ID NRDJ_STRAW Reviewed; 964 AA. AC Q82KE2; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 116. DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase; DE EC=1.17.4.1; DE AltName: Full=Ribonucleoside-diphosphate reductase NrdJ; GN Name=nrdJ; OrderedLocusNames=SAV_2461; OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680). OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=227882; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / RC NRRL 8165 / MA-4680; RX PubMed=11572948; DOI=10.1073/pnas.211433198; RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., RA Sakaki Y., Hattori M.; RT "Genome sequence of an industrial microorganism Streptomyces avermitilis: RT deducing the ability of producing secondary metabolites."; RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / RC NRRL 8165 / MA-4680; RX PubMed=12692562; DOI=10.1038/nbt820; RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., RA Sakaki Y., Hattori M., Omura S.; RT "Complete genome sequence and comparative analysis of the industrial RT microorganism Streptomyces avermitilis."; RL Nat. Biotechnol. 21:526-531(2003). CC -!- FUNCTION: Catalyzes the reduction of ribonucleotides to CC deoxyribonucleotides. May function to provide a pool of CC deoxyribonucleotide precursors for DNA repair during oxygen limitation CC and/or for immediate growth after restoration of oxygen (By CC 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=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408; CC Evidence={ECO:0000250}; CC Note=5'-deoxyadenosylcobalamine (coenzyme B12). {ECO:0000250}; CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase class-2 CC 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; BA000030; BAC70172.1; -; Genomic_DNA. DR RefSeq; WP_010983898.1; NZ_JZJK01000086.1. DR AlphaFoldDB; Q82KE2; -. DR SMR; Q82KE2; -. DR KEGG; sma:SAVERM_2461; -. DR eggNOG; COG0209; Bacteria. DR HOGENOM; CLU_000404_0_1_11; -. DR OrthoDB; 9762933at2; -. DR Proteomes; UP000000428; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW. DR GO; GO:0050897; F:cobalt ion binding; IEA:InterPro. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC. DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW. DR CDD; cd02888; RNR_II_dimer; 1. DR Gene3D; 3.20.70.20; -; 1. DR InterPro; IPR013678; RNR_2_N. DR InterPro; IPR000788; RNR_lg_C. DR InterPro; IPR013344; RNR_NrdJ/NrdZ. DR NCBIfam; TIGR02504; NrdJ_Z; 1. DR PANTHER; PTHR43371:SF1; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE; 1. DR PANTHER; PTHR43371; VITAMIN B12-DEPENDENT RIBONUCLEOTIDE REDUCTASE; 1. DR Pfam; PF08471; Ribonuc_red_2_N; 1. DR Pfam; PF02867; Ribonuc_red_lgC; 1. DR PRINTS; PR01183; RIBORDTASEM1. DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1. PE 3: Inferred from homology; KW Cobalamin; Cobalt; Disulfide bond; DNA synthesis; Nucleotide-binding; KW Oxidoreductase; Reference proteome. FT CHAIN 1..964 FT /note="Vitamin B12-dependent ribonucleotide reductase" FT /id="PRO_0000231661" FT REGION 1..21 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 363 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 365 FT /note="Cysteine radical intermediate" FT /evidence="ECO:0000250" FT ACT_SITE 367 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 142 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 158..159 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 187 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 363..367 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 553..557 FT /ligand="substrate" FT /evidence="ECO:0000250" FT DISULFID 159..376 FT /note="Redox-active" FT /evidence="ECO:0000250" SQ SEQUENCE 964 AA; 105012 MW; 2C634475A49C6B42 CRC64; MTETASGPAR GSRAKGTKAK GLRIERIHTT PGVHPYDEVE WARRDVVMTN WRDGSVNFEQ RGVEFPDFWS VNAVNIVTSK YFRGAVGTPQ REVSLRQLID RIVKTYRKAG EDYKYFASPA DAEIFEHELA YALLHQIFSF NSPVWFNVGT PQPQQVSACF ILAVDDSMES ILDWYKEEGM IFKGGSGAGL NLSRIRSSKE LLSSGGNASG PVSFMRGADA SAGTIKSGGA TRRAAKMVIL DVDHPDIEDF IETKVKEEEK IRALRDAGFD MDLGGDDITS VQYQNANNSV RVNDTFMKAV EEGGKFGLTS RMTGEVIEEV DAKSLFRKMA EAAWACADPG IQYDDTINHW HTCPESGRIN GSNPCSEYMH LDNTSCNLAS LNLMKFLKDD GKGRQSFEVE RFAKVVELVI TAMDISICFA DFPTQKIGEN TRAFRQLGIG YANLGALLMA TGHAYDSDGG RALAGAITSL MTGTSYKRSA ELAAVVGPYD GYARNAQPHQ RVMKQHSDAN GVAVRVDDLD TPIWAAATEA WQDVLHLGEK NGFRNAQASV IAPTGTIGLA MSCDTTGLEP DLALVKFKKL VGGGSMQIVN GTVPQALRRL GYQEEQIEAI VAHIAENGNV IDAPGLKHEH YEVFDCAMGE RSISAMGHVR MMAAIQPWIS GALSKTVNLP ETATVEDVEE VYFEAWKMGV KALAIYRDNC KVGQPLSAKK KETEKAEVTA KTEATIREAV EKVVEYRPVR KRLPKGRPGI TTSFTVGGAE GYMTANSYPD DGLGEVFLKM SKQGSTLAGM MDAFSIAVSV GLQYGVPLET YVSKFTNMRF EPAGMTDDPD VRMAQSIVDY IFRRLALDFL PFETRSALGI HSAEERQRHL ETGSYEPSDD VDMDVEGLAQ SAPRAQELKA VATPKAEVAA AVPAPKQAHT SAELVEMQLG IQADAPLCFS CGTKMQRAGS CYICEGCGST SGCS //