RIR2H_MYCBO
ID RIR2H_MYCBO Reviewed; 314 AA.
AC Q7U2I1; A0A1R3XVU1; X2BEH1;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=BQ2027_MB0238;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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; LT708304; SIT98733.1; -; Genomic_DNA.
DR RefSeq; NP_853903.1; NC_002945.3.
DR RefSeq; WP_003401270.1; NC_002945.4.
DR AlphaFoldDB; Q7U2I1; -.
DR SMR; Q7U2I1; -.
DR GeneID; 45424205; -.
DR PATRIC; fig|233413.5.peg.265; -.
DR OMA; GNAKFWN; -.
DR Proteomes; UP000001419; 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.
FT CHAIN 1..314
FT /note="R2-like ligand binding oxidase"
FT /id="PRO_0000375424"
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 314 AA; 35634 MW; 66E1927C5A03DD3F CRC64;
MTRTRSGSLA AGGLNWASLP LKLFAGGNAK FWDPADIDFT RDRADWEKLS DDERDYATRL
CTQFIAGEEA VTEDIQPFMS AMRAEGRLAD EMYLTQFAFE EAKHTQVFRM WLDAVGISED
LHRYLDDLPA YRQIFYAELP ECLNALSADP SPAAQVRASV TYNHIVEGML ALTGYYAWHK
ICVERAILPG MQELVRRIGD DERRHMAWGT FTCRRHVAAD DANWTVFETR MNELIPLALR
LIEEGFALYG DQPPFDLSKD DFLQYSTDKG MRRFGTISNA RGRPVAEIDV DYSPAQLEDT
FADEDRRTLA AASA