ID Q0PBS3_CAMJE Unreviewed; 340 AA. AC Q0PBS3; DT 19-SEP-2006, integrated into UniProtKB/TrEMBL. DT 19-SEP-2006, sequence version 1. DT 04-NOV-2026, entry version 111. DE RecName: Full=Ribonucleoside-diphosphate reductase subunit beta {ECO:0000256|PIRNR:PIRNR000355}; DE EC=1.17.4.1 {ECO:0000256|PIRNR:PIRNR000355}; GN Name=nrdB {ECO:0000313|EMBL:CAL34386.1}; GN OrderedLocusNames=Cj0231c {ECO:0000313|EMBL:CAL34386.1}; OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / OS NCTC 11168). OC Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria; OC Campylobacterales; Campylobacteraceae; Campylobacter. OX NCBI_TaxID=192222 {ECO:0000313|EMBL:CAL34386.1, ECO:0000313|Proteomes:UP000000799}; RN [1] {ECO:0000313|EMBL:CAL34386.1, ECO:0000313|Proteomes:UP000000799} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700819 / NCTC 11168 {ECO:0000313|Proteomes:UP000000799}; RX PubMed=10688204; DOI=10.1038/35001088; RA Parkhill J., Wren B.W., Mungall K., Ketley J.M., Churcher C., Basham D., RA Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., RA Karlyshev A., Moule S., Pallen M.J., Penn C.W., Quail M., Rajandream M.A., RA Rutherford K.M., VanVliet A., Whitehead S., Barrell B.G.; RT "The genome sequence of the food-borne pathogen Campylobacter jejuni RT reveals hypervariable sequences."; RL Nature 403:665-668(2000). CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis. CC Catalyzes the biosynthesis of deoxyribonucleotides from the CC corresponding ribonucleotides. {ECO:0000256|PIRNR:PIRNR000355}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + [thioredoxin]- CC disulfide + H2O = a ribonucleoside 5'-diphosphate + [thioredoxin]- CC dithiol; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA- CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, CC ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1; CC Evidence={ECO:0000256|PIRNR:PIRNR000355}; CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; CC Evidence={ECO:0000256|PIRNR:PIRNR000355, CC ECO:0000256|PIRSR:PIRSR000355-2}; CC Note=Binds 2 iron ions per subunit. {ECO:0000256|PIRNR:PIRNR000355, CC ECO:0000256|PIRSR:PIRSR000355-2}; CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small CC chain family. {ECO:0000256|ARBA:ARBA00009303, CC ECO:0000256|PIRNR:PIRNR000355}. 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; AL111168; CAL34386.1; -; Genomic_DNA. DR PIR; G81440; G81440. DR RefSeq; WP_002851758.1; NC_002163.1. DR AlphaFoldDB; Q0PBS3; -. DR SMR; Q0PBS3; -. DR IntAct; Q0PBS3; 35. DR STRING; 192222.Cj0231c; -. DR PaxDb; 192222-Cj0231c; -. DR EnsemblBacteria; CAL34386; CAL34386; Cj0231c. DR KEGG; cje:Cj0231c; -. DR PATRIC; fig|192222.6.peg.225; -. DR eggNOG; COG0208; Bacteria. DR HOGENOM; CLU_035339_1_0_7; -. DR OMA; AACNNHW; -. DR OrthoDB; 9766544at2; -. DR UniPathway; UPA00326; -. DR Proteomes; UP000000799; Chromosome. DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC. DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:InterPro. DR CDD; cd01049; RNRR2; 1. DR Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 1. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR012348; RNR-like. DR InterPro; IPR033909; RNR_small. DR InterPro; IPR000358; RNR_small_fam. DR NCBIfam; NF007184; PRK09614.1-3; 1. DR PANTHER; PTHR23409; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SMALL CHAIN; 1. DR PANTHER; PTHR23409:SF18; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SUBUNIT M2; 1. DR Pfam; PF00268; Ribonuc_red_sm; 1. DR PIRSF; PIRSF000355; NrdB; 1. DR SUPFAM; SSF47240; Ferritin-like; 1. PE 3: Inferred from homology; KW Deoxyribonucleotide synthesis {ECO:0000256|PIRNR:PIRNR000355}; KW Iron {ECO:0000256|PIRNR:PIRNR000355, ECO:0000256|PIRSR:PIRSR000355-2}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR000355, KW ECO:0000256|PIRSR:PIRSR000355-2}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000355, KW ECO:0000313|EMBL:CAL34386.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000799}. FT ACT_SITE 126 FT /evidence="ECO:0000256|PIRSR:PIRSR000355-1" FT BINDING 88 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2" FT BINDING 119 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2" FT BINDING 119 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2" FT BINDING 122 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2" FT BINDING 184 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2" FT BINDING 218 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2" FT BINDING 221 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2" SQ SEQUENCE 340 AA; 39648 MW; 2CE627184370800C CRC64; MQRKRIYNPS SNETLGDRKV FDGNPHGILN FTKAKYTWAL KLWDLMEANT WFPKEVDTTK DALDYRCNLT AGEKRMYDLV WSQLISMDSF QTNNLADNIN PYITAPEINA VLARQAYEEA NHSKSYAVMV EAICDNTDLI YEMEKHDETL REKNDFISSI YEELAGDVDD NKLLLAMVAN QILEGVYFYS GFTAIYALAR AGKMLGSAQM IRFIQRDEIT HLLLFQNMIN SVRKERPDLF HDENINKIYD MFKKAGDLEI KWGKYITQNQ IMGFTDDIIE EYIHYLVDQR LSAINLDKLY NAKHPIKWVD DFSKFNDQKS NFFESKVTNY SKGSISFDDF //