ID B0YPF7_BACTK Unreviewed; 694 AA.
AC B0YPF7;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 72.
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:ABW06045.1};
GN ORFNames=BG08_4450 {ECO:0000313|EMBL:AJK41731.1};
OS Bacillus thuringiensis subsp. kurstaki.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=29339 {ECO:0000313|EMBL:ABW06045.1};
RN [1] {ECO:0000313|EMBL:ABW06045.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HD-1 {ECO:0000313|EMBL:ABW06045.1};
RX PubMed=18032435; DOI=10.1093/nar/gkm1016;
RA Nord D., Sjoberg B.M.;
RT "Unconventional GIY-YIG homing endonuclease encoded in group I introns in
RT closely related strains of the Bacillus cereus group.";
RL Nucleic Acids Res. 36:300-310(2008).
RN [2] {ECO:0000313|EMBL:AJK41731.1, ECO:0000313|Proteomes:UP000031926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HD 1 {ECO:0000313|EMBL:AJK41731.1,
RC ECO:0000313|Proteomes:UP000031926};
RX PubMed=25931591; DOI=10.1128/genomea.00151-15;
RA Johnson S.L., Daligault H.E., Davenport K.W., Jaissle J., Frey K.G.,
RA Ladner J.T., Broomall S.M., Bishop-Lilly K.A., Bruce D.C., Gibbons H.S.,
RA Coyne S.R., Lo C.C., Meincke L., Munk A.C., Koroleva G.I., Rosenzweig C.N.,
RA Palacios G.F., Redden C.L., Minogue T.D., Chain P.S.;
RT "Complete genome sequences for 35 biothreat assay-relevant bacillus
RT species.";
RL Genome Announc. 3:0-0(2015).
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; EU043135; ABW06045.1; -; Genomic_DNA.
DR EMBL; CP010005; AJK41731.1; -; Genomic_DNA.
DR RefSeq; WP_001215839.1; NZ_PHSM01000001.1.
DR AlphaFoldDB; B0YPF7; -.
DR SMR; B0YPF7; -.
DR GeneID; 72448122; -.
DR HOGENOM; CLU_000404_4_1_9; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000031926; 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 552..574
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 694 AA; 79712 MW; 8F98F2637C4BB619 CRC64;
MRHIELNNEI TQMQDGFYQL HKDKEALEVF MEEARENTVP FNSVAERMEY MKEHDYYYNV
LDEYSLEEVE EVYNIAYGEN FEFQSYMAAS KFYKDYALKT NDQKQYLESY EDRVAIVSLY
LGRGDVSKAR QFASMIVKQN YQPATPTFLN AGRSRRGEMV SCFLLEMDDS LNSIGFNINT
AMQLSKIGGG VALNLSKLRA RGEQIKGIDN AASGVVPVMK LLEDSFSYAN QLGQRKGAGA
VYLNIFHWDI IEFLDTKKIN ADEKSRIQSL SIGIIVPSKF FELAEKNEPF HVFAPYTVYK
EYGKHLDDID IDEMYDELMS NPKVKKKPLD ISARDMLIKI AMIQLESGYP YLMFKSNANN
QHPLKDIGTV KMSNLCTEIF QLQETSEIND YGTDDIIRRD INCNLGSLNI VNVMENKEIR
EAVHAGMEAL TAVSDMTIIP NAPTVKKAND ELHSVGLGAM NLHGYLAKNK IAYESAEAKE
FARTFFMMLN YYSIEKSMEI ATEKGETFKD FDKSDYANGT YFEKYETTDY SPVTEKVQQL
FEGIHIPTKE DWTSLKEQVQ KNGLYNSYRL AIAPTQSISY VQNATSSVMP IVSQIESRTY
ANATTYYPMP YLSKDTFWYY KSSYDMNQFK LIDLIAEIQE HIDQGISTIL YVNSDISTRE
LARYYIYAHK KGLKSLYYTR TRKLSVEECV ACTV
//
