ID   E5AG35_9CAUD            Unreviewed;       744 AA.
AC   E5AG35;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
DE            EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
GN   ORFNames=P104_01040 {ECO:0000313|EMBL:CBX44447.1};
OS   Erwinia phage phiEa104.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Ounavirinae; Kolesnikvirus; Kolesnikvirus Ea214.
OX   NCBI_TaxID=925986 {ECO:0000313|EMBL:CBX44447.1, ECO:0000313|Proteomes:UP000006893};
RN   [1] {ECO:0000313|Proteomes:UP000006893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21097611; DOI=10.1128/JB.01293-10;
RA   Muller I., Kube M., Reinhardt R., Jelkmann W., Geider K.;
RT   "Complete genome sequences of three Erwinia amylovora phages isolated in
RT   north america and a bacteriophage induced from an Erwinia tasmaniensis
RT   strain.";
RL   J. Bacteriol. 193:795-796(2011).
CC   -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC       Catalyzes the biosynthesis of deoxyribonucleotides from the
CC       corresponding ribonucleotides. {ECO:0000256|RuleBase:RU003410}.
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:0000256|RuleBase:RU003410};
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC       chain family. {ECO:0000256|ARBA:ARBA00010406,
CC       ECO:0000256|RuleBase:RU003410}.
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DR   EMBL; FQ482083; CBX44447.1; -; Genomic_DNA.
DR   RefSeq; YP_004327079.1; NC_015292.1.
DR   GeneID; 10351168; -.
DR   KEGG; vg:10351168; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000006893; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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   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 {ECO:0000256|ARBA:ARBA00022533};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00492};
KW   Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW   ECO:0000256|RuleBase:RU003410};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00492};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003410}.
FT   DOMAIN          3..88
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
SQ   SEQUENCE   744 AA;  84809 MW;  26DF231537E8B653 CRC64;
     MIRNVKKSDG TVQPFDPSRL NRWAEWAANY GVDWAEIAVD AVKRCHDGCT TSDLQWAMIE
     ACIDRQTQAH ANMAGRLLIG NVYKEAFGGF RKIPTLTDFY DKMRTLNLWE DMGYSDSELD
     YLGLQINHYK DLNYGYAVVK QFRDKYAIKD ALTKRVYESP QFMFMGMALA VMQNQPKDRR
     IQDVIKLYEY LSDLKINAPT PYLNGLRSKK SGYASCCVIK GDDTAESIGI AEHIAYTMTC
     KQAGIGILLQ TRSKGDGVRN KTIVHQGKTP YFACINTAVK ANKQQTRGGS ATVGYTILDP
     EIDDLLRLNN PVTPPQKQLK FMDYQVGINE SFLRRVDKDD EWMLVSFKDA PELHKRMYGS
     YELFEVEYDR VMRNPGIKKK MVSARKLSKV FLKNRYETGR VYPFFTDNMN THTPFEDTIW
     NSNLCMEICL PTKAFKSMAE LYNPSVKAEG EIALCFLSSI VAGRVKPEEY EEVAYYTLLM
     IDNVMDIMEY PYEALKKSAQ YRRSVGVGIT NLAHYLASNF TNYSSPKGKR MMHNLAELHS
     YSLHRASLRL AKERGVCEGM EVSKYRNGWT PLEDYSQEVD NIVDSTLQFD WLQLHKDIKA
     NGGIRHSVLE AFMPNESSSL ATNTTNGLYP VRELKMFKKS PQGSVFFLAP DSEVIGDVYQ
     SAWDVPEKDM IECYAIFQKF TGQAISADFY MDYHKTGNKV SAKTALKSLI YAHRLGMKTQ
     YYMNSRVGVG ESSLKEMACE GCSL
//