PUCL_BACSB
ID PUCL_BACSB Reviewed; 502 AA.
AC Q45697; Q9F1Q5;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 3.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Uric acid degradation bifunctional protein;
DE Includes:
DE RecName: Full=2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase;
DE Short=OHCU decarboxylase;
DE EC=4.1.1.97;
DE Includes:
DE RecName: Full=Uricase;
DE EC=1.7.3.3;
DE AltName: Full=Urate oxidase;
GN Name=uao;
OS Bacillus sp. (strain TB-90).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=36824;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Nishiya Y., Hibi T., Oda J.;
RT "The full sequence of the gene encoding the diagnostic enzyme Bacillus
RT uricase.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-502.
RX PubMed=8907179; DOI=10.1093/oxfordjournals.jbchem.a021219;
RA Yamamoto K., Kojima Y., Kikuchi T., Shigyo T., Sugihara K., Takashio M.,
RA Emi S.;
RT "Nucleotide sequence of the uricase gene from Bacillus sp. TB-90.";
RL J. Biochem. 119:80-84(1996).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 171-489 IN COMPLEX WITH INHIBITOR
RP 8-AZAXANTHINE.
RG Mycobacterium tuberculosis structural genomics consortium (TB);
RT "Crystal structure of urate oxidase from Bacillus sp.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Catalyzes two steps in the degradation of uric acid, i.e. the
CC oxidation of uric acid to 5-hydroxyisourate (HIU) and the
CC stereoselective decarboxylation of 2-oxo-4-hydroxy-4-carboxy-5-
CC ureidoimidazoline (OHCU) to (S)-allantoin (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-
CC carboxylate + H(+) = (S)-allantoin + CO2; Xref=Rhea:RHEA:26301,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15678, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:58639; EC=4.1.1.97;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + urate = 5-hydroxyisourate + H2O2;
CC Xref=Rhea:RHEA:21368, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17775, ChEBI:CHEBI:18072; EC=1.7.3.3;
CC -!- PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from
CC urate: step 1/3.
CC -!- PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from
CC urate: step 3/3.
CC -!- MISCELLANEOUS: HIU and OHCU are unstable, they spontaneously decompose
CC to form a racemic mixture of allantoin.
CC -!- SIMILARITY: In the N-terminal section; belongs to the OHCU
CC decarboxylase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the uricase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA08723.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB048366; BAB20808.1; -; Genomic_DNA.
DR EMBL; D49974; BAA08723.1; ALT_INIT; Genomic_DNA.
DR PIR; JC4535; JC4535.
DR PDB; 1J2G; X-ray; 2.20 A; A/B/C/D=171-489.
DR PDB; 3WLV; X-ray; 1.75 A; A/B/C/D=178-489.
DR PDB; 4XFP; X-ray; 1.66 A; A/B/C/D=178-494.
DR PDB; 5AYJ; X-ray; 2.05 A; A/B/C/D=172-502.
DR PDB; 5Y2P; X-ray; 1.50 A; A/B=178-489.
DR PDB; 5Y52; X-ray; 1.63 A; A/B/C/D=172-502.
DR PDB; 5YJ2; X-ray; 1.71 A; A/B/C/D=178-489.
DR PDB; 5YJA; X-ray; 1.65 A; A/B/C/D=172-494.
DR PDB; 5Z27; X-ray; 1.60 A; A/B=172-494.
DR PDB; 5Z2B; X-ray; 1.90 A; A/B=172-494.
DR PDB; 7CMN; X-ray; 1.42 A; A/B=177-489.
DR PDB; 7CMQ; X-ray; 1.65 A; A/B=177-489.
DR PDB; 7CUC; X-ray; 1.44 A; A/B=177-489.
DR PDB; 7CUF; X-ray; 1.46 A; A/B=177-489.
DR PDB; 7CUG; X-ray; 1.62 A; A/B=177-489.
DR PDBsum; 1J2G; -.
DR PDBsum; 3WLV; -.
DR PDBsum; 4XFP; -.
DR PDBsum; 5AYJ; -.
DR PDBsum; 5Y2P; -.
DR PDBsum; 5Y52; -.
DR PDBsum; 5YJ2; -.
DR PDBsum; 5YJA; -.
DR PDBsum; 5Z27; -.
DR PDBsum; 5Z2B; -.
DR PDBsum; 7CMN; -.
DR PDBsum; 7CMQ; -.
DR PDBsum; 7CUC; -.
DR PDBsum; 7CUF; -.
DR PDBsum; 7CUG; -.
DR AlphaFoldDB; Q45697; -.
DR SMR; Q45697; -.
DR DrugBank; DB01875; 8-azaxanthine.
DR DrugBank; DB05321; PEG-uricase.
DR UniPathway; UPA00394; UER00650.
DR UniPathway; UPA00394; UER00652.
DR EvolutionaryTrace; Q45697; -.
DR GO; GO:0051997; F:2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase activity; IEA:RHEA.
DR GO; GO:0004846; F:urate oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0000255; P:allantoin metabolic process; IEA:InterPro.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019628; P:urate catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.3330.10; -; 1.
DR InterPro; IPR018020; OHCU_decarboxylase.
DR InterPro; IPR017580; OHCU_decarboxylase-1.
DR InterPro; IPR036778; OHCU_decarboxylase_sf.
DR InterPro; IPR002042; Uricase.
DR InterPro; IPR019842; Uricase_CS.
