RIR2H_MYCTA
ID RIR2H_MYCTA Reviewed; 314 AA.
AC A5TYV8;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=MRA_0241;
OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=419947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25177 / H37Ra;
RX PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA Wang H., Wang S., Zhao G., Zhang Y.;
RT "Genetic basis of virulence attenuation revealed by comparative genomic
RT analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL PLoS ONE 3:E2375-E2375(2008).
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; CP000611; ABQ71958.1; -; Genomic_DNA.
DR RefSeq; WP_003911100.1; NZ_CP016972.1.
DR AlphaFoldDB; A5TYV8; -.
DR SMR; A5TYV8; -.
DR STRING; 419947.MRA_0241; -.
DR EnsemblBacteria; ABQ71958; ABQ71958; MRA_0241.
DR KEGG; mra:MRA_0241; -.
DR eggNOG; COG0208; Bacteria.
DR HOGENOM; CLU_072736_0_0_11; -.
DR OMA; GNAKFWN; -.
DR OrthoDB; 1384440at2; -.
DR Proteomes; UP000001988; 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_0000375433"
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; 35656 MW; 0AE29D8CA604E94C CRC64;
MTRTRSGSLA AGGLNWASLP LKLFAGGNAK FWHPADIDFT 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