ID A0A249DDA7_LACRH Unreviewed; 723 AA.
AC A0A249DDA7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=BGK71_06810 {ECO:0000313|EMBL:ASX17130.1};
OS Lacticaseibacillus rhamnosus (Lactobacillus rhamnosus).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=47715 {ECO:0000313|EMBL:ASX17130.1, ECO:0000313|Proteomes:UP000215843};
RN [1] {ECO:0000313|EMBL:ASX17130.1, ECO:0000313|Proteomes:UP000215843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LR5 {ECO:0000313|EMBL:ASX17130.1,
RC ECO:0000313|Proteomes:UP000215843};
RA Nam Y.-D., Kang J., Chung W.-H.;
RT "Complete genome sequence of Lactobacillus rhamnosus LR5.";
RL Submitted (AUG-2016) 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; CP017063; ASX17130.1; -; Genomic_DNA.
DR RefSeq; WP_047677099.1; NZ_PZQM01000002.1.
DR AlphaFoldDB; A0A249DDA7; -.
DR GeneID; 69831950; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000215843; 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 560..582
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 723 AA; 82189 MW; EE13000D890768B8 CRC64;
MSLKTISPDE VTYYALNNEI NIPVNDQIPL NKDKEALQAF LTENVAPNTM KFASLQERLK
YLVEHHYYEA DFLKKYQPAF LEKLNQFLTA QHFQFKSFMA AYKYYAQYAL KTDDGTQYLE
DYKDRVFANA LFFADGNEDL AVDLADEMIH QRYQPATPSF LNAGRARRGE LVSCFLLQIT
DDMNSIGRAI NSALELSRIG GGVGLTLSNL REAGAPIKGI DGAASGVLPV MKLLEDSFSY
SNQLGQRQGA GVVYLNVFHP DIISFLGAKK ENADEKYRVK TLSLGVIVPD KYYELIKANA
DMYLFSPYSV ERAYGKPFSY VDITKEYDKM VANPDIKKYK IKARDLENEI SKLQQESGYP
YIINIDTANR ANPIEGKIIM SNLCSEIMQV QVPSKLNNRQ EYEVLGTDVS CNLGSTNIPN
LMHSRDFGHS VEAMVRALTY VTDHSNIDVV PSVQHGNHLA HSIGLGAMGL HTYFAKNHMY
YGSPESLDFT NIYFLLLNYY TLKASNKIAK ERGESFHNFE NSKYADGSYF DKYLNQTWAP
KYDKVRDLFK NIYIPTQADW QALKEDVMKN GLYHQNRMAV APNGSISYIN DTSASLQPIV
NRIEDRQEKK IGTIYYPAPG LSNDTMPYYQ SAYDIDMRKV IDVYAAAQQH VDQGMAMTLF
MRSTIPAGLY PWKDGRTDKM TTRDLNILRN YAHYKGIKSI YYIRTYTDDQ EEIGSNACES
CSI
//
