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Database: UniProt
Entry: F2F1M9_SOLSS
LinkDB: F2F1M9_SOLSS
Original site: F2F1M9_SOLSS 
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
//
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