ID I6DRB7_SHIBO Unreviewed; 304 AA. AC I6DRB7; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 10-FEB-2021, entry version 41. DE RecName: Full=Ribonucleoside-diphosphate reductase subunit beta {ECO:0000256|PIRNR:PIRNR000355}; DE EC=1.17.4.1 {ECO:0000256|PIRNR:PIRNR000355}; GN Name=nrdF {ECO:0000313|EMBL:EIQ34309.1}; GN ORFNames=SB444474_3513 {ECO:0000313|EMBL:EIQ34309.1}; OS Shigella boydii 4444-74. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=766140 {ECO:0000313|EMBL:EIQ34309.1, ECO:0000313|Proteomes:UP000004199}; RN [1] {ECO:0000313|EMBL:EIQ34309.1, ECO:0000313|Proteomes:UP000004199} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4444-74 {ECO:0000313|EMBL:EIQ34309.1, RC ECO:0000313|Proteomes:UP000004199}; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., Jones K., RA 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. {ECO:0000256|PIRNR:PIRNR000355}. 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 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 -!- PATHWAY: Genetic information processing; DNA replication. CC {ECO:0000256|ARBA:ARBA00005160, ECO:0000256|PIRNR:PIRNR000355}. CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC {ECO:0000256|ARBA:ARBA00011209}. CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small CC chain family. {ECO:0000256|ARBA:ARBA00009303, CC ECO:0000256|PIRNR:PIRNR000355}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EIQ34309.1}. 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 RefSeq; WP_000777980.1; NZ_AKNB01000271.1. DR EnsemblBacteria; EIQ34309; EIQ34309; SB444474_3513. DR PATRIC; fig|766140.3.peg.3577; -. DR UniPathway; UPA00326; -. DR Proteomes; UP000004199; Unassembled WGS sequence. 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:0009263; P:deoxyribonucleotide biosynthetic process; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway. DR CDD; cd01049; RNRR2; 1. DR Gene3D; 1.10.620.20; -; 1. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR012348; RNR-like. DR InterPro; IPR026494; RNR_NrdF-like. DR InterPro; IPR033909; RNR_small. DR InterPro; IPR030475; RNR_small_AS. DR InterPro; IPR000358; RNR_small_fam. 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 {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:EIQ34309.1}. FT ACT_SITE 105 FT /evidence="ECO:0000256|PIRSR:PIRSR000355-1" FT METAL 67 FT /note="Iron 1" FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2" FT METAL 98 FT /note="Iron 1" FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2" FT METAL 98 FT /note="Iron 2" FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2" FT METAL 101 FT /note="Iron 1" FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2" FT METAL 158 FT /note="Iron 2" FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2" FT METAL 192 FT /note="Iron 2" FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2" FT METAL 195 FT /note="Iron 2" FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2" 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 //