ID Q32CQ0_SHIDS Unreviewed; 616 AA.
AC Q32CQ0;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 100.
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:ABB62905.1};
GN OrderedLocusNames=SDY_2868 {ECO:0000313|EMBL:ABB62905.1};
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267 {ECO:0000313|EMBL:ABB62905.1, ECO:0000313|Proteomes:UP000002716};
RN [1] {ECO:0000313|EMBL:ABB62905.1, ECO:0000313|Proteomes:UP000002716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197 {ECO:0000313|EMBL:ABB62905.1,
RC ECO:0000313|Proteomes:UP000002716};
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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; CP000034; ABB62905.1; -; Genomic_DNA.
DR AlphaFoldDB; Q32CQ0; -.
DR STRING; 300267.SDY_2868; -.
DR EnsemblBacteria; ABB62905; ABB62905; SDY_2868.
DR KEGG; sdy:SDY_2868; -.
DR HOGENOM; CLU_000404_4_1_6; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000002716; 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 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:UP000002716}.
FT DOMAIN 553..575
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 616 AA; 69372 MW; D55C3FEFF2BB81B4 CRC64;
MDYHALNAML NLYDSAGRIQ FDKDRQAVDA FIATHVRPNS VTFSSQQQRL NWLVNEGYYD
ESVLNRYSRN FVITLFAHAH TSGFRFQTFL GAWKFYTSYT LKTFDGKRYL EDFADRVTMV
ALTLAQGDET LALQLTDEML SGRFQPATPT FPNCGKQQRG ELVSCFLLRI EDNMESIGRA
VNSALQLSKR GGGVAFLLSN LREAGAPIKR IENQSSGVIP VMKMLEDAFS YANQLGARQG
AGAVYLHAHH PDILRFLDTK RENADEKIRI KILSLGVVIP DITFHLAKEN AQMALFSPYD
VERVYGKPFA DVAISQHYDE LVADERIRKK YLNARDFFQR LVEIQFESGY PYIMYEDTVN
RANPIAGRIN MSNLCSEILQ VNSASEYDEN LDYTCTGHDI SCNLGSLNIA HTMDSPDFAR
TVETAVRGLT AVSDMSHIRS VPSIEAGNAA SHAIGLGQMN LHGYLAREGI AYGSPEALDF
TNLYFYAITW HALRTSMLLA RERGETFAGF KQSRYASGEY FSQYLQGNWQ PKTAKVGELF
TRSGITLPTH EMWAQLRDDV MRYGIYNQNL QAVPPTGSIS YINHATSSIH PIVAKVEIRK
EGKTGRVYYP APFMTN
//
