RIR2B_MYCTU
ID RIR2B_MYCTU Reviewed; 324 AA.
AC P9WH71; L0TBM8; Q50549; Q6MX16; Q7D680;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Ribonucleoside-diphosphate reductase subunit beta nrdF2;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleoside-diphosphate reductase nrdF2;
DE AltName: Full=Ribonucleotide reductase R2-2 small subunit;
GN Name=nrdF2; OrderedLocusNames=Rv3048c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, TYROSYL ACTIVE SITE,
RP ACTIVITY REGULATION, AND FUNCTION IN E.COLI.
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=9335290; DOI=10.1128/jb.179.20.6408-6415.1997;
RA Yang F., Curran S.C., Li L.S., Avarbock D., Graf J.D., Chua M.M., Lu G.,
RA Salem J., Rubin H.;
RT "Characterization of two genes encoding the Mycobacterium tuberculosis
RT ribonucleotide reductase small subunit.";
RL J. Bacteriol. 179:6408-6415(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [3]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=14573627; DOI=10.1128/iai.71.11.6124-6131.2003;
RA Dawes S.S., Warner D.F., Tsenova L., Timm J., McKinney J.D., Kaplan G.,
RA Rubin H., Mizrahi V.;
RT "Ribonucleotide reduction in Mycobacterium tuberculosis: function and
RT expression of genes encoding class Ib and class II ribonucleotide
RT reductases.";
RL Infect. Immun. 71:6124-6131(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-296 WITH REDUCED IRON COFACTOR,
RP AND TYROSYL ACTIVE SITE.
RX PubMed=15225619; DOI=10.1016/j.febslet.2004.05.059;
RA Uppsten M., Davis J., Rubin H., Uhlin U.;
RT "Crystal structure of the biologically active form of class Ib
RT ribonucleotide reductase small subunit from Mycobacterium tuberculosis.";
RL FEBS Lett. 569:117-122(2004).
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides. Two genes for this protein are present
CC in M.tuberculosis; this is the active form. When coexpressed in E.coli
CC with nrdE the 2 proteins complement a temperature-sensitive E.coli
CC mutant. {ECO:0000269|PubMed:9335290}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10014,
CC ECO:0000269|PubMed:9335290};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Note=Binds 2 iron ions per subunit.;
CC -!- ACTIVITY REGULATION: CDP reduction is stimulated by dATP.
CC {ECO:0000269|PubMed:9335290}.
CC -!- PATHWAY: Genetic information processing; DNA replication.
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000305}.
CC -!- INDUCTION: Initially decreases as oxygen levels drop, then rises again.
CC {ECO:0000269|PubMed:14573627}.
CC -!- DISRUPTION PHENOTYPE: Lethality. {ECO:0000269|PubMed:14573627}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC chain family. {ECO:0000305}.
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DR EMBL; U41100; AAB81406.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP45857.1; -; Genomic_DNA.
DR PIR; C70861; C70861.
DR RefSeq; WP_003415973.1; NZ_NVQJ01000011.1.
DR RefSeq; YP_177921.1; NC_000962.3.
DR PDB; 1UZR; X-ray; 2.20 A; A/B/C=1-296.
DR PDBsum; 1UZR; -.
DR AlphaFoldDB; P9WH71; -.
DR SMR; P9WH71; -.
DR STRING; 83332.Rv3048c; -.
DR PaxDb; P9WH71; -.
DR PRIDE; P9WH71; -.
DR DNASU; 888886; -.
DR GeneID; 45427041; -.
DR GeneID; 888886; -.
DR KEGG; mtu:Rv3048c; -.
DR TubercuList; Rv3048c; -.
DR eggNOG; COG0208; Bacteria.
DR OMA; IGYKYQR; -.
DR PhylomeDB; P9WH71; -.
DR BRENDA; 1.17.4.1; 3445.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IDA:MTBBASE.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IMP:MTBBASE.
DR GO; GO:0006260; P:DNA replication; IMP:MTBBASE.
DR CDD; cd01049; RNRR2; 1.
DR Gene3D; 1.10.620.20; -; 1.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR012348; RNR-like.
DR InterPro; IPR026494; RNR_NrdF-like.
DR InterPro; IPR033909; RNR_small.
DR InterPro; IPR030475; RNR_small_AS.
DR InterPro; IPR000358; RNR_small_fam.
DR PANTHER; PTHR23409; PTHR23409; 1.
DR Pfam; PF00268; Ribonuc_red_sm; 1.
DR PIRSF; PIRSF000355; NrdB; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
DR TIGRFAMs; TIGR04171; RNR_1b_NrdF; 1.
DR PROSITE; PS00368; RIBORED_SMALL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Deoxyribonucleotide synthesis; Iron; Metal-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..324
FT /note="Ribonucleoside-diphosphate reductase subunit beta
FT nrdF2"
FT /id="PRO_0000393356"
FT ACT_SITE 110
FT BINDING 103
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 103
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 106
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 163
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 197
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 197
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 200
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT HELIX 23..33
FT /evidence="ECO:0007829|PDB:1UZR"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:1UZR"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:1UZR"
FT HELIX 47..51
FT /evidence="ECO:0007829|PDB:1UZR"
FT HELIX 55..77
FT /evidence="ECO:0007829|PDB:1UZR"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:1UZR"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:1UZR"
FT HELIX 90..117
FT /evidence="ECO:0007829|PDB:1UZR"
FT HELIX 120..132
FT /evidence="ECO:0007829|PDB:1UZR"
FT HELIX 134..147
FT /evidence="ECO:0007829|PDB:1UZR"
FT HELIX 152..164
FT /evidence="ECO:0007829|PDB:1UZR"
FT HELIX 166..170
FT /evidence="ECO:0007829|PDB:1UZR"
FT HELIX 172..179
FT /evidence="ECO:0007829|PDB:1UZR"
FT HELIX 184..212
FT /evidence="ECO:0007829|PDB:1UZR"
FT HELIX 217..246
FT /evidence="ECO:0007829|PDB:1UZR"
FT TURN 247..250
FT /evidence="ECO:0007829|PDB:1UZR"
FT HELIX 252..269
FT /evidence="ECO:0007829|PDB:1UZR"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:1UZR"
FT HELIX 285..290
FT /evidence="ECO:0007829|PDB:1UZR"
SQ SEQUENCE 324 AA; 36992 MW; 310C3BEC9029099E CRC64;
MTGNAKLIDR VSAINWNRLQ DEKDAEVWDR LTGNFWLPEK VPVSNDIPSW GTLTAGEKQL
TMRVFTGLTM LDTIQGTVGA VSLIPDALTP HEEAVLTNIA FMESVHAKSY SQIFSTLCST
AEIDDAFRWS EENRNLQRKA EIVLQYYRGD EPLKRKVAST LLESFLFYSG FYLPMYWSSR
AKLTNTADMI RLIIRDEAVH GYYIGYKFQR GLALVDDVTR AELKDYTYEL LFELYDNEVE
YTQDLYDEVG LTEDVKKFLR YNANKALMNL GYEALFPRDE TDVNPAILSA LSPNADENHD
FFSGSGSSYV IGKAVVTEDD DWDF
