ID A0A142EZL6_9CAUD Unreviewed; 766 AA.
AC A0A142EZL6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 13-SEP-2023, entry version 27.
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=AAY80_086 {ECO:0000313|EMBL:AMQ65903.1};
OS Stenotrophomonas phage vB_SmaS-DLP_6.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes.
OX NCBI_TaxID=1651816 {ECO:0000313|EMBL:AMQ65903.1, ECO:0000313|Proteomes:UP000222594};
RN [1] {ECO:0000313|EMBL:AMQ65903.1, ECO:0000313|Proteomes:UP000222594}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Peters D.L., Dennis J.;
RT "The isolation and characterization of chimeric Stenotrophomonas
RT maltophilia phage DLP6.";
RL Submitted (FEB-2016) 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 -!- PATHWAY: Genetic information processing; DNA replication.
CC {ECO:0000256|ARBA:ARBA00005160, 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; KU682439; AMQ65903.1; -; Genomic_DNA.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000222594; 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:UniProtKB-UniPathway.
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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000222594}.
FT DOMAIN 2..92
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 745..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 766 AA; 86704 MW; 8DC5FC6F87CE7D5A CRC64;
MSTVTKRDGT REPRDLNKIH KVVFEACEGL TGVSASEVEL KAQLQFYEGM PTEHIQDSLV
RAAAGLISEE NPNYQYVAGR LINYDLRKRV YGEFEPPHIY DHVEKYVRLG YYHESLLTKY
TRADWDAIQA FIKHERDSDF VFAAMEQFRG KYLMKNRHTG EFYETPQMLC AILPAFAFQN
YPIDKRISYI KRTYDMLSTS EISLPTPIMA GVRTSQLQFS SCVLIECADS IDSIFTTTHA
VGKYVSQKAG IGIGAGAIRP LGSPIRNGDA FSTGAIPYFR TFQAATKSCS QGGVRGGAAT
IYYQMWHQEI EDLLVLKNNK GTEFNRVRQV DYGVQVNRLM YERLMQGGNI SCFNPKDVPG
LYESFFADQD KFRELYEAAE KNKKIPRKVY PAIELWSLFA GERKGTGRIY GMNVDNVNDH
GAFIPELAPI RMSNLCTEVT LPTKPLKHIA DPDGEIALCI LAAQNWGTAK TPHDFRDTAD
IIVRLLDELI DLQTYPVLAA EIGTRNRRSL GVGIINFAYW LAKHDLTYDG ITPEGLALID
EWAEWWSYYL LKASADLAVE KGACGWFEQT KYSKGILPND TYKKTVDELV PYKSRAPWAE
LRLQLLSTGI RNSTLMTLMP AETSAQIANA TNGIEAPREL VSIKQSKDGV LAQVVPEIRR
LKNKYNLKWD QKSPVGYLKI VAVLQKHIDQ AISVNTAYNP KFYENEEIPV SEILQHMIMH
YRYGGKTLYY FETYDGAGEL NIESKGEYTT PSDELPPEED CDSCKI
//