ID A0A242K598_9ENTE Unreviewed; 719 AA.
AC A0A242K598;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=A5888_002808 {ECO:0000313|EMBL:OTP14707.1};
OS Enterococcus sp. 9E7_DIV0242.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1834193 {ECO:0000313|EMBL:OTP14707.1, ECO:0000313|Proteomes:UP000195141};
RN [1] {ECO:0000313|EMBL:OTP14707.1, ECO:0000313|Proteomes:UP000195141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9E7_DIV0242 {ECO:0000313|EMBL:OTP14707.1,
RC ECO:0000313|Proteomes:UP000195141};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genomic Center for Infectious Diseases;
RA Earl A., Manson A., Schwartman J., Gilmore M., Abouelleil A., Cao P.,
RA Chapman S., Cusick C., Shea T., Young S., Neafsey D., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterococcus sp. 9E7_DIV0242.";
RL Submitted (MAY-2017) 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:OTP14707.1}.
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; NGMM01000004; OTP14707.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A242K598; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000195141; 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:UP000195141}.
FT DOMAIN 558..580
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 719 AA; 82095 MW; C9D800C893696842 CRC64;
MSLKEIKDVS YFKLNNEINR PVNGQIPLNK DQEALKAFFN ENVLPNTKKF ATATEKIHFL
TENEYIEKPF IQKYSIAFIE RLYQFLDEQN FQFKSFMATY KFYSQYALKN NAGTEYLETY
EDRVAFNALY FADGNEELAL TLADEMIHQR YQPATPSFLN AGRQRRGELV SCFLIQVTDD
MNSIGRSINS ALQLSRIGGG VGITLSNLRE GGAPIKGYEG AASGVVPVMK LFEDSFSYSN
QLGQRQGAGV VYLNVFHPDI EMFLSTKKEN ADEKIRVKTL SLGVLVPDKF YELARKNEDM
YLFSPYSVEK EYGVPFSYID ITEEYDNLVA NPNIRKKKIK ARDLENEISK LQQESGYPYI
VNIDTANKQN PIDGKIIMSN LCSEILQVQT PSVINGKQEY EVLGTDISCN LGSTNIVNLM
ESPDFGKSVR AMTRALTFVT DSSEIDVVPT IQNGNKLSHT IGLGAMGLHT FFAKNHMMYG
SEESLDFTNI YFMLLNYWTL VESNNIAREY KKSFHNFEKS AYADGTYFDK YTDGSFTPQF
DKVKELFGDI FIPTAEDWKQ LRDAIMTDGL YHQNRLAVAP NGSISYINDT SASIHPITRM
IEERQEKKIG KIYYPAAYLA NDTIPYYTSA YDMDMRKVID VYATAQQHVD QGMSLTLFMR
SEIPEGLYEW KEGTKQTTRD LNILRHYAFH KGIKSIYYVR TFTEDSEEIG SNQCESCVI
//
