ID A0A2I7RW25_9CAUD Unreviewed; 754 AA.
AC A0A2I7RW25;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=NVP1244A_151 {ECO:0000313|EMBL:AUR97853.1};
OS Vibrio phage 1.244.A._10N.261.54.C3.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Ackermannviridae.
OX NCBI_TaxID=1881412 {ECO:0000313|EMBL:AUR97853.1, ECO:0000313|Proteomes:UP000282353};
RN [1] {ECO:0000313|EMBL:AUR97853.1, ECO:0000313|Proteomes:UP000282353}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kauffman K.M., Hussain F.A., Yang J., Arevalo P., Brown J.M., Chang W.K.,
RA VanInsberghe D., Elsherbini J., Cutler M.B., Kelly L., Polz M.F.;
RT "A major lineage of nontailed dsDNA viruses as unrecognized killers of
RT marine bacteria.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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; MG592609; AUR97853.1; -; Genomic_DNA.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000282353; 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 754 AA; 85392 MW; 5162ABD0FAF30BC5 CRC64;
MTQIIKRNGE RTPLDVDRPN NVVMKACEGL DGVSWSEVMA VAKLQFVDGT TTERIQEILI
KAAEQLITPE SPNYQYVAAR LQMYDVRKRA YGKYKPPTFK EHCHNMVKLG KYDSDMIDFT
DEEFAQFEQF IDHKRDKSFS TAASGQLVDK YLIRDRTKHR AFFESPQMMY MAIAVTLLRG
DMVRIKRFYD GASLFKFSLP TPIMSGVRTP TRQFSSCVLI KSGDTLDSII ATSGAIAKYV
SKRAGIGVDE SSIRGVDAPI RGGEMVHTGV VPFLKYHVGA LKSCSQGGVR GGSATAYYPM
WHWQFEDIIV LKNNRGIDEN RERKVDYGIQ LNGEMIRRLL DNEDMWFFSP EEVPEMYKAF
FDDQEKFRVE YEKAITIAGA GLIRGRCIKA ADAWDMMLGE RSETGRIFFA FVDNMNIQGP
FSPHIDPVTQ SNLCLEIALP TRSFEHEFDE EGRIALCTLA SFNMSQFLDL DESLDELMMY
ADALVRALDG LLSYQDYPMI QAKIATDEFR TLGVGIVNLA DFLCRKGMKY GSKAALNEVN
EWMERFAYAL TSASVELAEE KGACERWEDT CYGEGKFPWE LRNRNIDAQL DTVCDMGDEW
ESLRSRISKS GIRNATLMAI APTESSSQVL NATNGVEQPK APMVIKASKS GLMKQIVPTP
ELVDQYEYLW GNANPTAYLI TCAVLQKWVD QSISTNTFYN PSKTNDVIER YQLLRDIIMF
YHLGGKTLYY QNVNDGAGDE LEPEKEPECD TCVV
//
