ID   K7NTG2_9CAUD            Unreviewed;       750 AA.
AC   K7NTG2;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
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:AEX26546.1};
GN   ORFNames=KP27_073 {ECO:0000313|EMBL:AEX26546.1};
OS   Klebsiella phage KP27.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Straboviridae; Slopekvirus; Slopekvirus kp27.
OX   NCBI_TaxID=1129147 {ECO:0000313|EMBL:AEX26546.1, ECO:0000313|Proteomes:UP000010073};
RN   [1] {ECO:0000313|Proteomes:UP000010073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Drulis-Kawa Z., Maciaszczyk-Dziubinska E., Villegas A., Kropinski A.M.;
RL   Submitted (JAN-2011) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; HQ918180; AEX26546.1; -; Genomic_DNA.
DR   RefSeq; YP_007348702.1; NC_020080.1.
DR   GeneID; 14516271; -.
DR   KEGG; vg:14516271; -.
DR   OrthoDB; 2980at10239; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000010073; 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; 1.10.1650.20; -; 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}.
FT   DOMAIN          5..94
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
SQ   SEQUENCE   750 AA;  85100 MW;  7A766955AEF32E95 CRC64;
     MNDIKVVVKS SGVRQPFDKE KIYKVLKWAC DGHNIDVRAF LENVLELIRD GMTTKQIQRI
     VIKYAADHIS VKEPDWQYVA SNLEMFALRK DVYGQFDPIP FYDHIVKMVE AGKYDKEILE
     KYSKQDIQVF ERAIDHDKDF EFSYAGSQQL IGKYLVQDRD TGEIFETPQY AFMLIAMCLH
     QEETGLAQVT HIVDFYNAIS DRKLSLPTPI MAGVRTPTRQ FSSCVVIESG DSLGSLNAVT
     SAIVKYISQR AGIGVNAGHI RAMGSKIRGG EAVHTGVIPF WKHIQTAVKS CSQGGVRGGA
     ATLYYPFWHL EVENLLVLKN NKGVEENRVR HLDYGVQLNQ LMYKRLMNRD YITLFSPDVA
     NDRLYDLFYE ADQTAFEELY ESLEKDPTVR KKRIKAVDLF QLLAQERAQT GRKYIFNTHH
     VNQQGSFTVP VRMSNLCCEI AIPTSPLDDD DKMAGEIGLC TLMAIVLDNA DISEFPKLTR
     IAVRALDNLL DYQNYPVKAA LKAKQRRSLG VGITNYASWL ASNYCDYSEA YTDKVHELME
     AFQFNLLVAS MELAKERGAC GLYNDTKYAR GLLPIDWYCK TVDELVAPVY NCDWEWLRSQ
     IKKYGLRNST LSALMPCESS SQVSNSTNGI EPPRGLVSIK SSKEGHYNQV VPNQNNQIDF
     YDLLWDMAKR GNKGYLSHVA VMQKFVDQSI SANTNYDPAN YEDGKVKTED IIDDLLYANY
     YGVKTLYYHN TRDGAGDEEE AAEDCAGCKI
//