ID A0A0R1QKS9_9LACO Unreviewed; 723 AA.
AC A0A0R1QKS9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=FD01_GL002171 {ECO:0000313|EMBL:KRL41587.1};
OS Lacticaseibacillus manihotivorans DSM 13343 = JCM 12514.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1423769 {ECO:0000313|EMBL:KRL41587.1, ECO:0000313|Proteomes:UP000051790};
RN [1] {ECO:0000313|EMBL:KRL41587.1, ECO:0000313|Proteomes:UP000051790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13343 {ECO:0000313|EMBL:KRL41587.1,
RC ECO:0000313|Proteomes:UP000051790};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRL41587.1}.
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DR EMBL; AZEU01000247; KRL41587.1; -; Genomic_DNA.
DR RefSeq; WP_056964716.1; NZ_AZEU01000247.1.
DR AlphaFoldDB; A0A0R1QKS9; -.
DR PATRIC; fig|1423769.4.peg.2332; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000051790; Unassembled WGS sequence.
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:UP000051790}.
FT DOMAIN 560..582
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 723 AA; 81342 MW; 2BBE6E0BCE3C792A CRC64;
MGLKAIDPEQ VTYFKLNNEI NIPVNGQIPL AKDKEALAAF FKENVDPNTL TFDSLKDRLD
YLVDNNYYEA DFLSKYSLEF MEQLRDYLAA QNFHFQSFMA AYKFYAQYAL KTDDNDHYLE
SFEDRVFANA LFFADGDETL AQSLADEMIH QRYQPATPSF LNAGRARRGE LVSCFLLQVS
DDMNSIGRAI NSALELSRIG GGVGITLSNL REGGAPIKGI EGAASGVLPV MKLLEDSFSY
SNQLGQRQGA GVVYLNVFHP DIIAFLGAKK ENADEKYRLK TLSLGVIVPD KFYDLVKADA
DMYLFSPYSV EREYGQPFSY IDITKEYDNL VANPNITKKK IRARDLETEI SKLQQESGYP
YIMNVDTANN ASPIAGKIIM SNLCSEIMQV QTPSVLNNRQ EYDVLGTDVS CNLGSTNIPN
LMQSPDFEKS VDAMVRALTY VTDHSAIDVV PSVQNGNDLA HSIGLGAMGL HTYFAKHHMH
YGSPESLDFT NQYFLLLNYY SLKASNQIAR ERGVVFHNFE ASKYADGSYF DKYLDQDWSI
KFDSVAEQFK NIHIPTKQDW ADLKAAVMKD GLYHQNRMAV APNGSISYIN DTSSSLHPIV
NRIEDRQEKT IGTIYYPASG LANDTLPYYQ SAYDTNMCKV VDVYAAAQQH VDQGMSMTFF
MRSTIPEGTY PWKDGRTNKM TTRDLNILRN YAHAKGIKSI YYIRTFTDDD SEIGANACES
CSI
//
