(data stored in SCRATCH zone)

SWISSPROT: D6XWK4_BACIE

ID   D6XWK4_BACIE            Unreviewed;       735 AA.
AC   D6XWK4;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 65.
DE   RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410};
DE            EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
GN   OrderedLocusNames=Bsel_0306 {ECO:0000313|EMBL:ADH97846.1};
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:ADH97846.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97846.1, 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|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,
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|RuleBase:RU003410};
CC   -!- PATHWAY: Genetic information processing; DNA replication.
CC       {ECO:0000256|RuleBase:RU003410}.
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase
CC       large chain family. {ECO:0000256|RuleBase:RU003410}.
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DR   EMBL; CP001791; ADH97846.1; -; Genomic_DNA.
DR   STRING; 439292.Bsel_0306; -.
DR   EnsemblBacteria; ADH97846; ADH97846; Bsel_0306.
DR   KEGG; bse:Bsel_0306; -.
DR   eggNOG; ENOG4105BZH; Bacteria.
DR   eggNOG; COG0209; LUCA.
DR   HOGENOM; HOG000057034; -.
DR   KO; K00525; -.
DR   OMA; LEIWHID; -.
DR   BioCyc; BSEL439292:G1GLR-331-MONOMER; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000000271; 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:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR013346; NrdE_NrdA.
DR   InterPro; IPR000788; RNR_lg_C.
DR   InterPro; IPR013509; RNR_lsu_N.
DR   InterPro; IPR008926; RNR_R1-su_N.
DR   InterPro; IPR039718; Rrm1.
DR   PANTHER; PTHR11573; PTHR11573; 1.
DR   Pfam; PF02867; Ribonuc_red_lgC; 1.
DR   Pfam; PF00317; Ribonuc_red_lgN; 1.
DR   PRINTS; PR01183; RIBORDTASEM1.
DR   SUPFAM; SSF48168; SSF48168; 1.
DR   TIGRFAMs; TIGR02506; NrdE_NrdA; 1.
DR   PROSITE; PS00089; RIBORED_LARGE; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6XWK4.
DR   SWISS-2DPAGE; D6XWK4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   DNA replication {ECO:0000256|RuleBase:RU003410};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003410,
KW   ECO:0000313|EMBL:ADH97846.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271}.
FT   DOMAIN      591    613       RIBORED_LARGE. {ECO:0000259|PROSITE:
FT                                PS00089}.
SQ   SEQUENCE   735 AA;  83904 MW;  8854F82B0848ADAF CRC64;
     MYEMERMTMS IRMEQTTRQT QMQDALNRVS MSEPHWTYKA AALFAEDLYE SAAKTRHLNT
     GEAYEDFPGL IFEGVRLGLY DNRLTEYYSP AELDEAASML NPDQDRLFTY PGLFLLADRY
     LTRTTDGELF ELPQERFLVI ALVLMMHEPQ EKRLALVREA YWAMSHLYMT VATPTLANAG
     KSHGQLSSCF IDTVDDSLDG IYLNNWDIAR LSKDGGGIGV YYGKVRALGS DIKGFKGNSS
     GVIPWIRQLN NTAVSVDQLG QRQGAIAVYL DVFHKDIMNG FLDLKTNNGD ERRKAHDIFT
     GVCLPDLFMK KLEETDENGR SIGEWHVFCP HEVKQIMGWK DKDGNPLGLE DFFDEADRPY
     FTEKYEEAVH HPLLPRETYR AMDIMARMMV SQLETGTPYF FYRDEVNRQN PNKIAGEPGR
     TTIYSSNLCT EIAQNMSPSV ITKEYETEEG DQVIVRKPGD FVVCNLSSVN LGNAGDPDIL
     KRLIPIQMRM LDNVIDLNQL PVQQARRTNS RYRAVGLGTF GWHHYLAKNQ IHWESDEAVQ
     EADRLYETIA YLAIEASAAL AREKGAYPAF KGSEWESGRY FERRGYTSAN WQTLKKTVSE
     SGVRNGWMMA VAPNSSTAKI GGSTDGIDPL YAVEFAEEKK NFKFLVTAPE LDHNTYPYYQ
     KTRHTLDQTW SIRQNAARQK HIDQGVSFNL YVHHAIRAKE LLSLHLEAWK QGLKTTYYIR
     STSQEEIESC DVCES
//

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