Ribonucleoside-diphosphate reductase subunit beta nrdF2

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Q50549 (RIR2B_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 83. History...

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

Documents (3) |

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

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. Source: MTBBASE deoxyribonucleoside diphosphate metabolic process Inferred from electronic annotation. Source: InterPro deoxyribonucleotide biosynthetic process Inferred from mutant phenotype. Source: MTBBASE growth Inferred from mutant phenotype. Source: MTBBASE
Cellular component	ribonucleoside-diphosphate reductase complex Inferred from direct assay Ref.1. Source: MTBBASE
Molecular function	protein binding Inferred from physical interaction Ref.1. Source: MTBBASE ribonucleoside-diphosphate reductase activity 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: 9335290] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, TYROSYL ACTIVE SITE, ENZYME REGULATION, FUNCTION IN ECOLI. 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: 9634230] [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: 12218036] [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: 14573627] [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: 15225619] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-296 WITH REDUCED IRON COFACTOR, TYROSYL ACTIVE SITE.
+	Additional computationally mapped references.

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.

PIR

C70861.

RefSeq

NP_337650.1. NC_002755.2.
YP_177921.1. NC_000962.2.

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.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBMYCT00000001867; EBMYCP00000001867; EBMYCG00000001865.
EBMYCT00000069712; EBMYCP00000067771; EBMYCG00000069707.

GeneID

888886.
922702.

GenomeReviews

Gene locus MT3133 in contig AE000516_GR.
Gene locus Rv3048c in contig AL123456_GR.

KEGG

mtc:MT3133.
mtu:Rv3048c.

PATRIC

18128652. VBIMycTub22151_3424.

TIGR

MT3133.

Organism-specific databases

TubercuList

Rv3048c.

Phylogenomic databases

GeneTree

EBGT00050000016987.

HOGENOM

HBG516660.

OMA

KYTEDLY.

PhylomeDB

Q50549.

ProtClustDB

PRK13966.

Family and domain databases

InterPro

IPR009078. Ferritin/RR-like.
IPR012348. Ribncl_red-rel.
IPR000358. Ribonucl_redctse.
[Graphical view]

Gene3D

G3DSA:1.10.620.20. Ribncl_red_rel. 1 hit.

K00526.

PANTHER

PTHR23409. Ribonucl_redctse. 1 hit.

Pfam

PF00268. Ribonuc_red_sm. 1 hit.
[Graphical view]

SUPFAM

SSF47240. Ferritin/RR_like. 1 hit.

PROSITE

PS00368. RIBORED_SMALL. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

RIR2B_MYCTU

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 20, 2010
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
This is version 83 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

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

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents