ID   HIUH_BRUSU              Reviewed;         118 AA.
AC   Q8G228; G0K756;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=5-hydroxyisourate hydrolase;
DE            Short=HIU hydrolase;
DE            Short=HIUHase;
DE            EC=3.5.2.17;
DE   AltName: Full=Transthyretin-like protein BR0508/BS1330_I0509;
GN   OrderedLocusNames=BR0508, BS1330_I0509;
OS   Brucella suis biovar 1 (strain 1330).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=204722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=12271122; DOI=10.1073/pnas.192319099;
RA   Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA   Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA   Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA   Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT   "The Brucella suis genome reveals fundamental similarities between animal
RT   and plant pathogens and symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=22038969; DOI=10.1128/jb.06181-11;
RA   Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT   "Revised genome sequence of Brucella suis 1330.";
RL   J. Bacteriol. 193:6410-6410(2011).
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   -!- 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; AE014291; AAN29450.1; -; Genomic_DNA.
DR   EMBL; CP002997; AEM17863.1; -; Genomic_DNA.
DR   RefSeq; WP_004690637.1; NZ_KN046804.1.
DR   AlphaFoldDB; Q8G228; -.
DR   SMR; Q8G228; -.
DR   EnsemblBacteria; AEM17863; AEM17863; BS1330_I0509.
DR   GeneID; 45051614; -.
DR   GeneID; 55590259; -.
DR   KEGG; bms:BR0508; -.
DR   KEGG; bsi:BS1330_I0509; -.
DR   PATRIC; fig|204722.21.peg.3384; -.
DR   HOGENOM; CLU_115536_1_1_5; -.
DR   OMA; MFRIDNG; -.
DR   PhylomeDB; Q8G228; -.
DR   Proteomes; UP000007104; Chromosome I.
DR   GO; GO:0033971; F:hydroxyisourate hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
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.
FT   CHAIN           1..118
FT                   /note="5-hydroxyisourate hydrolase"
FT                   /id="PRO_0000050610"
FT   BINDING         7
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         46
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         115
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   118 AA;  13032 MW;  78C73D93E0178485 CRC64;
     MGKLSTHVLD TAHGTPAAAM RVELYRIAAS GTPELLKRVV TNLDGRTDAP LLSGDKMRTG
     IYELQFHVAE YFEGRGAELA HEPFLDLIPI RFGIADEDGN YHVPLLVSPW SYSTYRGS