HIUH_DEIRA
ID HIUH_DEIRA Reviewed; 119 AA.
AC Q9RV69;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=5-hydroxyisourate hydrolase;
DE Short=HIU hydrolase;
DE Short=HIUHase;
DE EC=3.5.2.17;
GN OrderedLocusNames=DR_1161;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
CC -!- FUNCTION: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-
CC 4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-
CC dihydro-1H-imidazole-5-carboxylate + H(+); Xref=Rhea:RHEA:23736,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18072,
CC ChEBI:CHEBI:58639; EC=3.5.2.17;
CC -!- PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from
CC urate: step 2/3.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- MISCELLANEOUS: HIU hydrolysis also occurs spontaneously, but more
CC slowly.
CC -!- SIMILARITY: Belongs to the transthyretin family. 5-hydroxyisourate
CC hydrolase subfamily. {ECO:0000305}.
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DR EMBL; AE000513; AAF10734.1; -; Genomic_DNA.
DR PIR; D75430; D75430.
DR RefSeq; NP_294885.1; NC_001263.1.
DR RefSeq; WP_010887804.1; NZ_CP015081.1.
DR AlphaFoldDB; Q9RV69; -.
DR SMR; Q9RV69; -.
DR STRING; 243230.DR_1161; -.
DR EnsemblBacteria; AAF10734; AAF10734; DR_1161.
DR KEGG; dra:DR_1161; -.
DR PATRIC; fig|243230.17.peg.1359; -.
DR eggNOG; COG2351; Bacteria.
DR HOGENOM; CLU_115536_1_1_0; -.
DR InParanoid; Q9RV69; -.
DR OMA; ENQNYHI; -.
DR OrthoDB; 1955791at2; -.
DR UniPathway; UPA00394; UER00651.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0033971; F:hydroxyisourate hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IBA:GO_Central.
DR GO; GO:0019628; P:urate catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05822; TLP_HIUase; 1.
DR Gene3D; 2.60.40.180; -; 1.
DR InterPro; IPR014306; Hydroxyisourate_hydrolase.
DR InterPro; IPR023418; Thyroxine_BS.
DR InterPro; IPR000895; Transthyretin/HIU_hydrolase.
DR InterPro; IPR023416; Transthyretin/HIU_hydrolase_d.
DR InterPro; IPR036817; Transthyretin/HIU_hydrolase_sf.
DR InterPro; IPR023419; Transthyretin_CS.
DR PANTHER; PTHR10395; PTHR10395; 1.
DR Pfam; PF00576; Transthyretin; 1.
DR PRINTS; PR00189; TRNSTHYRETIN.
DR SUPFAM; SSF49472; SSF49472; 1.
DR TIGRFAMs; TIGR02962; hdxy_isourate; 1.
DR PROSITE; PS00768; TRANSTHYRETIN_1; 1.
DR PROSITE; PS00769; TRANSTHYRETIN_2; 1.
PE 3: Inferred from homology;
KW Hydrolase; Purine metabolism; Reference proteome.
FT CHAIN 1..119
FT /note="5-hydroxyisourate hydrolase"
FT /id="PRO_0000050612"
FT BINDING 10
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 119 AA; 12868 MW; CF86137F14DF5B2E CRC64;
MSGHPGLTTH VLDTARGKPA AGVRVQLCRV TGDTRTPVTE AVTNSDGRTD APLIERGSLK
QGTYELTFHV ADYFKGFVAA ADPPFLDVVT LRFTVGDTSG HYHVPLVMTP WSYSTYRGS
