ID   HPXO_KLEPN              Reviewed;         384 AA.
AC   B6D1N4;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=FAD-dependent urate hydroxylase;
DE            EC=1.14.13.113;
GN   Name=hpxO;
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PATHWAY, DISRUPTION PHENOTYPE, AND GENE
RP   NAME.
RC   STRAIN=KC2653;
RX   PubMed=18849434; DOI=10.1128/jb.01022-08;
RA   de la Riva L., Badia J., Aguilar J., Bender R.A., Baldoma L.;
RT   "The hpx genetic system for hypoxanthine assimilation as a nitrogen source
RT   in Klebsiella pneumoniae: gene organization and transcriptional
RT   regulation.";
RL   J. Bacteriol. 190:7892-7903(2008).
CC   -!- FUNCTION: Catalyzes the hydroxylation of uric acid to 5-
CC       hydroxyisourate. {ECO:0000250|UniProtKB:A6T923}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADH + O2 + urate = 5-hydroxyisourate + H2O + NAD(+);
CC         Xref=Rhea:RHEA:27329, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:17775, ChEBI:CHEBI:18072,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.13.113;
CC         Evidence={ECO:0000250|UniProtKB:A6T923};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:A6T923};
CC   -!- PATHWAY: Purine metabolism; urate degradation.
CC       {ECO:0000269|PubMed:18849434}.
CC   -!- DISRUPTION PHENOTYPE: Mutants show impaired utilization of both
CC       hypoxanthine and uric acid as nitrogen sources.
CC       {ECO:0000269|PubMed:18849434}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent urate hydroxylase family.
CC       {ECO:0000305}.
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DR   EMBL; EU653284; ACF60813.1; -; Genomic_DNA.
DR   RefSeq; WP_020804972.1; NZ_WULK01000014.1.
DR   AlphaFoldDB; B6D1N4; -.
DR   SMR; B6D1N4; -.
DR   BioCyc; MetaCyc:MON-15359; -.
DR   UniPathway; UPA00394; -.
DR   GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR   GO; GO:0102099; F:FAD-dependent urate hydroxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; ISS:UniProtKB.
DR   GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0019628; P:urate catabolic process; ISS:UniProtKB.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Monooxygenase; NAD; Oxidoreductase; Purine metabolism.
FT   CHAIN           1..384
FT                   /note="FAD-dependent urate hydroxylase"
FT                   /id="PRO_0000418847"
FT   BINDING         11
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         30..31
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         43
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         125
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         178
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         204
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         216..218
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         285
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         295..299
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   SITE            204
FT                   /note="Involved in substrate activation for the transfer of
FT                   oxygen from the flavin hydroperoxide"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
SQ   SEQUENCE   384 AA;  42054 MW;  51CFD520268D2435 CRC64;
     MKAIVIGAGI GGLSAAVALK QSGIDCDVYE AVKEIKPVGA AISVWPNGVK CMAHLGMGDI
     METFGGPLRR MAYRDFRSGE NMTQFSLAPL IERTGSRPCP VSRAELQREM LDYWGRDSVQ
     FGKRVTRCEE DADGVTVWFT DGSSASGDLL IAADGSHSAL RPWVLGFTPQ RRYAGYVNWN
     GLVEIDEALA PGDQWTTFVG EGKRVSLMPV SAGRFYFFFD VPLPAGLAED RDTLRADLSR
     YFAGWAPPVQ KLIAALDPQT TNRIEIHDIE PFSRLVRGRV ALLGDAGHST TPDIGQGGCA
     AMEDAVVLGA VFRQTRDIAA ALCEYEAQRC DRVRDLVLKA RKRCDITHGK DMQLTEAWYQ
     ELREETGERI INGMCDTILS GPLG