RIR2H_MYCTU
ID RIR2H_MYCTU Reviewed; 314 AA.
AC P9WH69; L0T624; P96416; Q7DA78;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 39.
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=Rv0233;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH IRON; MANGANESE AND
RP MYRISTIC ACID, FUNCTION, COFACTOR, SUBUNIT, AND VAL-TYR CROSS-LINK.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19321420; DOI=10.1073/pnas.0812971106;
RA Andersson C.S., Hoegbom M.;
RT "A Mycobacterium tuberculosis ligand-binding Mn/Fe protein reveals a new
RT cofactor in a remodeled R2-protein scaffold.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5633-5638(2009).
CC -!- FUNCTION: Probable oxidase that might be involved in lipid metabolism.
CC {ECO:0000269|PubMed:19321420}.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:19321420};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000269|PubMed:19321420};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:19321420};
CC Note=Binds 1 manganese ion per subunit. The iron and manganese ions
CC form a dinuclear manganese-iron cluster. {ECO:0000269|PubMed:19321420};
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:19321420}.
CC -!- INTERACTION:
CC P9WH69; P9WH69: nrdB; NbExp=2; IntAct=EBI-15765696, EBI-15765696;
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; AL123456; CCP42961.1; -; Genomic_DNA.
DR PIR; G70962; G70962.
DR RefSeq; NP_214747.1; NC_000962.3.
DR RefSeq; WP_003911100.1; NZ_NVQJ01000001.1.
DR PDB; 3EE4; X-ray; 1.90 A; A=1-314.
DR PDB; 4AC8; X-ray; 2.75 A; A/B/C/D=1-314.
DR PDBsum; 3EE4; -.
DR PDBsum; 4AC8; -.
DR AlphaFoldDB; P9WH69; -.
DR SMR; P9WH69; -.
DR STRING; 83332.Rv0233; -.
DR DrugBank; DB08231; Myristic acid.
DR PaxDb; P9WH69; -.
DR DNASU; 886699; -.
DR GeneID; 886699; -.
DR KEGG; mtu:Rv0233; -.
DR TubercuList; Rv0233; -.
DR eggNOG; COG0208; Bacteria.
DR OMA; GNAKFWN; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005506; F:iron ion binding; IDA:MTBBASE.
DR GO; GO:0030145; F:manganese ion binding; IDA:MTBBASE.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:MTBBASE.
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 1: Evidence at protein level;
KW 3D-structure; Iron; Lipoprotein; Manganese; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..314
FT /note="R2-like ligand binding oxidase"
FT /id="PRO_0000375432"
FT BINDING 68
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:19321420"
FT BINDING 101
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:19321420"
FT BINDING 101
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:19321420"
FT BINDING 104
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:19321420"
FT BINDING 167
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:19321420"
FT BINDING 202
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:19321420"
FT BINDING 205
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:19321420"
FT CROSSLNK 71..162
FT /note="3-(O4'-tyrosyl)-valine (Val-Tyr)"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:3EE4"
FT HELIX 19..29
FT /evidence="ECO:0007829|PDB:3EE4"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:3EE4"
FT HELIX 42..48
FT /evidence="ECO:0007829|PDB:3EE4"
FT HELIX 51..74
FT /evidence="ECO:0007829|PDB:3EE4"
FT HELIX 76..84
FT /evidence="ECO:0007829|PDB:3EE4"
FT HELIX 88..115
FT /evidence="ECO:0007829|PDB:3EE4"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:3EE4"
FT HELIX 129..136
FT /evidence="ECO:0007829|PDB:3EE4"
FT HELIX 138..148
FT /evidence="ECO:0007829|PDB:3EE4"
FT HELIX 152..162
FT /evidence="ECO:0007829|PDB:3EE4"
FT HELIX 163..169
FT /evidence="ECO:0007829|PDB:3EE4"
FT HELIX 170..182
FT /evidence="ECO:0007829|PDB:3EE4"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:3EE4"
FT HELIX 189..219
FT /evidence="ECO:0007829|PDB:3EE4"
FT HELIX 222..247
FT /evidence="ECO:0007829|PDB:3EE4"
FT TURN 248..251
FT /evidence="ECO:0007829|PDB:3EE4"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:4AC8"
FT HELIX 259..278
FT /evidence="ECO:0007829|PDB:3EE4"
FT TURN 279..282
FT /evidence="ECO:0007829|PDB:3EE4"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:3EE4"
FT HELIX 293..311
FT /evidence="ECO:0007829|PDB:4AC8"
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
