ID A0A1J4N0V5_9ACTN Unreviewed; 574 AA.
AC A0A1J4N0V5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
GN ORFNames=UG56_018985 {ECO:0000313|EMBL:OIJ25154.1};
OS Nocardioides luteus.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1844 {ECO:0000313|EMBL:OIJ25154.1, ECO:0000313|Proteomes:UP000033772};
RN [1] {ECO:0000313|EMBL:OIJ25154.1, ECO:0000313|Proteomes:UP000033772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAFB {ECO:0000313|EMBL:OIJ25154.1,
RC ECO:0000313|Proteomes:UP000033772};
RA Murphy D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OIJ25154.1, ECO:0000313|Proteomes:UP000033772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAFB {ECO:0000313|EMBL:OIJ25154.1,
RC ECO:0000313|Proteomes:UP000033772};
RA Brown L., Ruiz O.N., Gunasekera T.;
RT "Draft Genome Sequence of Nocardioides luteus Strain BAFB, an Alkane-
RT Degrading Bacterium Isolated from JP-7 Polluted Soil.";
RL Submitted (OCT-2016) 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|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:OIJ25154.1}.
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DR EMBL; JZDQ02000028; OIJ25154.1; -; Genomic_DNA.
DR RefSeq; WP_045551828.1; NZ_JZDQ02000028.1.
DR AlphaFoldDB; A0A1J4N0V5; -.
DR STRING; 1844.UG56_018985; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000033772; 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:InterPro.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR039718; Rrm1.
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; 3.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
PE 3: Inferred from homology;
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003410};
KW Reference proteome {ECO:0000313|Proteomes:UP000033772}.
FT DOMAIN 27..100
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 104..199
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 231..390
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 401..549
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 574 AA; 63810 MW; 53A02894F515488D CRC64;
MSSNSWEALS AERKALQAEG TVPAFMTTAG YAMFKAKYTV AGQSVRERYE TIARTAGELA
DEMYAREDGG SWTERFFEAI WNGWLSPSTP VLSNLGTDRG LPVSCEGSYV EDSVWGFYET
LKEAAILSQN GFGTSAYLGD VRPRGAKFSD NGKANGVVPV FCNFVEMTNQ ISQGATRRGS
WAGYLPVDHP DFYELADLIF REPANKNVGW IFSQEFIDRM LAGDKDALER YQRVLKIRVV
LGKGYIWKVD TVNAAQTESY RANGLANKAS NLCSEITLFS DEDHSYTCVL SSLNLSTYDE
WKDQDTAYVA TVFLDAVAEA FVRKARTIRG LERAVRYTEK ARSLGLGVMG YHDYLQKHRV
PFESDKAAAL NKDIFERIST RADAASRWMG SVAGIPEWCV GRRNSHLMAI APTMSTAVIV
GGTSQGIEPY VANVWNQTTS AGEMPRANQN LVEVMKERGV YDQAHISDII DHGGSVQHVS
WLDDHEKEVF RTGYEIDQEI LLARASDRQV YIDQSQSLNL FFQADATPQY ISKIHKLALL
DPNIKSLYYL RSRAGIQASK QSASTTSTTS TAKA
//
