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O32141 (PUCL_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Uric acid degradation bifunctional protein PucL

Including the following 2 domains:

  1. 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase
    Short name=OHCU decarboxylase
    EC=4.1.1.n1
  2. Uricase
    EC=1.7.3.3
    Alternative name(s):
    Urate oxidase
Gene names
Name:pucL
Synonyms:yunL
Ordered Locus Names:BSU32450
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.4 Ref.5

Catalytic activity

5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate = (S)-allantoin + CO2. Ref.4 Ref.5

Urate + O2 + H2O = 5-hydroxyisourate + H2O2. Ref.4 Ref.5

Pathway

Purine metabolism; urate degradation; (S)-allantoin from urate: step 1/3.

Purine metabolism; urate degradation; (S)-allantoin from urate: step 3/3.

Induction

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. Ref.2 Ref.3

Miscellaneous

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

Sequence similarities

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

In the C-terminal section; belongs to the uricase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 8. Ref.5

Temperature dependence:

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 494494Uric acid degradation bifunctional protein PucL
PRO_0000166006

Regions

Region1 – 174174OHCU decarboxylase
Region81 – 855Substrate binding By similarity
Region116 – 1205Substrate binding By similarity
Region175 – 494320Urate oxidase
Region414 – 4152Substrate binding By similarity

Sites

Active site681Proton donor; for OHCU decarboxylase activity
Active site3661Charge relay system; for urate oxidase activity By similarity
Active site4151Charge relay system; for urate oxidase activity By similarity
Binding site691Substrate; via carbonyl oxygen By similarity
Binding site2391Substrate By similarity
Binding site3661Substrate By similarity

Experimental info

Mutagenesis681H → A: Loss of OHCU decarboxylase activity. Ref.4
Mutagenesis841E → A: Loss of OHCU decarboxylase activity. Ref.4
Mutagenesis1581R → A: Loss of OHCU decarboxylase activity. Ref.4

Sequences

Sequence LengthMass (Da)Tools
O32141 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: C16D0BB42F67BFC5

FASTA49456,560
        10         20         30         40         50         60 
MFTMDDLNQM DTQTLTDTLG SIFEHSSWIA ERSAALRPFS SLSDLHRKMT GIVKAADRET 

        70         80         90        100        110        120 
QLDLIKKHPR LGTKKTMSDD SVREQQNAGL GKLEQQEYEE FLMLNEHYYD RFGFPFILAV 

       130        140        150        160        170        180 
KGKTKQDIHQ ALLARLESER ETEFQQALIE IYRIARFRLA DIITEKGETQ MKRTMSYGKG 

       190        200        210        220        230        240 
NVFAYRTYLK PLTGVKQIPE SSFAGRDNTV VGVDVTCEIG GEAFLPSFTD GDNTLVVATD 

       250        260        270        280        290        300 
SMKNFIQRHL ASYEGTTTEG FLHYVAHRFL DTYSHMDTIT LTGEDIPFEA MPAYEEKELS 

       310        320        330        340        350        360 
TSRLVFRRSR NERSRSVLKA ERSGNTITIT EQYSEIMDLQ LVKVSGNSFV GFIRDEYTTL 

       370        380        390        400        410        420 
PEDGNRPLFV YLNISWQYEN TNDSYASDPA RYVAAEQVRD LASTVFHELE TPSIQNLIYH 

       430        440        450        460        470        480 
IGCRILARFP QLTDVSFQSQ NHTWDTVVEE IPGSKGKVYT EPRPPYGFQH FTVTREDAEK 

       490 
EKQKAAEKCR SLKA

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[2]"Functional analysis of 14 genes that constitute the purine catabolic pathway in Bacillus subtilis and evidence for a novel regulon controlled by the PucR transcription activator."
Schultz A.C., Nygaard P., Saxild H.H.
J. Bacteriol. 183:3293-3302(2001) [PubMed: 11344136] [Abstract]
Cited for: FUNCTION AS A URATE OXIDASE, INDUCTION.
Strain: 168.
[3]"Identification of additional TnrA-regulated genes of Bacillus subtilis associated with a TnrA box."
Yoshida K., Yamaguchi H., Kinehara M., Ohki Y.-H., Nakaura Y., Fujita Y.
Mol. Microbiol. 49:157-165(2003) [PubMed: 12823818] [Abstract]
Cited for: INDUCTION BY TNRA.
[4]"Structural and functional basis for (S)-allantoin formation in the ureide pathway."
Kim K., Park J., Rhee S.
J. Biol. Chem. 282:23457-23464(2007) [PubMed: 17567580] [Abstract]
Cited for: FUNCTION AS A OHCU DECARBOXYLASE, CATALYTIC ACTIVITY, REACTION MECHANISM, MUTAGENESIS OF HIS-68; GLU-84 AND ARG-158.
[5]"Cloning, purification, and partial characterization of Bacillus subtilis urate oxidase expressed in Escherichia coli."
Pfrimer P., de Moraes L.M., Galdino A.S., Salles L.P., Reis V.C., De Marco J.L., Prates M.V., Bloch C. Jr., Torres F.A.
J. Biomed. Biotechnol. 2010:674908-674908(2010) [PubMed: 20168977] [Abstract]
Cited for: FUNCTION AS URATE OXIDASE, CATALYTIC ACTIVITY, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: 168 / NCCB 69003.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL009126 Genomic DNA. Translation: CAB15235.1.
PIRG70016.
RefSeqNP_391125.1. NC_000964.3.

3D structure databases

ProteinModelPortalO32141.
SMRO32141. Positions 9-166, 173-477.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000000329; EBBACP00000000329; EBBACG00000000329.
GeneID936669.
GenomeReviewsGene locus BSU32450 in contig AL009126_GR.
KEGGbsu:BSU32450.
NMPDRfig|224308.1.peg.3251.
PATRIC18978462. VBIBacSub10457_3394.

Organism-specific databases

GenoListBSU32450. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000006115.
OMAVYTEPRP.
ProtClustDBCLSK552104.

Enzyme and pathway databases

BioCycBSUB:BSU32450-MONOMER.

Family and domain databases

InterProIPR018020. OHCU_decarboxylase.
IPR017580. OHCU_decarboxylase-1.
IPR002042. Uricase.
IPR019842. Uricase_CS.
[Graphical view]
Gene3DG3DSA:1.10.3330.10. G3DSA:1.10.3330.10. 1 hit.
G3DSA:3.10.270.10. Uricase. 1 hit.
KOK00365.
PANTHERPTHR10395:SF1. Uricase. 1 hit.
PfamPF09349. OHCU_decarbox. 1 hit.
PF01014. Uricase. 2 hits.
[Graphical view]
PRINTSPR00093. URICASE.
TIGRFAMsTIGR03164. UHCUDC. 1 hit.
TIGR03383. Urate_oxi. 1 hit.
PROSITEPS00366. URICASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePUCL_BACSU
AccessionPrimary (citable) accession number: O32141
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: January 25, 2012
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents