ID E3SIK7_9CAUD Unreviewed; 769 AA.
AC E3SIK7;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
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 Name=nrdA {ECO:0000313|EMBL:ADO97150.1};
GN ORFNames=SSM1_200 {ECO:0000313|EMBL:ADO97150.1};
OS Synechococcus phage S-SM1.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Kyanoviridae; Thetisvirus; Thetisvirus ssm1.
OX NCBI_TaxID=444859 {ECO:0000313|EMBL:ADO97150.1, ECO:0000313|Proteomes:UP000006523};
RN [1] {ECO:0000313|EMBL:ADO97150.1, ECO:0000313|Proteomes:UP000006523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6501-1 {ECO:0000313|EMBL:ADO97150.1};
RX PubMed=20662890; DOI=10.1111/j.1462-2920.2010.02280.x;
RA Sullivan M.B., Huang K.H., Ignacio-Espinoza J.C., Berlin A.M., Kelly L.,
RA Weigele P.R., DeFrancesco A.S., Kern S.E., Thompson L.R., Young S.,
RA Yandava C., Fu R., Krastins B., Chase M., Sarracino D., Osburne M.S.,
RA Henn M.R., Chisholm S.W.;
RT "Genomic analysis of oceanic cyanobacterial myoviruses compared with T4-
RT like myoviruses from diverse hosts and environments.";
RL Environ. Microbiol. 12:3035-3056(2010).
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; GU071094; ADO97150.1; -; Genomic_DNA.
DR RefSeq; YP_004323091.1; NC_015282.1.
DR GeneID; 10327428; -.
DR KEGG; vg:10327428; -.
DR OrthoDB; 2980at10239; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000006523; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006523}.
FT DOMAIN 8..98
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 769 AA; 87146 MW; A7550212ED149E51 CRC64;
MEKGMKEIHV IKRNGEKTPL NLDKVHAMVE HACRGLAGVS ESQVEMNANL QFFDGIKTSD
IQEILIRSAN DLISLDAPNY QFVAARLLLF GLRKAVYNGH PDGHPPLLEH VKKCVGIGVY
DSAILQKYTD EEWEKLNDFM DHERDFLFTY AGIRQVTDKY LVQDRSSGEI YETPQFMYMM
VAATLFQDDD KFYRLEYVKK YYDAISKHRL NIPTPIMAGV RTPLRQFASC VLVDVDDTLD
SIFSSDMAIG QYVAQRAGIG INAGRIRGIN AKIRGGEVQH TGVIPFLKKF EATVRCCTQN
GIRGGSATVH FPIWHQEIED ILVLKNNKGT EDNRVRKLDY SIQISKLFYE RFIQNGTISL
FSPHDVPGLY DAFGTDSFDA RYVDYESDQS IPRKTVDAQK LILDLLKERA ETGRVYIMNI
DHCNSHSSFK DKVNMSNLCQ EITLPTDPLQ HIDGQGEIAL CILSAINVGK LKNLDELDEL
CDLAVRGLDA LIDYQEYPVK AAEQSTTNRR SLGIGYIGLA HYLAKNGAKY DSAKAHDLVH
KLTERFQYAL LTASNRMAME KGPCGYFGKT KYADGILPID TYKSDVDEIV PNELQCDWEF
LRSRILQYGL RHSTLSAQMP SESSSVVSNA TNGIEPPRAY LSIKKSKKGP LKQIVPSYTT
LKNAYTLLWD MHNNDGYIKV TAVMQKFFDQ AISGNWSYNP ENYPDNEVPV SEMAKDLLNT
YKYGWKTSYY QNTYDIKKDG DDEEVKTNVD NLIDELLNTE EEDCDSCKV
//
