ID   NRDJ_STRCL              Reviewed;         961 AA.
AC   O54196;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 2.
DT   24-JAN-2024, entry version 89.
DE   RecName: Full=Vitamin B12-dependent ribonucleotide reductase;
DE            EC=1.17.4.1;
DE   AltName: Full=Ribonucleoside-diphosphate reductase NrdJ;
GN   Name=nrdJ;
OS   Streptomyces clavuligerus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 /
RC   NRRL 3585 / VKM Ac-602;
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).
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   -!- SUBUNIT: Homotetramer.
CC   -!- DEVELOPMENTAL STAGE: Expressed during the exponential phase of growth.
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase class-2
CC       family. {ECO:0000305}.
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DR   EMBL; AJ224870; CAA12167.1; -; Genomic_DNA.
DR   AlphaFoldDB; O54196; -.
DR   SMR; O54196; -.
DR   STRING; 1901.BB341_05480; -.
DR   eggNOG; COG0209; Bacteria.
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   2: Evidence at transcript level;
KW   Cobalamin; Cobalt; Disulfide bond; DNA synthesis; Nucleotide-binding;
KW   Oxidoreductase.
FT   CHAIN           1..961
FT                   /note="Vitamin B12-dependent ribonucleotide reductase"
FT                   /id="PRO_0000229028"
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   961 AA;  104791 MW;  9C9D30730047A9F7 CRC64;
     MTETTSGPAR GSRTKGTKAT KGLRIERVHT TPGVHPYDEV VWERRDVVMT NWRDGSVNFE
     QRGVEFPDFW SVNAVNIVTS KYFRGAVGTP QRETGLKQLI DRIVKTYRKA GEEYKYFASP
     ADAEIFEHEL AYALLHQIFS FNSPVWFNVG TPQPQQVSAC FILSVDDSME SILDWYKEEG
     MIFKGGSGAG LNLSRIRSSK ELLSSGGNAS GPVSFMRGAD ASAGTIKSGG ATRRAAKMVI
     LDVDHPDIEG FIETKVKEEE KIRALRDAGF DMDLGGDDIT SVQYQNANNS VRVNDEFMRA
     VESGSAFGLR ARMTGEIIEQ VDAKALFRKM AQAAWACADP GIQYDDTINR WHTCPESGRI
     NGSNPCSEYM HLDNTSCNLA SLNLMKFLTD DGEGNQSFDV ERFAKVVELV ITAMDISICF
     ADFPTQKIGE NTRAFRQLGI GYANLGALLM ATGHAYDSDG GRAIAGAISS LMTGTSYRRS
     AELAAVVGPY DGYARNAAPH NQVMRQHADA NDTAVRMDDL DTPIWAAATE TWQDVLRLGE
     KNGFRNAQAS VIAPTGTIGL AMSCDTTGLE PDLALVKFKK LVGGGSMQIV NGTVPQALRR
     LGYQAEQIEA IVEHIAEHGN VLDAPGLKTE HYKVFDCAMG ERSISAMGHV RMMAAIQPWI
     SGALSKTVNM PESATVEEVE EIYFEAWKMG VKALAIYRDN CKVGQPLSAK TKEKEQDGIA
     EKTEDTIRAA VEKVIEYRPV RKRLPKGRPG ITTSFTVGGA EGYMTANSYP DDGLGEVFLK
     MSKQGSTLAG MMDAFSIAVS VGLQYGVPLE TYVSKFTNMR FEPAGMTDDP DVRMAQSIVD
     NIFRRLALDF LPFETRSALG IHSAEERQRH LDTGSYEQVI EEDELDVEGL AQSAPRQQIP
     AVPAAPAEIP APKQAHTSAE LVEMQLGISA DAPLCFSCGT KMQRAGSCYI CEGCGSTSGC
     S
//