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Reviewed, UniProtKB/Swiss-Prot O32141 (PUCL_BACSU)

Last modified June 16, 2009. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Uric acid degradation bifunctional protein pucL
Including the following 2 domains:
    1- Recommended name:
            2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase
                Short name=OHCU decarboxylase
              EC=4.1.1.n1
    2- Recommended name:
            Uricase
              EC=1.7.3.3
        Alternative name(s):
            Urate oxidase
Gene names
Name: pucL
Synonyms: yunL
Ordered Locus Names: BSU32450
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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.3

Catalytic activity

5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate = (S)-allantoin + CO2. Ref.3

Urate + O2 + H2O = 5-hydroxyisourate + H2O2. Ref.3

Pathway

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

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

Induction

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

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.

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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.3
Mutagenesis841E → A: Loss of OHCU decarboxylase activity. Ref.3
Mutagenesis1581R → A: Loss of OHCU decarboxylase activity. Ref.3

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Sequences

Sequence LengthMass (Da)Tools
O32141-1 [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

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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]"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.

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Cross-references

Sequence databases

AL009126 Genomic DNA. Translation: CAB15235.1.
PIRG70016.
RefSeqNP_391125.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID936669.
GenomeReviewsGene locus BSU32450 in contig AL009126_GR.
KEGGbsu:BSU32450.
NMPDRfig|224308.1.peg.3251.

Organism-specific databases

SubtiListBG13986. pucL. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMO32141.
OMAO32141. KVYTEPR.

Enzyme and pathway databases

BioCycBSUB224308:BSU3242-MON.
BRENDA1.7.3.3. 150.

Family and domain databases

InterProIPR018020. OHCU_decarboxylase.
IPR017580. OHCU_decarboxylase-1.
IPR002042. Uricase.
IPR019842. Uricase_CS.
[Graphical view]
Gene3DG3DSA:3.10.270.10. Uricase. 1 hit.
PfamPF09349. OHCU_decarbox. 1 hit.
PF01014. Uricase. 2 hits.
[Graphical view]
PRINTSPR00093. URICASE.
ProDomPD003367. Uricase. 2 hits.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR03164. UHCUDC. 1 hit.
TIGR03383. urate_oxi. 1 hit.
PROSITEPS00366. URICASE. 1 hit.
[Graphical view]
ProtoNetSearch...

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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: June 16, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents