ID A0A0R1RZ81_9LACO Unreviewed; 723 AA.
AC A0A0R1RZ81;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=FC69_GL000953 {ECO:0000313|EMBL:KRL62081.1};
OS Latilactobacillus fuchuensis DSM 14340 = JCM 11249.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Latilactobacillus.
OX NCBI_TaxID=1423747 {ECO:0000313|EMBL:KRL62081.1, ECO:0000313|Proteomes:UP000051264};
RN [1] {ECO:0000313|EMBL:KRL62081.1, ECO:0000313|Proteomes:UP000051264}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14340 {ECO:0000313|EMBL:KRL62081.1,
RC ECO:0000313|Proteomes:UP000051264};
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:KRL62081.1}.
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DR EMBL; AZEX01000001; KRL62081.1; -; Genomic_DNA.
DR RefSeq; WP_035438814.1; NZ_BAMJ01000003.1.
DR AlphaFoldDB; A0A0R1RZ81; -.
DR STRING; 1423747.FC69_GL000953; -.
DR PATRIC; fig|1423747.3.peg.973; -.
DR eggNOG; COG0209; Bacteria.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000051264; 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 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 Coiled coil {ECO:0000256|SAM:Coils};
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"
FT COILED 329..356
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 723 AA; 81719 MW; 4148D23217F7CB97 CRC64;
MSLKEIRTED VTYYELNNQI NIPVDGQIPL HKDQEALDAF LEQNVQPNMV TFKSLQDRLD
YLVTENYYEA DFLKAYSITF MEQLNQYLID QDFHFKSFMA AYKFYAQYAL KTNDNGFYLE
DFKDRIFVNA LYFADGDETL AMNLADEMVH QRYQPATPSF LNAGRSRRGE LVSCFLLQTT
DDMNSIGRTI NSALELSRIG GGVGISLSNL RGAGDPIKGI DGAASGVLPV MKLLEDSFSY
SNQLGQRQGA GVVYLNAFHP DVIAFLGAKK ENADEKYRLK TLSLGLIVPD KYYELVANDA
DMYLFSPYGV EKEYGVPYSY VDITKEYDNL VANDQIKKTK IKARDLENEI SKLQQESGYP
YIVNIDTANK ANPIDGKIIM SNLCSEVLQV QTPSQINNRQ EYDVLGTDIS CNLGSTNIPN
MMTSPDFGHS IEAMVRALTY VTDHSDIDVV PSVAHGNELA HTIGLGGMGL HTYFATHQML
YGSPESIDFT SNYFMLLNYW TLVASNKIAK ERHETFANFD KSKYADGTYF DQYLNEDWAP
QSTQVKTLFE GIFIPTKADW IALRDAIMAD GLYHQNRLAV APNGSISYIN DTSASLQPIV
NRVEDRQEKK IGTIYYPAPG LSNETMPFYE SAYDIDMRKV IDIYAAAQKH VDQGMSMTLF
MRSTIPAGLY EWKDGRTDKM TTRDLNILRN YAHHKGIKSI YYIRTYTDDE NEVGANACES
CTI
//
