RIHB_ECO57
ID RIHB_ECO57 Reviewed; 313 AA.
AC Q8XE94; Q7AC81;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=Z3419, ECs3054;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG57300.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36477.1; -; Genomic_DNA.
DR PIR; F91010; F91010.
DR PIR; H85854; H85854.
DR RefSeq; NP_311081.1; NC_002695.1.
DR RefSeq; WP_000415416.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8XE94; -.
DR SMR; Q8XE94; -.
DR STRING; 155864.EDL933_3326; -.
DR EnsemblBacteria; AAG57300; AAG57300; Z3419.
DR EnsemblBacteria; BAB36477; BAB36477; ECs_3054.
DR GeneID; 916758; -.
DR KEGG; ece:Z3419; -.
DR KEGG; ecs:ECs_3054; -.
DR PATRIC; fig|386585.9.peg.3183; -.
DR eggNOG; COG1957; Bacteria.
DR HOGENOM; CLU_036838_2_0_6; -.
DR OMA; REKAHEW; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0045437; F:uridine nucleosidase activity; IEA:UniProt.
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; IPR015910; I/U_nuclsd_hydro_CS.
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.
DR PROSITE; PS01247; IUNH; 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_0000206825"
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; 33720 MW; D002996A6873F5C9 CRC64;
MEKRKIILDC DPGHDDAIAI MMAAKHPAID LLGITIVAGN QTLDKTLING LNVCQKLEIN
VPVYAGMPQP IMRQQIVADN IHGDTGLDGP VFEPLTRQAE STHAVKYIID TLMASDGDIT
LVPVGPLSNI AVAMRMQPAI LPKIREIVLM GGAYGTGNFT PSAEFNIFAD PEAARVVFTS
GVPLVMMGLD LTNQTVCTPD VIARMERAGG PAGELFSDIM NFTLKTQFEN YGLAGGPVHD
ATCIGYLINP DGIKTQEMYV EVDVNSGPCY GRTVCDELGV LGKPANTKVG ITIDSDWFWG
LVEECVRGYI KTH
