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Uric acid degradation bifunctional protein [Includes: 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase (OHCU decarboxylase) (EC 4.1.1.97); Uricase (EC 1.7.3.3) (Urate oxidase)]

 PUCL_BACSB              Reviewed;         502 AA.
Q45697; Q9F1Q5;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
06-JUN-2002, sequence version 3.
25-OCT-2017, entry version 90.
RecName: Full=Uric acid degradation bifunctional protein;
Includes:
RecName: Full=2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase;
Short=OHCU decarboxylase;
EC=4.1.1.97;
Includes:
RecName: Full=Uricase;
EC=1.7.3.3;
AltName: Full=Urate oxidase;
Name=uao;
Bacillus sp. (strain TB-90).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=36824;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Nishiya Y., Hibi T., Oda J.;
"The full sequence of the gene encoding the diagnostic enzyme Bacillus
uricase.";
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-502.
PubMed=8907179; DOI=10.1093/oxfordjournals.jbchem.a021219;
Yamamoto K., Kojima Y., Kikuchi T., Shigyo T., Sugihara K.,
Takashio M., Emi S.;
"Nucleotide sequence of the uricase gene from Bacillus sp. TB-90.";
J. Biochem. 119:80-84(1996).
[3]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 171-489 IN COMPLEX WITH
INHIBITOR 8-AZAXANTHINE.
Mycobacterium tuberculosis structural genomics consortium (TB);
"Crystal structure of urate oxidase from Bacillus sp.";
Submitted (FEB-2009) to the PDB data bank.
-!- 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 (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-
imidazole-5-carboxylate = (S)-allantoin + CO(2).
-!- CATALYTIC ACTIVITY: Urate + O(2) + H(2)O = 5-hydroxyisourate +
H(2)O(2).
-!- PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from
urate: step 1/3.
-!- PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from
urate: step 3/3.
-!- MISCELLANEOUS: HIU and OHCU are unstable, they spontaneously
decompose to form a racemic mixture of allantoin.
-!- SIMILARITY: In the N-terminal section; belongs to the OHCU
decarboxylase family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the uricase
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA08723.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AB048366; BAB20808.1; -; Genomic_DNA.
EMBL; D49974; BAA08723.1; ALT_INIT; Genomic_DNA.
PIR; JC4535; JC4535.
PDB; 1J2G; X-ray; 2.20 A; A/B/C/D=171-489.
PDB; 3WLV; X-ray; 1.75 A; A/B/C/D=178-489.
PDB; 4XFP; X-ray; 1.66 A; A/B/C/D=178-494.
PDB; 5AYJ; X-ray; 2.05 A; A/B/C/D=172-502.
PDBsum; 1J2G; -.
PDBsum; 3WLV; -.
PDBsum; 4XFP; -.
PDBsum; 5AYJ; -.
ProteinModelPortal; Q45697; -.
SMR; Q45697; -.
DrugBank; DB01875; 8-Azaxanthine.
DrugBank; DB05321; PEG-uricase.
UniPathway; UPA00394; UER00650.
UniPathway; UPA00394; UER00652.
EvolutionaryTrace; Q45697; -.
GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
GO; GO:0004846; F:urate oxidase activity; IEA:UniProtKB-EC.
GO; GO:0019428; P:allantoin biosynthetic process; IEA:InterPro.
GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
GO; GO:0019628; P:urate catabolic process; IEA:UniProtKB-UniPathway.
Gene3D; 1.10.3330.10; -; 1.
InterPro; IPR018020; OHCU_decarboxylase.
InterPro; IPR017580; OHCU_decarboxylase-1.
InterPro; IPR036778; OHCU_decarboxylase_sf.
InterPro; IPR002042; Uricase.
InterPro; IPR019842; Uricase_CS.
Pfam; PF09349; OHCU_decarbox; 1.
Pfam; PF01014; Uricase; 2.
PRINTS; PR00093; URICASE.
SUPFAM; SSF158694; SSF158694; 1.
TIGRFAMs; TIGR03164; UHCUDC; 1.
TIGRFAMs; TIGR03383; urate_oxi; 1.
PROSITE; PS00366; URICASE; 1.
1: Evidence at protein level;
3D-structure; Decarboxylase; Lyase; Multifunctional enzyme;
Oxidoreductase; Purine metabolism.
CHAIN 1 502 Uric acid degradation bifunctional
protein.
/FTId=PRO_0000166005.
REGION 1 178 OHCU decarboxylase.
REGION 81 85 OHCU binding. {ECO:0000250}.
REGION 116 120 OHCU binding. {ECO:0000250}.
REGION 179 502 Urate oxidase.
REGION 243 244 Urate binding. {ECO:0000305|Ref.3}.
REGION 419 420 Urate binding. {ECO:0000305|Ref.3}.
ACT_SITE 68 68 Proton donor; for OHCU decarboxylase
activity. {ECO:0000250}.
ACT_SITE 183 183 Charge relay system; for urate oxidase
activity. {ECO:0000250|UniProtKB:D0VWQ1}.
ACT_SITE 243 243 Charge relay system; for urate oxidase
activity. {ECO:0000250|UniProtKB:D0VWQ1}.
BINDING 69 69 OHCU; via carbonyl oxygen. {ECO:0000250}.
BINDING 354 354 Urate. {ECO:0000305|Ref.3}.
BINDING 371 371 Urate. {ECO:0000305|Ref.3}.
STRAND 179 192 {ECO:0000244|PDB:4XFP}.
STRAND 213 224 {ECO:0000244|PDB:4XFP}.
HELIX 226 228 {ECO:0000244|PDB:4XFP}.
HELIX 229 233 {ECO:0000244|PDB:4XFP}.
HELIX 243 256 {ECO:0000244|PDB:4XFP}.
STRAND 259 261 {ECO:0000244|PDB:4XFP}.
HELIX 262 276 {ECO:0000244|PDB:4XFP}.
STRAND 282 289 {ECO:0000244|PDB:4XFP}.
STRAND 292 299 {ECO:0000244|PDB:4XFP}.
STRAND 302 312 {ECO:0000244|PDB:4XFP}.
STRAND 317 326 {ECO:0000244|PDB:4XFP}.
STRAND 332 352 {ECO:0000244|PDB:4XFP}.
STRAND 368 370 {ECO:0000244|PDB:4XFP}.
STRAND 374 385 {ECO:0000244|PDB:4XFP}.
HELIX 386 389 {ECO:0000244|PDB:4XFP}.
STRAND 391 393 {ECO:0000244|PDB:4XFP}.
HELIX 394 396 {ECO:0000244|PDB:4XFP}.
HELIX 400 413 {ECO:0000244|PDB:4XFP}.
HELIX 419 433 {ECO:0000244|PDB:4XFP}.
STRAND 437 446 {ECO:0000244|PDB:4XFP}.
STRAND 450 453 {ECO:0000244|PDB:3WLV}.
STRAND 463 465 {ECO:0000244|PDB:4XFP}.
STRAND 471 479 {ECO:0000244|PDB:4XFP}.
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


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