ID   RIR2_MYCGA              Reviewed;         339 AA.
AC   Q9XC20;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 121.
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=MYCGA0450; ORFNames=MGA_0698;
OS   Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
OS   (Mycoplasmoides gallisepticum).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=710127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A5969Var.B;
RA   Skamrov A.V., Gol'dman M.A., Feoktistova E.S., Bibilashvili R.S.;
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R(low / passage 15 / clone 2);
RX   PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA   Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA   Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT   "The complete genome sequence of the avian pathogen Mycoplasma
RT   gallisepticum strain R(low).";
RL   Microbiology 149:2307-2316(2003).
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; AF152114; AAD45275.1; -; Genomic_DNA.
DR   EMBL; AE015450; AAP56395.1; -; Genomic_DNA.
DR   RefSeq; WP_011113274.1; NC_004829.2.
DR   AlphaFoldDB; Q9XC20; -.
DR   SMR; Q9XC20; -.
DR   GeneID; 57203322; -.
DR   KEGG; mga:MGA_0698; -.
DR   HOGENOM; CLU_052495_0_0_14; -.
DR   OMA; IGYKYQR; -.
DR   OrthoDB; 1384440at2; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000001418; 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..339
FT                   /note="Ribonucleoside-diphosphate reductase subunit beta"
FT                   /id="PRO_0000190482"
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;  39168 MW;  A8711B1B51E4F47F CRC64;
     MSNNNKYYDK SFSPLGYVAN GQKGVMRSIN WNVINDPKDL EVWTRVTQNF WLPEKIPVSN
     DLKSWNELTP EWKQLVTRTF TGLTLLDTIQ CTLGDIAQIP NSLTDHEQFV YANFSFMVGV
     HARSYGTIFS TLNTSDEIEE AHEWVINNEK LQARAKFLVP YYTSDDPLKS KIAAALMPGF
     LLYGGFYLPF YLAARGKLPN TSDIIRLILR DKVIHNYYSG YKYRLKVQKL PKEKQEEYKK
     FVFEILYKLI ELEKDFLREL YDGFGLADEA IAFSLYNAGK FLQNCGYESP FTPEETKISP
     EVFAQLSARA DENHDFFSGN GSSYIMGVTE ETQDDDWEF