ID   RIR2H_MYCGI             Reviewed;         312 AA.
AC   A4TB76;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=Mflv_3061;
OS   Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS   PYR-GCK)).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PYR-GCK;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium gilvum PYR-GCK.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable oxidase that might be involved in lipid metabolism.
CC       {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; CP000656; ABP45538.1; -; Genomic_DNA.
DR   RefSeq; WP_011893938.1; NC_009338.1.
DR   AlphaFoldDB; A4TB76; -.
DR   SMR; A4TB76; -.
DR   STRING; 350054.Mflv_3061; -.
DR   EnsemblBacteria; ABP45538; ABP45538; Mflv_3061.
DR   KEGG; mgi:Mflv_3061; -.
DR   eggNOG; COG0208; Bacteria.
DR   HOGENOM; CLU_072736_0_0_11; -.
DR   OMA; GNAKFWN; -.
DR   OrthoDB; 1384440at2; -.
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.
FT   CHAIN           1..312
FT                   /note="R2-like ligand binding oxidase"
FT                   /id="PRO_0000375426"
FT   BINDING         68
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         101
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         101
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         167
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         202
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         205
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        71..162
FT                   /note="3-(O4'-tyrosyl)-valine (Val-Tyr)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   312 AA;  35533 MW;  84AFCC88F7C8D8F4 CRC64;
     MNRTRSDSLA AGGLNWDSLP LRLFAGGNAK FWDPADIDFS RDRADWESLS TMERDWATRL
     CAEFIAGEEA VTQDIQPFMA AMRAEGRLGD EMYLTQFAFE EAKHTQVFRM WLDAVGITED
     LQGYLDDLPA YRQMFYEELP ASLDALATDP SPQAQVRASV TYNHVIEGMM ALTGYYAWHR
     ICVDRHILPG MQELVRRIGD DERRHMAWGT FTCRRHVAAD DANWTVFEDR MNELIPLALQ
     NTDDAFALYD EIPFGLTIEE FQQYAADKGM RRFGTISSAR GRPLAEIDVD YTPLHLEDSF
     ADEDRKALAA SA