HIUH_SALDU
ID HIUH_SALDU Reviewed; 136 AA.
AC Q4VYA5; O85301;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 75.
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 AltName: Full=Transthyretin-related protein;
DE Short=TRP;
DE Flags: Precursor;
GN Name=hiuH; Synonyms=yedX;
OS Salmonella dublin.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=98360;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=2229;
RX PubMed=9723926; DOI=10.1046/j.1365-2958.1998.00984.x;
RA Wood M.W., Jones M.A., Watson P.R., Hedges S., Wallis T.S., Galyov E.E.;
RT "Identification of a pathogenicity island required for Salmonella
RT enteropathogenicity.";
RL Mol. Microbiol. 29:883-891(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-30, LACK OF
RP THYROID HORMONE BINDING, SUBUNIT, SUBCELLULAR LOCATION, AND MASS
RP SPECTROMETRY.
RX PubMed=16783790; DOI=10.1002/prot.21033;
RA Hennebry S.C., Wright H.M., Likic V.A., Richardson S.J.;
RT "Structural and functional evolution of transthyretin and transthyretin-
RT like proteins.";
RL Proteins 64:1024-1045(2006).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 27-136, CATALYTIC ACTIVITY,
RP SUBUNIT, AND MUTAGENESIS OF HIS-31; HIS-120 AND TYR-133.
RX PubMed=16787778; DOI=10.1016/j.jmb.2006.04.057;
RA Hennebry S.C., Law R.H.P., Richardson S.J., Buckle A.M., Whisstock J.C.;
RT "The crystal structure of the transthyretin-like protein from Salmonella
RT dublin, a prokaryote 5-hydroxyisourate hydrolase.";
RL J. Mol. Biol. 359:1389-1399(2006).
CC -!- FUNCTION: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-
CC 4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
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 Evidence={ECO:0000269|PubMed:16787778};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16783790,
CC ECO:0000269|PubMed:16787778}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:16783790}.
CC -!- MASS SPECTROMETRY: Mass=12872; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:16783790};
CC -!- MISCELLANEOUS: Despite its homology to transthyretins, is not able to
CC bind to the thyroid hormones thyroxine (T4) and triiodothyronine (T3).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAC33718.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF060858; AAC33718.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AJ972893; CAI99863.1; -; Genomic_DNA.
DR RefSeq; WP_000820358.1; NZ_VDCP01000004.1.
DR PDB; 2GPZ; X-ray; 2.50 A; A/C=27-136.
DR PDBsum; 2GPZ; -.
DR AlphaFoldDB; Q4VYA5; -.
DR SMR; Q4VYA5; -.
DR PATRIC; fig|98360.39.peg.3134; -.
DR OMA; ENQNYHI; -.
DR BRENDA; 3.5.2.17; 10258.
DR EvolutionaryTrace; Q4VYA5; -.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hydrolase; Periplasm;
KW Purine metabolism; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:16783790"
FT CHAIN 23..136
FT /note="5-hydroxyisourate hydrolase"
FT /id="PRO_5000074934"
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"
FT MUTAGEN 31
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16787778"
FT MUTAGEN 120
FT /note="H->A: Reduces activity by 90%."
FT /evidence="ECO:0000269|PubMed:16787778"
FT MUTAGEN 133
FT /note="Y->F: Reduces activity by 90%."
FT /evidence="ECO:0000269|PubMed:16787778"
FT STRAND 27..34
FT /evidence="ECO:0007829|PDB:2GPZ"
FT TURN 35..38
FT /evidence="ECO:0007829|PDB:2GPZ"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:2GPZ"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:2GPZ"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:2GPZ"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:2GPZ"
FT HELIX 90..96
FT /evidence="ECO:0007829|PDB:2GPZ"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:2GPZ"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:2GPZ"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:2GPZ"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:2GPZ"
SQ SEQUENCE 136 AA; 15105 MW; 6515448D6B1F889D CRC64;
MKRHILATVI ASLVAAPAMA LAAGNNILSV HILDQQTGKP APGVEVVLEQ KKDNGWTQLN
TGHTDQDGRI KALWPEKAAA PGDYRVIFKT GQYFESKKLD TFFPEIPVEF HISKTNEHYH
VPLLLSQYGY STYRGS
