ID   RIR2H_RHOJR             Reviewed;         324 AA.
AC   Q0S392;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=R2-like ligand binding oxidase;
DE            EC=1.-.-.-;
DE   AltName: Full=Ribonucleotide reductase R2 subunit homolog;
DE   AltName: Full=Ribonucleotide reductase small subunit homolog;
GN   OrderedLocusNames=RHA1_ro06217;
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=101510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1;
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC   -!- FUNCTION: Probable oxidase. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC       Note=Binds 1 Fe cation per subunit.;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 1 manganese ion per subunit. The iron and manganese ions
CC       form a dinuclear manganese-iron cluster. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC       chain family. R2-like ligand binding oxidase subfamily. {ECO:0000305}.
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DR   EMBL; CP000431; ABG97994.1; -; Genomic_DNA.
DR   RefSeq; WP_009479428.1; NC_008268.1.
DR   AlphaFoldDB; Q0S392; -.
DR   SMR; Q0S392; -.
DR   STRING; 101510.RHA1_ro06217; -.
DR   PRIDE; Q0S392; -.
DR   EnsemblBacteria; ABG97994; ABG97994; RHA1_ro06217.
DR   KEGG; rha:RHA1_ro06217; -.
DR   eggNOG; COG0208; Bacteria.
DR   HOGENOM; CLU_072736_0_0_11; -.
DR   OMA; GNAKFWN; -.
DR   Proteomes; UP000008710; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:InterPro.
DR   CDD; cd07911; RNRR2_Rv0233_like; 1.
DR   Gene3D; 1.10.620.20; -; 1.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR033908; R2LOX.
DR   InterPro; IPR012348; RNR-like.
DR   InterPro; IPR000358; RNR_small_fam.
DR   PANTHER; PTHR23409; PTHR23409; 1.
DR   Pfam; PF00268; Ribonuc_red_sm; 1.
DR   SUPFAM; SSF47240; SSF47240; 1.
PE   3: Inferred from homology;
KW   Iron; Manganese; Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..324
FT                   /note="R2-like ligand binding oxidase"
FT                   /id="PRO_0000375435"
FT   REGION          304..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         79
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         115
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         178
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         213
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         216
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        82..173
FT                   /note="3-(O4'-tyrosyl)-valine (Val-Tyr)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   324 AA;  36810 MW;  20D5E1B284907C19 CRC64;
     MSTLTPGRPY APGRQGFSSL RAGGLNWDAF PLRLFTKGNA KFWNPTDLDF SRDAEDWEGL
     NSEQQRNSTY LVAQFIAGEE AVTEDIQPFM KAMAAEGRFG DEMYLTQFCF EEAKHTQVFR
     LWMDAVGLTR DLHPFVAENP YYRQLFYEEL PGSLKVLETD PSPVNQVRAS VTYNHVIEGS
     LALTGYYAWQ KVCTTRGILP GMQELVRRIG DDERRHMAWG TFTCRRHVAA DDSNWGVVQE
     RMAELMPLAL GMIDWVNKQF EVQPYGLDDQ EFIAYAADRA QRRLGAIESA RGRPVEEIDL
     DYSPEALEEK FGEEDAKAMS EAAG