ID Q8DV42_STRMU Unreviewed; 719 AA.
AC Q8DV42;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 122.
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 OrderedLocusNames=SMU_668c {ECO:0000313|EMBL:AAN58402.1};
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007 {ECO:0000313|EMBL:AAN58402.1, ECO:0000313|Proteomes:UP000002512};
RN [1] {ECO:0000313|EMBL:AAN58402.1, ECO:0000313|Proteomes:UP000002512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159 {ECO:0000313|Proteomes:UP000002512};
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H., Lin S., Qian Y., Li S., Zhu H.,
RA Najar F., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AE014133; AAN58402.1; -; Genomic_DNA.
DR RefSeq; NP_721096.1; NC_004350.2.
DR RefSeq; WP_002261873.1; NC_004350.2.
DR AlphaFoldDB; Q8DV42; -.
DR STRING; 210007.SMU_668c; -.
DR KEGG; smu:SMU_668c; -.
DR PATRIC; fig|210007.7.peg.593; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_4_1_9; -.
DR OrthoDB; 9762933at2; -.
DR PhylomeDB; Q8DV42; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000002512; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002512}.
FT DOMAIN 558..580
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 719 AA; 81479 MW; 3A98F2EE60ED5DF2 CRC64;
MSLKNLGDIS YFRLNNEINR PINGQIPLHK DKEALEAFFK ENVKPNTKTF DSITDKIQFL
VANDYIEAEF IAKYKSEFIE QLSQDLHAYD FQFKSFMAAY KFHQQYALKT NDGEEYLESI
EDRVLFNALY FADGNENLAH DLAMEMIAQR YQPATPSFLN AGRSRRGELV SCFLIQVTDD
MNSIGRSINS ALQLSRIGGG VGISLSNLRE AGAPIKGFAG AASGVVPVMK LFEDSFSYSN
QLGQRQGAGV VYLDVFHPDI MAFLSTKKEN ADEKVRVKTL SLGVTIPDKF YELARRNEDM
YLFSPYSIER EYGVPYNYLD ITEKYDELVA NPKIIKTKIK ARDLETEISK LQQESGYPYV
VNIDTANRAN PIDGKIIMSN LCSEILQVQK PSLINDAQEF VKMGTDISCN LGSTNVVNMM
TSPDFGRSIK AMTRALTFVT DSSHIDAVPS IKNGNKQAHT FGLGAMGLHS YLAQNHIEYG
SPESIEFTDI YFMLMNYWTL VESNNIARER QETFVGFEKS KYADGSYFDK YVTGQFIPKS
DKIKELFKNH FIPQAEDWEA LRQAVIKDGL YHQNRLAVAP NGSISYINDV SASIHPITRR
IEERQEKKIG KIYYPAAGLS TDTIPYYTSA YDMDMRKVID VYAAATQHVD QGMSLTLFMR
SDIPQGIYEW KTESKQTTRD LSILRNYAFN KGIKSIYYIR TFTDDGDEVG ANECESCVI
//
