ID A0A430ALD4_9ENTE Unreviewed; 720 AA.
AC A0A430ALD4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=CBF29_12785 {ECO:0000313|EMBL:RSU08931.1};
OS Vagococcus elongatus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX NCBI_TaxID=180344 {ECO:0000313|EMBL:RSU08931.1, ECO:0000313|Proteomes:UP000287605};
RN [1] {ECO:0000313|EMBL:RSU08931.1, ECO:0000313|Proteomes:UP000287605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 51432 {ECO:0000313|EMBL:RSU08931.1,
RC ECO:0000313|Proteomes:UP000287605};
RA Gulvik C.A.;
RT "Vagococcus spp. assemblies.";
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:RSU08931.1}.
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; NGKA01000030; RSU08931.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A430ALD4; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000287605; 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:UP000287605}.
FT DOMAIN 558..580
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 720 AA; 81876 MW; BDD1D0B7636A3B77 CRC64;
MSLKELNDVS YFKLNNEINR PVDGQIPLHK DKEALKAFFE ENVEPNTMTF PSVEEKINYL
IAQDYLEEAF IQKYSMAFIS SLFDYLKAQK FTFKSFMAAY KFYSQYALKN NEGTLYLESF
EDRVAFNALY FADGDEKLAM KLADEMIHQR YQPATPSFLN AGRKRRGELV SCFLLQVTDD
MNSIGRSINS ALQLSRIGGG VGISLSNLRE AGAPIKGYEG AASGVVPVMK LFEDSFSYSN
QLGQRQGAGV VYLDVFHPDI EMFLSTKKEN ADEKIRVKTL SLGLTIPDKF YELARNNEEM
YLFSPYSVER EYGVPFSYID ITQKYDELVA NPNIRKTKIL ARDLENEISK LQQESGYPYI
INIDEANRQN PIDGKIIMSN LCSEILQVQT PSVINDRQEY EVLGTDISCN LGSTNIPNLM
SSPDFGESVR AMTRALTYIT DSSDIDVVPS IQNGNSLNHT IGLGAMGLHT FFAKNQMSYG
SPESIEFTDV YFSLLNYWTL VESNQIAKER KVSFNNFENS AYADGTYFDR YINQPVVPHS
EKIKDIFNGI FIPAAEDWSA LRDNIQADGL YHQNRLAVAP NGSISYINDT SASIHPITRL
IEERQEKKIG KIYYPAPNLS NETLPYYTSA YDMDMRQVID VYAAAQKHVD QGMSLTLFMR
SEIPEGLYEW KTETSKQTTR DLTILRHYAF NQGIKSIYYV RTFTEDEEEI GSNQCESCVI
//
