ID C9XYX8_CROTZ Unreviewed; 716 AA.
AC C9XYX8;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
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=nrdE {ECO:0000313|EMBL:CBA33171.1};
GN OrderedLocusNames=Ctu_32780 {ECO:0000313|EMBL:CBA33171.1};
OS Cronobacter turicensis (strain DSM 18703 / CCUG 55852 / LMG 23827 / z3032).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=693216 {ECO:0000313|EMBL:CBA33171.1, ECO:0000313|Proteomes:UP000002069};
RN [1] {ECO:0000313|Proteomes:UP000002069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18703 / CCUG 55852 / LMG 23827 / z3032
RC {ECO:0000313|Proteomes:UP000002069};
RX PubMed=21037008; DOI=10.1128/JB.01162-10;
RA Stephan R., Lehner A., Tischler P., Rattei T.;
RT "Complete genome sequence of Cronobacter turicensis LMG 23827, a food-borne
RT pathogen causing deaths in neonates.";
RL J. Bacteriol. 193:309-310(2011).
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; FN543093; CBA33171.1; -; Genomic_DNA.
DR AlphaFoldDB; C9XYX8; -.
DR KEGG; ctu:CTU_32780; -.
DR PATRIC; fig|693216.3.peg.3097; -.
DR HOGENOM; CLU_000404_4_1_6; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000002069; 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 568..590
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 716 AA; 80395 MW; 306381968F15C293 CRC64;
MATTTLTGDA VRQTTPDYHA LNAMLNLYDA DGRIQFEKDR EAVEAFMAAH VQPRSVTFPD
THARLAYLVS EGYYDENVLK RYDPDFAAGL FDEAHRDGFT FKTFLGAWKF YTSYTLKTFD
GKRYLEHFPD RACMVALTLA CGDETLARQI LKEILSGRFQ PATPTFLNGG KQQRGELVSC
FLLRIEDNME SIGRAVNAAL QLSKRGGGVA FSLSNLREAG APIKRIENQS SGVIPVMKML
EDAFSYANQL GARQGAGAVY LNAHHPDILR FLDTKRENAD EKIRIKTLSL GVVIPDITFE
LAKANAQMAL FSPYDVEHIY GKPFGDISVS EMYTQLVEDE RIRKRYISAR ELFQRLAEIQ
FESGYPYIMF EDTVNRANPI AGRINMSNLC SEILQVNSAS TFDENLNYAT TGHDISCNLG
SLNIAHTMDS PDFGRTVETA VRALTAVSDM SHIRSVPSIE AGNAASHAIG LGQMNLHGYL
AREGIAYGSP EGLDFTNLYF YTVTWHALNT SMMLARERGE RFEGFEASRY ASGEYFDKYL
TQTWTPRTAR VAELFARAGI TLPTPEMWRQ LRDDVMRHGL YNRNLQAVPP TGSISYINHA
TSSIHPIVSK IEIRKEGKIG RVYYPAPFMT NENLARYQDA YEIGPEKIID TYAEATRHVD
QGLSLTLFFP DTATTRDINK AQIYAWKKGI KTLYYIRLRQ LALEGTEIEG CVSCAL
//
