RIR1_ENCCU
ID RIR1_ENCCU Reviewed; 768 AA.
AC Q8SR37;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Ribonucleoside-diphosphate reductase large chain;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleotide reductase;
GN OrderedLocusNames=ECU10_0920;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(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 to separate specificity
CC and activation sites on the large subunit. The type of nucleotide bound
CC 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. Stimulated by ATP and
CC inhibited by dATP binding to the activity site (By similarity).
CC {ECO:0000250}.
CC -!- PATHWAY: Genetic information processing; DNA replication.
CC -!- SUBUNIT: Heterodimer of a large and a small subunit. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000305}.
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DR EMBL; AL590449; CAD25811.1; -; Genomic_DNA.
DR RefSeq; NP_586207.1; NM_001042040.1.
DR AlphaFoldDB; Q8SR37; -.
DR SMR; Q8SR37; -.
DR STRING; 284813.Q8SR37; -.
DR GeneID; 859856; -.
DR KEGG; ecu:ECU10_0920; -.
DR VEuPathDB; MicrosporidiaDB:ECU10_0920; -.
DR HOGENOM; CLU_000404_1_0_1; -.
DR InParanoid; Q8SR37; -.
DR OMA; RGSIQNI; -.
DR OrthoDB; 156716at2759; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000000819; Chromosome X.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; ISS:UniProtKB.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
DR InterPro; IPR013346; NrdE_NrdA.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_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 PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF48168; SSF48168; 1.
DR TIGRFAMs; TIGR02506; NrdE_NrdA; 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..768
FT /note="Ribonucleoside-diphosphate reductase large chain"
FT /id="PRO_0000187200"
FT ACT_SITE 420
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 422
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 424
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 7..8
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:P23921"
FT BINDING 13..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:P23921"
FT BINDING 196
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000250|UniProtKB:P23921"
FT BINDING 211
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000250|UniProtKB:P23921"
FT BINDING 220..222
FT /ligand="dTTP"
FT /ligand_id="ChEBI:CHEBI:37568"
FT /ligand_note="allosteric effector that controls substrate
FT specificity"
FT /evidence="ECO:0000250|UniProtKB:P23921"
FT BINDING 237
FT /ligand="dTTP"
FT /ligand_id="ChEBI:CHEBI:37568"
FT /ligand_note="allosteric effector that controls substrate
FT specificity"
FT /evidence="ECO:0000250|UniProtKB:P23921"
FT BINDING 250
FT /ligand="dTTP"
FT /ligand_id="ChEBI:CHEBI:37568"
FT /ligand_note="allosteric effector that controls substrate
FT specificity"
FT /evidence="ECO:0000250|UniProtKB:P23921"
FT BINDING 420
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000250|UniProtKB:P23921"
FT BINDING 424
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000250|UniProtKB:P23921"
FT SITE 212
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 437
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 729
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 730
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 763
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT SITE 766
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT DISULFID 212..437
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 768 AA; 87941 MW; 3E6BF6826805E20D CRC64;
MENFSNSKRI KSEKLGIDLI RSRIEGYVKD LKLRHVDVDE LVERIVSGWC EDMTRKETID
YCSETAASMI TKHPEYGQIS SRIIVSYIHE ITMDSFVEKI KYIQKHRGMV SEEMYGIILE
HGETIEGMIN YENDFLFSYF GILTLMKSYL IKVGEEIIER PQDMFMRVAL QIHKTDFEKV
REVYNLLSGH YFTHATPTLY NSCLKNPQLA SCFLITPRED SIEGVYHMIN QAAIITKYSG
GIGLNLHGIR SKGSSLRSTG GRSNGIIPLI QVLNATKRYI NQGAERRPGS IAIFLEPWHM
EIFDFLELRK NTGPEEFRAR DIFTALWIND LFMERVKNNE EWSLFCPSQA VGLSDVWGEE
FNALYCKYEK TISRTVVPAQ KLWKAIIEAQ IETGTPYMCY KDACNRLSNQ QHLGTIKSSN
LCAEIVEYSS GEETSVCNLA SICLPMFVKD GWFDFEAFRR VVKILTVNLN RVIDFNYYPV
EEARRSNMRN RPIGIGVQGL ADLFAILRLA FESDGARSLN QDIFEAMYYS AMEASCELAE
KEGPFPSYEG SPISKGIFHF ELAGRKASGN WDWEGLRERI RRHGVRNSLL IALMPTAGTS
QIFGNNEAFE PHASNIYTRR THAGEFQIVN QHLVNDLVRL GLWSYEMKNL VIENEGSIQN
ITSIPHEIRE IYKTAWEIKM KSVIDLAADR QVFVDQSQSL NIFIAKPTYS QLTSMHFYGY
HCGLKTGMYY LRTRPITSAI KFTVDKKLAE KTLSSMNDTD DPCSMCSS
