Ribonucleoside-diphosphate reductase subunit beta nrdF2

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Q50549 (RIR2B_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 96. History...

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

Documents (4) |

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 subunit beta nrdF2
EC=1.17.4.1

Alternative name(s):
Ribonucleoside-diphosphate reductase nrdF2
Ribonucleotide reductase R2-2 small subunit

Gene names

Name:	nrdF2
Ordered Locus Names:	Rv3048c, MT3133

Organism

Mycobacterium tuberculosis [Reference proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	324 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Two genes for this protein are present in M.tuberculosis; this is the active form. When coexpressed in E.coli with nrdE the 2 proteins complement a temperature-sensitive E.coli mutant. Ref.1
Catalytic activity	2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H₂O = ribonucleoside diphosphate + thioredoxin. Ref.1
Cofactor	Binds 2 iron ions per subunit. Ref.5
Enzyme regulation	CDP reduction is stimulated by dATP. Ref.1
Pathway	Genetic information processing; DNA replication.
Subunit structure	Tetramer of two alpha and two beta subunits Probable.
Induction	Initially decreases as oxygen levels drop, then rises again. Ref.1 Ref.4
Disruption phenotype	Lethality. Ref.4
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	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication Inferred from mutant phenotype PubMed 19028890. Source: MTBBASE deoxyribonucleoside diphosphate metabolic process Inferred from electronic annotation. Source: InterPro deoxyribonucleotide biosynthetic process Inferred from mutant phenotype PubMed 19028890. Source: MTBBASE growth Inferred from mutant phenotype PubMed 12657046. Source: MTBBASE
Cellular_component	ribonucleoside-diphosphate reductase complex Inferred from direct assay Ref.1. Source: MTBBASE
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 – 324

324

Ribonucleoside-diphosphate reductase subunit beta nrdF2

PRO_0000393356

Sites

Active site

110

Ref.1 Ref.5

Metal binding

103

Iron 1

Metal binding

103

Iron 2

Metal binding

106

Iron 1

Metal binding

163

Iron 2

Metal binding

197

Iron 1

Metal binding

197

Iron 2

Metal binding

200

Iron 2

Secondary structure

324

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q50549 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 310C3BEC9029099E
Show »

FASTA

324

36,992

        10         20         30         40         50         60 
MTGNAKLIDR VSAINWNRLQ DEKDAEVWDR LTGNFWLPEK VPVSNDIPSW GTLTAGEKQL 

        70         80         90        100        110        120 
TMRVFTGLTM LDTIQGTVGA VSLIPDALTP HEEAVLTNIA FMESVHAKSY SQIFSTLCST 

       130        140        150        160        170        180 
AEIDDAFRWS EENRNLQRKA EIVLQYYRGD EPLKRKVAST LLESFLFYSG FYLPMYWSSR 

       190        200        210        220        230        240 
AKLTNTADMI RLIIRDEAVH GYYIGYKFQR GLALVDDVTR AELKDYTYEL LFELYDNEVE 

       250        260        270        280        290        300 
YTQDLYDEVG LTEDVKKFLR YNANKALMNL GYEALFPRDE TDVNPAILSA LSPNADENHD 

       310        320 
FFSGSGSSYV IGKAVVTEDD DWDF

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of two genes encoding the Mycobacterium tuberculosis ribonucleotide reductase small subunit." Yang F., Curran S.C., Li L.S., Avarbock D., Graf J.D., Chua M.M., Lu G., Salem J., Rubin H. J. Bacteriol. 179:6408-6415(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, TYROSYL ACTIVE SITE, ENZYME REGULATION, FUNCTION IN E.COLI. Strain: ATCC 35801 / TMC 107 / Erdman.
[2]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. Barrell B.G. Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[3]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[4]	"Ribonucleotide reduction in Mycobacterium tuberculosis: function and expression of genes encoding class Ib and class II ribonucleotide reductases." Dawes S.S., Warner D.F., Tsenova L., Timm J., McKinney J.D., Kaplan G., Rubin H., Mizrahi V. Infect. Immun. 71:6124-6131(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION, DISRUPTION PHENOTYPE. Strain: ATCC 25618 / H37Rv.
[5]	"Crystal structure of the biologically active form of class Ib ribonucleotide reductase small subunit from Mycobacterium tuberculosis." Uppsten M., Davis J., Rubin H., Uhlin U. FEBS Lett. 569:117-122(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-296 WITH REDUCED IRON COFACTOR, TYROSYL ACTIVE SITE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U41100 Genomic DNA. Translation: AAB81406.1.
AE000516 Genomic DNA. Translation: AAK47464.1.
BX842581 Genomic DNA. Translation: CAE55544.1.
AL123456 Genomic DNA. Translation: CCP45857.1.

PIR

C70861.

RefSeq

NP_337650.1. NC_002755.2.
YP_006516508.1. NC_018143.1.
YP_177921.1. NC_000962.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UZR	X-ray	2.20	A/B/C	1-296	[»]

ProteinModelPortal

Q50549.

SMR

Q50549. Positions 9-323.

ModBase

Search...

Protein-protein interaction databases

STRING

83332.Rv3048c.

Proteomic databases

PRIDE

Q50549.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAK47464; AAK47464; MT3133.

GeneID

13317851.
888886.
922702.

KEGG

mtc:MT3133.
mtu:Rv3048c.
mtv:RVBD_3048c.

PATRIC

18128652. VBIMycTub22151_3424.

Organism-specific databases

TubercuList

Rv3048c.

Phylogenomic databases

eggNOG

COG0208.

HOGENOM

HOG000246153.

K00526.

OMA

IGYKYQR.

ProtClustDB

PRK13966.

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.
IPR026494. RNR_1b_NrdF.
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.

TIGRFAMs

TIGR04171. RNR_1b_NrdF. 1 hit.

PROSITE

PS00368. RIBORED_SMALL. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q50549.

Entry information

Entry name

RIR2B_MYCTU

Accession

Primary (citable) accession number: Q50549
Secondary accession number(s): L0TBM8, Q6MX16, Q7D680

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 20, 2010
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents