ID C3SY97_ECOLX Unreviewed; 714 AA.
AC C3SY97;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 92.
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=C9E67_06645 {ECO:0000313|EMBL:QCL46893.1}, ECs3538
GN {ECO:0000313|EMBL:ACI79436.1};
OS Escherichia coli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:ACI79436.1};
RN [1] {ECO:0000313|EMBL:ACI79436.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=493/89 {ECO:0000313|EMBL:ACI79436.1}, 86-24
RC {ECO:0000313|EMBL:ACI79437.1}, 87-14 {ECO:0000313|EMBL:ACI79438.1},
RC TB182A {ECO:0000313|EMBL:ACI79439.1}, and TW14359
RC {ECO:0000313|EMBL:ACI79440.1};
RX PubMed=19439656; DOI=10.1073/pnas.0812949106;
RA Leopold S.R., Magrini V., Holt N.J., Shaikh N., Mardis E.R., Cagno J.,
RA Ogura Y., Iguchi A., Hayashi T., Mellmann A., Karch H., Besser T.E.,
RA Sawyer S.A., Whittam T.S., Tarr P.I.;
RT "A precise reconstruction of the emergence and constrained radiations of
RT Escherichia coli O157 portrayed by backbone concatenomic analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8713-8718(2009).
RN [2] {ECO:0000313|EMBL:QCL46893.1, ECO:0000313|Proteomes:UP000298553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=143 {ECO:0000313|EMBL:QCL46893.1,
RC ECO:0000313|Proteomes:UP000298553};
RA Bono J.L., Arthur T.M.;
RT "WGA of Escherichia coli O157:H7: comparison of multiple isolates.";
RL Submitted (APR-2018) 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|ARBA:ARBA00000206,
CC 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; EU896880; ACI79436.1; -; Genomic_DNA.
DR EMBL; EU896881; ACI79437.1; -; Genomic_DNA.
DR EMBL; EU896882; ACI79438.1; -; Genomic_DNA.
DR EMBL; EU896883; ACI79439.1; -; Genomic_DNA.
DR EMBL; EU896884; ACI79440.1; -; Genomic_DNA.
DR EMBL; CP028607; QCL46893.1; -; Genomic_DNA.
DR RefSeq; WP_000246553.1; NZ_WJRH01000021.1.
DR PATRIC; fig|562.7073.peg.1107; -.
DR OMA; TLFMTDK; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000298553; Chromosome.
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 CDD; cd01679; RNR_I; 1.
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.
DR PROSITE; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410}.
FT DOMAIN 566..588
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 714 AA; 80378 MW; F3A8FE84362E81CF CRC64;
MATTTAECLT QKTMDYHALN AMLNLYDSAG RIQFDKDRQA VDAFMATHVR PNSVTFSSQQ
QRLNWLVNEG YYDESVLNRY SRDFVITLFA HAHTSGFRFQ TFLGAWKFYT SYTLKTFDGK
RYLEDFADRV TMVALTLAQG DETLALQLTD EMLSGRFQPA TPTFLNCGKQ QRGELVSCFL
LRIEDNMESI GRAVNSALQL SKRGGGVAFL LSNLREAGAP IKRIENQSSG VIPVMKMLED
AFSYANQLGA RQGAGAVYLH AHHPDILRFL DTKRENADEK IRIKTLSLGV VIPDITFHLA
KENAQMALFS PYDVERVYGK PFADVAISQH YDELVADERI RKKYLNARDF FQRLAEIQFE
SGYPYIMYED TVNRANPVAG RINMSNLCSE ILQVNSASEY DENLDYARTG HDISCNLGSL
NIAHTMDSPD FARTVETAVR GLTAVSDMSH IRSVPSIEAG NAASHAIGLG QMNLHGYLAR
EGIAYGSPEA LDFTNLYFYA ITWHALRTSM LLARERGETF AGFKQSRYAS GEYFSQYLQG
NWQPKTGKVG ELFARSGITL PTREMWAQLR DDVMRYGIYN QNLQAVPPTG SISYINHATS
SIHPIVAKVE IRKEGKTGRV YYPAPFMTNE NLALYQDAYE IGAEKIIDTY AEATRHVDQG
LSLTLFFPDT ATTRDINKAQ IYAWRKGIKT LYYIRLRQMA LEGTEIEGCV SCAL
//
