ID   HIUH_PSEAE              Reviewed;         126 AA.
AC   Q9I3J5;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=5-hydroxyisourate hydrolase;
DE            Short=HIU hydrolase;
DE            Short=HIUHase;
DE            EC=3.5.2.17;
GN   OrderedLocusNames=PA1518;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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}.
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; AE004091; AAG04907.1; -; Genomic_DNA.
DR   PIR; A83456; A83456.
DR   RefSeq; NP_250209.1; NC_002516.2.
DR   RefSeq; WP_003087207.1; NZ_CP053028.1.
DR   AlphaFoldDB; Q9I3J5; -.
DR   SMR; Q9I3J5; -.
DR   STRING; 287.DR97_504; -.
DR   PaxDb; Q9I3J5; -.
DR   PRIDE; Q9I3J5; -.
DR   DNASU; 879293; -.
DR   EnsemblBacteria; AAG04907; AAG04907; PA1518.
DR   GeneID; 879293; -.
DR   KEGG; pae:PA1518; -.
DR   PATRIC; fig|208964.12.peg.1570; -.
DR   PseudoCAP; PA1518; -.
DR   HOGENOM; CLU_115536_1_1_6; -.
DR   InParanoid; Q9I3J5; -.
DR   OMA; SVDPITC; -.
DR   PhylomeDB; Q9I3J5; -.
DR   BioCyc; PAER208964:G1FZ6-1545-MON; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0033971; F:hydroxyisourate hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006144; P:purine nucleobase metabolic process; IBA:GO_Central.
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..126
FT                   /note="5-hydroxyisourate hydrolase"
FT                   /id="PRO_0000050613"
FT   BINDING         16
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   126 AA;  13974 MW;  0C09578EE59D78F7 CRC64;
     MSASGRPQPM GRLTTHVLDS AHGCPGHGIK IELYRVEGQQ LELIATTLTN HDGRCDQPVL
     QGEDFRPGVY QLVFNAGDYY RARGVQLPEP AFLDQVVLRF GIASADDHYH VPLLISPYSY
     STYRGS