Q9ZKC3 (RIR2_HELPJ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Ribonucleotide reductase small subunit

Gene names

Name:	nrdB
Ordered Locus Names:	jhp_1016

Organism

Helicobacter pylori (strain J99) (Campylobacter pylori J99) [Complete proteome] [HAMAP]

Taxonomic identifier

85963 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter › Helicobacter pylori

Protein attributes

Sequence length	341 AA.
Sequence status	Complete.
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 By similarity.
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 and two beta subunits 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
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: UniProtKB-UniPathway deoxyribonucleoside diphosphate metabolic process Inferred from electronic annotation. Source: InterPro deoxyribonucleotide biosynthetic 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
	Chain	1 – 341	341	Ribonucleoside-diphosphate reductase subunit beta		PRO_0000190481
Sites
	Active site	127	1	By similarity
	Metal binding	89	1	Iron 1 By similarity
	Metal binding	120	1	Iron 1 By similarity
	Metal binding	120	1	Iron 2 By similarity
	Metal binding	123	1	Iron 1 By similarity
	Metal binding	185	1	Iron 2 By similarity
	Metal binding	219	1	Iron 2 By similarity
	Metal binding	222	1	Iron 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9ZKC3 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 248E7E1AE1E4CD74	FASTA	341	39,528
	10 20 30 40 50 60 MEVSRKKIYN PNSTESVNER KIFGGNPTSM FDLNKIKYQW ADHLWKTMLA NTWFAEEVSM 70 80 90 100 110 120 NDDKRDYLKL SAEEKIGYDR ALAQLIFMDS LQANNLIDNI NPFITSPEIN LCLVRQAYEE 130 140 150 160 170 180 ALHSHAYAVM VESISANTEE IYDMWRNDMQ LKSKNDYIAQ VYMELAKNPT EENILKALFA 190 200 210 220 230 240 NQILEGIYFY SGFSYFYTLA RSGKMLGSAQ MIRFIQRDEV THLILFQNMI NALRNERADL 250 260 270 280 290 300 FTPQLINEVI EMFKKAVEIE ASWGDYITQG KILGLTSSLI EQYIQFLADS RLSKVGIAKV 310 320 330 340 YGVQHPIKWV ESFSSFNEQR SNFFEARVSN YAKGSVSFDD F

References

[1]

"Genomic sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori." Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D. , Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J. Nature 397:176-180(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: J99.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE001439 Genomic DNA. Translation: AAD06604.1.
PIR	C71858.
RefSeq	NP_223733.1. NC_000921.1.
3D structure databases
ProteinModelPortal	Q9ZKC3.
ModBase	Search...
Protein-protein interaction databases
STRING	85963.jhp1016.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAD06604; AAD06604; jhp_1016.
GeneID	889653.
KEGG	hpj:jhp1016.
PATRIC	20606824. VBIHelPyl98156_1104.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0208.
KO	K00526.
OMA	LEPMFLG.
ProtClustDB	PRK09614.
Enzyme and pathway databases
BioCyc	HPYL85963:GJB9-1042-MONOMER.
UniPathway	UPA00326.
Family and domain databases
Gene3D	1.10.620.20. 1 hit.
InterPro	IPR009078. Ferritin-like_SF. IPR012348. RNR-rel. IPR026023. RNR_bsu_prok. IPR000358. RNR_small. [Graphical view]
PANTHER	PTHR23409. PTHR23409. 1 hit.
Pfam	PF00268. Ribonuc_red_sm. 1 hit. [Graphical view]
PIRSF	PIRSF000355. NrdB. 1 hit.
SUPFAM	SSF47240. Ferritin/RR_like. 1 hit.
PROSITE	PS00368. RIBORED_SMALL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RIR2_HELPJ

Accession

Primary (citable) accession number: Q9ZKC3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program