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Protein

Uric acid degradation bifunctional protein PucL

Gene

pucL

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 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.3 Publications

Catalytic activityi

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

pH dependencei

Optimum pH is 8.1 Publication

Temperature dependencei

Optimum temperature is 37 degrees Celsius. Retains 90% of its activity after 72 hours of incubation at 20 degrees Celsius or -4 degrees Celsius, but loses 50% of its activity after 12 hours of incubation at 37 degrees Celsius.1 Publication

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 PucL (pucL)
  2. 5-hydroxyisourate hydrolase (pucM)
  3. Uric acid degradation bifunctional protein PucL (pucL)
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 activity
Binding sitei69 – 691Substrate; via carbonyl oxygenBy similarity
Binding sitei239 – 2391SubstrateBy similarity
Active sitei366 – 3661Charge relay system; for urate oxidase activityBy similarity
Binding sitei366 – 3661SubstrateBy similarity
Active sitei415 – 4151Charge 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

BioCyciBSUB:BSU32450-MONOMER.
SABIO-RKO32141.
UniPathwayiUPA00394; UER00650.
UPA00394; UER00652.

Names & Taxonomyi

Protein namesi
Recommended name:
Uric acid degradation bifunctional protein PucL
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:pucL
Synonyms:yunL
Ordered Locus Names:BSU32450
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi68 – 681H → A: Loss of OHCU decarboxylase activity. 1 Publication
Mutagenesisi84 – 841E → A: Loss of OHCU decarboxylase activity. 1 Publication
Mutagenesisi158 – 1581R → A: Loss of OHCU decarboxylase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 494494Uric acid degradation bifunctional protein PucLPRO_0000166006Add
BLAST

Proteomic databases

PaxDbiO32141.

Expressioni

Inductioni

Expression is very low in excess nitrogen (glutamate plus ammonia) and is induced by TnrA during imiting-nitrogen conditions (glutamate). Expression is further induced when allantoin or uric acid are added during limiting-nitrogen conditions.2 Publications

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100017601.

Structurei

3D structure databases

ProteinModelPortaliO32141.
SMRiO32141. Positions 9-166, 173-477.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 174174OHCU decarboxylaseAdd
BLAST
Regioni81 – 855Substrate bindingBy similarity
Regioni116 – 1205Substrate bindingBy similarity
Regioni175 – 494320Urate oxidaseAdd
BLAST
Regioni414 – 4152Substrate bindingBy similarity

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

Phylogenomic databases

eggNOGiENOG4105FFA. Bacteria.
COG3195. LUCA.
COG3648. LUCA.
HOGENOMiHOG000115797.
InParanoidiO32141.
KOiK16838.
OMAiVYTEPRP.
PhylomeDBiO32141.

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.

O32141-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFTMDDLNQM DTQTLTDTLG SIFEHSSWIA ERSAALRPFS SLSDLHRKMT
60 70 80 90 100
GIVKAADRET QLDLIKKHPR LGTKKTMSDD SVREQQNAGL GKLEQQEYEE
110 120 130 140 150
FLMLNEHYYD RFGFPFILAV KGKTKQDIHQ ALLARLESER ETEFQQALIE
160 170 180 190 200
IYRIARFRLA DIITEKGETQ MKRTMSYGKG NVFAYRTYLK PLTGVKQIPE
210 220 230 240 250
SSFAGRDNTV VGVDVTCEIG GEAFLPSFTD GDNTLVVATD SMKNFIQRHL
260 270 280 290 300
ASYEGTTTEG FLHYVAHRFL DTYSHMDTIT LTGEDIPFEA MPAYEEKELS
310 320 330 340 350
TSRLVFRRSR NERSRSVLKA ERSGNTITIT EQYSEIMDLQ LVKVSGNSFV
360 370 380 390 400
GFIRDEYTTL PEDGNRPLFV YLNISWQYEN TNDSYASDPA RYVAAEQVRD
410 420 430 440 450
LASTVFHELE TPSIQNLIYH IGCRILARFP QLTDVSFQSQ NHTWDTVVEE
460 470 480 490
IPGSKGKVYT EPRPPYGFQH FTVTREDAEK EKQKAAEKCR SLKA
Length:494
Mass (Da):56,560
Last modified:January 1, 1998 - v1
Checksum:iC16D0BB42F67BFC5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB15235.1.
PIRiG70016.
RefSeqiNP_391125.1. NC_000964.3.
WP_003242600.1. NZ_JNCM01000033.1.

Genome annotation databases

EnsemblBacteriaiCAB15235; CAB15235; BSU32450.
GeneIDi936669.
KEGGibsu:BSU32450.
PATRICi18978462. VBIBacSub10457_3394.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB15235.1.
PIRiG70016.
RefSeqiNP_391125.1. NC_000964.3.
WP_003242600.1. NZ_JNCM01000033.1.

3D structure databases

ProteinModelPortaliO32141.
SMRiO32141. Positions 9-166, 173-477.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100017601.

Proteomic databases

PaxDbiO32141.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15235; CAB15235; BSU32450.
GeneIDi936669.
KEGGibsu:BSU32450.
PATRICi18978462. VBIBacSub10457_3394.

Phylogenomic databases

eggNOGiENOG4105FFA. Bacteria.
COG3195. LUCA.
COG3648. LUCA.
HOGENOMiHOG000115797.
InParanoidiO32141.
KOiK16838.
OMAiVYTEPRP.
PhylomeDBiO32141.

Enzyme and pathway databases

UniPathwayiUPA00394; UER00650.
UPA00394; UER00652.
BioCyciBSUB:BSU32450-MONOMER.
SABIO-RKO32141.

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_BACSU
AccessioniPrimary (citable) accession number: O32141
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: September 7, 2016
This is version 115 of the entry and version 1 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

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.