ID A0A0R2CNU7_9LACO Unreviewed; 721 AA.
AC A0A0R2CNU7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=FC56_GL000135 {ECO:0000313|EMBL:KRM93423.1};
OS Lentilactobacillus senioris DSM 24302 = JCM 17472.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lentilactobacillus.
OX NCBI_TaxID=1423802 {ECO:0000313|EMBL:KRM93423.1, ECO:0000313|Proteomes:UP000051256};
RN [1] {ECO:0000313|EMBL:KRM93423.1, ECO:0000313|Proteomes:UP000051256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24302 {ECO:0000313|EMBL:KRM93423.1,
RC ECO:0000313|Proteomes:UP000051256};
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:KRM93423.1}.
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DR EMBL; AYZR01000008; KRM93423.1; -; Genomic_DNA.
DR RefSeq; WP_056978065.1; NZ_AYZR01000008.1.
DR AlphaFoldDB; A0A0R2CNU7; -.
DR STRING; 1423802.FC56_GL000135; -.
DR PATRIC; fig|1423802.4.peg.137; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000051256; 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:UP000051256}.
FT DOMAIN 558..580
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 721 AA; 81909 MW; B10616600D59A124 CRC64;
MALTKLEDVT YFDLNNQINI PIDGQIPLNK DQEALEAFLA ENVEPNTIKF DSIKQRLDYL
TKNQYYETDF LTKYSLTFIE KLYDYLNSQD FHFKSFMAAY KFYAQYALQT DDKEHYLESF
VDRAAVNALY FADGDQQLAM DLADEIIHQR YQPATPSFLN AGRQRRGELV SCFLIQTTDD
MNTIGRTINS ALQLSRIGGG VGINLTNLRG AGDPIKHITG AASGVVPVMK LLEDSFSYSN
QLGQRQGAGV VYLSVFHPDI IAFLGAKKEN ADEKIRLKTL SLGIVVPDKF YDLIKEDADM
YLFSPYDVER EYNTPFAYVD ITKEYDNLVA NENIHKKKIK ARDLETEISK LQQESGYPYV
INIDTANHSN PIHGRIVMSN LCSEILQVQT PSTVNDRQEY TQLGTDVSCN LGSTNINNLM
SSPNFGHSVE AMVRALTFVT DHSNIDVVPS VQKGNQEAHS IGLGAMGLHS FLAKNHIYYG
SPESIEFTGV YFMLLNYWTL MASNQIAKER NQTFVNFEKS KYADGSYFDK YLTHSYGPTS
DKVKSLFDGV FIPQPADWEK LKEAVMNYGL YHQNRLAVAP NGSISYINDT TASLHPIINR
IEERQESKIG KIYYPAPYLS NDTMPYYQSA YDIDMRQVID VYAAAQEHVD QGMSLTLFMR
STIPEGLYEW KDGRTDKMTT RDLNILRNYA HYKGIKSIYY IRTFTDDQSE VGANQCESCV
I
//
