RIHB_ECO5E
ID RIHB_ECO5E Reviewed; 313 AA.
AC B5YWV3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=ECH74115_3298;
OS Escherichia coli O157:H7 (strain EC4115 / EHEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=444450;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC4115 / EHEC;
RX PubMed=22135463; DOI=10.1073/pnas.1107176108;
RA Eppinger M., Mammel M.K., Leclerc J.E., Ravel J., Cebula T.A.;
RT "Genomic anatomy of Escherichia coli O157:H7 outbreaks.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20142-20147(2011).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001164; ACI35147.1; -; Genomic_DNA.
DR RefSeq; WP_000415416.1; NC_011353.1.
DR AlphaFoldDB; B5YWV3; -.
DR SMR; B5YWV3; -.
DR KEGG; ecf:ECH74115_3298; -.
DR HOGENOM; CLU_036838_2_0_6; -.
DR OMA; REKAHEW; -.
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.
FT CHAIN 1..313
FT /note="Pyrimidine-specific ribonucleoside hydrolase RihB"
FT /id="PRO_1000145828"
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