HPXO_ACIAD
ID HPXO_ACIAD Reviewed; 385 AA.
AC Q6F6Y2;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=ACIAD3540 {ECO:0000312|EMBL:CAG70183.1};
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP DISRUPTION PHENOTYPE, SUBUNIT, AND PATHWAY.
RC STRAIN=ATCC 33305 / BD413 / ADP1;
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 involved in the urate degradation pathway to allantoin.
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=76 uM for urate {ECO:0000269|PubMed:23760935};
CC KM=511 uM for NADPH {ECO:0000269|PubMed:23760935};
CC Note=kcat is 23.6 sec(-1) for the NADH-dependent oxidation of urate.
CC Exhibits a Michaelian behavior toward urate and NADPH and a
CC cooperative behavior toward NADH. {ECO:0000269|PubMed:23760935};
CC -!- PATHWAY: Purine metabolism; urate degradation.
CC {ECO:0000269|PubMed:23760935}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23760935}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are auxotrophic for
CC urate. Growth defect can be complemented by introduction of XCC0279
CC from X.campestris or Mvan_5278 from M.vanbaalenii.
CC {ECO:0000269|PubMed:23760935}.
CC -!- SIMILARITY: Belongs to the FAD-dependent urate hydroxylase family.
CC {ECO:0000305}.
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DR EMBL; CR543861; CAG70183.1; -; Genomic_DNA.
DR RefSeq; WP_004923273.1; NC_005966.1.
DR AlphaFoldDB; Q6F6Y2; -.
DR SMR; Q6F6Y2; -.
DR STRING; 62977.ACIAD3540; -.
DR EnsemblBacteria; CAG70183; CAG70183; ACIAD3540.
DR GeneID; 45235716; -.
DR KEGG; aci:ACIAD3540; -.
DR eggNOG; COG0654; Bacteria.
DR HOGENOM; CLU_009665_19_5_6; -.
DR OMA; RWMLGYD; -.
DR OrthoDB; 504558at2; -.
DR BioCyc; ASP62977:ACIAD_RS16010-MON; -.
DR UniPathway; UPA00394; -.
DR Proteomes; UP000000430; 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; IMP: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..385
FT /note="FAD-dependent urate hydroxylase"
FT /id="PRO_0000435886"
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 385 AA; 42916 MW; 96A17E3B4AB22FFE CRC64;
MNVVIIGAGM GGLTTGIALK KFGHQVTIFE QAEQILPVGA AISLWSNGVK CLNYLGLNEQ
IAKLGGQMDN LAYVDGLTGD VMTEFSLQPL IEEVGQRPYP VSRAELQNML MDEFGREDIH
LGKRMVALQQ KDDQVEIEFA DGSSILADVL VGADGTHSIT RTYVLGEKVE RRYAGYVNWN
GLVDISSDLA PADQWTTYVG EGKRASLMPV ADNRFYFFLD VPLEAGLEND KCKYKETLQS
YFKGWCPQVQ TLIERLDPQK TNRVEICDIE PFAQFYKGRV VLVGDAAHST TPDIGQGGCQ
AMEDAIYLAR SLQINTLSVE DALRRYQEKR NQRANELVLR ARKRCDVTHM KDEAVTTAWY
AELRQEKGLH IMNGIISNIV GNPLD
