HIUH1_RHIME
ID HIUH1_RHIME Reviewed; 123 AA.
AC Q92VB9;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=5-hydroxyisourate hydrolase 1;
DE Short=HIU hydrolase 1;
DE Short=HIUHase 1;
DE EC=3.5.2.17;
GN OrderedLocusNames=RB0789; ORFNames=SMb21285;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymB (megaplasmid 2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481431; DOI=10.1073/pnas.161294698;
RA Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J.,
RA Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.;
RT "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing
RT endosymbiont Sinorhizobium meliloti.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(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; AL591985; CAC49189.1; -; Genomic_DNA.
DR PIR; E95940; E95940.
DR RefSeq; NP_437329.1; NC_003078.1.
DR RefSeq; WP_010975645.1; NC_003078.1.
DR AlphaFoldDB; Q92VB9; -.
DR SMR; Q92VB9; -.
DR STRING; 266834.SM_b21285; -.
DR EnsemblBacteria; CAC49189; CAC49189; SM_b21285.
DR GeneID; 25013732; -.
DR GeneID; 61600765; -.
DR KEGG; sme:SM_b21285; -.
DR PATRIC; fig|266834.11.peg.5719; -.
DR eggNOG; COG2351; Bacteria.
DR HOGENOM; CLU_115536_1_1_5; -.
DR OMA; MFRIDNG; -.
DR PRO; PR:Q92VB9; -.
DR Proteomes; UP000001976; Plasmid pSymB.
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; Plasmid; Purine metabolism; Reference proteome.
FT CHAIN 1..123
FT /note="5-hydroxyisourate hydrolase 1"
FT /id="PRO_0000050616"
FT BINDING 14
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 123 AA; 13512 MW; AFDA50E2550B1CE2 CRC64;
MQVQDGTPGR LTTHVLDTAS GRPASNLRID LYRIEGERPE LLSSTRTNDD GRCDAPLLNG
STMETGTYEL RFHAGEYLGT AAERGANPFL DVIPIRFGIA DRAAHYHVPL LLSPYGYSTY
RGS
