ID   H6BIE3_9CAUD            Unreviewed;       772 AA.
AC   H6BIE3;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
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=SXDG_00161 {ECO:0000313|EMBL:AFB17677.1};
OS   Synechococcus phage S-RIM8 A.HR1.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Kyanoviridae; Neptunevirus; Neptunevirus srim18.
OX   NCBI_TaxID=869724 {ECO:0000313|EMBL:AFB17677.1, ECO:0000313|Proteomes:UP000007566};
RN   [1] {ECO:0000313|EMBL:AFB17677.1, ECO:0000313|Proteomes:UP000007566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S-RIM8 A.HR1 {ECO:0000313|EMBL:AFB17677.1};
RX   PubMed=22388749; DOI=10.1073/pnas.1120310109;
RA   Marston M.F., Pierciey F.J.Jr., Shepard A., Gearin G., Qi J., Yandava C.,
RA   Schuster S.C., Henn M.R., Martiny J.B.;
RT   "Rapid diversification of coevolving marine Synechococcus and a virus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:4544-4549(2012).
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; JF974288; AFB17677.1; -; Genomic_DNA.
DR   RefSeq; YP_007518271.1; NC_020486.1.
DR   GeneID; 14697047; -.
DR   KEGG; vg:14697047; -.
DR   OrthoDB; 2980at10239; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000007566; 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; 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   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          8..98
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
SQ   SEQUENCE   772 AA;  87910 MW;  C2042DE180687167 CRC64;
     MEKGMKEIHV IKRNGEQETL DLDKIHVMVE HACRGLAGVS ESQVEMNANL QFFDGIETAA
     IQEILVRSAN DLISLDAPNY QFVAARLLLF GLRKAVYNGH PDGHPPLYDH VQKCTELGLY
     DGTLVNAYSA EEWEKLNSFI DHDRDFLFTY AGIRQVVDKY LVQDRSSGKV YETPQFMYMM
     IAATLFQDDD KFYRLEYVKK YYDAISKHKI NIPTPIMAGV RTPLRQFASC VLVDVDDTLD
     SIFSSDMAIG KYVAQRAGIG INAGRIRGIN SKIRGGEVQH TGVVPFLKKF ESTVRCCTQN
     GIRGGSATVH FPIWHQEIED IIVLKNNKGT EDNRVRKLDY SIQFSKLFYE RFISNGEISL
     FSPHNVPGLY DAFGTDGFDE LYVRYERDES IPRKTIGAQE LFLDLLKERA ETGRLYIMNI
     DHCNTHSSFK DKVNMSNLCQ EITLPTDPIQ HIDGRGEIAL CILSAINVGK LKSLDELDEL
     CELAVRGLDA LIDYQEYPVK AAEESTRNRR SLGIGYIGLA HYLAKHGAKY DTTKAHDLVH
     KLTERFQYAL LNASMRMAME KGPCGYFGKT KYADGILPID TYKKEVDEIV PNELQCDWEF
     LRERILQYGL RHSTLSAQMP SESSSVVSNA TNGIEPPRDF LSVKKSKKGP LKQIVPQYNT
     LKNNYTLLWD MPNNDGYIKV TAVIQKFFDQ AISGNWSYNP EQYPDNEVPV SVMAKDLLTT
     YKYGWKTSYY QNTYDNKKDA DVEENMQRAS EIDNLIEQLL ESEEEDCESC KI
//