HIUH_CAUVC
ID HIUH_CAUVC Reviewed; 115 AA.
AC Q9A545;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, 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;
GN OrderedLocusNames=CC_2620;
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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}.
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DR EMBL; AE005673; AAK24588.1; -; Genomic_DNA.
DR PIR; H87573; H87573.
DR RefSeq; NP_421420.1; NC_002696.2.
DR RefSeq; WP_010920473.1; NC_002696.2.
DR AlphaFoldDB; Q9A545; -.
DR SMR; Q9A545; -.
DR STRING; 190650.CC_2620; -.
DR EnsemblBacteria; AAK24588; AAK24588; CC_2620.
DR KEGG; ccr:CC_2620; -.
DR PATRIC; fig|190650.5.peg.2634; -.
DR eggNOG; COG2351; Bacteria.
DR HOGENOM; CLU_115536_1_1_5; -.
DR OMA; MFRIDNG; -.
DR BioCyc; CAULO:CC2620-MON; -.
DR Proteomes; UP000001816; 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; -; 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..115
FT /note="5-hydroxyisourate hydrolase"
FT /id="PRO_0000050611"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 7
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 115 AA; 12394 MW; FE4968B434F66D04 CRC64;
MSGLTTHILD QASGKPAAGV GVRVSRRDGE QTQWLAELRT DADGRARLVA GEDLAVGGYR
LEFAIGDHFK ASGLPVSDPP FLDVVVIDFA VSNLDQHWHV PLLVSPYGYS TYRGS
