RIR1_FRG3G
ID RIR1_FRG3G Reviewed; 565 AA.
AC Q6GZT8;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Putative ribonucleoside-diphosphate reductase large subunit;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleotide reductase large subunit;
GN ORFNames=FV3-038R;
OS Frog virus 3 (isolate Goorha) (FV-3).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Pimascovirales; Iridoviridae; Alphairidovirinae; Ranavirus.
OX NCBI_TaxID=654924;
OH NCBI_TaxID=30343; Dryophytes versicolor (chameleon treefrog).
OH NCBI_TaxID=8404; Lithobates pipiens (Northern leopard frog) (Rana pipiens).
OH NCBI_TaxID=45438; Lithobates sylvaticus (Wood frog) (Rana sylvatica).
OH NCBI_TaxID=8316; Notophthalmus viridescens (Eastern newt) (Triturus viridescens).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15165820; DOI=10.1016/j.virol.2004.02.019;
RA Tan W.G., Barkman T.J., Gregory Chinchar V., Essani K.;
RT "Comparative genomic analyses of frog virus 3, type species of the genus
RT Ranavirus (family Iridoviridae).";
RL Virology 323:70-84(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 -!- PATHWAY: Genetic information processing; DNA replication.
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}.
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DR EMBL; AY548484; AAT09697.1; -; Genomic_DNA.
DR RefSeq; YP_031616.1; NC_005946.1.
DR SMR; Q6GZT8; -.
DR GeneID; 2947817; -.
DR KEGG; vg:2947817; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000008770; Genome.
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; IPR000788; RNR_lg_C.
DR InterPro; IPR039718; Rrm1.
DR PANTHER; PTHR11573; PTHR11573; 2.
DR Pfam; PF02867; Ribonuc_red_lgC; 2.
DR PRINTS; PR01183; RIBORDTASEM1.
PE 3: Inferred from homology;
KW Deoxyribonucleotide synthesis; Disulfide bond; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..565
FT /note="Putative ribonucleoside-diphosphate reductase large
FT subunit"
FT /id="PRO_0000410591"
FT ACT_SITE 256
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 258
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 260
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 74..75
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 256..260
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 400..404
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 75
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 82
FT /note="Allosteric effector binding"
FT /evidence="ECO:0000250"
FT SITE 112
FT /note="Allosteric effector binding"
FT /evidence="ECO:0000250"
FT SITE 273
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 534
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 535
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 560
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT SITE 563
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT DISULFID 75..273
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 565 AA; 62363 MW; 790187621FAFC2E7 CRC64;
MTSAVSFPIT SQASDMLSKF YGSDLGSLYG TLAEKYSGGK PELAEKLRDY ACKGWFGYSS
PILTSVTGSG LPISCFLLYV PDTIEGLVDH TSELRWLSVM GGGVAGHWDD VRGPSAKSCG
TIPFLHTVDA DMSAYWQGKV RRGSYAAYMS ISHPDLIEFI TMRTPTGDVN RKNLNLHHGV
NITDTFMRCV ERGENWDLVD PKSGAVAHTV SARELWERIL ETRFRTGEPY LNFIDTANRG
LHPALKRKGL KIRGSNLCNE IHLPTAADRT AVCCLSSVNL ERYDEWRETD LVECLVEMLD
NVIQTFVDEA PLKTPHTARA VRSAAGERSI GLGAMGWARY LQKHRIPFDS EEAVRLTGII
FRGIKSAAVR ATRALAKERG EAPDLTGYGV RNAHLLAVAP NANSALLLGT SPSVEPEIGA
AYVHRTRVGS HQAVNPYLKR DLESLGLDTE EVWDSIVSNK GSVQHIAALP DSLKKVYKTS
FEMDQRVIVR QAAERQRHLC QGQSLNLFFP IGADKTNLSD VHRLAWKSGC KGLYYLRTCA
GRTGHKIFEA KKNPEKTEEC TACQG
