ID A0A0E3G5G3_9CAUD Unreviewed; 773 AA.
AC A0A0E3G5G3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=Syn7803C2_160 {ECO:0000313|EMBL:AIX45079.1}, Syn7803C85_163
GN {ECO:0000313|EMBL:AIX20626.1}, Syn7803US33_160
GN {ECO:0000313|EMBL:AIX29841.1};
OS Synechococcus phage ACG-2014e.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Kyanoviridae; Chalconvirus; Chalconvirus acg2014e.
OX NCBI_TaxID=1493510 {ECO:0000313|EMBL:AIX45079.1, ECO:0000313|Proteomes:UP000033005};
RN [1] {ECO:0000313|Proteomes:UP000033005, ECO:0000313|Proteomes:UP000185283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Syn7803C2 {ECO:0000313|EMBL:AIX45079.1}, Syn7803C85
RC {ECO:0000313|EMBL:AIX20626.1}, and Syn7803US33
RC {ECO:0000313|EMBL:AIX29841.1};
RA Gregory A.C., LaButti K., Copeland A., Woyke T., Sullivan M.B.;
RT "Ecological redundancy of diverse viral populations within a natural
RT community.";
RL Submitted (DEC-2013) 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; KJ019054; AIX20626.1; -; Genomic_DNA.
DR EMBL; KJ019094; AIX29841.1; -; Genomic_DNA.
DR EMBL; KJ019156; AIX45079.1; -; Genomic_DNA.
DR RefSeq; YP_009134662.1; NC_026928.1.
DR GeneID; 24172304; -.
DR KEGG; vg:24172304; -.
DR OrthoDB; 2980at10239; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000033005; Genome.
DR Proteomes; UP000185283; Genome.
DR Proteomes; UP000185284; 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}; Coiled coil {ECO:0000256|SAM:Coils};
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:UP000033005}.
FT DOMAIN 7..98
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT COILED 739..766
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 773 AA; 87540 MW; B8C4BA0F8CFE8919 CRC64;
MTNGHGIKVQ KRDGAVEALN LDKIHKMVEE ACEGLGGGVS ASQVEMSSGL QFFDGIKTSD
IQEILVRSAS DLISLDNPNY QFVAARLLLF AVRKQVFGPD WVQGYPTVLD HAQKCVSTGV
YDDSILRKYT QEEWNKIDSY MDHDRDMLFT YAGLRQVVDK YLVQDRSCGE MYETPQYMYM
MIAATLFQNY PTETRLDYVR RYYNAISKHK INIPTPIMAG VRTPLRQFAS CVLVDANDSL
DSIFSSDMAI GRYVAQRAGI GINAGRIRGI NSKIRGGEVQ HTGVVPFLKK FESTVRCCTQ
NGIRGGSATV HFPIWHQEIE DIIVLKNNKG TEDNRVRKLD YSIQISKLFY ERFIANGEIS
LFSPHDVPGL YDAFGTDAFD ACYVDYESDQ SIPRKTIGAQ ELFLDILKER AETGRLYLMN
IDHCNSHSSF KDKVSMSNLC QEITLPTKPL EHIDDPNGEI ALCILSAVNI GKVSKKDELE
EICDLAVRGL EELVDYQEYP VEAAELSTKN RRSLGIGYIG LAHYLAKQGE HYDDPKAWKL
VHDLSESFQY YLLKSSNTIA KEKGKCGYFD RTKYADGILP IDTYKRDIDE FCGTELNHDW
DSLRTSITTY GLRHSTLSAQ MPSESSSVVS NATNGIEPPR AFLSTKKSKK GPLKQIVPQY
GSLKNNYTLL WDMKGNDGYI KIVAAMQKFF DQAISGNWSY NPENYENNEV PVSVMAGDFL
KTYKYGWKTS YYQNTYDNKD DLQELTEEKK ESIEDLLSQI LETEEEDCDS CKI
//
