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Database: UniProt
Entry: A0A2N9JKL3_9ACTN
LinkDB: A0A2N9JKL3_9ACTN
Original site: A0A2N9JKL3_9ACTN 
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
//
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