RIR1_MYCLE
ID RIR1_MYCLE Reviewed; 721 AA.
AC Q9CBQ0;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 108.
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=ML1734;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC30687.1; 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; AL583923; CAC30687.1; ALT_INIT; Genomic_DNA.
DR PIR; H87125; H87125.
DR AlphaFoldDB; Q9CBQ0; -.
DR SMR; Q9CBQ0; -.
DR STRING; 272631.ML1734; -.
DR EnsemblBacteria; CAC30687; CAC30687; CAC30687.
DR KEGG; mle:ML1734; -.
DR Leproma; ML1734; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_4_1_11; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000000806; 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; Reference proteome.
FT CHAIN 1..721
FT /note="Ribonucleoside-diphosphate reductase subunit alpha"
FT /id="PRO_0000187220"
FT ACT_SITE 393
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 395
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 397
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 184..185
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 393..397
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 595..599
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 185
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 192
FT /note="Allosteric effector binding"
FT /evidence="ECO:0000250"
FT SITE 222
FT /note="Allosteric effector binding"
FT /evidence="ECO:0000250"
FT SITE 422
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 699
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 700
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 716
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT SITE 719
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT DISULFID 185..422
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 721 AA; 82024 MW; 22B365A016228872 CRC64;
MPPTATAEPV TASTHMLSNE TDYHALNAML NLYDADGKIQ FDKDVLAARQ FFLQHVNQNT
VFFHNQDEKL DYLIRENYYE REVLDQYSRN FVKSLLDRAY AKKFRFSTFL GAFKYYTSYT
LKTFDGKRYL ERLEDRVCMV ALTLAAGDTG LAEKLVDEII DGRFQPATPT FLNSGKKQRG
EPVSCFLLRI EDNMESIGRS VNSALQLSKR GGGVALLLSN IREHGAPIKN IEHQSSGVIP
IMKLLEDAFS YANQLGARQG AGAVYLHAHH PDIYRFLDTK RENADEKIRI KTLSLGVIIP
DITFELAKRN EDMYLFSSYD VERVYEVPFA DISVTEKYYE MLDDARIRKT KIKAREFFQK
LAELQFESGY PYVMFEDTVN RANPIEGKIT HSNLCSEILQ VSTPSLFNDD LSYAKVGKDI
SCNLGSLNIA KTMDSPDFAQ TVEVAIRALT AVSDQTHIKS VPSIEQGNND SHAIGLGQMN
LHGYLSREGI FYGSEEGVDF TNIYFYTVLF HVLLASNSIA IERGTFFKGF ERSKYASGEF
FDKYIEQTWE PKTDKVRQLF AEAAIRIPTQ NDWKRLKELV VAHGIYNQNL QAVPPTGSIS
YINHSTSSIH PIVSKVEIRK EGKIGRVYYP APYMTNDNLQ YYQDAYEIGY QKIIDTYAAA
TQHVDQGLSL TLFFKDTATT RDVNKAQIYA WRKGIKTLYY IRLRQMALEG TEVEGCVSCT
L
