ID   RIR2_MYCPN              Reviewed;         339 AA.
AC   P75461;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 133.
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=MPN_322; ORFNames=MP514;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1)
OS   (Mycoplasmoides pneumoniae).
OC   Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC   Mycoplasmoides.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129 / Subtype 1;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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   -!- 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; U00089; AAB96162.1; -; Genomic_DNA.
DR   PIR; S73840; S73840.
DR   RefSeq; NP_110010.1; NC_000912.1.
DR   RefSeq; WP_010874678.1; NZ_OU342337.1.
DR   AlphaFoldDB; P75461; -.
DR   SMR; P75461; -.
DR   IntAct; P75461; 4.
DR   STRING; 272634.MPN_322; -.
DR   EnsemblBacteria; AAB96162; AAB96162; MPN_322.
DR   GeneID; 66609022; -.
DR   KEGG; mpn:MPN_322; -.
DR   PATRIC; fig|272634.6.peg.346; -.
DR   HOGENOM; CLU_052495_0_0_14; -.
DR   OrthoDB; 9766544at2; -.
DR   BioCyc; MPNE272634:G1GJ3-513-MONOMER; -.
DR   Proteomes; UP000000808; 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:UniProtKB-KW.
DR   CDD; cd01049; RNRR2; 1.
DR   Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 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   NCBIfam; TIGR04171; RNR_1b_NrdF; 1.
DR   PANTHER; PTHR23409; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SMALL CHAIN; 1.
DR   PANTHER; PTHR23409:SF18; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SUBUNIT M2; 1.
DR   Pfam; PF00268; Ribonuc_red_sm; 1.
DR   SUPFAM; SSF47240; Ferritin-like; 1.
PE   3: Inferred from homology;
KW   Deoxyribonucleotide synthesis; Iron; Metal-binding; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..339
FT                   /note="Ribonucleoside-diphosphate reductase subunit beta"
FT                   /id="PRO_0000190484"
FT   ACT_SITE        125
FT                   /evidence="ECO:0000250"
FT   BINDING         87
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         121
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
SQ   SEQUENCE   339 AA;  39413 MW;  AE2FA78C2B745176 CRC64;
     MANTKKYFLE SVSPLEYAQK KFQGNLRSVN WNLVDDEKDL EVWNRITQNF WLPEKIPVSN
     DIPSWKQLSK EWQDLITKTF TGLTLLDTIQ ATIGDIKQID YALTDHEQVI YANFAFMVGV
     HARSYGTIFS TLCTSEQITE AHEWVVKTES LQKRAKALIP YYTGKDPLKS KVAAALMPGF
     LLYGGFYLPF YLSSRKQLPN TSDIIRLILR DKVIHNYYSG YKFQRKVEKM SKEKQAEMKR
     FVFDLMYELI ELEKAYLKEL YEGFGIVEDA IKFSIYNAGK FLQNLGYDSP FTEEETRIKP
     EIFAQLSARA DENHDFFSGN GSSYVMGISE ETEDKDWDF
//