ID   A0A2S1H214_9BACI        Unreviewed;       697 AA.
AC   A0A2S1H214;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
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   ORFNames=DCE79_09940 {ECO:0000313|EMBL:AWE07683.1};
OS   Lysinibacillus sp. 2017.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=2169540 {ECO:0000313|EMBL:AWE07683.1, ECO:0000313|Proteomes:UP000244315};
RN   [1] {ECO:0000313|Proteomes:UP000244315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2017 {ECO:0000313|Proteomes:UP000244315};
RA   Li J.;
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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; CP029002; AWE07683.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S1H214; -.
DR   KEGG; lyz:DCE79_09940; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000244315; Chromosome.
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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244315}.
FT   DOMAIN          555..577
FT                   /note="Ribonucleotide reductase large subunit"
FT                   /evidence="ECO:0000259|PROSITE:PS00089"
SQ   SEQUENCE   697 AA;  80072 MW;  5B748C4ACAFF5D3C CRC64;
     MKQYLKLNND ILNRYRATGD LDLTKDKEAT RRYFLEDVNV RLRYFIDIEE KVRYLVDEGY
     YEKEFLEQYS MDFIKEMYKK AYAYKFRFPS FMSASKFYES YAMKSRDGKE ILEKYEDRIV
     IISLYLAQGD EKLAEQAIDA IMTAYQPATP TALNSGKKAR GELVSCFKLT MDDTMNSIAE
     NIGYCLELSR LGGGVGVNLT DLRPLGDPIK GILNRASGVM PVAKLLENSF SYSNQLGQRN
     GSGVVYLNVF HGDIESFISS KKPNADDKIR LATLSTGIIL PDIFFELMRR DKDIVLFSSY
     DIYKEYGKRM SEISMTEMYY ELLDNPNIRK LKRLNARKLY TEIKKAQFES GYPFEIFDDN
     VNNVHPLKQI GRVKMSNLCT EILQYQQTSV ITDQNMPNEY GLDVSCNLGS IDIHEASKVY
     DFKQLVDTAM RLLTNVSTMT DIVNVPSVSK ANKKMHSVGL GVMNLHGHLV QAGIRYGSKE
     SIEFIDAFME AMNYYSLVSS VAIAKEKQET FYRFEESEYA SGAYFESYVN KKEIELSPEV
     LNALGNVPII TAQMWQELKQ QVMQHGLFHS YRIAIAPTGS ISYIRSCTAS IAPVTERVEV
     RDYADSRTIY PMPFLTNDNK ELYTEAYEVH PYELIDLYAA AQKHIDQGIS MTLYVTDQWN
     TEQLAKAYIY SWTKGIKTVY YVRQRLLTIE ECVACQI
//