ID   A0A1A9BTK7_9ACTN        Unreviewed;       783 AA.
AC   A0A1A9BTK7;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
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=GA0115233_103151 {ECO:0000313|EMBL:SBT91532.1};
OS   Streptomyces sp. DI166.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1839783 {ECO:0000313|EMBL:SBT91532.1, ECO:0000313|Proteomes:UP000198690};
RN   [1] {ECO:0000313|Proteomes:UP000198690}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DI166 {ECO:0000313|Proteomes:UP000198690};
RA   Varghese N., Submissions Spin;
RL   Submitted (JUN-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|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}.
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DR   EMBL; FLSP01000031; SBT91532.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1A9BTK7; -.
DR   STRING; 1839783.GA0115233_103151; -.
DR   OrthoDB; 9762933at2; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000198690; 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:UP000198690}.
FT   DOMAIN          585..607
FT                   /note="Ribonucleotide reductase large subunit"
FT                   /evidence="ECO:0000259|PROSITE:PS00089"
SQ   SEQUENCE   783 AA;  86180 MW;  67F09813905213ED CRC64;
     MTIAPADPAS AAPVETDGPG AALLRTLTEL TADLPDADPG RVAAAALRGR SARADEAELR
     ELATEAAAGL ISEDPAYSRL AARLLTVSIA AEAASQGVTR FTESVAVGHR EGLIADRTAE
     FVRLHGERLD AVIDPAADDR FGYFGLRTLH SRYLLRHPIT RKVVETPQHF MLRVAAGLAE
     DDSARSVDEV TALYGLMSRL DYLPSSPTLF NSGTRHPQMS SCYLLDSPKD ELDSIYDRYH
     QVARLSKHAG GIGLSYSRIR SRGSLIRGTN GHSNGIVPFL KTLDASVAAV NQGGRRKGAA
     AVYLETWHSD IEEFLELRDN TGEDARRTHN LNLAHWIPDE FMRRVNADEQ WSLFSPADVP
     ELVDLWGEEF DAAYRKAEQA GLARRTIAAR DLYGRMMRTL AQTGNGWMTF KDAANRTANQ
     TALPGHVVHS SNLCTEILEV TDDGETAVCN LGSVNLGAFV RDGDLDWERL DATVRTAVTF
     LDRVVDINFY PTEQAGRSNA KWRPVGLGAM GLQDVFFQLR LPFDSPEAKA LSTRIAERIM
     LAAYEASADL AERNGPLPAW EKTRTARGVL HPDHYDVELT WPERWAALRS RVAEVGLRNS
     LLLAIAPTAT IASIAGVYEC IEPQVSNLFK RETLSGEFLQ VNSYLVRDLK ELGVWDARTR
     EALRDANGSV QGFAWIPEDV RKLYRTAWEI PQRGLIDMAA ARTPFLDQSQ SLNLFLETPT
     IGKLSSMYAY AWKSGLKTTY YLRSRPATRI ARAAQATVPV QQAADPEAVA CSLENPESCE
     ACQ
//