(data stored in ACNUC7421 zone)

SWISSPROT: D6XWK3_BACIE

ID   D6XWK3_BACIE            Unreviewed;       347 AA.
AC   D6XWK3;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 64.
DE   RecName: Full=Ribonucleoside-diphosphate reductase subunit beta {ECO:0000256|PIRNR:PIRNR000355};
DE            EC=1.17.4.1 {ECO:0000256|PIRNR:PIRNR000355};
GN   OrderedLocusNames=Bsel_0305 {ECO:0000313|EMBL:ADH97845.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97845.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97845.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) 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|PIRNR:PIRNR000355}.
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,
CC         Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:50058, ChEBI:CHEBI:57930, ChEBI:CHEBI:73316;
CC         EC=1.17.4.1; Evidence={ECO:0000256|PIRNR:PIRNR000355};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000355,
CC         ECO:0000256|PIRSR:PIRSR000355-2};
CC       Note=Binds 2 iron ions per subunit.
CC       {ECO:0000256|PIRNR:PIRNR000355, ECO:0000256|PIRSR:PIRSR000355-2};
CC   -!- PATHWAY: Genetic information processing; DNA replication.
CC       {ECO:0000256|PIRNR:PIRNR000355}.
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase
CC       small chain family. {ECO:0000256|PIRNR:PIRNR000355}.
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DR   EMBL; CP001791; ADH97845.1; -; Genomic_DNA.
DR   RefSeq; WP_013171274.1; NC_014219.1.
DR   STRING; 439292.Bsel_0305; -.
DR   EnsemblBacteria; ADH97845; ADH97845; Bsel_0305.
DR   KEGG; bse:Bsel_0305; -.
DR   eggNOG; ENOG4105E05; Bacteria.
DR   eggNOG; COG0208; LUCA.
DR   HOGENOM; HOG000056923; -.
DR   KO; K00526; -.
DR   OMA; HWESLKP; -.
DR   OrthoDB; 1384440at2; -.
DR   BioCyc; BSEL439292:G1GLR-330-MONOMER; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000000271; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
DR   CDD; cd01049; RNRR2; 1.
DR   Gene3D; 1.10.620.20; -; 1.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR012348; RNR-like.
DR   InterPro; IPR033909; RNR_small.
DR   InterPro; IPR000358; RNR_small_fam.
DR   PANTHER; PTHR23409; PTHR23409; 1.
DR   Pfam; PF00268; Ribonuc_red_sm; 1.
DR   PIRSF; PIRSF000355; NrdB; 1.
DR   SUPFAM; SSF47240; SSF47240; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6XWK3.
DR   SWISS-2DPAGE; D6XWK3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   DNA replication {ECO:0000256|PIRNR:PIRNR000355};
KW   Iron {ECO:0000256|PIRNR:PIRNR000355, ECO:0000256|PIRSR:PIRSR000355-2};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000355,
KW   ECO:0000256|PIRSR:PIRSR000355-2};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000355,
KW   ECO:0000313|EMBL:ADH97845.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271}.
FT   ACT_SITE    127    127       {ECO:0000256|PIRSR:PIRSR000355-1}.
FT   METAL        90     90       Iron 1. {ECO:0000256|PIRSR:PIRSR000355-
FT                                2}.
FT   METAL       120    120       Iron 1. {ECO:0000256|PIRSR:PIRSR000355-
FT                                2}.
FT   METAL       120    120       Iron 2. {ECO:0000256|PIRSR:PIRSR000355-
FT                                2}.
FT   METAL       123    123       Iron 1. {ECO:0000256|PIRSR:PIRSR000355-
FT                                2}.
FT   METAL       187    187       Iron 2. {ECO:0000256|PIRSR:PIRSR000355-
FT                                2}.
FT   METAL       221    221       Iron 2. {ECO:0000256|PIRSR:PIRSR000355-
FT                                2}.
FT   METAL       224    224       Iron 2. {ECO:0000256|PIRSR:PIRSR000355-
FT                                2}.
SQ   SEQUENCE   347 AA;  40431 MW;  7EE8597B06003A60 CRC64;
     MIHEPMIRIP LLNPTHPNRS TGLIQGEASG ILNWNDIAYP HMYDLYQTLL ANFWKAQEIN
     MQDDIKQWAE LTPAEQDVFL RINTQLASLD SLQTPTMSQV MDYVTDPSFK AIFAIVAQQE
     AVHNESYSYV LSSLVNQQEQ TRRFQEAKED PLIQRRNDVI LSAYERFRQH PSPQHLFELA
     VQSLNLEGVY FYAGFAFFYH LARQQKMMKT STMISYIQRD EMQHAYFMSQ FVRILLTDHP
     ELNTRENVQY VYDAMASAAG LEQEWAAVIL ADIDGIDLGE FNGYVEYLVN KRLRQLGLSN
     LFPERDNPMP WIHVFSDTMM NQTKSDFFEQ KSRSYTKVTS DNGFDEL
//

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