ID RIR1_MIMIV Reviewed; 881 AA. AC Q7T6Y8; DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 07-DEC-2004, sequence version 2. DT 27-MAR-2024, entry version 92. DE RecName: Full=Ribonucleoside-diphosphate reductase large subunit; DE EC=1.17.4.1; DE AltName: Full=Ribonucleotide reductase large subunit; GN Name=RNR1; OrderedLocusNames=MIMI_R313; OS Acanthamoeba polyphaga mimivirus (APMV). OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes; OC Imitervirales; Mimiviridae; Megamimivirinae; Mimivirus; OC Mimivirus bradfordmassiliense. OX NCBI_TaxID=212035; OH NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba). RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Rowbotham-Bradford; RX PubMed=15486256; DOI=10.1126/science.1101485; RA Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H., RA La Scola B., Susan M., Claverie J.-M.; RT "The 1.2-megabase genome sequence of Mimivirus."; RL Science 306:1344-1350(2004). 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 (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 -!- SUBUNIT: Heterotetramer composed of a homodimer of the large subunit CC (R1) and a homodimer of the small subunit (R2). Larger multisubunit CC protein complex are also active, composed of (R1)n(R2)n (By CC similarity). {ECO:0000250}. 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; AY653733; AAQ09572.2; -; Genomic_DNA. DR RefSeq; YP_003986816.1; NC_014649.1. DR SMR; Q7T6Y8; -. DR GeneID; 9924930; -. DR KEGG; vg:9924930; -. DR OrthoDB; 2980at10239; -. DR Proteomes; UP000001134; Genome. 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; 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. PE 3: Inferred from homology; KW Allosteric enzyme; ATP-binding; Deoxyribonucleotide synthesis; KW Disulfide bond; Early protein; Nucleotide-binding; Oxidoreductase; KW Reference proteome. FT CHAIN 1..881 FT /note="Ribonucleoside-diphosphate reductase large subunit" FT /id="PRO_0000187229" FT DOMAIN 69..160 FT /note="ATP-cone" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00492" FT ACT_SITE 493 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 495 FT /note="Cysteine radical intermediate" FT /evidence="ECO:0000250" FT ACT_SITE 497 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 271 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 286..287 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 315 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 493..497 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 675..679 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 287 FT /note="Important for hydrogen atom transfer" FT /evidence="ECO:0000250" FT SITE 294 FT /note="Allosteric effector binding" FT /evidence="ECO:0000250" FT SITE 324 FT /note="Allosteric effector binding" FT /evidence="ECO:0000250" FT SITE 510 FT /note="Important for hydrogen atom transfer" FT /evidence="ECO:0000250" FT SITE 809 FT /note="Important for electron transfer" FT /evidence="ECO:0000250" FT SITE 810 FT /note="Important for electron transfer" FT /evidence="ECO:0000250" FT SITE 876 FT /note="Interacts with thioredoxin/glutaredoxin" FT /evidence="ECO:0000250" FT SITE 879 FT /note="Interacts with thioredoxin/glutaredoxin" FT /evidence="ECO:0000250" FT DISULFID 287..510 FT /note="Redox-active" FT /evidence="ECO:0000250" SQ SEQUENCE 881 AA; 101472 MW; BC4A893F2212E068 CRC64; MNSKNSIILD NLADVSDIID YEQNSIDYQR SIKNIEQLKS TEATEITNKL AINKAKKSSN ILLEVPKETI YLDHNGSIQV ITSEIIRTYV EKIFEKMEVT HLDIDKMTKN IFPKLKSINT IKDIDNQIIS TASEMVTDHY DYPKIAVWIL MTNLHDNTSD DFLETAEKLY NNKSESNKNA PIISENIYNF IKKHIKEINR VIRYDRDYNL TIFGFRTLEK SYLKRINKKI VERPQHLFMR VAITLHYRKN DLDRIFETYK YLSKGYFTHA TPTLFNAGTT HEQLSSCFLL GIGDSLEEIS ECWKECALIS KHAGGIGIHM TNIRVEGAYI ASTQGEAGGL RVLTIFNDIS RYANQGGKRP GSFAIFIEPW HGDIFFFLDL KKNTGAETER ARDLFLGLMI NDIFMERVYK DDVWSLMCPS QCPNLLNKYG DEFTKEYLKY ESEGIYLKQI RAIDLWFKIM ESQIETGVPY VMFKDAINDK SNQINIGVVN GSNLCCEIVE VSDKNNFSVC NLSSICLPRF VKIIDEVPTF NYQKLFKISR ILTRNLNNII DINFYPLDKT RITNLRDRPI GIGVQGLADV FAMFKTPFDS EIARDLNRKI FETIYYGALT ESNKLAREFG TYQTYQGSPI SQGKFQFDLW NFDKSQLSGM WDWELLRQEI LNHGVRNSLV TTCMPTASTS QIMGWNECIE PYTENIYSRS TMAGEYFVIN KHLIKDLIEL GVWNSEMVDL IKYYKGSVAN IPNIPDNIKA IYRTVWEIPQ KSIIEMAADR APFVDQTQSM NLYIDKPSFA RLNSCLFYAW RKGLKTGMYY LRSKPASSAN QFGIDIDKIK EIESKNGIKK QEDTFDLTDL TNTINQQVSG MVCRFVPAHL RKPGECLSCD G //