HIUH_DANRE
ID HIUH_DANRE Reviewed; 138 AA.
AC Q06S87; Q0P422;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=5-hydroxyisourate hydrolase;
DE Short=HIU hydrolase;
DE Short=HIUHase;
DE EC=3.5.2.17;
DE AltName: Full=Transthyretin-related protein;
GN Name=urah;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), X-RAY CRYSTALLOGRAPHY (1.7
RP ANGSTROMS) OF 20-138, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-69, AND
RP SUBUNIT.
RX PubMed=16952372; DOI=10.1016/j.jmb.2006.07.079;
RA Zanotti G., Cendron L., Ramazzina I., Folli C., Percudani R., Berni R.;
RT "Structure of zebra fish HIUase: insights into evolution of an enzyme to a
RT hormone transporter.";
RL J. Mol. Biol. 363:1-9(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 44-138 (ISOFORM 2).
RC TISSUE=Liver;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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:16952372};
CC -!- PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from
CC urate: step 2/3.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q06S87-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q06S87-2; Sequence=VSP_030524;
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; DQ640307; ABG21128.1; -; mRNA.
DR EMBL; BC122322; AAI22323.1; -; mRNA.
DR RefSeq; XP_009291914.1; XM_009293639.2.
DR PDB; 2H1X; X-ray; 1.98 A; A/B/C/D=22-138.
DR PDB; 2H6U; X-ray; 1.70 A; A/B/C/D/E/F/G/H=22-138.
DR PDB; 3IWU; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-138.
DR PDB; 3IWV; X-ray; 1.68 A; A/B/C/D=1-138.
DR PDB; 3Q1E; X-ray; 1.95 A; A/B/C/D=20-138.
DR PDBsum; 2H1X; -.
DR PDBsum; 2H6U; -.
DR PDBsum; 3IWU; -.
DR PDBsum; 3IWV; -.
DR PDBsum; 3Q1E; -.
DR AlphaFoldDB; Q06S87; -.
DR SMR; Q06S87; -.
DR STRING; 7955.ENSDARP00000090143; -.
DR PaxDb; Q06S87; -.
DR Ensembl; ENSDART00000163471; ENSDARP00000138143; ENSDARG00000100719. [Q06S87-2]
DR ZFIN; ZDB-GENE-060825-253; uraha.
DR eggNOG; KOG3006; Eukaryota.
DR GeneTree; ENSGT00940000153229; -.
DR InParanoid; Q06S87; -.
DR OMA; ENQNYHI; -.
DR PhylomeDB; Q06S87; -.
DR BRENDA; 3.5.2.17; 928.
DR UniPathway; UPA00394; UER00651.
DR EvolutionaryTrace; Q06S87; -.
DR PRO; PR:Q06S87; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 18.
DR Bgee; ENSDARG00000100719; Expressed in liver and 16 other tissues.
DR ExpressionAtlas; Q06S87; baseline and differential.
DR GO; GO:0005777; C:peroxisome; NAS:ZFIN.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IDA:ZFIN.
DR GO; GO:0033971; F:hydroxyisourate hydrolase activity; IDA:ZFIN.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IDA:ZFIN.
DR GO; GO:0019628; P:urate catabolic process; IEA:UniProtKB-UniPathway.
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 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.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Hydrolase; Peroxisome;
KW Purine metabolism; Reference proteome.
FT CHAIN 1..138
FT /note="5-hydroxyisourate hydrolase"
FT /id="PRO_0000315283"
FT BINDING 31
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 71
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..43
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_030524"
FT MUTAGEN 69
FT /note="D->A: Reduces activity by 50%."
FT /evidence="ECO:0000269|PubMed:16952372"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:2H6U"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:3IWV"
FT TURN 35..38
FT /evidence="ECO:0007829|PDB:3IWV"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:3IWV"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:3IWV"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:3IWV"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:3IWV"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:3IWV"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:3IWV"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:3IWV"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:3IWV"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:3IWV"
SQ SEQUENCE 138 AA; 15486 MW; BC8EEBCFF5116862 CRC64;
MNRLQHIRGH IVSADKHINM SATLLSPLST HVLNIAQGVP GANMTIVLHR LDPVSSAWNI
LTTGITNDDG RCPGLITKEN FIAGVYKMRF ETGKYWDALG ETCFYPYVEI VFTITNTSQH
YHVPLLLSRF SYSTYRGS