ID   HPXO_KLEOX              Reviewed;         384 AA.
AC   B5B0J6;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=FAD-dependent urate hydroxylase;
DE            EC=1.14.13.113;
GN   Name=hpxO;
OS   Klebsiella oxytoca.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=571;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=M5a1;
RX   PubMed=19060149; DOI=10.1128/jb.01281-08;
RA   Pope S.D., Chen L.L., Stewart V.;
RT   "Purine utilization by Klebsiella oxytoca M5al: genes for ring-oxidizing
RT   and -opening enzymes.";
RL   J. Bacteriol. 191:1006-1017(2009).
CC   -!- FUNCTION: Catalyzes the hydroxylation of uric acid to 5-
CC       hydroxyisourate. {ECO:0000305|PubMed:19060149}.
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:19060149}.
CC   -!- DISRUPTION PHENOTYPE: Mutants fail to grow with hypoxanthine, xanthine
CC       or urate as the sole nitrogen source, but can grow with allantoin and
CC       allantoate. {ECO:0000269|PubMed:19060149}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent urate hydroxylase family.
CC       {ECO:0000305}.
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DR   EMBL; EU884423; ACG63335.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5B0J6; -.
DR   SMR; B5B0J6; -.
DR   STRING; 571.MC52_18915; -.
DR   eggNOG; COG0654; Bacteria.
DR   BRENDA; 1.14.13.113; 2811.
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_0000418846"
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;  42130 MW;  E5C78368377D6ED4 CRC64;
     MKALVIGGGI GGLSAAVGLK NAGIHCEVFE AVKEIKPVGA AISIWPNGVK CMKHLGMGDI
     IESYGGPMHF LAYKDYLRGE DLTQFSLAPL VERTGGRPCP VPALNLQREM LDFWGRDAVQ
     FGKRVTRCEE HADGVRVWFT DGSMAEGDFL IAADGSHSAL RPYVLGYTPE RRYAGYVNWN
     GLVEIDEAIA PGNQWTTFVG EGKRVSLMPV SDGRFYFFFD VPLPAGLAED RSTLRADLSR
     YFSGWAPQVQ KLIAALDPQT TNRIEIHDIE PFERLVRGKV ALLGDAGHST TPDIGQGGCA
     ALEDAVVLGD LFRESRDIAG VLRQYEAQRC DRVRDLVLKA RKRCDVTHGK DMALTQAWYQ
     ELETETGERI INGLCETIQG GPLG