ID   RIHB_SHIBS              Reviewed;         242 AA.
AC   Q31YW9;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Putative pyrimidine-specific ribonucleoside hydrolase RihB;
DE            EC=3.2.2.8;
DE   AltName: Full=Cytidine/uridine-specific hydrolase;
GN   Name=rihB; OrderedLocusNames=SBO_2165;
OS   Shigella boydii serotype 4 (strain Sb227).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300268;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sb227;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a pyrimidine ribonucleoside + H2O = a pyrimidine nucleobase +
CC         D-ribose; Xref=Rhea:RHEA:56816, ChEBI:CHEBI:15377, ChEBI:CHEBI:26432,
CC         ChEBI:CHEBI:47013, ChEBI:CHEBI:141014; EC=3.2.2.8;
CC   -!- SIMILARITY: Belongs to the IUNH family. RihB subfamily. {ECO:0000305}.
CC   -!- CAUTION: This sequence is 71 amino acid shorter than orthologs and
CC       therefore lacks two conserved residues involved in calcium binding and
CC       active site activity. The two other residues involved in calcium
CC       binding are present but it is not known if they still bind calcium.
CC       {ECO:0000305}.
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DR   EMBL; CP000036; ABB66739.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q31YW9; -.
DR   SMR; Q31YW9; -.
DR   EnsemblBacteria; ABB66739; ABB66739; SBO_2165.
DR   KEGG; sbo:SBO_2165; -.
DR   HOGENOM; CLU_036838_2_2_6; -.
DR   OMA; REKAHEW; -.
DR   Proteomes; UP000007067; Chromosome.
DR   GO; GO:0050263; F:ribosylpyrimidine nucleosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:UniProt.
DR   GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR   Gene3D; 3.90.245.10; -; 1.
DR   InterPro; IPR001910; Inosine/uridine_hydrolase_dom.
DR   InterPro; IPR023186; IUNH.
DR   InterPro; IPR036452; Ribo_hydro-like.
DR   PANTHER; PTHR12304; PTHR12304; 1.
DR   Pfam; PF01156; IU_nuc_hydro; 1.
DR   SUPFAM; SSF53590; SSF53590; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase.
FT   CHAIN           1..242
FT                   /note="Putative pyrimidine-specific ribonucleoside
FT                   hydrolase RihB"
FT                   /id="PRO_0000206827"
FT   BINDING         156
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   242 AA;  26073 MW;  3405CA6FE71E399A CRC64;
     MRKQIVADNI HGETGLDGPV FESLTRQAES THAVKYIIDT LMASDGDITL VPVGPLSNIA
     VAMRMQPAIL PKIREIVLMG GAYGTGNFTP SAEFNIFADP EAARVVFTSG VPLVMIGLDL
     TNQTVCTPDV IARMERAGGP AGELFSDIMN FTLKTQFENY GLAGGPVHDA TCIGYLINPD
     GIKTQEMYVE VDVNSGPCYG RTVCDELGVL GKPANTKVGI TIDTDWFWGL VEECVRGYIK
     TH