HPYO_XANCP
ID HPYO_XANCP Reviewed; 473 AA.
AC Q8PDQ6;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=FAD-dependent urate hydroxylase {ECO:0000305|PubMed:23760935};
DE EC=1.14.13.- {ECO:0000269|PubMed:23760935};
DE EC=1.14.13.113 {ECO:0000269|PubMed:23760935};
DE AltName: Full=Flavoprotein urate hydroxylase {ECO:0000303|PubMed:23760935};
GN Name=hpyO {ECO:0000303|PubMed:23760935};
GN OrderedLocusNames=XCC0279 {ECO:0000312|EMBL:AAM39598.1};
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, COFACTOR, SUBUNIT, AND PATHWAY.
RX PubMed=23760935; DOI=10.1111/j.1758-2229.2012.00390.x;
RA Michiel M., Perchat N., Perret A., Tricot S., Papeil A., Besnard M.,
RA de Berardinis V., Salanoubat M., Fischer C.;
RT "Microbial urate catabolism: characterization of HpyO, a non-homologous
RT isofunctional isoform of the flavoprotein urate hydroxylase HpxO.";
RL Environ. Microbiol. Rep. 4:642-647(2012).
CC -!- FUNCTION: Catalyzes the hydroxylation of urate to 5-hydroxyisourate
CC (HIU). Is likely to be involved in the urate degradation pathway to
CC allantoin. Is slightly more efficient (about 2.6 times) with NADPH than
CC NADH as the electron donor. {ECO:0000269|PubMed:23760935}.
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:0000269|PubMed:23760935};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 + urate = 5-hydroxyisourate + H2O + NADP(+);
CC Xref=Rhea:RHEA:51532, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17775, ChEBI:CHEBI:18072,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000269|PubMed:23760935};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:23760935};
CC Note=FAD cannot be replaced by FMN or riboflavin.
CC {ECO:0000269|PubMed:23760935};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=29 uM for urate {ECO:0000269|PubMed:23760935};
CC KM=24 uM for NADH {ECO:0000269|PubMed:23760935};
CC KM=55 uM for NADPH {ECO:0000269|PubMed:23760935};
CC Note=kcat is 1.06 sec(-1) for the NADPH-dependent oxidation of urate.
CC {ECO:0000269|PubMed:23760935};
CC -!- PATHWAY: Purine metabolism; urate degradation.
CC {ECO:0000305|PubMed:23760935}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23760935}.
CC -!- SIMILARITY: Belongs to the HpyO family. {ECO:0000305|PubMed:23760935}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE008922; AAM39598.1; -; Genomic_DNA.
DR RefSeq; NP_635674.1; NC_003902.1.
DR RefSeq; WP_011035534.1; NC_003902.1.
DR AlphaFoldDB; Q8PDQ6; -.
DR SMR; Q8PDQ6; -.
DR STRING; 340.xcc-b100_0304; -.
DR DNASU; 999991; -.
DR EnsemblBacteria; AAM39598; AAM39598; XCC0279.
DR KEGG; xcc:XCC0279; -.
DR PATRIC; fig|190485.4.peg.310; -.
DR eggNOG; COG2072; Bacteria.
DR HOGENOM; CLU_044076_0_0_6; -.
DR OMA; NPYRWME; -.
DR BioCyc; MetaCyc:MON-18267; -.
DR BRENDA; 1.14.13.113; 6708.
DR UniPathway; UPA00394; -.
DR Proteomes; UP000001010; Chromosome.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0102099; F:FAD-dependent urate hydroxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0070404; F:NADH binding; IDA:UniProtKB.
DR GO; GO:0070402; F:NADPH binding; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019628; P:urate catabolic process; IGI:UniProtKB.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR038732; HpyO_NAD-binding.
DR Pfam; PF13454; NAD_binding_9; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Monooxygenase; NAD; NADP; Oxidoreductase;
KW Purine metabolism; Reference proteome.
FT CHAIN 1..473
FT /note="FAD-dependent urate hydroxylase"
FT /id="PRO_0000435888"
SQ SEQUENCE 473 AA; 51696 MW; A7F67F4C9BBC2963 CRC64;
MSLAQLEHAL QHDLQRLAHG GEPWVRPRVH PAGHVYDVVI VGAGQSGLGA AFALQRERVH
NVLVIDENPP GQEGPWVTYA RMQTLRTPKQ ITSIDLGVPT LTFRAWWEAQ HGAAGWDALD
KIPRGTWMDY LRWYRAALRL PVRNATQLVR IEPDAAPGIH RLHLAMGAPL MARKIILATG
IQGGGQWQVP EWITQALPAQ RYAHTSGPID YAALAGKRVG ILGGGASAFD NACFALDQGV
ARAEVFVRRA ALPRVNPIRH MEQAGIIPRF AALPDADKYR MMASFFGRNQ PPTNDTFQRA
CAHAGFALHL DAPWLGVEEH NDVVVVRTPQ GEHRFDFLAI ATGLVTDPRL RPELAALSGR
IACWADRYQA PPGQANPVLD AHPYLGPGFE LLPRTPDDAA AVDGLFAFNY SALINHGLSA
AALSGLKVAL PRLARAVADQ LFLDDRQAMV EAYLGYDQAE FVGQWPQPTQ AVA
