ID M1U339_9CAUD Unreviewed; 764 AA.
AC M1U339;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=CYWG_00139 {ECO:0000313|EMBL:AGG54423.1};
OS Cyanophage S-SSM6b.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Kyanoviridae; Greenvirus.
OX NCBI_TaxID=682651 {ECO:0000313|EMBL:AGG54423.1, ECO:0000313|Proteomes:UP000225635};
RN [1] {ECO:0000313|EMBL:AGG54423.1, ECO:0000313|Proteomes:UP000225635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S-SSM6b {ECO:0000313|EMBL:AGG54423.1,
RC ECO:0000313|Proteomes:UP000225635};
RG The Broad Institute Genome Sequencing Platform;
RA Henn M.R., Sullivan M.S., Osburne M.S., Levin J., Malboeuf C., Casali M.,
RA Russ C., Lennon N., Erlich R., Young S.K., Koehrsen M., Yandava C.,
RA Zeng Q., Alvarado L., Anderson S., Berlin A., Borenstein D., Chen Z.,
RA Engels R., Freedman E., Gellesch M., Goldberg J., Green L., Griggs A.,
RA Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA Mehta T., Park D., Pearson M., Roberts A., Ryan E., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yu Q.,
RA Coleman M.L., Huang K.H., Weigele P.R., DeFrancesco A.S., Kern S.E.,
RA Thompson L.R., Fu R., Hombeck B., Chisholm S.W., Haas B., Nusbaum C.,
RA Galagan J., Birren B.;
RT "The Genome Sequence of Cyanophage S-SSM6b.";
RL Submitted (MAR-2010) 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; HQ316603; AGG54423.1; -; Genomic_DNA.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000225635; 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 5..95
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 764 AA; 87016 MW; C009B35216C3002E CRC64;
MSNGNTVIKR DGSVTPIDLN KVHTMVEHAC RGLAGVSESQ VEMNANLQFF DGIETKDIQE
ILIRSANDLI SLDTPNYQFV AARLLLFSLR KGVYKRHPDE RPHLLQQLRD GIAKGIYDPS
LEDIYTEDEW DQLDSYIDHD RDYLFTYAGL RQVVDKYLVQ DRSTGEVYET PQFMYMLIAA
TLFRDYEGSR LEYVRKYYNA ISKHKINIPT PVMAGVRTAL RQFASCVLVD SDDTLSSIFT
SDMAIGKYVA QRAGIGINAG RIRGINAKIR GGEVQHTGVI PFLKKFEATV RCCTQNGIRG
GSATVHFPIW HQEIQDIIVL KNNKGTEDNR VRKLDYSIQL SKLFYERFIS NAEITLFSPH
DVPGLYDAFG TDRFDDLYTQ YEQDETKPKT TIGAQKLILD LLKERAETGR IYLMNIDHCN
SHSSFKDKVN MSNLCQEITL PTDPLEHIDG EGEIALCILS AINVGKIRKH DDLEELCELA
VRGLEELIDY QEYPVKAAEV STRARRSLGI GYIGLAHYLA KKGYYYNDPE AWKEVHDLTE
AFQYYLLKAS MRIASEKGAC EYFDRTKYAD GLLPIDTYKS EVDELVPNEL NYDWNSLRDD
IKKYGLRHST LSAQMPSESS SVVSNATNGI EPPRDYLSVK KSKKGPLKQI VPAFNTLKNN
YTLLWDMKSN QGYINIVAVM QKFFDQAISG NWSYNPENYP KNEVPVSEMA KDLLTTYKYG
WKTSYYQNTY DAKKDGDEPA EGNVDDLIQT LLTTEEEDCD SCKV
//
