RIHB_SHIFL
ID RIHB_SHIFL Reviewed; 313 AA.
AC Q83KF1; Q7C0V4;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Pyrimidine-specific ribonucleoside hydrolase RihB {ECO:0000255|HAMAP-Rule:MF_01433};
DE EC=3.2.2.8 {ECO:0000255|HAMAP-Rule:MF_01433};
DE AltName: Full=Cytidine/uridine-specific hydrolase {ECO:0000255|HAMAP-Rule:MF_01433};
GN Name=rihB {ECO:0000255|HAMAP-Rule:MF_01433};
GN OrderedLocusNames=SF2247, S2376;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: Hydrolyzes cytidine or uridine to ribose and cytosine or
CC uracil, respectively. Has a clear preference for cytidine over uridine.
CC Strictly specific for ribonucleosides. {ECO:0000255|HAMAP-
CC Rule:MF_01433}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_01433};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01433};
CC Note=Binds 1 Ca(2+) ion per monomer. {ECO:0000255|HAMAP-Rule:MF_01433};
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01433}.
CC -!- SIMILARITY: Belongs to the IUNH family. RihB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01433}.
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DR EMBL; AE005674; AAN43766.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP17583.1; -; Genomic_DNA.
DR RefSeq; NP_708059.1; NC_004337.2.
DR RefSeq; WP_000415462.1; NZ_WPGW01000017.1.
DR AlphaFoldDB; Q83KF1; -.
DR SMR; Q83KF1; -.
DR STRING; 198214.SF2247; -.
DR EnsemblBacteria; AAN43766; AAN43766; SF2247.
DR EnsemblBacteria; AAP17583; AAP17583; S2376.
DR GeneID; 1027307; -.
DR GeneID; 58388981; -.
DR KEGG; sfl:SF2247; -.
DR KEGG; sfx:S2376; -.
DR PATRIC; fig|198214.7.peg.2692; -.
DR HOGENOM; CLU_036838_2_0_6; -.
DR OMA; REKAHEW; -.
DR OrthoDB; 1763387at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050263; F:ribosylpyrimidine nucleosidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046133; P:pyrimidine ribonucleoside catabolic process; IEA:InterPro.
DR Gene3D; 3.90.245.10; -; 1.
DR HAMAP; MF_01433; Pyrim_hydro_RihB; 1.
DR InterPro; IPR001910; Inosine/uridine_hydrolase_dom.
DR InterPro; IPR023186; IUNH.
DR InterPro; IPR022977; Pyrim_hydro_RihB.
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 Calcium; Glycosidase; Hydrolase; Metal-binding; Reference proteome.
FT CHAIN 1..313
FT /note="Pyrimidine-specific ribonucleoside hydrolase RihB"
FT /id="PRO_0000206829"
FT ACT_SITE 11
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01433"
FT BINDING 11
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01433"
FT BINDING 16
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01433"
FT BINDING 124
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01433"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01433"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01433"
FT BINDING 240
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01433"
SQ SEQUENCE 313 AA; 33843 MW; 536DF74A9CEB5BBD CRC64;
MEKRKIILDC EPGHDDAIAM MMAAKHPAID LLGITIVAGN QTLDKTLING LNVCQKLEIN
VPVYAGMPQP IMRKQIVADN IHGETGLDGP VFEPLTRQAE STHAVKYIID TLMASDGDIT
LVPVGPLSNI AVAMRMQPAI LPKIREIVLM GGAYGTGNFT PSAEFNIFAD PEAARVVFTS
GVPLVMMGLD LTNQTVCTPD VIARMERVGG PAGELFSDIM NFTLKTQFEY YGLAGGPVHD
ATCIGYLINP DGIKTQDMYV EVDVNSGPCY GRTVCDELGV LGKPANTKVG ITIDTDWFWG
LVEECVRGYI KTH
