RIR1_MYCTO
ID RIR1_MYCTO Reviewed; 725 AA.
AC P9WH74; L0TD07; O53296; P0A5W8; P50640;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Ribonucleoside-diphosphate reductase subunit alpha;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleotide reductase R1 subunit;
GN Name=nrdE; OrderedLocusNames=MT3137;
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).
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 -!- ACTIVITY REGULATION: Under complex allosteric control mediated by
CC deoxynucleoside triphosphates and ATP binding. The type of nucleotide
CC bound at the specificity site determines substrate preference. It seems
CC probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP
CC reduction and dTTP favors GDP reduction (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Genetic information processing; DNA replication.
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000305}.
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DR EMBL; AE000516; AAK47468.1; -; Genomic_DNA.
DR PIR; F70861; F70861.
DR RefSeq; WP_003914457.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WH74; -.
DR SMR; P9WH74; -.
DR EnsemblBacteria; AAK47468; AAK47468; MT3137.
DR KEGG; mtc:MT3137; -.
DR HOGENOM; CLU_000404_4_1_11; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
DR InterPro; IPR013346; NrdE_NrdA.
DR InterPro; IPR026459; RNR_1b_NrdE.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR013554; RNR_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR PANTHER; PTHR11573; PTHR11573; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR Pfam; PF08343; RNR_N; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF48168; SSF48168; 1.
DR TIGRFAMs; TIGR02506; NrdE_NrdA; 1.
DR TIGRFAMs; TIGR04170; RNR_1b_NrdE; 1.
DR PROSITE; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme; ATP-binding; Deoxyribonucleotide synthesis;
KW Disulfide bond; Nucleotide-binding; Oxidoreductase.
FT CHAIN 1..725
FT /note="Ribonucleoside-diphosphate reductase subunit alpha"
FT /id="PRO_0000428236"
FT ACT_SITE 397
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 399
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 401
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 188..189
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 397..401
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 599..603
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 189
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 196
FT /note="Allosteric effector binding"
FT /evidence="ECO:0000250"
FT SITE 226
FT /note="Allosteric effector binding"
FT /evidence="ECO:0000250"
FT SITE 426
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 703
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 704
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 720
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT SITE 723
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT DISULFID 189..426
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 725 AA; 82441 MW; 38C315D149331D55 CRC64;
MPPTVIAEPV ASGAHASYSG GPGETDYHAL NAMLNLYDAD GKIQFDKDRE AAHQYFLQHV
NQNTVFFHNQ DEKLDYLIRE NYYEREVLDQ YSRNFVKTLL DRAYAKKFRF PTFLGAFKYY
TSYTLKTFDG KRYLERFEDR VVMVALTLAA GDTALAELLV DEIIDGRFQP ATPTFLNSGK
KQRGEPVSCF LLRVEDNMES IGRSINSALQ LSKRGGGVAL LLTNIREHGA PIKNIENQSS
GVIPIMKLLE DAFSYANQLG ARQGAGAVYL HAHHPDIYRF LDTKRENADE KIRIKTLSLG
VVIPDITFEL AKRNDDMYLF SPYDVERVYG VPFADISVTE KYYEMVDDAR IRKTKIKARE
FFQTLAELQF ESGYPYIMFE DTVNRANPID GKITHSNLCS EILQVSTPSL FNEDLSYAKV
GKDISCNLGS LNIAKTMDSP DFAQTIEVAI RALTAVSDQT HIKSVPSIEQ GNNDSHAIGL
GQMNLHGYLA RERIFYGSDE GIDFTNIYFY TVLYHALRAS NRIAIERGTH FKGFERSKYA
SGEFFDKYTD QIWEPKTQKV RQLFADAGIR IPTQDDWRRL KESVQAHGIY NQNLQAVPPT
GSISYINHST SSIHPIVSKV EIRKEGKIGR VYYPAPYMTN DNLEYYEDAY EIGYEKIIDT
YAAATQHVDQ GLSLTLFFKD TATTRDVNKA QIYAWRKGIK TLYYIRLRQM ALEGTEVEGC
VSCML
