ID A0A410T6P8_9CAUD Unreviewed; 781 AA.
AC A0A410T6P8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 14.
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=ValB1MD_236 {ECO:0000313|EMBL:QAU04533.1};
OS Vibrio phage Va1.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes.
OX NCBI_TaxID=2508852 {ECO:0000313|EMBL:QAU04533.1, ECO:0000313|Proteomes:UP000289494};
RN [1] {ECO:0000313|EMBL:QAU04533.1, ECO:0000313|Proteomes:UP000289494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Li C., Zhang Y., Liang Y.;
RL Submitted (JAN-2019) 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 -!- PATHWAY: Genetic information processing; DNA replication.
CC {ECO:0000256|ARBA:ARBA00005160, 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; MK387337; QAU04533.1; -; Genomic_DNA.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000289494; 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:UniProtKB-UniPathway.
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:UP000289494}.
FT DOMAIN 36..125
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 781 AA; 89943 MW; 788B4CC110EF8788 CRC64;
MSKRYNKLSL DKVSEAVQQN EKIDISNQDT MKASQITIIK RKGHKEPFKP EKLRKVCLWA
ADNKEYLADE LIRDTEIKLH KEIHIKDMYQ QLIVTAVNKI SMLQPVWEEI AAKLQLLSYY
KETYNIASDN QYPHLRDVLA LGVERKIYDK ETVQSYTPQE IDALNDAIKP ERDLLFNFKG
LVSFFDKYCL NYTKTKKLEL PQHAYMRVAM ALMANEKERV KRVIEEYNNV SSHNYTRATP
IMLNALTPGQ QLSSCVLSTL ADDSHSILDT GKNLGIYSKF KGGTALDISA MRAKGGYIEG
TQGYSSGPVP FNKFFEAIMK AWNQGGKRPG ALAVYFSWWH LDVMDLLSLK SNGGTDENRA
RGLQFGCKLN DLFIEAVIED EDIHLFDPKD TPELIGKFGE EFNELYRSYV QKTNVRSKKV
RAREIWNKIF KERSETGNIY LFHEENVNES TLLKRYIGSS NLCTEILLPS RPSESISEQL
VTMEDGSTEI VKRYKAGEIA LCNLSSFNLL KWYYMSTEER METIRTLVRG LDNTVDLANY
PVKEGKHSNM MYRYLGVGVL NYTNYLALKE IVIDSKAAAE ETDALFDEFS YMVISASCEL
AIEKGKFEKF YETEWSEGIL PIHKANQNAM KLTDYEPDWN RWNELAEKVR TFGIRNAQLM
AIAPTATSGK AINAIESIEP IHDFFYKEEG TMTVPTVVPN FRKNNRFYKK SFDCNQYALI
NNAAVRQKWL DQTQSVNVYY KRPDSLWDMS KLHIYGFKLG MCTFYYLKQT KDSDDACESC
T
//