ID B7USY0_ECO27 Unreviewed; 137 AA. AC B7USY0; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 24-JAN-2024, entry version 65. DE RecName: Full=5-hydroxyisourate hydrolase {ECO:0000256|ARBA:ARBA00017539, ECO:0000256|RuleBase:RU361270}; DE Short=HIU hydrolase {ECO:0000256|RuleBase:RU361270}; DE Short=HIUHase {ECO:0000256|RuleBase:RU361270}; DE EC=3.5.2.17 {ECO:0000256|ARBA:ARBA00012609, ECO:0000256|RuleBase:RU361270}; GN Name=yedX {ECO:0000313|EMBL:CAS09629.1}; GN OrderedLocusNames=E2348C_2081 {ECO:0000313|EMBL:CAS09629.1}; OS Escherichia coli O127:H6 (strain E2348/69 / EPEC). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS09629.1, ECO:0000313|Proteomes:UP000008205}; RN [1] {ECO:0000313|EMBL:CAS09629.1, ECO:0000313|Proteomes:UP000008205} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205}; RX PubMed=18952797; DOI=10.1128/JB.01238-08; RA Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R., RA Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A., RA Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.; RT "Complete genome sequence and comparative genome analysis of RT enteropathogenic Escherichia coli O127:H6 strain E2348/69."; RL J. Bacteriol. 191:347-354(2009). CC -!- FUNCTION: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo- CC 4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU). CC {ECO:0000256|ARBA:ARBA00002704}. 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:0000256|ARBA:ARBA00001043, CC ECO:0000256|RuleBase:RU361270}; CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881, CC ECO:0000256|RuleBase:RU361270}. CC -!- SIMILARITY: Belongs to the transthyretin family. 5-hydroxyisourate CC hydrolase subfamily. {ECO:0000256|ARBA:ARBA00009850, CC ECO:0000256|RuleBase:RU361270}. 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; FM180568; CAS09629.1; -; Genomic_DNA. DR RefSeq; WP_000920124.1; NC_011601.1. DR AlphaFoldDB; B7USY0; -. DR KEGG; ecg:E2348C_2081; -. DR HOGENOM; CLU_115536_3_0_6; -. DR OMA; CSENQNY; -. DR Proteomes; UP000008205; Chromosome. 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; Transthyretin/hydroxyisourate hydrolase domain; 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 NCBIfam; TIGR02962; hdxy_isourate; 1. DR PANTHER; PTHR10395:SF7; 5-HYDROXYISOURATE HYDROLASE; 1. DR PANTHER; PTHR10395; URICASE AND TRANSTHYRETIN-RELATED; 1. DR Pfam; PF00576; Transthyretin; 1. DR PRINTS; PR00189; TRNSTHYRETIN. DR SMART; SM00095; TR_THY; 1. DR SUPFAM; SSF49472; Transthyretin (synonym: prealbumin); 1. DR PROSITE; PS00768; TRANSTHYRETIN_1; 1. DR PROSITE; PS00769; TRANSTHYRETIN_2; 1. PE 3: Inferred from homology; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361270}; KW Purine metabolism {ECO:0000256|ARBA:ARBA00022631, KW ECO:0000256|RuleBase:RU361270}; KW Reference proteome {ECO:0000313|Proteomes:UP000008205}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..23 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 24..137 FT /note="5-hydroxyisourate hydrolase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5002864873" FT DOMAIN 24..136 FT /note="Transthyretin/hydroxyisourate hydrolase" FT /evidence="ECO:0000259|SMART:SM00095" FT BINDING 32 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR600895-51" FT BINDING 70 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR600895-51" FT BINDING 134 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR600895-51" SQ SEQUENCE 137 AA; 15479 MW; 0836235A3042E0AD CRC64; MLKRYLVLSV ATAAFSLPSL VYAAQQNILS VHILNQQTGK PAADVAVTLE KKADNGWLQL NTAKTDKDGR IKALWPEQTA TTGDYRVVFK TGDYFKKQNL ESFFPEIPVE FHINKVNEHY HVPLLLSQYG YSTYRGS //