RIR2_SALTY
ID RIR2_SALTY Reviewed; 376 AA.
AC P37427;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Ribonucleoside-diphosphate reductase 1 subunit beta;
DE EC=1.17.4.1;
DE AltName: Full=Protein B2;
DE AltName: Full=Protein R2;
DE AltName: Full=Ribonucleotide reductase 1;
GN Name=nrdB; OrderedLocusNames=STM2278;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-122.
RX PubMed=8195103; DOI=10.1128/jb.176.11.3420-3427.1994;
RA Jordan A., Gibert I., Barbe J.;
RT "Cloning and sequencing of the genes from Salmonella typhimurium encoding a
RT new bacterial ribonucleotide reductase.";
RL J. Bacteriol. 176:3420-3427(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 123-376.
RA Jordan A.;
RL Submitted (JUL-1994) 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. R2 contains the tyrosyl radical required
CC for catalysis.
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 (R1) and two beta (R2) subunits. The B1
CC protein is a dimer of alpha subunits. A radical transfer pathway occurs
CC between Tyr-123 of R2 and R1 (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: A substrate-binding catalytic site, located on R1, is
CC formed only in the presence of the second subunit R2. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC chain family. {ECO:0000305}.
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DR EMBL; AE006468; AAL21179.1; -; Genomic_DNA.
DR EMBL; X72948; CAA51453.1; -; Genomic_DNA.
DR PIR; S32630; S32630.
DR RefSeq; NP_461220.1; NC_003197.2.
DR RefSeq; WP_000332026.1; NC_003197.2.
DR AlphaFoldDB; P37427; -.
DR SMR; P37427; -.
DR STRING; 99287.STM2278; -.
DR PaxDb; P37427; -.
DR PRIDE; P37427; -.
DR EnsemblBacteria; AAL21179; AAL21179; STM2278.
DR GeneID; 1253800; -.
DR KEGG; stm:STM2278; -.
DR PATRIC; fig|99287.12.peg.2411; -.
DR HOGENOM; CLU_062403_0_0_6; -.
DR OMA; KVGEYQR; -.
DR PhylomeDB; P37427; -.
DR BioCyc; SENT99287:STM2278-MON; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000001014; 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; IPR030475; RNR_small_AS.
DR InterPro; IPR000358; RNR_small_fam.
DR PANTHER; PTHR23409; PTHR23409; 1.
DR Pfam; PF00268; Ribonuc_red_sm; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
DR PROSITE; PS00368; RIBORED_SMALL; 1.
PE 3: Inferred from homology;
KW Deoxyribonucleotide synthesis; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..376
FT /note="Ribonucleoside-diphosphate reductase 1 subunit beta"
FT /id="PRO_0000190478"
FT ACT_SITE 123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 85
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 116
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 116
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 205
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 376 AA; 43552 MW; A82E9F1ABE058226 CRC64;
MAYTTFSQTK NDQLKEPMFF GQPVNVARYD QQKYDIFEKL IEKQLSFFWR PEEVDVSRDR
IDYQALPEHE KHIFISNLKY QTLLDSIQGR SPNVALLPLI SIPELETWVE TWAFSETIHS
RSYTHIIRNI VNDPAVVFDD IVTNEQIQKR AEGISAYYDE LIEMTSYWHL LGEGTHTVNG
KTVVVNLREL KKKLYLCLMS VNALEAIRFY VSFACSFAFA ERELMEGNAK IIRLIARDEA
LHLTGTQHML NLLRSGVDDP EMAEIAEECK QECYDLFVQA AQQEKEWADY LFRDGSMIGL
NKDILCQYVE YITNIRMQAV GLDLPFQTRS NPIPWINTWL VSDNVQVAPQ EVEVSSYLVG
QIDSEVDTDD LSNFQL