DR Pfam; PF09349; OHCU_decarbox; 1.
DR Pfam; PF01014; Uricase; 2.
DR PRINTS; PR00093; URICASE.
DR SUPFAM; SSF158694; SSF158694; 1.
DR TIGRFAMs; TIGR03164; UHCUDC; 1.
DR TIGRFAMs; TIGR03383; urate_oxi; 1.
DR PROSITE; PS00366; URICASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Decarboxylase; Lyase; Multifunctional enzyme; Oxidoreductase;
KW Purine metabolism.
FT CHAIN 1..502
FT /note="Uric acid degradation bifunctional protein"
FT /id="PRO_0000166005"
FT REGION 1..178
FT /note="OHCU decarboxylase"
FT REGION 179..502
FT /note="Urate oxidase"
FT ACT_SITE 68
FT /note="Proton donor; for OHCU decarboxylase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 183
FT /note="Charge relay system; for urate oxidase activity"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT ACT_SITE 243
FT /note="Charge relay system; for urate oxidase activity"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT BINDING 69
FT /ligand="5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-
FT 5-carboxylate"
FT /ligand_id="ChEBI:CHEBI:58639"
FT /evidence="ECO:0000250"
FT BINDING 81..85
FT /ligand="5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-
FT 5-carboxylate"
FT /ligand_id="ChEBI:CHEBI:58639"
FT /evidence="ECO:0000250"
FT BINDING 116..120
FT /ligand="5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-
FT 5-carboxylate"
FT /ligand_id="ChEBI:CHEBI:58639"
FT /evidence="ECO:0000250"
FT BINDING 243..244
FT /ligand="urate"
FT /ligand_id="ChEBI:CHEBI:17775"
FT /evidence="ECO:0000305|Ref.3"
FT BINDING 354
FT /ligand="urate"
FT /ligand_id="ChEBI:CHEBI:17775"
FT /evidence="ECO:0000305|Ref.3"
FT BINDING 371
FT /ligand="urate"
FT /ligand_id="ChEBI:CHEBI:17775"
FT /evidence="ECO:0000305|Ref.3"
FT BINDING 419..420
FT /ligand="urate"
FT /ligand_id="ChEBI:CHEBI:17775"
FT /evidence="ECO:0000305|Ref.3"
FT STRAND 179..192
FT /evidence="ECO:0007829|PDB:7CMN"
FT STRAND 213..224
FT /evidence="ECO:0007829|PDB:7CMN"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:7CMN"
FT HELIX 229..233
FT /evidence="ECO:0007829|PDB:7CMN"
FT HELIX 243..256
FT /evidence="ECO:0007829|PDB:7CMN"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:7CUC"
FT HELIX 262..276
FT /evidence="ECO:0007829|PDB:7CMN"
FT STRAND 282..289
FT /evidence="ECO:0007829|PDB:7CMN"
FT STRAND 292..297
FT /evidence="ECO:0007829|PDB:7CMN"
FT STRAND 304..312
FT /evidence="ECO:0007829|PDB:7CMN"
FT STRAND 317..326
FT /evidence="ECO:0007829|PDB:7CMN"
FT STRAND 332..347
FT /evidence="ECO:0007829|PDB:7CMN"
FT STRAND 349..352
FT /evidence="ECO:0007829|PDB:7CMN"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:7CMN"
FT STRAND 374..385
FT /evidence="ECO:0007829|PDB:7CMN"
FT HELIX 386..390
FT /evidence="ECO:0007829|PDB:7CMN"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:7CMN"
FT HELIX 394..396
FT /evidence="ECO:0007829|PDB:7CMN"
FT HELIX 400..413
FT /evidence="ECO:0007829|PDB:7CMN"
FT HELIX 419..433
FT /evidence="ECO:0007829|PDB:7CMN"
FT STRAND 437..446
FT /evidence="ECO:0007829|PDB:7CMN"
FT STRAND 450..454
FT /evidence="ECO:0007829|PDB:7CMN"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:7CMN"
FT STRAND 471..479
FT /evidence="ECO:0007829|PDB:7CMN"
SQ SEQUENCE 502 AA; 57978 MW; F810FB7C64726DB0 CRC64;
MMRLKQLNEM SASEFIHLLG GVFENSSWVA ERAEPNRPYS SFQSLYNKMV EIVETASDNE
QLKLIQMHPH LGTNVKITDF SQEEQKHAGL NELTKDEQNH LILLNQKYKD KFGFPFVMAV
RGKIKQEIFR TIKERLQNNH QTEFKQALEE IKKIAMFRLQ EIFREGENNS MTKHKERVMY
YGKGDVFAYR TYLKPLTGVR TIPESPFSGR DHILFGVNVK ISVGGTKLLT SFTKGDNSLV
VATDSMKNFI QKHLASYTGT TIEGFLEYVA TSFLKKYSHI EKISLIGEEI PFETTFAVKN
GNRAASELVF KKSRNEYATA YLNMVRNEDN TLNITEQQSG LAGLQLIKVS GNSFVGFIRD
EYTTLPEDSN RPLFVYLNIK WKYKNTEDSF GTNPENYVAA EQIRDIATSV FHETETLSIQ
HLIYLIGRRI LERFPQLQEV YFESQNHTWD KIVEEIPESE GKVYTEPRPP YGFQCFTVTQ
EDLPHENILM FSDEPDHKGA LK
