ID   NRDJ_STRCT              Reviewed;         599 AA.
AC   Q9XD73;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   13-SEP-2023, entry version 70.
DE   RecName: Full=Vitamin B12-dependent ribonucleotide reductase;
DE            EC=1.17.4.1;
DE   AltName: Full=Ribonucleoside-diphosphate reductase NrdJ;
DE   Flags: Fragment;
GN   Name=nrdJ;
OS   Streptantibioticus cattleyicolor (Streptomyces cattleya).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptantibioticus.
OX   NCBI_TaxID=29303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=18726346; DOI=10.1007/bf02879307;
RA   Shang G., Wang Y.;
RT   "Cloning of a regulatory gene from Streptomyces cattleya and study on its
RT   cis-acting element.";
RL   Sci. China, Ser. C, Life Sci. 43:418-424(2000).
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}.
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DR   EMBL; AF111267; AAD37499.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9XD73; -.
DR   SMR; Q9XD73; -.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
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   Gene3D; 3.20.70.20; -; 1.
DR   InterPro; IPR000788; RNR_lg_C.
DR   PANTHER; PTHR43371:SF1; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE; 1.
DR   PANTHER; PTHR43371; VITAMIN B12-DEPENDENT RIBONUCLEOTIDE REDUCTASE; 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; DNA synthesis; Nucleotide-binding; Oxidoreductase.
FT   CHAIN           1..599
FT                   /note="Vitamin B12-dependent ribonucleotide reductase"
FT                   /id="PRO_0000231662"
FT   REGION          519..555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         193..197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   599 AA;  64236 MW;  8679481ADA46B037 CRC64;
     MHLDNSSCNL ASLNLMKFLR DDTASDGASG AGGNMSLDAE RFAKVVELVI TAMDISICFA
     DFPTEKIGET TRAFRQLGIG YANLGALLMA TGHAYDSDGG RALAGAITSL MTGTSYRRSA
     ELAAVVGPYE GYARNADAHK RVMRQHADAN TAAQRMDDLD TPVWAAATEA WQDVLRLGEQ
     NRFRNAQASV LAPTGTIGLM MDCDTTGVEP DLALVKFKKL VGGGSMQIVN NTVPKALKRL
     GYQPEQVEAV VAHIAEHGNV IDAPGLKPEH YEVFDCAMGE RAISPMGHVR MMAAAQPFLS
     GAISKTVNMP ESATVEEIEE IYYEGWKLGL KALAIYRDNC KVGQPLSAKK KEEAKTEAPA
     EVEKVVEYRP VRKRLPKGRP GITTSFTVGG AEGYMTANSY PDDGLGEVFL KMSKQGSTLA
     GMMDAFSIAV SVGLQYGVPL ETYVSKFTNM RFEPAGLTDD PDVRMAQSIV DYIFRRLALD
     FLPFETRSAL GIHSAEERQR HLDTGSYEPA EDELDVEGLA QSAPRQAGPA KAATTAPAAK
     AQEPAAAPSP KQAHNSTELL EIQQGLNADA PLCFSCGTKM RRAGSCYVCE GCGSTSGCS
//