ID A0A081BJZ9_9LACO Unreviewed; 721 AA.
AC A0A081BJZ9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
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:GAK48367.1};
GN ORFNames=LOSG293_270020 {ECO:0000313|EMBL:GAK48367.1};
OS Secundilactobacillus oryzae JCM 18671.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Secundilactobacillus.
OX NCBI_TaxID=1291743 {ECO:0000313|EMBL:GAK48367.1, ECO:0000313|Proteomes:UP000028700};
RN [1] {ECO:0000313|EMBL:GAK48367.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG293 {ECO:0000313|EMBL:GAK48367.1};
RA Tanizawa Y., Fujisawa T., Mochizuki T., Kaminuma E., Nakamura Y., Tohno M.;
RT "Draft Genome Sequence of Lactobacillus oryzae Strain SG293T.";
RL Genome Announc. 2:e00861-14(2014).
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:GAK48367.1}.
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DR EMBL; BBJM01000027; GAK48367.1; -; Genomic_DNA.
DR RefSeq; WP_034528816.1; NZ_BBJM01000027.1.
DR AlphaFoldDB; A0A081BJZ9; -.
DR STRING; 1291743.LOSG293_270020; -.
DR eggNOG; COG0209; Bacteria.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000028700; 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}.
FT DOMAIN 558..580
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 721 AA; 82388 MW; 3557FA6B535C1FD3 CRC64;
MTLKNISNPT YYDLNNEINI PVNGQIPLHK DQEALEAFLK ENVAPNMYHF DSLRERFDYL
LQHDYIEVDF FNKYDFSFIE KLYDYLNQQN FHFKSFMAAY KFYAQYALKT DDGDYYLENF
ADRAAMNALY FADGDEKLAM NLADEIIHQR YQPATPSFLN AGRKRRGELV SCFLIQTTDD
MNTIGRTINS ALQLSRIGGG VGINLSNLRG AGDPIKHIDG AASGVVPVMK LLEDSFSYSN
QLGQRQGAGV VYLSVFHPDI VDFLSAKKEN ADEKIRLKTL SLGVTVPDKF YELAKANEDM
YLFSPYDVER EYGEPFSYID ITKEYDNMVA NKNIRKKKMP ARELETEIGK LQQESGYPYI
INIDLANRAN PIDGKIVMSN LCSEILQVQT PSTVDNRQEY TQLGRDISCN LGSTNIMNLM
NSPHFGQSVE TMVRALTFVT DASDIDVVPS IQNGNKLAHT IGLGAMGLHS FLAKNHIYYG
STTSTDFTSV YFMLLNYWTL KASNEIAKER HTTFYNFEKS DYASGKYFDK YITKDWGPQS
EEVKTLFKDI FIPSKEDWNA LKSAVMKDGL YHQNRLAVAP NGSISYINDT TASLHPIINR
VEERQEKKIG KIYYPAPYLS NDTMPYYMSA YDMDMRKVIN VYAAAQEHVD QGMSLTLFMR
STIPAGLYEW KNGRTDKMTT RDLSILRNYA YRKGIKSIYY VRTFTDDQDE VGSNQCESCV
I
//
