HPXO_MYCVP
ID HPXO_MYCVP Reviewed; 395 AA.
AC A1TFU9;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=FAD-dependent urate hydroxylase {ECO:0000305|PubMed:23760935};
DE EC=1.14.13.113 {ECO:0000269|PubMed:23760935};
DE AltName: Full=Flavoprotein urate hydroxylase {ECO:0000303|PubMed:23760935};
GN Name=hpxO {ECO:0000303|PubMed:23760935};
GN OrderedLocusNames=Mvan_5278 {ECO:0000312|EMBL:ABM16049.1};
OS Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350058;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC PYR-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Anderson I.J., Miller C., Richardson P.;
RT "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, 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. Prefers NADH over NADPH as the electron donor.
CC {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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:23760935};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=413 uM for urate {ECO:0000269|PubMed:23760935};
CC Note=kcat is 56.0 sec(-1) for the NADH-dependent oxidation of urate.
CC Exhibits a Michaelian behavior only toward urate and a cooperative
CC behavior toward NADH and NADPH. {ECO:0000269|PubMed:23760935};
CC -!- PATHWAY: Purine metabolism; urate degradation.
CC {ECO:0000305|PubMed:23760935}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23760935}.
CC -!- SIMILARITY: Belongs to the FAD-dependent urate hydroxylase family.
CC {ECO:0000305}.
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; CP000511; ABM16049.1; -; Genomic_DNA.
DR RefSeq; WP_011782419.1; NC_008726.1.
DR AlphaFoldDB; A1TFU9; -.
DR SMR; A1TFU9; -.
DR STRING; 350058.Mvan_5278; -.
DR EnsemblBacteria; ABM16049; ABM16049; Mvan_5278.
DR KEGG; mva:Mvan_5278; -.
DR eggNOG; COG0654; Bacteria.
DR HOGENOM; CLU_009665_19_5_11; -.
DR OMA; PSQWAIF; -.
DR OrthoDB; 504558at2; -.
DR UniPathway; UPA00394; -.
DR Proteomes; UP000009159; 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; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Monooxygenase; NAD; Oxidoreductase; Purine metabolism;
KW Reference proteome.
FT CHAIN 1..395
FT /note="FAD-dependent urate hydroxylase"
FT /id="PRO_0000435887"
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 180
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 218..220
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 287
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 297..301
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT SITE 206
FT /note="Involved in substrate activation for the transfer of
FT oxygen from the flavin hydroperoxide"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
SQ SEQUENCE 395 AA; 42521 MW; 6A474A938E8C8CBC CRC64;
MKVVIVGAGM GGMSAAIALR QIGIDTVVYE RVTENKPVGA AISVWSNGVK CLNYLGLQEE
TAELGGKVET MSYVDGHTGD TMCRFSMHPL IEQVGQRPYP IARAELQLML MKAYGIDDIN
FGMKMVGVEN DTAGSAAKAT FADGTTVSAD VIIGADGAGS ITREYVLGGP VSRRYAGYVN
YNGLVSTDDA IGPATEWTTY VGDGKRVSVM PVSDDRFYFF FDVVEPQGSP YEEGRVREVL
RAHFAGWTPG VQTLIDTLDP LATNRVEILD LDPFHTWVKG RVAVLGDAAH NTTPDIGQGG
CSAMEDAIAL QWAFKDHPDD VHAALAAYQS ARTERAADLV LRARKRCDVT HAKDPQVTSR
WYDELRNEDG TNIIRGIVGN IVGGPLTPVT AATEG
