ID B5XQR7_KLEP3 Unreviewed; 384 AA.
AC B5XQR7;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=FAD-dependent urate hydroxylase {ECO:0000256|ARBA:ARBA00035262};
DE EC=1.14.13.113 {ECO:0000256|ARBA:ARBA00035128};
GN OrderedLocusNames=KPK_2712 {ECO:0000313|EMBL:ACI09147.1};
OS Klebsiella pneumoniae (strain 342).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=507522 {ECO:0000313|EMBL:ACI09147.1, ECO:0000313|Proteomes:UP000001734};
RN [1] {ECO:0000313|EMBL:ACI09147.1, ECO:0000313|Proteomes:UP000001734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=342 {ECO:0000313|EMBL:ACI09147.1,
RC ECO:0000313|Proteomes:UP000001734};
RX PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA Khouri H., Roesch L.F., Krogfelt K.A., Struve C., Triplett E.W.,
RA Methe B.A.;
RT "Complete genome sequence of the N2-fixing broad host range endophyte
RT Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL PLoS Genet. 4:E1000141-E1000141(2008).
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:0000256|ARBA:ARBA00035099};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Purine metabolism; urate degradation.
CC {ECO:0000256|ARBA:ARBA00004705}.
CC -!- SIMILARITY: Belongs to the FAD-dependent urate hydroxylase family.
CC {ECO:0000256|ARBA:ARBA00035121}.
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DR EMBL; CP000964; ACI09147.1; -; Genomic_DNA.
DR AlphaFoldDB; B5XQR7; -.
DR KEGG; kpe:KPK_2712; -.
DR HOGENOM; CLU_009665_19_5_6; -.
DR BioCyc; KPNE507522:GI0B-2702-MONOMER; -.
DR Proteomes; UP000001734; Chromosome.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProt.
DR GO; GO:0004846; F:urate oxidase activity; IEA:InterPro.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019628; P:urate catabolic process; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR047712; HpxO.
DR NCBIfam; NF033623; urate_HpxO; 1.
DR PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR PANTHER; PTHR13789:SF309; PUTATIVE (AFU_ORTHOLOGUE AFUA_6G14510)-RELATED; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Purine metabolism {ECO:0000256|ARBA:ARBA00022631}.
FT DOMAIN 2..337
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 384 AA; 42116 MW; A9118428794EC72F CRC64;
MKAIVIGAGI GGLSAAVALK QSGIDCDVYE AVKEIKPVGA AISVWPNGVK CMAHLGMGDI
METFGGPLRR MAYRDFRSGE NMTQFSLAPL IERTGSRPCP VSRAELQREM LDFWGRESVQ
FGKRVTRCEE DADGVTVWFT DGSSASGDLL IAADGSHSAL RPWVLGFTPQ RRYAGYVNWN
GLVEIDEALA PGDQWTTFVG EGKRVSLMPV SAGRFYFFFD VPLPAGLAED RDTLRADLSR
YFAGWAPPVQ QLIATLDPQT TNRIEIHDIE PFSRLVRGRV ALLGDAGHST TPDIGQGGCA
AMEDAVVLGA VFRQTHDIAA ALREYEAQRC DRVRDLVLKA RKRCDITHGK DMQLTEAWYQ
ELREETGERI INGMCDTILS GPLG
//
