ID A0A2S4Z3K7_9ACTN Unreviewed; 790 AA.
AC A0A2S4Z3K7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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 ORFNames=C3489_09655 {ECO:0000313|EMBL:POX55571.1};
OS Streptomyces sp. Ru71.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2080746 {ECO:0000313|EMBL:POX55571.1, ECO:0000313|Proteomes:UP000237414};
RN [1] {ECO:0000313|EMBL:POX55571.1, ECO:0000313|Proteomes:UP000237414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ru71 {ECO:0000313|EMBL:POX55571.1,
RC ECO:0000313|Proteomes:UP000237414};
RA Suneja G., Sharma R.;
RT "Genome sequencing of cellulose degrading bacteria.";
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 -!- 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:POX55571.1}.
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DR EMBL; PQSS01000011; POX55571.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4Z3K7; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000237414; 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; 3.20.70.20; -; 1.
DR InterPro; IPR013346; NrdE_NrdA_C.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR NCBIfam; TIGR02506; NrdE_NrdA; 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 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:UP000237414}.
FT DOMAIN 590..612
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 790 AA; 86835 MW; BEAD9F986985D53C CRC64;
MTIAPADPAS VSDDAVDGLK TDGPGAALLR TLTELTADLP DADPGRVAAA ALRGRSAHAD
EAELRELATE AAAGLISEDP AYSRLAARLL TLTIRAEAAS QGVTSFTESV AVGHREGLVA
DRTAEFVRLH AERLDALVDT GADDRFGYFG LRTLHSRYLL RHPITRKVIE TPQHFLLRVA
SGLAEDDTAR SVDEVAALYG LMSRLDYLPS SPTLFNSGTR HPQMSSCYLL DSPLDELDSI
YDRYHQVARL SKHAGGIGLS YSRIRSRGSL IRGTNGHSNG IVPFLKTLDA SVAAVNQGGR
RKGAAAVYLE TWHSDIEEFL ELRDNTGEDA RRTHNLNLAH WIPDEFMRRV GADEQWSLFS
PADVPELVDL WGEEFDAAYR KAEAAGLAKK TIPARDLYGR MMRTLAQTGN GWMTFKDAAN
RTANQTALPG HVVHSSNLCT EILEVTDDGE TAVCNLGSVN LGAFVAGGDI DWERLDATVR
TAVTFLDRVV DINFYPTEQA GRSNAKWRPV GLGAMGLQDV FFKLRLPFDS PEAKALSTRI
AERIMLAAYE ASADLAERNG PLPAWEKTRT AQGVLHPDHY DVELTWPERW EALRRRIADT
GMRNSLLLAI APTATIASIA GVYECIEPQV SNLFKRETLS GEFLQVNSYL VAELKKLGVW
DARTREALRE SSGSVQDFAW IPEDVRRLYR TAWEIPQRGL IDMAAARTPF LDQAQSLNLF
METPTIGKLS SMYAYAWKSG LKTTYYLRSR PATRIARAAR AQATVPVQQV SSEEAVACSL
ENPESCEACQ
//
