ID I6DRB7_SHIBO Unreviewed; 304 AA. AC I6DRB7; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 03-SEP-2014, entry version 12. DE RecName: Full=Ribonucleoside-diphosphate reductase subunit beta; DE EC=1.17.4.1; GN Name=nrdF; ORFNames=SB444474_3513; OS Shigella boydii 4444-74. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=766140; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=4444-74; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis. CC Catalyzes the biosynthesis of deoxyribonucleotides from the CC corresponding ribonucleotides (By similarity). CC -!- CATALYTIC ACTIVITY: 2'-deoxyribonucleoside diphosphate + CC thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + CC thioredoxin. CC -!- COFACTOR: Binds 2 iron ions per subunit (By similarity). CC -!- PATHWAY: Genetic information processing; DNA replication. CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase CC small chain family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. 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; AKNB01000271; EIQ34309.1; -; Genomic_DNA. DR ProteinModelPortal; I6DRB7; -. DR SMR; I6DRB7; 4-289. DR EnsemblBacteria; EIQ34309; EIQ34309; SB444474_3513. DR UniPathway; UPA00326; -. DR GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IEA:InterPro. 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:0009186; P:deoxyribonucleoside diphosphate metabolic process; IEA:InterPro. DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.620.20; -; 1. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR012348; RNR-rel. DR InterPro; IPR026023; RNR_bsu_prok. DR InterPro; IPR026494; RNR_NrdF. DR InterPro; IPR000358; RNR_small. DR PANTHER; PTHR23409; PTHR23409; 1. DR Pfam; PF00268; Ribonuc_red_sm; 1. DR PIRSF; PIRSF000355; NrdB; 1. DR SUPFAM; SSF47240; SSF47240; 1. DR TIGRFAMs; TIGR04171; RNR_1b_NrdF; 1. DR PROSITE; PS00368; RIBORED_SMALL; 1. PE 3: Inferred from homology; KW DNA replication; Iron; Metal-binding; Oxidoreductase. SQ SEQUENCE 304 AA; 34772 MW; 62700FE3625AE5EF CRC64; MKLSRISAIN WNKISDDKDL EVWNRLTSNF WLPEKVPLSN DIPAWQTLTV VEQQLTMRVF TGLTLLDTLQ NVIGAPSLMP YALTPHEEAV LSNISFMEAV HARSYSSIFS TLCQTKDVDA AYAWSEENAP LQRKAQIIQQ HYRGDDPLKK KIASVFLESF LFYSGFWLPM YFSSRGKLTN TADLIRLIIR DEAVHGYYIG YKYQKNMEKI SLGQREELKS FAFDLLLELY DNELQYSDEL YAETPWADDV KAFLCYNANK ALMNLGYEPL FPAEMAEVNP AILAALSPNA DENHDFFSGS RIGN //