Q10840 (RIR2A_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribonucleoside-diphosphate reductase subunit beta nrdF1
EC=1.17.4.1

Alternative name(s):
Ribonucleotide reductase R2-1 small subunit
Ribonucleotide reductase small subunit 1

Gene names

Name:	nrdF1
Ordered Locus Names:	Rv1981c, MT2033
ORF Names:	MTCY39.38

Organism

Mycobacterium tuberculosis [Reference proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	322 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 By similarity. Two genes for this protein are present in M.tuberculosis; this is thought to not be the active form. When coexpressed in E.coli with nrdE the 2 proteins do not complement a temperature-sensitive E.coli mutant, whereas the other gene (nrdF2) does complement. Ref.1
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.
Induction	Expressed in growing cells (at protein level). Transcription not induced under oxygen-limiting conditions. 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	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 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 – 322	322	Ribonucleoside-diphosphate reductase subunit beta nrdF1		PRO_0000190486
Sites
	Active site	108	1	By similarity
	Metal binding	70	1	Iron 1 By similarity
	Metal binding	101	1	Iron 1 By similarity
	Metal binding	101	1	Iron 2 By similarity
	Metal binding	104	1	Iron 1 By similarity
	Metal binding	161	1	Iron 2 By similarity
	Metal binding	195	1	Iron 2 By similarity
	Metal binding	198	1	Iron 2 By similarity
Experimental info
	Sequence conflict	151 – 155	5	LKRKA → QAQR in AAB81405. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q10840 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 320B939E259E4432	FASTA	322	36,590
	10 20 30 40 50 60 MTGKLVERVH AINWNRLLDA KDLQVWERLT GNFWLPEKIP LSNDLASWQT LSSTEQQTTI 70 80 90 100 110 120 RVFTGLTLLD TAQATVGAVA MIDDAVTPHE EAVLTNMAFM ESVHAKSYSS IFSTLCSTKQ 130 140 150 160 170 180 IDDAFDWSEQ NPYLQRKAQI IVDYYRGDDA LKRKASSVML ESFLFYSGFY LPMYWSSRGK 190 200 210 220 230 240 LTNTADLIRL IIRDEAVHGY YIGYKCQRGL ADLTDAERAD HREYTCELLH TLYANEIDYA 250 260 270 280 290 300 HDLYDELGWT DDVLPYMRYN ANKALANLGY QPAFDRDTCQ VNPAVRAALD PGAGENHDFF 310 320 SGSGSSYVMG THQPTTDTDW DF

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], IDENTIFICATION, LACK OF 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. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., 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. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., 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. Strain: ATCC 25618 / H37Rv.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U41099 Genomic DNA. Translation: AAB81405.1. BX842578 Genomic DNA. Translation: CAE55444.1. AE000516 Genomic DNA. Translation: AAK46308.1. AL123456 Genomic DNA. Translation: CCP44750.1.
PIR	C70756.
RefSeq	NP_336494.1. NC_002755.2. YP_006515387.1. NC_018143.1. YP_177853.1. NC_000962.3.
3D structure databases
ProteinModelPortal	Q10840.
SMR	Q10840. Positions 8-289.
ModBase	Search...
Protein-protein interaction databases
STRING	83332.Rv1981c.
Proteomic databases
PRIDE	Q10840.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAK46308; AAK46308; MT2033.
GeneID	13316778. 885923. 923454.
KEGG	mtc:MT2033. mtu:Rv1981c. mtv:RVBD_1981c.
PATRIC	18126236. VBIMycTub22151_2230.
Organism-specific databases
TubercuList	Rv1981c.
Phylogenomic databases
eggNOG	COG0208.
HOGENOM	HOG000246153.
KO	K00526.
OMA	FNEVEYA.
ProtClustDB	PRK13967.
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...

Entry information

Entry name

RIR2A_MYCTU

Accession

Primary (citable) accession number: Q10840
Secondary accession number(s): L0TAZ9, Q50548

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program