ID   RIHB_SHIDS              Reviewed;         271 AA.
AC   Q32ER0;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=SDY_2104;
OS   Shigella dysenteriae serotype 1 (strain Sd197).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sd197;
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 42 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; CP000034; ABB62195.1; -; Genomic_DNA.
DR   RefSeq; YP_403686.1; NC_007606.1.
DR   AlphaFoldDB; Q32ER0; -.
DR   SMR; Q32ER0; -.
DR   STRING; 300267.SDY_2104; -.
DR   EnsemblBacteria; ABB62195; ABB62195; SDY_2104.
DR   KEGG; sdy:SDY_2104; -.
DR   PATRIC; fig|300267.13.peg.2534; -.
DR   HOGENOM; CLU_036838_2_0_6; -.
DR   OMA; REKAHEW; -.
DR   Proteomes; UP000002716; 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; Reference proteome.
FT   CHAIN           1..271
FT                   /note="Putative pyrimidine-specific ribonucleoside
FT                   hydrolase RihB"
FT                   /id="PRO_0000206828"
FT   BINDING         185
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   271 AA;  29164 MW;  044B86FD8E8074DD CRC64;
     MAALPINGLN VCQKLEINVP VYAGMPQPIM RQQIVADNIH GETGLDGPVF EPLTRQAEST
     HAVKYIIDTL MASDGDITLV PVGPLSNIAV AMRMQPAILP KIREIVLMGG AYGTGNFTPS
     AEFNIFADPE AARVVFTSGV PLVMMGLDLT NQTVCTPDVI ARMERAGGPA GELFSDIMNF
     TLKTQFENYG LAGGPVHDAT CIGYLINPDG IKTQDMYVEV DVNSGPCYGR TVCDELGVLG
     KPANTKVGIT IDTDWFWGLV EECVRGYIKT H