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Protein

Uric acid degradation bifunctional protein PucL

Gene

pucL

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: -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

Miscellaneous

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

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)DescriptionActionsGraphical viewLength
Active sitei68Proton donor; for OHCU decarboxylase activity1 Publication1
Binding sitei69OHCU; via carbonyl oxygenBy similarity1
Active sitei179Charge relay system; for urate oxidase activityBy similarity1
Active sitei239Charge relay system; for urate oxidase activityBy similarity1
Binding sitei349UrateBy similarity1
Binding sitei366UrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDecarboxylase, Lyase, Multifunctional enzyme, Oxidoreductase
Biological processPurine 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)DescriptionActionsGraphical viewLength
Mutagenesisi68H → A: Loss of OHCU decarboxylase activity. 1 Publication1
Mutagenesisi84E → A: Loss of OHCU decarboxylase activity. 1 Publication1
Mutagenesisi158R → A: Loss of OHCU decarboxylase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001660061 – 494Uric acid degradation bifunctional protein PucLAdd BLAST494

Proteomic databases

PaxDbiO32141
PRIDEiO32141

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
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 174OHCU decarboxylaseAdd BLAST174
Regioni81 – 85OHCU binding1 Publication5
Regioni116 – 120OHCU bindingBy similarity5
Regioni175 – 494Urate oxidaseAdd BLAST320
Regioni239 – 240Urate bindingBy similarity2
Regioni414 – 415Urate bindingBy similarity2

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
OMAiKDRCFAT
PhylomeDBiO32141

Family and domain databases

Gene3Di1.10.3330.10, 1 hit
InterProiView protein in InterPro
IPR018020 OHCU_decarboxylase
IPR017580 OHCU_decarboxylase-1
IPR036778 OHCU_decarboxylase_sf
IPR002042 Uricase
IPR019842 Uricase_CS
PfamiView protein in Pfam
PF09349 OHCU_decarbox, 1 hit
PF01014 Uricase, 2 hits
PRINTSiPR00093 URICASE
SUPFAMiSSF158694 SSF158694, 1 hit
TIGRFAMsiTIGR03164 UHCUDC, 1 hit
TIGR03383 urate_oxi, 1 hit
PROSITEiView protein in PROSITE
PS00366 URICASE, 1 hit

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
PATRICifig|224308.179.peg.3512

Similar proteinsi

Entry informationi

Entry nameiPUCL_BACSU
AccessioniPrimary (citable) accession number: O32141
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: May 23, 2018
This is version 121 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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

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