ID   B0YPG6_BACTL            Unreviewed;       694 AA.
AC   B0YPG6;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
DE            EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
GN   Name=nrdE {ECO:0000313|EMBL:ABW06054.1};
OS   Bacillus thuringiensis subsp. alesti.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1440 {ECO:0000313|EMBL:ABW06054.1};
RN   [1] {ECO:0000313|EMBL:ABW06054.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AUCT 10114 {ECO:0000313|EMBL:ABW06054.1};
RX   PubMed=18032435; DOI=10.1093/nar/gkm1016;
RA   Nord D., Sjoberg B.M.;
RT   "Unconventional GIY-YIG homing endonuclease encoded in group I introns in
RT   closely related strains of the Bacillus cereus group.";
RL   Nucleic Acids Res. 36:300-310(2008).
CC   -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC       Catalyzes the biosynthesis of deoxyribonucleotides from the
CC       corresponding ribonucleotides. {ECO:0000256|RuleBase:RU003410}.
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:RU003410};
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC       chain family. {ECO:0000256|ARBA:ARBA00010406,
CC       ECO:0000256|RuleBase:RU003410}.
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DR   EMBL; EU043138; ABW06054.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0YPG6; -.
DR   UniPathway; UPA00326; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR   GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR   CDD; cd01679; RNR_I; 1.
DR   Gene3D; 1.10.1650.20; -; 1.
DR   Gene3D; 3.20.70.20; -; 1.
DR   InterPro; IPR013346; NrdE_NrdA_C.
DR   InterPro; IPR026459; RNR_1b_NrdE.
DR   InterPro; IPR000788; RNR_lg_C.
DR   InterPro; IPR013509; RNR_lsu_N.
DR   InterPro; IPR013554; RNR_N.
DR   InterPro; IPR008926; RNR_R1-su_N.
DR   InterPro; IPR039718; Rrm1.
DR   NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR   NCBIfam; TIGR04170; RNR_1b_NrdE; 1.
DR   PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR   PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR   Pfam; PF02867; Ribonuc_red_lgC; 1.
DR   Pfam; PF00317; Ribonuc_red_lgN; 1.
DR   Pfam; PF08343; RNR_N; 1.
DR   PRINTS; PR01183; RIBORDTASEM1.
DR   SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR   SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1.
DR   PROSITE; PS00089; RIBORED_LARGE; 1.
PE   3: Inferred from homology;
KW   Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW   ECO:0000256|RuleBase:RU003410};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003410}.
FT   DOMAIN          552..574
FT                   /note="Ribonucleotide reductase large subunit"
FT                   /evidence="ECO:0000259|PROSITE:PS00089"
SQ   SEQUENCE   694 AA;  79566 MW;  0D58AB781FC58A31 CRC64;
     MRHIELNNEI TQMQDGFYQL HKDKEALEVF MEEARENTVP FNSVAERMEY MKEHDYYYNV
     LDEYSLEEVE GVYNIAYGEN FEFQSYMAAS KFYKDYALKT NDQKQYLESY EDRVAIVSLY
     LGRGDVSKAK QFASMIVKQN YQPATPTFLN AGRSRRGEMV SCFLLEMDDS LNSIGFNINT
     AMQLSNIGGG VALNLSKLRA RGEQIKGIDN AACGVVPVMK LLEDSFSYAN QLGQRKGAGA
     VYLNIFHWDI IEFLDTKKIN ADEKSRIQSL SIGIIVPSKF FELAEKNEPF HVFAPYTVYK
     EYGKHLDDID IDEMYDELMS NPKVKKKPLD ISARDMLIKI AMIQLESGYP YLMFKSNANN
     QHPLKDIGTV KMSNLCTEIF QLQETSEIND YGTDDIIRRD INCNLGSLNI VNVMENKEIR
     EAVHAGMEAL TAVSDMTIIP NAPTVKKAND ELHSVGLGAM NLHGYLAKNK IADESAEAKE
     FARTFFMMLN YYSIEKSMEI ATEKGETFKD FDKSDYANGT YFEKYETTDY SPVTEKVQQL
     FEGIHIPTKE DWTSLKEQVQ KNGLYNSYRL AIAPTQSISY VQNATSSVMP IVSQIESRTY
     ANATTYYPMP YLSKDTFWYY KSSYDMNQFK LIDLIAEIQE HIDQGISTIL YVNSDISTRE
     LARYYIYAHK KGLKSLYYTR TRKLSVEECV ACTV
//