ID A0A2H4P767_9CAUD Unreviewed; 753 AA.
AC A0A2H4P767;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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:ATW58011.1};
GN ORFNames=CNR34_00078 {ECO:0000313|EMBL:ATW58011.1};
OS Pseudomonas phage nickie.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Nickievirus; Nickievirus nickie.
OX NCBI_TaxID=2048977 {ECO:0000313|EMBL:ATW58011.1, ECO:0000313|Proteomes:UP000241592};
RN [1] {ECO:0000313|EMBL:ATW58011.1, ECO:0000313|Proteomes:UP000241592}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-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; MG018927; ATW58011.1; -; Genomic_DNA.
DR OrthoDB; 2980at10239; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000241592; 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 CDD; cd01679; RNR_I; 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:UP000241592}.
FT DOMAIN 1..90
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 753 AA; 84830 MW; C4072DD852446AC5 CRC64;
MQVTKSNGSK QDFDIAKIMA HSEWACRGLN VCQSELDASL QIQFYEGMST SEIAQAQIQT
ASSLISLAQP EFDKVTARFV LQRIYKQVTG GDIKYPSIRA MLSQGTLFQQ LDNRLLDGRF
DLEALDAAIQ PERDDLFAYL GIQTIADRYL LTRPLTANGS KAIYEMPQHF WMRVAMGLSL
LEADPTASAI EFYNVFSQMD YVPSTPTLFN SGTRHAQMSS CYLSYVPDDL ELIFDLGITQ
SALLSKFAGG VGTDWTEVRA NKSVIKSTNG KSNGIVPFLK IYNQTAVAVN QGGKRKGAFS
PYLEIWHDDF TDYCDLRLQT GDDNLRTHDI HPAAWVPDLF MERKEAGGMW SFFCPSDVPG
LHDLYGDDFK KAYEAAEAAG LARRQLPAMD VWKNHLDKLV RTGYPWITFK DACNRRNPQA
HAGVVHNSNL CTEITLINSK DETAVCNLGS IVLGNHVRNG QIDTDKLQRT VKTAVRALDN
VIDLNFYPTP ETERSNLRHR PIGLGVMGYA EAMLQCGIDW ESQDHLQWAD ETFEQINFYS
IKASMELAKE RGAYPTFPGS TWSQGKLTID TAKDQKVNFF SPVEWQLLRE DVVKYGIRNS
NIMAIAPTAT IANIVGTTEC IQLINERELT KDNLSGRFLQ INPLHKYNRP ELVKTVWEVD
QLWTIKAAAR RQKWICQSQS LNLYKTKDVK GRTLDLWYTT AWKLDVKTTY YLRNQGATDG
AGRIEDKAEV TAAPEVVVAP EVITEYFQCE ACQ
//