ID RIR2_HALH5 Reviewed; 345 AA. AC Q9KFH7; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 143. DE RecName: Full=Ribonucleoside-diphosphate reductase subunit beta; DE EC=1.17.4.1; DE AltName: Full=Ribonucleotide reductase small subunit; GN Name=nrdB; OrderedLocusNames=BH0502; OS Halalkalibacterium halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 OS / JCM 9153 / C-125) (Bacillus halodurans). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; OC Halalkalibacterium (ex Joshi et al. 2022). OX NCBI_TaxID=272558; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125; RX PubMed=11058132; DOI=10.1093/nar/28.21.4317; RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.; RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans RT and genomic sequence comparison with Bacillus subtilis."; RL Nucleic Acids Res. 28:4317-4331(2000). CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis. CC Catalyzes the biosynthesis of deoxyribonucleotides from the CC corresponding ribonucleotides (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'- CC diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'- CC diphosphate; 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 -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250}; CC Note=Binds 2 iron ions per subunit. {ECO:0000250}; CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small CC chain family. {ECO:0000305}. 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; BA000004; BAB04221.1; -; Genomic_DNA. DR PIR; F83712; F83712. DR RefSeq; WP_010896680.1; NC_002570.2. DR PDB; 2RCC; X-ray; 1.90 A; A/B/C=1-345. DR PDBsum; 2RCC; -. DR AlphaFoldDB; Q9KFH7; -. DR SMR; Q9KFH7; -. DR STRING; 272558.gene:10726355; -. DR KEGG; bha:BH0502; -. DR eggNOG; COG0208; Bacteria. DR HOGENOM; CLU_035339_1_0_9; -. DR OrthoDB; 9766544at2; -. DR EvolutionaryTrace; Q9KFH7; -. DR Proteomes; UP000001258; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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:UniProtKB-KW. 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 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 1: Evidence at protein level; KW 3D-structure; Deoxyribonucleotide synthesis; Iron; Metal-binding; KW Oxidoreductase; Reference proteome. FT CHAIN 1..345 FT /note="Ribonucleoside-diphosphate reductase subunit beta" FT /id="PRO_0000190468" FT ACT_SITE 125 FT /evidence="ECO:0000250" FT BINDING 88 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 118 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 118 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 121 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 185 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 219 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 222 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250" FT STRAND 21..23 FT /evidence="ECO:0007829|PDB:2RCC" FT HELIX 40..49 FT /evidence="ECO:0007829|PDB:2RCC" FT HELIX 54..56 FT /evidence="ECO:0007829|PDB:2RCC" FT HELIX 60..65 FT /evidence="ECO:0007829|PDB:2RCC" FT HELIX 66..68 FT /evidence="ECO:0007829|PDB:2RCC" FT HELIX 71..86 FT /evidence="ECO:0007829|PDB:2RCC" FT TURN 87..90 FT /evidence="ECO:0007829|PDB:2RCC" FT HELIX 94..99 FT /evidence="ECO:0007829|PDB:2RCC" FT HELIX 105..132 FT /evidence="ECO:0007829|PDB:2RCC" FT HELIX 135..146 FT /evidence="ECO:0007829|PDB:2RCC" FT HELIX 149..167 FT /evidence="ECO:0007829|PDB:2RCC" FT HELIX 171..186 FT /evidence="ECO:0007829|PDB:2RCC" FT TURN 187..189 FT /evidence="ECO:0007829|PDB:2RCC" FT HELIX 190..201 FT /evidence="ECO:0007829|PDB:2RCC" FT HELIX 206..236 FT /evidence="ECO:0007829|PDB:2RCC" FT HELIX 238..240 FT /evidence="ECO:0007829|PDB:2RCC" FT HELIX 243..267 FT /evidence="ECO:0007829|PDB:2RCC" FT TURN 268..270 FT /evidence="ECO:0007829|PDB:2RCC" FT HELIX 277..294 FT /evidence="ECO:0007829|PDB:2RCC" SQ SEQUENCE 345 AA; 40242 MW; D89208F7518152BC CRC64; MEQLQKRKIY DTTASNASTG ILNGKSSNVL NWDDVRFSWA YPLYKNMLAN FWTPFEINMS HDAKQFPTLT ETEQEAFKKI IGLLAFLDSV QTDYSMRAAE YLTDSSLAAL MSVLSFQEVV HNQSYSYVLS SLVPKATQDE IFEYWKHDDV LKERNEFIID GYEKFVDNPT PKTFLESIVY DVILEGLNFY SGFAFFYNLA RNQKMVSTST MINYINRDEQ LHVYLFTNIF KELLVEFPEL NTEETKTFVK TTLMKAADLE KDWFRYIIGD KIPGINPEDM ETYISFIANK RAVQLGMEKP YPEIKHNPMK WIRAYEDVNS GKSDFFEQKS RQYAKVSADN GFDEL //