ID Q8D1U6_WIGBR Unreviewed; 704 AA.
AC Q8D1U6;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 113.
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:BAC24756.1};
OS Wigglesworthia glossinidia brevipalpis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Wigglesworthia.
OX NCBI_TaxID=36870 {ECO:0000313|EMBL:BAC24756.1, ECO:0000313|Proteomes:UP000000562};
RN [1] {ECO:0000313|EMBL:BAC24756.1, ECO:0000313|Proteomes:UP000000562}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12219091; DOI=10.1038/ng986;
RA Akman L., Yamashita A., Watanabe H., Oshima K., Shiba T., Hattori M.,
RA Aksoy S.;
RT "Genome sequence of the endocellular obligate symbiont of tsetse flies,
RT Wigglesworthia glossinidia.";
RL Nat. Genet. 32:402-407(2002).
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; BA000021; BAC24756.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8D1U6; -.
DR STRING; 36870.gene:10369128; -.
DR KEGG; wbr:nrdE; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_4_1_6; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000000562; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000000562}.
FT DOMAIN 556..578
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 704 AA; 80685 MW; AEEAB7C3D9797135 CRC64;
MHKIDYHALN AMLNLYDKNG LLQIEKDVFA INSYYEQHVL PNKKKFSSLE DRITYLLKEE
YYESNVFENY KKDFIKNIFF QSKKQGFKFK TFMGAIKFYS SYALKTFDNK YYLEDFEDRA
CMVALTLGGG NEKFAINIMQ EILSGRFQPA TPTFLNCGKK QRGEYVSCFL LRIEDNMESI
GRALNSALQL SKRGGGVSFL LTNLRESGAP IKCIKNQSSG IVPVMKMLED AFSYANQLGA
RQGAGAVYLH AHHPDILNFL DTKRENADEK IRIKTLSLGV IIPDITFKLA KENQNMCLFS
PYDIKKVYNK PFSELIISKI YYKLINDIRI KKISINARSF FQKLAEVQFE SGYPYIMFED
TVNKENPIYG KINMSNLCSE ILQVNTASEY NEDLSYKKIG RDISCNLGSL NIAKTMDSSN
LGKTVEVAIR CLTAVSDITK INSVSSVVKG NKKSHSIGLG QMNLHGYLAR ENIFYGSPEA
IEFTNFYFYV ITYHAIRTSN LLAIERKKTF SGFSRSKYAN GKFFKKYTKK TWIPKSDRIL
NLFNNNNIHL PTLKEWKILE NSVMKYGLYN QNLQAIPPTG SISYINYSTS SIHPVVSRIE
IRKEGKIGRV YYPAPYMTNK NLCYYQDAYE IGPKKIIDTY AAATKHVDQG LSLTLFFRDD
ATTRDINKAQ IYAWKKGIKT LYYVRIRQLT LKGTELFGCV SCSL
//
