RIR2_MYCGE
ID RIR2_MYCGE Reviewed; 340 AA.
AC P47471; Q49443;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Ribonucleoside-diphosphate reductase subunit beta;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleotide reductase small subunit;
GN Name=nrdF; OrderedLocusNames=MG229;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 234-340.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL J. Bacteriol. 175:7918-7930(1993).
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides (By similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 2 iron ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Genetic information processing; DNA replication.
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC chain family. {ECO:0000305}.
CC -!- CAUTION: Seems to lack two of the iron-binding residues. {ECO:0000305}.
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DR EMBL; L43967; AAC71450.1; -; Genomic_DNA.
DR EMBL; U01739; AAD10549.1; -; Genomic_DNA.
DR PIR; C64225; C64225.
DR AlphaFoldDB; P47471; -.
DR SMR; P47471; -.
DR STRING; 243273.MG_229; -.
DR EnsemblBacteria; AAC71450; AAC71450; MG_229.
DR KEGG; mge:MG_229; -.
DR eggNOG; COG0208; Bacteria.
DR HOGENOM; CLU_052495_0_0_14; -.
DR OMA; IGYKYQR; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000000807; Chromosome.
DR GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IEA:InterPro.
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; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
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; IPR000358; RNR_small_fam.
DR PANTHER; PTHR23409; PTHR23409; 1.
DR Pfam; PF00268; Ribonuc_red_sm; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
DR TIGRFAMs; TIGR04171; RNR_1b_NrdF; 1.
PE 3: Inferred from homology;
KW Deoxyribonucleotide synthesis; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..340
FT /note="Ribonucleoside-diphosphate reductase subunit beta"
FT /id="PRO_0000190483"
FT ACT_SITE 126
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT CONFLICT 234..243
FT /note="AKQKEMKAFV -> SKTKGDESIC (in Ref. 2; AAD10549)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 340 AA; 39152 MW; F0ED1BDAFB2B9CFD CRC64;
MAANNKKYFL ESFSPLGYVK NNFQGNLRSV NWNLVDDEKD LEVWNRIVQN FWLPEKIPVS
NDIPSWKKLS KDWQDLITKT FTGLTLLDTI QATIGDICQI DHALTDHEQV IYANFAFMVG
VHARSYGTIF STLCTSEQIN AAHEWVVNTE SLQKRAKALI PYYTGNDPLK SKVAAALMPG
FLLYGGFYLP FYLSSRKQLP NTSDIIRLIL RDKVIHNYYS GYKYQRKLEK LPLAKQKEMK
AFVFELMYRL IELEKDYLKE LYEGFGIVDD AIKFSVYNAG KFLQNLGYDS PFTAAETRIK
PEIFAQLSAR ADENHDFFSG NGSSYVMGVS EETNDDDWNF
