P43755 (RIR2_HAEIN) 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:	HI_1660

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus › Haemophilus influenzae

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 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 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	1	1	Removed By similarity
	Chain	2 – 376	375	Ribonucleoside-diphosphate reductase subunit beta		PRO_0000190479
Sites
	Active site	123	1	By similarity
	Metal binding	85	1	Iron 1 By similarity
	Metal binding	116	1	Iron 1 By similarity
	Metal binding	116	1	Iron 2 By similarity
	Metal binding	119	1	Iron 1 By similarity
	Metal binding	205	1	Iron 2 By similarity
	Metal binding	239	1	Iron 2 By similarity
	Metal binding	242	1	Iron 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	P43755 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: F3B8FD9EAF9C7238	FASTA	376	43,326
	10 20 30 40 50 60 MAYTTFSQNK NDQLKEPMFF GQNVNVARYD QQKYETFEKL IEKQLSFFWR PEEVDVSQDR 70 80 90 100 110 120 IDYAALPEHE KHIFISNLKY QTLLDSIQGR SPNVALLPLV SIPELETWIE TWTFSETIHS 130 140 150 160 170 180 RSYTHIIRNI VNDPSIVFDD IVTNEEIIKR AQDISSYYDD LIRDSQLYGL YGEGTYTVDG 190 200 210 220 230 240 KECVVTLRSL KKQLYLCLMS VNALEAIRFY VSFACSFAFA ERRLMEGNAK IIKFIARDEA 250 260 270 280 290 300 LHLTGTQHIL NIMAAGQDDP EMAEIAEECK QEAYDLFVAA AEQEKAWADY LFKDGSMIGL 310 320 330 340 350 360 NRDILVQYVE YITNIRMQAV GLPLPFQTRS NPIPWINAWL VSDNVQVAPQ EVEVSSYLVG 370 QIDSKVDTND FDDFSL

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42023 Genomic DNA. Translation: AAC23306.1.
PIR	C64135.
RefSeq	NP_439802.1. NC_000907.1.
3D structure databases
ProteinModelPortal	P43755.
SMR	P43755. Positions 2-342.
ModBase	Search...
Protein-protein interaction databases
STRING	71421.HI1660.
Proteomic databases
PRIDE	P43755.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC23306; AAC23306; HI_1660.
GeneID	950858.
KEGG	hin:HI1660.
PATRIC	20192069. VBIHaeInf48452_1738.
Phylogenomic databases
eggNOG	COG0208.
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_HAEIN

Accession

Primary (citable) accession number: P43755

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 103 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program