ID A0A418UZL8_9DEIO Unreviewed; 695 AA.
AC A0A418UZL8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 16.
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 Name=nrdE {ECO:0000313|EMBL:RJF68917.1};
GN ORFNames=D3875_21445 {ECO:0000313|EMBL:RJF68917.1};
OS Deinococcus cavernae.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=2320857 {ECO:0000313|EMBL:RJF68917.1, ECO:0000313|Proteomes:UP000286287};
RN [1] {ECO:0000313|EMBL:RJF68917.1, ECO:0000313|Proteomes:UP000286287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K2S05-167 {ECO:0000313|EMBL:RJF68917.1,
RC ECO:0000313|Proteomes:UP000286287};
RA Zhu H.;
RL Submitted (SEP-2018) 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 -!- PATHWAY: Genetic information processing; DNA replication.
CC {ECO:0000256|ARBA:ARBA00005160, 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:RJF68917.1}.
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DR EMBL; QYUJ01000030; RJF68917.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418UZL8; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000286287; 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:UniProtKB-UniPathway.
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:SF30; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE 2 SUBUNIT ALPHA; 1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 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:UP000286287}.
FT DOMAIN 553..575
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 695 AA; 78403 MW; 927B0BC6D8B07FFE CRC64;
MEPWIELNNK VLAGSAVDTR FDTDALQVYF QEKVNPNTVF FHDLAEKIRY LTEHGVWDRA
IFERYRPEEV QAVFDRAYSY KFRFRSFMGA YKFYSEYATM TPNRTRWLER YEDRLSITAL
SRSETVEDAL ELVHHLVNQT FTPATPTLMN AGKANTGRLV SCFLLQDCTD NLDSITKTLA
FVAELSKGGG GIGVEVSNLR ARGEALRGIQ NVTKGVMGVA KMLDNMLRYA DQAGQRPGAG
AVYLSVMHAD FSDLLNAKKI ATDEDARLKT LSVGATIPDV FMEKVRAGED IYQFYPHSLF
QHTGREFTDI DWTREYQALA DNPLIRKKRV PARRVLEDIA VTQGESGYPY LLFEGHANRA
NPIPNVGSIK MSNLCSEILQ PTTPSYFHSY GQEHRDRIGL DVSCNLASLV IEQTMHSGEI
GRVVGAAVRM LDHVARSTSI TEVPAVRRAN DEMRSIGLGA MGLHSFLAGK ELIYGSPEAL
EFVDVFFAAV HYHARKASME IARETGFVFG GFEGSRYQSG EHFAQYLERD FHPQTPEVAA
LFEGHTLPTR ADWRQLVQDI RTHGLAHSFV MAIAPTGSIS YVSHASASIM PITEKVETRT
SNKARTIYPM PHLSDDTEWY YEEAYDMDQR RVLDTVAAAQ RHVDQGISCT LFVPASATTR
TLQRYYLYAY RLGIKTLYYT RLRKTNVQDC LSCVV
//