ID I6PC44_9CAUD Unreviewed; 704 AA.
AC I6PC44;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
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=GH15_135 {ECO:0000313|EMBL:AFF28607.1};
OS Staphylococcus phage G15.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Herelleviridae; Twortvirinae; Kayvirus; Kayvirus G15.
OX NCBI_TaxID=760530 {ECO:0000313|EMBL:AFF28607.1, ECO:0000313|Proteomes:UP000006134};
RN [1] {ECO:0000313|EMBL:AFF28607.1, ECO:0000313|Proteomes:UP000006134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22843868; DOI=10.1128/JVI.01313-12;
RA Gu J., Liu X., Lu R., Li Y., Song J., Lei L., Sun C., Feng X., Du C.,
RA Yu H., Yang Y., Han W.;
RT "Complete Genome Sequence of Staphylococcus aureus Bacteriophage GH15.";
RL J. Virol. 86:8914-8915(2012).
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; JQ686190; AFF28607.1; -; Genomic_DNA.
DR RefSeq; YP_007002258.1; NC_019448.1.
DR GeneID; 14005919; -.
DR KEGG; vg:14005919; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000006134; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 1.10.1650.20; -; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR013346; NrdE_NrdA_C.
DR InterPro; IPR026459; RNR_1b_NrdE.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR013554; RNR_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR NCBIfam; TIGR04170; RNR_1b_NrdE; 1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR Pfam; PF08343; RNR_N; 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.
PE 3: Inferred from homology;
KW Deoxyribonucleotide synthesis {ECO:0000256|RuleBase:RU003410};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410}.
FT DOMAIN 7..86
FT /note="Ribonucleotide reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08343"
FT DOMAIN 88..163
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 168..689
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 704 AA; 80218 MW; 4B4421E8930DC143 CRC64;
MATYGKWIEL NNEITQLDDN GKNKLYKDQE ALDEYLKYIE DNTRKFNNEV ERIRVLTKEG
TYDKIFDKVP DTIIDEMTKL AYSFNFKFPS FMAGQKFYES YASKQYDENK KPIFVEDYEQ
HNVRVALYLF QNDYVKAREL LVQLMEQTFQ PSTPTYNNSG QANRGELSSC YLFVVDDSIE
SLNFVEDSVA NASSNGGGVA IDLTRIRPKG APVRNRPNSS KGVIAFAKAI EHKVSIYDQG
GVRQGSGAVY LNIFHNDILD LLSSKKINAS ESVRLDKLSI GVTIPNKFME LVKEGKPFYT
FDTYDINKVY GKYLDELNID EWYEELLNND KIGKVKHDAR EVMTDIAKTQ LESGYPYVFY
IDNANDNHPL KNLGKVKMSN LCTEISQLQE VSEIYPYSYS NQNVINRDVV CTLGSLNLVN
VVEKGLLNES VDIGTRALTK VTDIMDLPYL PSVQKANDDI RAIGLGSMNL HGLLAKNMIS
YGSREALDLV NSLYSAINFQ SIKTSMLMAK ETGKPFKGFE KSDYATGEYF VRYIRESNQP
KTDKAKKVLS KVYIPTQDDW DELAKAVKVH GLYNGYRKAE APTQSISYVQ NATSSIMPVP
SAIENRQYGD METYYPMPYL SPITQFFYEG ETAYKIDNKR IINTSAVVQK HTDQAVSTIL
YVESEIPTNK LVSLYYYAWE QGLKSLYYTR SRKLSVIECE TCSV
//
