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HIUH_SALTI
ID   HIUH_SALTI              Reviewed;         136 AA.
AC   Q8Z7Q6;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 128.
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;
DE            Short=TLP;
DE   Flags: Precursor;
GN   Name=hiuH; OrderedLocusNames=STY1129, t1822;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
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   -!- SUBCELLULAR LOCATION: Periplasm {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; AL513382; CAD08223.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO69443.1; -; Genomic_DNA.
DR   RefSeq; NP_455594.1; NC_003198.1.
DR   RefSeq; WP_000833187.1; NZ_WSUR01000018.1.
DR   AlphaFoldDB; Q8Z7Q6; -.
DR   SMR; Q8Z7Q6; -.
DR   STRING; 220341.16502271; -.
DR   EnsemblBacteria; AAO69443; AAO69443; t1822.
DR   KEGG; stt:t1822; -.
DR   KEGG; sty:STY1129; -.
DR   PATRIC; fig|220341.7.peg.1130; -.
DR   eggNOG; COG2351; Bacteria.
DR   HOGENOM; CLU_115536_3_0_6; -.
DR   OMA; ENQNYHI; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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   SMART; SM00095; TR_THY; 1.
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; Periplasm; Purine metabolism; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..136
FT                   /note="5-hydroxyisourate hydrolase"
FT                   /id="PRO_0000035774"
FT   BINDING         31
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         69
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         133
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   136 AA;  15076 MW;  BC57F7430907CB0E CRC64;
     MKRYILATAI ASLVAAPAMA LAAGSNILSV HILDQQTGKP APGVEVVLEQ KKDNGWTQLN
     TGHTDQDGRI KALWPEKAAA PGDYRVIFKT GQYFESKKLD TFFPEIPVEF HISKTNEHYH
     VPLLLSQYGY STYRGS
 
 
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