ID   A0A0N9SI45_9CAUD        Unreviewed;       744 AA.
AC   A0A0N9SI45;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
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};
OS   Escherichia phage SUSP2.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Ounavirinae; Suspvirus; Suspvirus SUSP2.
OX   NCBI_TaxID=1718669 {ECO:0000313|EMBL:ALH47091.1, ECO:0000313|Proteomes:UP000202045};
RN   [1] {ECO:0000313|EMBL:ALH47091.1, ECO:0000313|Proteomes:UP000202045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=28096488;
RA   Keen E.C., Bliskovsky V.V., Malagon F., Baker J.D., Prince J.S.,
RA   Klaus J.S., Adhya S.L.;
RT   "Novel 'Superspreader' Bacteriophages Promote Horizontal Gene Transfer by
RT   Transformation.";
RL   MBio 8:0-0(2017).
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; KT454806; ALH47091.1; -; Genomic_DNA.
DR   RefSeq; YP_009210966.1; NC_028935.1.
DR   GeneID; 26637513; -.
DR   KEGG; vg:26637513; -.
DR   OrthoDB; 2980at10239; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000202045; 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;  85233 MW;  F84FAE55A8D0CB2C CRC64;
     MIKTIRKSDG TIVPFEPERL NKWASWADKR GIIWSEVTME AMKRVYEGCS TKEMHQAMID
     VCIDKQTQEY SDMAGRLLLG IIYKEAFGGF TKVPQLFNFV MKMEQMGLWE HMDYTEQEID
     YLQGHIVHSK DISYGYAVLK QFRDKYGIRD IKSGRLFESP QFMFMGMAMK AFERQPKHRR
     LEDVIKLYTY LSDLKINAPT PYLNGLRATK SGYASCCLIK ANDTAESLGI ATKVAYDMTT
     KQAGIGMLME TRTIGDGIRQ NTIEHMGKLP YYKLVRAAVE ANKQKSRGGS ANNFYTALDP
     QIEDLLRLKH PTTVPSKRIN EMDYSFGAND YFWQCVQYDT DWLLFSYKDA PKLYDMFYTA
     SADEFAMAVG HAVHSGVKHK RVKAREVAKL FIQQRYATGR VYPFFTNNAN THTPFKELLK
     MSNLCMEIVL PVHGFEDERD LYSYTAPKED GEVALCFLAS LVAGRITEDE YADVAYYALA
     MVDSVIDLMD YPYPSMRNHV QKRRSVGIGL TNVAHYLAKN YVNYSSRAGK TKLHELAEMH
     SYYLHEASLR LAKERGVPEY MQFTKYPEGW VPPKTANRKI DTKHDAKLRY DWDDLADRIK
     ANGGIRNSVL EAYMPNESSS LATNTTNGLY PIRDFILTKK SATGNVLFIV PDYEELKYVY
     EIAWDIDTFD MIDCYAIVQK FTGQAISSDF YVDYSKSKKV SLEQALKYMI YANSVGMKTM
     YYLNSRIGVG KSALQDAYCE GCGV
//