ID   NRDJ_STRCO              Reviewed;         967 AA.
AC   O69981;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 125.
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=SCO5805; ORFNames=SC4H2.26;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=11832503; DOI=10.1099/00221287-148-2-391;
RA   Borovok I., Kreisberg-Zakarin R., Yanko M., Schreiber R., Myslovati M.,
RA   Aaslund F., Holmgren A., Cohen G., Aharonowitz Y.;
RT   "Streptomyces spp. contain class Ia and class II ribonucleotide reductases:
RT   expression analysis of the genes in vegetative growth.";
RL   Microbiology 148:391-404(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND REGULATION.
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=15522084; DOI=10.1111/j.1365-2958.2004.04325.x;
RA   Borovok I., Gorovitz B., Yanku M., Schreiber R., Gust B., Chater K.,
RA   Aharonowitz Y., Cohen G.;
RT   "Alternative oxygen-dependent and oxygen-independent ribonucleotide
RT   reductases in Streptomyces: cross-regulation and physiological role in
RT   response to oxygen limitation.";
RL   Mol. Microbiol. 54:1022-1035(2004).
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.
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:0000305};
CC       Note=5'-deoxyadenosylcobalamine (coenzyme B12). {ECO:0000305};
CC   -!- DEVELOPMENTAL STAGE: Expressed during the exponential phase of growth.
CC   -!- INDUCTION: Induced by NrdR.
CC   -!- MISCELLANEOUS: Can grow normally using either of its two RNR systems.
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase class-2
CC       family. {ECO:0000305}.
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DR   EMBL; AL939125; CAA18341.1; -; Genomic_DNA.
DR   EMBL; AM039891; CAJ01782.1; -; Genomic_RNA.
DR   PIR; T35125; T35125.
DR   RefSeq; NP_629929.1; NC_003888.3.
DR   RefSeq; WP_011030467.1; NZ_VNID01000007.1.
DR   AlphaFoldDB; O69981; -.
DR   SMR; O69981; -.
DR   STRING; 100226.SCO5805; -.
DR   GeneID; 1101247; -.
DR   KEGG; sco:SCO5805; -.
DR   PATRIC; fig|100226.15.peg.5897; -.
DR   eggNOG; COG0209; Bacteria.
DR   HOGENOM; CLU_000404_0_1_11; -.
DR   InParanoid; O69981; -.
DR   OMA; WACADPG; -.
DR   PhylomeDB; O69981; -.
DR   Proteomes; UP000001973; 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; IBA:GO_Central.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR   CDD; cd02888; RNR_II_dimer; 1.
DR   InterPro; IPR013678; RNR_2_N.
DR   InterPro; IPR000788; RNR_lg_C.
DR   InterPro; IPR013344; RNR_NrdJ/NrdZ.
DR   Pfam; PF08471; Ribonuc_red_2_N; 1.
DR   Pfam; PF02867; Ribonuc_red_lgC; 1.
DR   PRINTS; PR01183; RIBORDTASEM1.
DR   TIGRFAMs; TIGR02504; NrdJ_Z; 1.
PE   2: Evidence at transcript level;
KW   Cobalamin; Cobalt; Disulfide bond; DNA synthesis; Nucleotide-binding;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..967
FT                   /note="Vitamin B12-dependent ribonucleotide reductase"
FT                   /id="PRO_0000229029"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        364
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        366
FT                   /note="Cysteine radical intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        368
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         159..160
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         364..368
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         554..558
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        160..377
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   967 AA;  105285 MW;  1A6522C328673A29 CRC64;
     MTETASGPAR SSRAKGTKAG KGLRVERVHT TPGVHPYDEV AWERRDVVMT NWRDGSVNFE
     QRGVEFPEFW SVNAVNIVTS KYFRGAVGTP QREVSLKQLI DRIVKTYRKA GEDNKYFASP
     ADAEIFEHEL AYALLHQIFS FNSPVWFNVG TPQPQQVSAC FILSVDDSME SILDWYKEEG
     MIFKGGSGAG LNLSRIRSSK ELLSSGGNAS GPVSFMRGAD ASAGTIKSGG ATRRAAKMVI
     LDVDHPDIED FIQTKVKEEE KIRALRDAGF DMDLGGDDIT SVQYQNANNS VRVNDTFMKA
     VQDGGKFGLT SRMTGEVIEE VDAKALFRKM AEAAWACADP GIQYDDTINA WHTCPESGRI
     NGSNPCSEYM HLDNTSCNLA SLNLMKFLKD DGKGNQSFDA ERFSKVVELV ITAMDISICF
     ADFPTQKIGE NTRAFRQLGI GYANLGALLM ATGHAYDSDG GRALAGAITS LMTGTSYRRS
     AELAAIVGPY DGYARNAKPH LRVMKQHSDE NAKAVRMDDL DTPIWAAATE AWQDVLRLGE
     KNGFRNSQAS VIAPTGTIGL AMSCDTTGLE PDLALVKFKK LVGGGSMQIV NGTVPQALRR
     LGYQEEQIEA IVAHIAENGN VIDAPGLKPE HYEVFDCAMG ERSISAMGHV RMMAAIQPWI
     SGALSKTVNL PESATVEDVE EVYFEAWKMG VKALAIYRDN CKVGQPLSAK TKTVKDTEKA
     EITEKTEAAI RETVEKVVEY RPVRKRLPKG RPGITTSFTV GGAEGYMTAN SYPDDGLGEV
     FLKMSKQGST LAGMMDAFSI AVSVGLQYGV PLETYVSKFT NMRFEPAGMT DDPDVRMAQS
     IVDYIFRRLA LDFLPFETRS ALGIHSAEER QRHLETGSYE PSDDELDVEG LAQSAPRAQE
     LVAVATPKAE AEAAKPAPQQ AHTSAELVEM QLGIQADAPL CFSCGTKMQR AGSCYICEGC
     GSTSGCS