity
Binding sitei371 – 3711Substrate
Active sitei420 – 4201Charge relay system; for urate oxidase activityBy similarity

GO - Molecular functioni

GO - Biological processi

Keywords - Molecular functioni

Decarboxylase, Lyase, Oxidoreductase

Keywords - Biological processi

Purine metabolism

Enzyme and pathway databases

UniPathwayiUPA00394; UER00650.
UPA00394; UER00652.

Names & Taxonomyi

Protein namesi
Recommended name:
Uric acid degradation bifunctional protein
Including the following 2 domains:
2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase (EC:4.1.1.97)
Short name:
OHCU decarboxylase
Uricase (EC:1.7.3.3)
Alternative name(s):
Urate oxidase
Gene namesi
Name:uao
OrganismiBacillus sp. (strain TB-90)
Taxonomic identifieri36824 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 502502Uric acid degradation bifunctional proteinPRO_0000166005Add
BLAST

Structurei

Secondary structure

1
502
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi179 – 19214Combined sources
Beta strandi213 – 22412Combined sources
Helixi226 – 2283Combined sources
Helixi229 – 2335Combined sources
Helixi243 – 25614Combined sources
Beta strandi259 – 2613Combined sources
Helixi262 – 27615Combined sources
Beta strandi282 – 2898Combined sources
Beta strandi292 – 2998Combined sources
Beta strandi302 – 31211Combined sources
Beta strandi317 – 32610Combined sources
Beta strandi332 – 35221Combined sources
Beta strandi368 – 3703Combined sources
Beta strandi374 – 38512Combined sources
Helixi386 – 3894Combined sources
Beta strandi391 – 3933Combined sources
Helixi394 – 3963Combined sources
Helixi400 – 41314Combined sources
Helixi419 – 43315Combined sources
Beta strandi437 – 44610Combined sources
Beta strandi450 – 4534Combined sources
Beta strandi463 – 4653Combined sources
Beta strandi471 – 4799Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J2GX-ray2.20A/B/C/D171-489[»]
3WLVX-ray1.75A/B/C/D178-489[»]
4XFPX-ray1.66A/B/C/D178-494[»]
5AYJX-ray2.05A/B/C/D172-502[»]
ProteinModelPortaliQ45697.
SMRiQ45697. Positions 177-482.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ45697.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 178178OHCU decarboxylaseAdd
BLAST
Regioni81 – 855Substrate bindingBy similarity
Regioni116 – 1205Substrate bindingBy similarity
Regioni179 – 502324Urate oxidaseAdd
BLAST
Regioni419 – 4202Substrate binding

Sequence similaritiesi

In the N-terminal section; belongs to the OHCU decarboxylase family.Curated
In the C-terminal section; belongs to the uricase family.Curated

Family and domain databases

Gene3Di1.10.3330.10. 1 hit.
InterProiIPR018020. OHCU_decarboxylase.
IPR017580. OHCU_decarboxylase-1.
IPR002042. Uricase.
IPR019842. Uricase_CS.
[Graphical view]
PfamiPF09349. OHCU_decarbox. 1 hit.
PF01014. Uricase. 2 hits.
[Graphical view]
PRINTSiPR00093. URICASE.
TIGRFAMsiTIGR03164. UHCUDC. 1 hit.
TIGR03383. urate_oxi. 1 hit.
PROSITEiPS00366. URICASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q45697-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMRLKQLNEM SASEFIHLLG GVFENSSWVA ERAEPNRPYS SFQSLYNKMV
60 70 80 90 100
EIVETASDNE QLKLIQMHPH LGTNVKITDF SQEEQKHAGL NELTKDEQNH
110 120 130 140 150
LILLNQKYKD KFGFPFVMAV RGKIKQEIFR TIKERLQNNH QTEFKQALEE
160 170 180 190 200
IKKIAMFRLQ EIFREGENNS MTKHKERVMY YGKGDVFAYR TYLKPLTGVR
210 220 230 240 250
TIPESPFSGR DHILFGVNVK ISVGGTKLLT SFTKGDNSLV VATDSMKNFI
260 270 280 290 300
QKHLASYTGT TIEGFLEYVA TSFLKKYSHI EKISLIGEEI PFETTFAVKN
310 320 330 340 350
GNRAASELVF KKSRNEYATA YLNMVRNEDN TLNITEQQSG LAGLQLIKVS
360 370 380 390 400
GNSFVGFIRD EYTTLPEDSN RPLFVYLNIK WKYKNTEDSF GTNPENYVAA
410 420 430 440 450
EQIRDIATSV FHETETLSIQ HLIYLIGRRI LERFPQLQEV YFESQNHTWD
460 470 480 490 500
KIVEEIPESE GKVYTEPRPP YGFQCFTVTQ EDLPHENILM FSDEPDHKGA

LK
Length:502
Mass (Da):57,978
Last modified:June 6, 2002 - v3
Checksum:iF810FB7C64726DB0
GO

Sequence cautioni

The sequence BAA08723 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB048366 Genomic DNA. Translation: BAB20808.1.
D49974 Genomic DNA. Translation: BAA08723.1. Different initiation.
PIRiJC4535.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB048366 Genomic DNA. Translation: BAB20808.1.
D49974 Genomic DNA. Translation: BAA08723.1. Different initiation.
PIRiJC4535.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J2GX-ray2.20A/B/C/D171-489[»]
3WLVX-ray1.75A/B/C/D178-489[»]
4XFPX-ray1.66A/B/C/D178-494[»]
5AYJX-ray2.05A/B/C/D172-502[»]
ProteinModelPortaliQ45697.
SMRiQ45697. Positions 177-482.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00394; UER00650.
UPA00394; UER00652.

Miscellaneous databases

EvolutionaryTraceiQ45697.

Family and domain databases

Gene3Di1.10.3330.10. 1 hit.
InterProiIPR018020. OHCU_decarboxylase.
IPR017580. OHCU_decarboxylase-1.
IPR002042. Uricase.
IPR019842. Uricase_CS.
[Graphical view]
PfamiPF09349. OHCU_decarbox. 1 hit.
PF01014. Uricase. 2 hits.
[Graphical view]
PRINTSiPR00093. URICASE.
TIGRFAMsiTIGR03164. UHCUDC. 1 hit.
TIGR03383. urate_oxi. 1 hit.
PROSITEiPS00366. URICASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPUCL_BACSB
AccessioniPrimary (citable) accession number: Q45697
Secondary accession number(s): Q9F1Q5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 6, 2002
Last modified: April 13, 2016
This is version 84 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

HIU and OHCU are unstable, they spontaneously decompose to form a racemic mixture of allantoin.

Keywords - Technical termi

3D-structure, Multifunctional enzyme

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.