ID A0A0B6VP05_9CAUD Unreviewed; 751 AA.
AC A0A0B6VP05;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, 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};
GN Name=nrdA {ECO:0000313|EMBL:BAQ22898.1};
OS Edwardsiella phage PEi20.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Straboviridae; Tevenvirinae; Kanagawavirus; Kanagawavirus pei20.
OX NCBI_TaxID=1608310 {ECO:0000313|EMBL:BAQ22898.1, ECO:0000313|Proteomes:UP000204657};
RN [1] {ECO:0000313|EMBL:BAQ22898.1, ECO:0000313|Proteomes:UP000204657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Yasuike M., Nishiki I., Iwasaki Y., Nakamura Y., Fujiwara A., Hassan E.S.,
RA Mahmoud M.M., Kawato Y., Nagai S., Kobayashi T., Ototake M., Nakai T.;
RT "Complete genome sequences of Edwardsiella bacteriophages, PEi20 and
RT PEi26.";
RL Submitted (FEB-2015) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP014714; BAQ22898.1; -; Genomic_DNA.
DR RefSeq; YP_009190406.1; NC_028683.1.
DR GeneID; 26519265; -.
DR KEGG; vg:26519265; -.
DR OrthoDB; 2980at10239; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000204657; 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; 1.10.1650.20; -; 1.
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:UP000204657}.
FT DOMAIN 1..90
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 618..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 751 AA; 85046 MW; C42C828FD2A2CA53 CRC64;
MQVVKSSGIA TLFEPHKIIQ VLDWATKNTN IDPYDLYERV KPYLQDGMST RDIQIAIIKV
AANAISVQEP DFQYVASNLA MFALRKDVYG QFEPPSFIDH ISSVVNAGLY DKEILQKWSA
EEIAYLESRI DHDRDFELTY AGTMQLKEKY LVKNRSNGKV YETPQFAFML IGMCLHQDEP
VDRIKHAVRF YDAVSKRQIS LPTPIMAGVR TPTRQFSSCV VIEGGDSLDS INTTNASIIK
YISKRAGIGV NAGMIRAEGS KIGHGEVKHT GVIPFWKTIQ ASVKSCSQGG VRGGAATLYY
PIWHLEVENL LVLKNNKGVD ENRIRHLDYG VQINDLMLER LIKNDYITLF SPEVCGGLLY
EDYFKDPEAF RNLYQTLERD PTVRKKRIKA LELFETFFTE RSGTARIYPY FVDNVGGHGP
FIRDIATVKQ SNLCCEIALP TKDVGGDDPE IALCTLAAFV LDSFDYQDQD MVNELAEIQV
RALDNLLDYQ DYPVKEALKA KKRRALGVGV TNYAGFLANN FATYDDANDL THELFERLQY
GLITASVKLA KEKGRCEYYS DTRWSRGELP IDWYNKKIDN VAAPNYVCDW SKLREDLATY
GIRNSTLSAL MPCESSSQVS NSTNGIEPPR GPVSVKESKE GSFNQVVPKV EDNIELYDYL
WQMTKRGMRG YLTQAAIMQK FVCQSISTNF DYDPQNFPKG KVEMSTMMRD MLYFWSLGGK
TAYYHNTRDG SGTDDYEIEM PKADDCAACK L
//
