ID   A0A120JTY4_9FIRM        Unreviewed;       705 AA.
AC   A0A120JTY4;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
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=AOC36_10170 {ECO:0000313|EMBL:AMC94323.1};
OS   Erysipelothrix larvae.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Erysipelothrix.
OX   NCBI_TaxID=1514105 {ECO:0000313|EMBL:AMC94323.1, ECO:0000313|Proteomes:UP000063781};
RN   [1] {ECO:0000313|EMBL:AMC94323.1, ECO:0000313|Proteomes:UP000063781}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LV19 {ECO:0000313|EMBL:AMC94323.1,
RC   ECO:0000313|Proteomes:UP000063781};
RA   Lim S., Kim B.-C.;
RT   "Erysipelothrix larvae sp. LV19 isolated from the larval gut of the
RT   rhinoceros beetle, Trypoxylus dichotomus.";
RL   Submitted (OCT-2015) 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; CP013213; AMC94323.1; -; Genomic_DNA.
DR   RefSeq; WP_067633922.1; NZ_CP013213.1.
DR   AlphaFoldDB; A0A120JTY4; -.
DR   STRING; 1514105.AOC36_10170; -.
DR   KEGG; erl:AOC36_10170; -.
DR   OrthoDB; 9762933at2; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000063781; Chromosome.
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; 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; 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   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:UP000063781}.
FT   DOMAIN          564..586
FT                   /note="Ribonucleotide reductase large subunit"
FT                   /evidence="ECO:0000259|PROSITE:PS00089"
SQ   SEQUENCE   705 AA;  80416 MW;  6A83E7CA066F282C CRC64;
     MTVQNKGSHQ IPEWIILNNQ IIDENGAIKD LNKDKEAVRS YFLNEINKKT QFFHSLKEQL
     DYLIENDYYE EEFLKKYTFE DIESVFKIAY DAKFRFPTYM GAFKFYNDYA LKSNDERRVF
     LERYEDRLSI IALYHADGDV DLARALITRL IAQDFTPATP TLLNTGKKKR GEFVSCFLLE
     VDDSLNDIAR VQEFAMQLSK LGGGVSINLT NLRAKGESIK DIPNVAKGVV GVAKLLDNAF
     RYADQMGQRQ GAGAVYLNVF HSDIEDFLST KKLNADDDVR VKTLSMGVVV PDKMIELARE
     DKDMYVFYPH TVYQEYGLPF SDVAIKMDEY YDELVANPNV RKRKINPRRL LDMIAQLQGE
     SGYPYIMYAD NVNSANPLAD PIKFSNLCTE ILQPSIVSHY ADYHEHDKDV LGMDISCNLA
     SGHMGNMMKH NSIKETVFAS MDVMNSVSNK TNIAHVPSVA RANKMMRSVG FGIMGHHGYI
     AENYIAFGSK EDIELVDVFF NAVNFYSLEH SMLKAKETNQ TFYGFERSAY ADGSYFENRG
     AIYPKLEVVQ QLFNDITLPS DEDWANLKED VMKYGLYNSN RLAVAPNGSI AYVMSATPSL
     TPIKQVVEER TYGNSKTYFP MPASDVASFM YESAYTMDKY KVIDVIATAQ KHVDQGISFE
     LCITSDETTR SLQRYYLYAH YQGIKTLYYT RTQKLRVDEC VSCAV
//