ID A0A0C5PV43_9CAUD Unreviewed; 760 AA.
AC A0A0C5PV43;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, 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 Name=83 {ECO:0000313|EMBL:AJQ20902.1};
GN ORFNames=DET7_83 {ECO:0000313|EMBL:AJQ20902.1};
OS Salmonella phage Det7.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Ackermannviridae; Cvivirinae; Kuttervirus; Kuttervirus Det7.
OX NCBI_TaxID=454798 {ECO:0000313|EMBL:AJQ20902.1, ECO:0000313|Proteomes:UP000032405};
RN [1] {ECO:0000313|EMBL:AJQ20902.1, ECO:0000313|Proteomes:UP000032405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=25953168;
RA Casjens S.R., Jacobs-Sera D., Hatfull G.F., Hendrix R.W.;
RT "Genome Sequence of Salmonella enterica Phage Det7.";
RL Genome Announc. 3:0-0(2015).
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; KP797973; AJQ20902.1; -; Genomic_DNA.
DR RefSeq; YP_009140260.1; NC_027119.1.
DR GeneID; 24366628; -.
DR KEGG; vg:24366628; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000032405; 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 2..92
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 760 AA; 86353 MW; 2336B7FA87C49054 CRC64;
MINIIKRDGS SVPFDIEKLH TVIERACDGL EGVSVSEVEA ASKIQFTDNM KTERIQDIII
QAAATLISVD KPNYQYVAAR LKSYDLRKVV YGQYKPPHLL DIFAKNTKLG VYDREFLELY
SKEEFEELNT VINHKRDKNF TWAAMGQLTQ KYLLRDRSSD SKVYYETPQV MYMAIAMALF
SAWDKESRLT MVKKFYEYAS TGKFSLPTPI MSGVRTPTRQ FSSCVLIKTG DTLDSINATA
KSIVDYVSKR AGIGFDVGAI RGIGSPIRKG EMVHTGLVPF IKYLTGALKS CSQGGIRGGS
ATCYVPIWHY QFDDVVVLKN NRGLEENRER RIDYGIQINR VMFERLVNKQ PLYLFDPKDN
REMYEAFFSD VNKFREMYDN MIKAADAGLC RSKKLQAEEV FQMLLDQRSD TGRIYVAFVD
HMNEYSPFNL DTIYSSNLCL EIALPTREFQ QYDDEDGRIA LCTLASFNLT AFEDPTEMED
VAFVLVSALD MLLEYQDYPA RQARLAVEEY RPLGIGIVNV AHFLAKNFTG YGSPIGLELL
DKWMAHLHFY LVKASNRLAM RFGSCKKSTI HDSGFVTADL QPLPLDILPN GKKPVGQAYG
LDWEGLKQNL SEYGIRNATL LAVAPTESSS QVLNATNGIE PPKGLISIKG SKDGVYKQIV
PDVETLGPLY DLKWNLDCIE YLKTAAVIQR WVDQSISTNT WYDPEKYPEG KIPRSLMMQD
ILSFYMWGGK TLYYNTNKDS KEDEELKQIE DPNHCDTCVV
//
