BNRDF_BPSPB
ID BNRDF_BPSPB Reviewed; 329 AA.
AC O64174;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Ribonucleoside-diphosphate reductase subunit beta;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleotide reductase small subunit;
GN Name=bnrdF; Synonyms=yosP;
OS Bacillus phage SPbeta (Bacillus phage SPBc2) (Bacteriophage SP-beta).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae; Spbetavirus.
OX NCBI_TaxID=66797;
OH NCBI_TaxID=1408; Bacillus pumilus (Bacillus mesentericus).
OH NCBI_TaxID=1423; Bacillus subtilis.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND SPLICING.
RX PubMed=9465078; DOI=10.1073/pnas.95.4.1692;
RA Lazarevic V., Soldo B., Duesterhoeft A., Hilbert H., Maueel C.,
RA Karamata D.;
RT "Introns and intein coding sequence in the ribonucleotide reductase genes
RT of Bacillus subtilis temperate bacteriophage SPbeta.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:1692-1697(1998).
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides (By similarity). {ECO:0000250}.
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:0000255|PROSITE-ProRule:PRU10014};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 2 iron ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Genetic information processing; DNA replication.
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000250}.
CC -!- MISCELLANEOUS: This gene has an intron within which is encoded yosQ, a
CC putative homing endonuclease.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC chain family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF020713; AAC13135.1; -; Genomic_DNA.
DR PIR; T12926; T12926.
DR RefSeq; NP_046714.1; NC_001884.1.
DR SMR; O64174; -.
DR GeneID; 1261446; -.
DR KEGG; vg:1261446; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000009091; Genome.
DR GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IEA:InterPro.
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; IPR026494; RNR_NrdF-like.
DR InterPro; IPR033909; RNR_small.
DR InterPro; IPR030475; RNR_small_AS.
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.
DR TIGRFAMs; TIGR04171; RNR_1b_NrdF; 1.
DR PROSITE; PS00368; RIBORED_SMALL; 1.
PE 2: Evidence at transcript level;
KW Deoxyribonucleotide synthesis; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..329
FT /note="Ribonucleoside-diphosphate reductase subunit beta"
FT /id="PRO_0000389011"
FT ACT_SITE 105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 66
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 97
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 97
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 164
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 329 AA; 38181 MW; EC36E9DFC12BD269 CRC64;
MTKIYDAANW SKHEDDFTQM FYNQNVKQFW LPEEIALNGD LLTWKYLGKN EQDTYMKVLA
GLTLLDTEQG NTGMPIVAEH VDGHQRKAVL NFMAMMENAV HAKSYSNIFL TLAPTEQINE
VFEWVKNNRF LQKKARTIVS VYKTIKKNDE ISLFKGMVAS VFLESFLFYS GFYYPLYFYG
QGKLMQSGEI INLIIRDEAI HGVYVGLLAQ EIYKKQTPQK QKELYAWALN LLQELYENEL
EYTEDVYDQV GLAPDVKKFI RYNANKALNN LGFDHWFEEE DVNPIVINGL NTKTKSHDFF
STKGNGYKKA TVEPLKDSDF IFTEKGCIQ
