ID   RIR2H_MYCVP             Reviewed;         312 AA.
AC   A1TAR1;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=Mvan_3466;
OS   Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS   KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC   PYR-1;
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   Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Anderson I.J., Miller C., Richardson P.;
RT   "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL   Submitted (DEC-2006) 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; CP000511; ABM14261.1; -; Genomic_DNA.
DR   RefSeq; WP_011780665.1; NC_008726.1.
DR   AlphaFoldDB; A1TAR1; -.
DR   SMR; A1TAR1; -.
DR   STRING; 350058.Mvan_3466; -.
DR   EnsemblBacteria; ABM14261; ABM14261; Mvan_3466.
DR   KEGG; mva:Mvan_3466; -.
DR   eggNOG; COG0208; Bacteria.
DR   HOGENOM; CLU_072736_0_0_11; -.
DR   OMA; GNAKFWN; -.
DR   OrthoDB; 1384440at2; -.
DR   Proteomes; UP000009159; 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..312
FT                   /note="R2-like ligand binding oxidase"
FT                   /id="PRO_0000375434"
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;  35328 MW;  2C4221D24EAFA80A CRC64;
     MARTRSDSLA AGGLNWDSLP LRLFAGGNAK FWDPADIDFS RDRADWESLT DLERDWATRL
     CAEFIAGEEA VTQDIQPFMA AMRAEGRLGD EMYLTQFAFE EAKHTQVFRM WLDAVGITED
     LQGYLDELPA YCQMFYEELP ASLDALATDP SPAAQVRASV TYNHVIEGMM ALTGYYAWHR
     ICVDRGILPG MQELVRRIGD DERRHMAWGT FTCRRHVAAD DANWAVFETR MNELIPLALR
     NTEDGFALYD EVPFGLTMEE FQQYAADKGM RRFGTISSAR GRPLAEIDVD YSPLHLEDTF
     ADEDRKSLAA SA