Ribonucleoside-diphosphate reductase 1 subunit beta - Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

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P37427 (RIR2_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 104. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Ribonucleoside-diphosphate reductase 1 subunit beta
EC=1.17.4.1

Alternative name(s):
Protein B2
Protein R2
Ribonucleotide reductase 1

Gene names

Name:	nrdB
Ordered Locus Names:	STM2278

Organism

Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]

Taxonomic identifier

99287 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella ›

Protein attributes

Sequence length	376 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R2 contains the tyrosyl radical required for catalysis.
Catalytic activity	2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H₂O = ribonucleoside diphosphate + thioredoxin.
Cofactor	Binds 2 iron ions per subunit By similarity.
Pathway	Genetic information processing; DNA replication.
Subunit structure	Tetramer of two alpha (R1) and two beta (R2) subunits. The B1 protein is a dimer of alpha subunits. A radical transfer pathway occurs between Tyr-123 of R2 and R1 By similarity.
Miscellaneous	A substrate-binding catalytic site, located on R1, is formed only in the presence of the second subunit R2 By similarity.
Sequence similarities	Belongs to the ribonucleoside diphosphate reductase small chain family.

Ontologies

Keywords
Biological process	DNA replication
Ligand	Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: UniProtKB-UniPathway deoxyribonucleoside diphosphate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	ribonucleoside-diphosphate reductase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Inferred from electronic annotation. Source: EC transition metal ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 376

375

Ribonucleoside-diphosphate reductase 1 subunit beta

PRO_0000190478

Sites

Active site

123

By similarity

Metal binding

Iron 1 By similarity

Metal binding

116

Iron 1 By similarity

Metal binding

116

Iron 2 By similarity

Metal binding

119

Iron 1 By similarity

Metal binding

205

Iron 2 By similarity

Metal binding

239

Iron 2 By similarity

Metal binding

242

Iron 2 By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P37427 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A82E9F1ABE058226
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FASTA

376

43,552

        10         20         30         40         50         60 
MAYTTFSQTK NDQLKEPMFF GQPVNVARYD QQKYDIFEKL IEKQLSFFWR PEEVDVSRDR 

        70         80         90        100        110        120 
IDYQALPEHE KHIFISNLKY QTLLDSIQGR SPNVALLPLI SIPELETWVE TWAFSETIHS 

       130        140        150        160        170        180 
RSYTHIIRNI VNDPAVVFDD IVTNEQIQKR AEGISAYYDE LIEMTSYWHL LGEGTHTVNG 

       190        200        210        220        230        240 
KTVVVNLREL KKKLYLCLMS VNALEAIRFY VSFACSFAFA ERELMEGNAK IIRLIARDEA 

       250        260        270        280        290        300 
LHLTGTQHML NLLRSGVDDP EMAEIAEECK QECYDLFVQA AQQEKEWADY LFRDGSMIGL 

       310        320        330        340        350        360 
NKDILCQYVE YITNIRMQAV GLDLPFQTRS NPIPWINTWL VSDNVQVAPQ EVEVSSYLVG 

       370 
QIDSEVDTDD LSNFQL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. Wilson R.K. Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
[2]	"Cloning and sequencing of the genes from Salmonella typhimurium encoding a new bacterial ribonucleotide reductase." Jordan A., Gibert I., Barbe J. J. Bacteriol. 176:3420-3427(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-122.
[3]	Jordan A. Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 123-376.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE006468 Genomic DNA. Translation: AAL21179.1. X72948 Genomic DNA. Translation: CAA51453.1.
PIR	S32630.
RefSeq	NP_461220.1. NC_003197.1.
3D structure databases
ProteinModelPortal	P37427.
SMR	P37427. Positions 2-342.
ModBase	Search...
Protein-protein interaction databases
STRING	99287.STM2278.
Proteomic databases
PaxDb	P37427.
PRIDE	P37427.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAL21179; AAL21179; STM2278.
GeneID	1253800.
KEGG	stm:STM2278.
PATRIC	32383163. VBISalEnt20916_2411.
Phylogenomic databases
eggNOG	COG0208.
HOGENOM	HOG000278087.
KO	K00526.
OMA	LEPMFLG.
ProtClustDB	PRK09101.
Enzyme and pathway databases
UniPathway	UPA00326.
Family and domain databases
Gene3D	1.10.620.20. 1 hit.
InterPro	IPR009078. Ferritin-like_SF. IPR012348. RNR-rel. IPR000358. RNR_small. [Graphical view]
PANTHER	PTHR23409. PTHR23409. 1 hit.
Pfam	PF00268. Ribonuc_red_sm. 2 hits. [Graphical view]
SUPFAM	SSF47240. Ferritin/RR_like. 1 hit.
PROSITE	PS00368. RIBORED_SMALL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RIR2_SALTY

Accession

Primary (citable) accession number: P37427

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 104 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents