ID   RIR2H_MYCS2             Reviewed;         320 AA.
AC   A0QPD3; I7FW62;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
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   Name=nrdB; OrderedLocusNames=MSMEG_0358, MSMEI_0351;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
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; CP000480; ABK72528.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP36832.1; -; Genomic_DNA.
DR   RefSeq; WP_003891679.1; NZ_SIJM01000018.1.
DR   RefSeq; YP_884771.1; NC_008596.1.
DR   AlphaFoldDB; A0QPD3; -.
DR   SMR; A0QPD3; -.
DR   STRING; 246196.MSMEI_0351; -.
DR   EnsemblBacteria; ABK72528; ABK72528; MSMEG_0358.
DR   EnsemblBacteria; AFP36832; AFP36832; MSMEI_0351.
DR   GeneID; 66738545; -.
DR   KEGG; msg:MSMEI_0351; -.
DR   KEGG; msm:MSMEG_0358; -.
DR   PATRIC; fig|246196.19.peg.355; -.
DR   eggNOG; COG0208; Bacteria.
DR   OMA; GNAKFWN; -.
DR   OrthoDB; 1384440at2; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; 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..320
FT                   /note="R2-like ligand binding oxidase"
FT                   /id="PRO_0000375428"
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   320 AA;  35999 MW;  BEFE210EC9E26F23 CRC64;
     MTRTHFDSIR AGGLNWSSLP LKLFAGGNAK FWDPADIDFS RDRADWEALT EREREYATRL
     CAEFIAGEEA VTKDIQPFMS AMRAEGRLGD EMYLTQFAFE EAKHTQVFRM WLDAVGVTDD
     LHSLIEEVPA YVQIFCEELP AALEALTSDP SPAAQVRASV VYNHVVEGML ALTGYYAWHR
     ICVDRGILPG MQELVRRIGD DERRHMAWGT FTCRRHVAAD DANWAVFETH MNELIPVALR
     LTQEGFALYG DDIPFGLEEG EFLQYSSDRG MRRFGTISSA RGRPLAEIDV DYTPLQLEDT
     FADEDERALT AVKAAAAAAN