NRDZ_MYCTO
ID NRDZ_MYCTO Reviewed; 692 AA.
AC P9WH76; L0T6W6; O53767; Q8VKI9;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Vitamin B12-dependent ribonucleoside-diphosphate reductase;
DE Short=B12-dependent RNR;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleotide reductase;
GN Name=nrdZ; OrderedLocusNames=MT0596;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
RN [2]
RP INDUCTION BY NITRIC OXIDE (NO) AND BY HYPOXIA, AND DORMANCY REGULON.
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12953092; DOI=10.1084/jem.20030205;
RA Voskuil M.I., Schnappinger D., Visconti K.C., Harrell M.I., Dolganov G.M.,
RA Sherman D.R., Schoolnik G.K.;
RT "Inhibition of respiration by nitric oxide induces a Mycobacterium
RT tuberculosis dormancy program.";
RL J. Exp. Med. 198:705-713(2003).
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1;
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000250};
CC Note=5'-deoxyadenosylcobalamine (coenzyme B12). {ECO:0000250};
CC -!- PATHWAY: Genetic information processing; DNA replication.
CC -!- INDUCTION: A member of the dormancy regulon. Induced in response to
CC reduced oxygen tension (hypoxia) and low levels of nitric oxide (NO).
CC {ECO:0000269|PubMed:12953092}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase class-2
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK44819.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000516; AAK44819.1; ALT_INIT; Genomic_DNA.
DR PIR; A70933; A70933.
DR AlphaFoldDB; P9WH76; -.
DR SMR; P9WH76; -.
DR EnsemblBacteria; AAK44819; AAK44819; MT0596.
DR KEGG; mtc:MT0596; -.
DR HOGENOM; CLU_000404_2_3_11; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
DR CDD; cd02888; RNR_II_dimer; 1.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR013344; RNR_NrdJ/NrdZ.
DR InterPro; IPR008926; RNR_R1-su_N.
DR Pfam; PF03477; ATP-cone; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 2.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF48168; SSF48168; 1.
DR TIGRFAMs; TIGR02504; NrdJ_Z; 1.
DR PROSITE; PS51161; ATP_CONE; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cobalamin; Cobalt; Deoxyribonucleotide synthesis;
KW Disulfide bond; DNA synthesis; Nucleotide-binding; Oxidoreductase.
FT CHAIN 1..692
FT /note="Vitamin B12-dependent ribonucleoside-diphosphate
FT reductase"
FT /id="PRO_0000428235"
FT DOMAIN 7..95
FT /note="ATP-cone"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00492"
FT ACT_SITE 375
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 377
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 379
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 192..193
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 375..379
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 520..524
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 193..388
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 692 AA; 74445 MW; 035EF5EAF946656E CRC64;
MGVSWPAKVR RRDGTLVPFD IARIEAAVTR AAREVACDDP DMPGTVAKAV ADALGRGIAP
VEDIQDCVEA RLGEAGLDDV ARVYIIYRQR RAELRTAKAL LGVRDELKLS LAAVTVLRER
YLLHDEQGRP AESTGELMDR SARCVAAAED QYEPGSSRRW AERFATLLRN LEFLPNSPTL
MNSGTDLGLL AGCFVLPIED SLQSIFATLG QAAELQRAGG GTGYAFSHLR PAGDRVASTG
GTASGPVSFL RLYDSAAGVV SMGGRRRGAC MAVLDVSHPD ICDFVTAKAE SPSELPHFNL
SVGVTDAFLR AVERNGLHRL VNPRTGKIVA RMPAAELFDA ICKAAHAGGD PGLVFLDTIN
RANPVPGRGR IEATNPCGEV PLLPYESCNL GSINLARMLA DGRVDWDRLE EVAGVAVRFL
DDVIDVSRYP FPELGEAARA TRKIGLGVMG LAELLAALGI PYDSEEAVRL ATRLMRRIQQ
AAHTASRRLA EERGAFPAFT DSRFARSGPR RNAQVTSVAP TGTISLIAGT TAGIEPMFAI
AFTRAIVGRH LLEVNPCFDR LARDRGFYRD ELIAEIAQRG GVRGYPRLPA EVRAAFPTAA
EIAPQWHLRM QAAVQRHVEA AVSKTVNLPA TATVDDVRAI YVAAWKAKVK GITVYRYGSR
EGQVLSSAAP KPLLAQADTE FSGGCAGRSC EF
