ID   A0A1H1RJA4_9ACTN        Unreviewed;       969 AA.
AC   A0A1H1RJA4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|ARBA:ARBA00014409, ECO:0000256|RuleBase:RU364064};
DE            EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU364064};
GN   ORFNames=SAMN04488570_1705 {ECO:0000313|EMBL:SDS35867.1};
OS   Nocardioides scoriae.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=642780 {ECO:0000313|EMBL:SDS35867.1, ECO:0000313|Proteomes:UP000198859};
RN   [1] {ECO:0000313|Proteomes:UP000198859}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22127 {ECO:0000313|Proteomes:UP000198859};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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       {ECO:0000256|ARBA:ARBA00025437, ECO:0000256|RuleBase:RU364064}.
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|ARBA:ARBA00000206,
CC         ECO:0000256|RuleBase:RU364064};
CC   -!- COFACTOR:
CC       Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC         Evidence={ECO:0000256|ARBA:ARBA00001922,
CC         ECO:0000256|RuleBase:RU364064};
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase class-2
CC       family. {ECO:0000256|ARBA:ARBA00007405, ECO:0000256|RuleBase:RU364064}.
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DR   EMBL; LT629757; SDS35867.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1RJA4; -.
DR   STRING; 642780.SAMN04488570_1705; -.
DR   OrthoDB; 9762933at2; -.
DR   Proteomes; UP000198859; Chromosome i.
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 {ECO:0000256|ARBA:ARBA00022628, ECO:0000256|RuleBase:RU364064};
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285, ECO:0000256|RuleBase:RU364064};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   DNA synthesis {ECO:0000256|ARBA:ARBA00022634,
KW   ECO:0000256|RuleBase:RU364064};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU364064};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU364064}.
FT   DOMAIN          49..132
FT                   /note="Ribonucleotide reductase class II vitamin B12-
FT                   dependent N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08471"
FT   DOMAIN          153..688
FT                   /note="Ribonucleotide reductase large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02867"
SQ   SEQUENCE   969 AA;  105405 MW;  87E8C0305CE80229 CRC64;
     MTETVSSTGT ARGRRKGLKI EQTFSTPGVH PYDELTWERR DVVQTNWKTG ATVFEQRGVE
     YPDFWSVNAS TIVTTKYFRG AVGTDSREWS LKQLVDRVVK TYVAAGLEHG YFATEKDAQV
     FEHELTWLLV HQYFSFNSPV WFNVGTPSPQ QVSACFILSV DDSMDSILNW YKEEGFIFKG
     GSGAGLNLSR IRSSKELLSS GGTASGPVSF MRGADASAGT IKSGGATRRA AKMVVLDVDH
     PDIVEFVETK MKEEDKIRAL RDAGFDMDLG GNDITSVQYQ NANNSVRVSD EFMRAVEDGT
     GFGLRARDTG EVIETVDARA LFTKISEAAW ACADPGLQYD DTINDWHTNP ETGRITASNP
     CSEYMSLDNS SCNLASLNLL KFLKDDDTFD APLFAQAVEL IITAMDISIC FADFPTEPIG
     ETTRNYRQLG IGYANLGALL MAMGLGYDSD GGRSMAATIT SLMTGVSYKR SAELAAVVGP
     YAGYARNADA HKRVMRKHQA ANDVVRTLHG TDAAVHKLAT QAWADVQKLG EKNGFRNAQA
     SVLAPTGTIG FMMDCDTTGI EPDFSLVKFK KLVGGGSMQI VNQTIPRALK KLGYQTESIE
     AIVEFIADKG HVIDAPGLKT EHYEIFDTAM GARSLKPMGH VRMMAACQPF LSGAISKTVN
     LPESATVEEI EDVYLQSWKL GLKATAIYRD NCKVGQPLSD GKSDQAKKDQ GQSVDAPVVE
     TKVVEVHKPF RKRLPKSRAS LTTSFTVGGA EGYMTSGAHA DGELGEVFLK LGKQGSTLAG
     VMDAFSIAVS IGLQYGVPLE TYVSKFTNLR FEPSGMTDDP DIRMSQSLMD YVFRRLALDY
     LSFEERSMLG IYSAEERQRH LETGSYEPLE ETGGAAELKI AEAAPQEKGT GKDVDNRADD
     LETKDTHGAE AREVPAKVTS HEARTSAELL EKITGSAIDS PLCMTCGTKM RPAGSCYVCE
     GCGSTSGCS
//