ID A0A2N9JKL3_9ACTN Unreviewed; 718 AA.
AC A0A2N9JKL3;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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:SPD88550.1};
GN ORFNames=MPLG2_3520 {ECO:0000313|EMBL:SPD88550.1};
OS Micropruina glycogenica.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Micropruina.
OX NCBI_TaxID=75385 {ECO:0000313|EMBL:SPD88550.1, ECO:0000313|Proteomes:UP000238164};
RN [1] {ECO:0000313|EMBL:SPD88550.1, ECO:0000313|Proteomes:UP000238164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1 {ECO:0000313|EMBL:SPD88550.1};
RA Cohen D.B., Kent A.D.;
RL Submitted (FEB-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}.
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DR EMBL; LT985188; SPD88550.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N9JKL3; -.
DR KEGG; mgg:MPLG2_3520; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000238164; Chromosome 1.
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:UP000238164}.
FT DOMAIN 570..592
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 718 AA; 80845 MW; 2A6073B09A11FA5A CRC64;
MATTLLTDTG VEAVPAEVDY HALNALLNLY DADGRIQFEA DRKAAHQYFL QHVNQNTVFF
HSLKEKLDYL VEQGYYEQQV LAKYDFDYIK SLFKRAYAVK FRFPTFMGAF KYYTSYTLKT
FDGTRYLERF EDRVCMVALA LADGDRVLAE HIVDEVMSGR FQPATPTFLN AGKAQRGELV
SCFLLRVEDN MESIARAINS SLQLSKRGGG VALSLTNIRE AGAPIKKIQN QSSGVIPVMK
LLEDSFSYAN QLGARQGAGA VYLNAHHPDI LSFLDTKREN ADEKIRIKTL SLGVVIPDIT
FELARDNEDM YLFSPYDIER VYGVPFTDIS VTEKYREMVD DRRITKKKIN ARKFFQTLAE
IQFESGYPYI MFEDTVNRAN PIDGRITMSN LCSEILQVST PSTFNEDLSF DQVGKDISCN
LGSLNIAKAM DSPHFGRTIE TAIRALTAVS DQSNIACAPS IARGNAMSHA IGLGAMNLHG
YLARESVHYG SDEGLDFTNM YFYTVTFHAI AASCRIARER GESFDGFERS KYASGEFFRK
YLTGDWTPRT TKVKELFAGA GIELPTPDDW RALAAEVAEY GMYNQNLQAI PPTGSISYIN
HSTSSIHPIV SKIEIRKEGK IGRVYYPAPF MTNNNIEYYR DAYEIGPEAI IDTYAEATKH
VDQGLSLTLF FPDNVTTRDL NRAQIYAWKK GIKTLYYIRL RQLALEGTEV EGCVSCAL
//