ID F2F1M9_SOLSS Unreviewed; 697 AA.
AC F2F1M9;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 51.
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 OrderedLocusNames=SSIL_2469 {ECO:0000313|EMBL:BAK16892.1};
OS Solibacillus silvestris (strain StLB046) (Bacillus silvestris).
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Solibacillus.
OX NCBI_TaxID=1002809 {ECO:0000313|EMBL:BAK16892.1, ECO:0000313|Proteomes:UP000006691};
RN [1] {ECO:0000313|Proteomes:UP000006691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StLB046 {ECO:0000313|Proteomes:UP000006691};
RA Morohoshi T., Someya N., Ikeda T.;
RT "Genome sequence of Solibacillus silvestris StLB046.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAK16892.1, ECO:0000313|Proteomes:UP000006691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StLB046 {ECO:0000313|EMBL:BAK16892.1,
RC ECO:0000313|Proteomes:UP000006691};
RX PubMed=22019407; DOI=10.1016/j.jbiosc.2011.09.006;
RA Morohoshi T., Tominaga Y., Someya N., Ikeda T.;
RT "Complete genome sequence and characterization of the N-acylhomoserine
RT lactone-degrading gene of the potato leaf-associated Solibacillus
RT silvestris.";
RL J. Biosci. Bioeng. 113:20-25(2012).
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 -!- PATHWAY: Genetic information processing; DNA replication.
CC {ECO:0000256|ARBA:ARBA00005160, 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; AP012157; BAK16892.1; -; Genomic_DNA.
DR RefSeq; WP_014824129.1; NC_018065.1.
DR AlphaFoldDB; F2F1M9; -.
DR STRING; 1002809.SSIL_2469; -.
DR KEGG; siv:SSIL_2469; -.
DR PATRIC; fig|1002809.3.peg.2484; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_4_1_9; -.
DR OMA; RGSIQNI; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000006691; 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:UniProtKB-UniPathway.
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:SF30; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE 2 SUBUNIT ALPHA; 1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 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:UP000006691}.
FT DOMAIN 555..577
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 697 AA; 79859 MW; 1CF4DB7E42BE6340 CRC64;
MKQYLKLNND ILNRYRATGD LDLAKDKEAT RRYFLEDVNV RLRYFIDIEE KVRYLVDEGY
YEKEFLELYS MDFIKQMYKK AYSYKFRFPS FMSASKFYES YAMKSRDGKE ILEKYEDRIV
IIALYLAQGD EALAEKAIEA VMTAYQPATP TALNSGKKAR GELVSCFKLT MDDTMNSIAE
NIGYCLELSR LGGGVGVNLT DLRPLGDPIK GILNRASGVM PVAKLLENSF SYSNQLGQRN
GSGVVYLNVF HGDIEAFISS KKPNADDKIR LATLSTGIIL PDIFFELMRR DKDIVLFSSY
DIFKEYGKRM SEISITEMYY EFLDNPNIRK LKRLNARKLY TEIKKAQFES GYPFEIFDDN
VNNTHPLKEI GRVKMSNLCT EILQYQQTSV VTDQNEPNEY GLDVSCNLGS IDIHEATKVQ
DFGQLVDTAM RLLTNVSTMT DIVNVPSVSK ANKVMHSVGL GVMNLHGHLV QSGIRYGSKE
SIEFIDAFME SLNYHSLKAS MEIAKQKNET FYRFEESDYA SGVYFESYVN KEEKELTPEV
IKALGGTPII TRNMWEQLKS DVLKHGLFHS YRLAIAPTGS ISYIRSCTAS ISPVTERVEV
RDYADSRTIY PMPFLTNDNQ ELYTEAYEVN PYELIDLYAA AQKHVDQGIS MTLYVTDQWN
TEQLAKAYIY AWTKGIKTVY YVRQRLLTIE ECVACQI
//