ID RIR1_VACCA Reviewed; 771 AA. AC Q76RD8; DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 76. DE RecName: Full=Ribonucleoside-diphosphate reductase large subunit; DE EC=1.17.4.1; DE AltName: Full=Ribonucleotide reductase large subunit; DE AltName: Full=Ribonucleotide reductase subunit 1; DE Short=RNR1; GN Name=OPG080; OrderedLocusNames=MVA065L, ACAM3000_MVA_065; OS Vaccinia virus (strain Ankara) (VACV). OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes; OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus. OX NCBI_TaxID=126794; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=9601507; DOI=10.1006/viro.1998.9123; RA Antoine G., Scheiflinger F., Dorner F., Falkner F.G.; RT "The complete genomic sequence of the modified vaccinia Ankara strain: RT comparison with other orthopoxviruses."; RL Virology 244:365-396(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate Acambis 3000; RA Esposito J.J., Frace M., Sammons S.A., Olsen-Rasmussen M.S., Osborne J., RA Khristova M., Wohlhueter R.M.; RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Ribonucleoside-diphosphate reductase holoenzyme provides the CC precursors necessary for viral DNA synthesis. Allows virus growth in CC non-dividing cells. Catalyzes the biosynthesis of deoxyribonucleotides CC from the corresponding ribonucleotides. {ECO:0000250|UniProtKB:P12848}. 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 Evidence={ECO:0000250|UniProtKB:P12848}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:23254; CC Evidence={ECO:0000250|UniProtKB:P12848}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P12848}; CC Note=Maximal ribonucleotide reductase activity requires the presence of CC Mg(2+) ions. {ECO:0000250|UniProtKB:P12848}; CC -!- SUBUNIT: Interacts with RNR2/OPG047 subunit. CC {ECO:0000250|UniProtKB:P12848}. CC -!- INDUCTION: Expressed early in the viral replicative cycle. CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large CC chain family. {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; U94848; AAB96436.1; -; Genomic_DNA. DR EMBL; AY603355; AAT10463.1; -; Genomic_DNA. DR SMR; Q76RD8; -. DR Proteomes; UP000159908; Segment. DR Proteomes; UP000172909; Segment. 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:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR CDD; cd01679; RNR_I; 1. DR Gene3D; 3.20.70.20; -; 1. DR InterPro; IPR005144; ATP-cone_dom. DR InterPro; IPR013346; NrdE_NrdA_C. DR InterPro; IPR000788; RNR_lg_C. DR InterPro; IPR013509; RNR_lsu_N. DR InterPro; IPR008926; RNR_R1-su_N. DR InterPro; IPR039718; Rrm1. DR NCBIfam; TIGR02506; NrdE_NrdA; 1. DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1. DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1. DR Pfam; PF03477; ATP-cone; 1. DR Pfam; PF02867; Ribonuc_red_lgC; 1. DR Pfam; PF00317; Ribonuc_red_lgN; 1. DR PRINTS; PR01183; RIBORDTASEM1. DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1. DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1. DR PROSITE; PS51161; ATP_CONE; 1. DR PROSITE; PS00089; RIBORED_LARGE; 1. PE 2: Evidence at transcript level; KW Allosteric enzyme; ATP-binding; Deoxyribonucleotide synthesis; KW Early protein; Magnesium; Nucleotide-binding; Oxidoreductase. FT CHAIN 1..771 FT /note="Ribonucleoside-diphosphate reductase large subunit" FT /id="PRO_0000187230" FT DOMAIN 1..92 FT /note="ATP-cone" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00492" FT ACT_SITE 427 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P21524" FT ACT_SITE 429 FT /note="Cysteine radical intermediate" FT /evidence="ECO:0000250|UniProtKB:P21524" FT ACT_SITE 431 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P21524" FT BINDING 5..6 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250|UniProtKB:P23921" FT BINDING 11..17 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250|UniProtKB:P23921" FT BINDING 53 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250|UniProtKB:P23921" FT BINDING 57 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250|UniProtKB:P23921" FT BINDING 88 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250|UniProtKB:P00452" FT BINDING 202 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:P23921" FT BINDING 217 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:P23921" FT BINDING 226..228 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 243 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 256 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 427 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:P23921" FT BINDING 431 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:P23921" FT BINDING 603..606 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:P23921" SQ SEQUENCE 771 AA; 87754 MW; 6CA07F0C58EDC4F9 CRC64; MFVIKRNGYK ENVMFDKITS RIRKLCYGLN TDHIDPIKIA MKVIQGIYNG VTTVELDTLA AEIAATCTTQ HPDYAILAAR IAVSNLHKET KKLFSEVMED LFNYVNPKNG KHSPIISSIT MDIVNKYKDK LNSVIIYERD FSYNYFGFKT LEKSYLLKIN NKIVERPQHM LMRVAVGIHQ WDIDSAIETY NLLSEKWFTH ASPTLFNAGT SRHQMSSCFL LNMIDDSIEG IYDTLKRCAL ISKMAGGIGL SISNIRASGS YISGTNGISN GIIPMLRVYN NTARYIDQGG NKRPGVMAIY LEPWHSDIMA FLDLKKNTGN EEHRTRDLFI ALWIPDLFMK RVKDDGEWSL MCPDECPGLD NVWGDEFERL YTLYERERRY KSIIKARVVW KAIIESQIET GTPFILYKDA CNKKSNQQNL GTIKCSNLCT EIIQYADANE VAVCNLASVA LNMFVIDGRF DFLKLKDVVK VIVRNLNKII DINYYPIPEA EISNKRHRPI GIGVQGLADA FILLNYPFDS LEAQDLNKKI FETIYYGALE ASCELAEKEG PYDTYVGSYA SNGILQYDLW NVVPSDLWNW EPLKDKIRTY GLRNSLLVAP MPTASTAQIL GNNESVEPYT SNIYTRRVLS GEFQVVNPHL LRVLTERKLW NDEIKNRIMA DGGSIQNTNL PEDIKRVYKT IWEIPQKTII KMAADRGAFI DQSQSMNIHI ADPSYSKLTS MHFYGWSLGL KTGMYYLRTK PASAPIQFTL DKDKIKPLVV CDSEICTSCS G //