ID A0A0F3RW96_9LACO Unreviewed; 721 AA.
AC A0A0F3RW96;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=VC81_04810 {ECO:0000313|EMBL:KJW13062.1};
OS Levilactobacillus spicheri.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Levilactobacillus.
OX NCBI_TaxID=216463 {ECO:0000313|EMBL:KJW13062.1, ECO:0000313|Proteomes:UP000033491};
RN [1] {ECO:0000313|EMBL:KJW13062.1, ECO:0000313|Proteomes:UP000033491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LP38 {ECO:0000313|EMBL:KJW13062.1,
RC ECO:0000313|Proteomes:UP000033491};
RA Zheng J., Ganezle M.;
RL Submitted (MAR-2015) 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}.
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:KJW13062.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JZCR01000011; KJW13062.1; -; Genomic_DNA.
DR RefSeq; WP_045807014.1; NZ_JZCR01000011.1.
DR AlphaFoldDB; A0A0F3RW96; -.
DR STRING; 216463.VC81_04810; -.
DR PATRIC; fig|216463.3.peg.67; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000033491; 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}.
FT DOMAIN 558..580
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 721 AA; 82000 MW; 6CD90AED59AC3336 CRC64;
MSLKDLKNVT YYDLNNEINI PVDGQIPLNK DQEALQAFLK ENVQPNTKQF GSLRERFDFL
IKDNYVEAAV VNQYPFSFIE DLYTYLKDQH FHFKSFMAAY KFYAQYALKT DDNAYYLENF
IDRVAMNALD FGGGDQQLAH DLADEIIHQR YQPATPSFLN AGRARRGELV SCFLIQSTDD
MNTIGRTINS ALQLSRIGGG VGISLSNLRG AGDPIKHIDG AASGVVPVMK LLEDSFSYSN
QLGQRQGAGV VYLSVFHPDI IAFLGAKKEN ADEKIRLKTL SLGVTVPDKF YQLCEQDADM
YLFSPYDVER IYGKPFSYVD ITAEYDKMVA NPDIRKKKLK ARELETEIGK LQQESGYPYI
VNIDTANREN PIKGRIVMSN LCSEIMQVQT PTTYNNKQEY EKLGTDISCN LGSTNIVNLM
TSPDFGHSVE TMVRALTYVT DHSDIDVVPS IQHGNHLAHT IGLGAMGLHS YFAKNHMMYG
SHDSIAFTSV YFMLLNYWTL KASNQIAKER HETFHNFAES KYADGSYFDR YTQTDWRPTS
AKVQGLFSNV WLPSPEDWAQ LKADVMRDGL YHQNRMAVAP NGSISYINDT TASLHPIINR
IEERQEKKIG KIYYPAPYLS NDTMPYYKSA YDTDMRRVID VYAAAQKHVD QGMSLTLFMR
STIPAGLYEW KNGRTDKMTT RDLSILRNYA YRKGIKSIYY VRTFTDDNNE VGANQCESCV
I
//
