ID W8EIM2_9CAUD Unreviewed; 576 AA.
AC W8EIM2;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
OS Pseudomonas phage phiPsa374.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Otagovirus; Otagovirus Psa374.
OX NCBI_TaxID=1458843 {ECO:0000313|EMBL:AHJ87387.1, ECO:0000313|Proteomes:UP000203637};
RN [1] {ECO:0000313|EMBL:AHJ87387.1, ECO:0000313|Proteomes:UP000203637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24487530; DOI=10.1128/AEM.00062-14;
RA Frampton R.A., Taylor C., Holguin Moreno A.V., Visnovsky S.B., Petty N.K.,
RA Pitman A.R., Fineran P.C.;
RT "Identification of Bacteriophages for Biocontrol of the Kiwifruit Canker
RT Phytopathogen Pseudomonas syringae pv. actinidiae.";
RL Appl. Environ. Microbiol. 80:2216-2228(2014).
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 -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|ARBA:ARBA00001922};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|RuleBase:RU003410}.
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DR EMBL; KJ409772; AHJ87387.1; -; Genomic_DNA.
DR RefSeq; YP_009009427.1; NC_023601.1.
DR GeneID; 18500790; -.
DR KEGG; vg:18500790; -.
DR OrthoDB; 2980at10239; -.
DR Proteomes; UP000203637; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:InterPro.
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; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR PANTHER; PTHR43371:SF1; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE; 1.
DR PANTHER; PTHR43371; VITAMIN B12-DEPENDENT RIBONUCLEOTIDE REDUCTASE; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 3.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
PE 3: Inferred from homology;
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Deoxyribonucleotide synthesis {ECO:0000256|RuleBase:RU003410};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Reference proteome {ECO:0000313|Proteomes:UP000203637}.
FT DOMAIN 22..101
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 106..224
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 230..395
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 408..547
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 576 AA; 65441 MW; D0C7FB60E6774F63 CRC64;
MIDYSALRKQ QIEDGVCPPW YTTGGIQLFY DKYSYNNETV KSRFKTVAAA LAVHAPEVYP
EWWNVVPYWA GKTWEDAFFQ VMWDGFVSPS TPLLANGGIR KRGTTVSCAG GNVANNLQNR
YDFLTEAAIL TKHSHGTSYC LDDWPAEGDK IRGGRSQGLM PLIRDIINVM EEVAQGPRRG
SCAYSLRPQH GDFDKVCDYL YERTESNNVG WLIDDEFVDL MNDENAEALR KFSKMLGVKM
PRGKGYFTFI DKMNRKLAKA FKRAGLRARA SNLCQETNLP SNEKYTFSCV ILNYNLELYR
SWPEHLVFVG QVMSDCNISE YIECMDEMSE EDKKAMEKIY RFTTEFRALG SGVLGWHTLL
QTEMLSVSSM EAMMLNIKVF RGIRAQADKA NEWLAYTLGE PVGCVGLGIR NATMLMMPPT
KSTAELMAGA SEGVGLDVAM CFTKQSAGGE FFRINKVLLA LIKKKGLNIE QCVRDMNKHK
GSVQFVDWLT DHEKLVFRTG FEIPMEDHLM QCSQRQPYID QGQSINLYFT SNDTPQYIGK
IHRIAFNDPN ILSLYYIYSM RGAGEITRVE SCEMCQ
//
