ID   A0A1I3PKX3_9BACL        Unreviewed;       694 AA.
AC   A0A1I3PKX3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
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=SAMN05518846_102411 {ECO:0000313|EMBL:SFJ22188.1};
OS   Brevibacillus centrosporus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=54910 {ECO:0000313|EMBL:SFJ22188.1, ECO:0000313|Proteomes:UP000198915};
RN   [1] {ECO:0000313|Proteomes:UP000198915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK042 {ECO:0000313|Proteomes:UP000198915};
RA   Varghese N., Submissions S.;
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|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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FORT01000002; SFJ22188.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I3PKX3; -.
DR   STRING; 1884381.SAMN05518846_102411; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000198915; 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; 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:UP000198915}.
FT   DOMAIN          552..574
FT                   /note="Ribonucleotide reductase large subunit"
FT                   /evidence="ECO:0000259|PROSITE:PS00089"
SQ   SEQUENCE   694 AA;  79691 MW;  20FC693A258AAB32 CRC64;
     MRHIELNNEL MQRGEDGFYQ LEKDREAVEV FLEEVQAKTL TFNSVGERMD YLIQNDYYEN
     VYERYTEEQV EEVFRLAKDA SFQFASYMAV SKFYKDYALK TDDKSMYLEQ YPDRVAIVAL
     SLAQGDFDRA KRLTVSMMDQ RLQPATPTFL NAGKSRRGEM VSCFLLEMDD SLNSINYILG
     TCMQLSKIGG GVAVNLSKLR GRGEPIKGVE GAAKGIMPVL KLLEDAFSYA DQMGQRKGSG
     AAYYNIFGWD INEFLDCKKI NADEKSRIKT LSIGLIVPNM FYKLAEENKP LTIFAPYSVY
     KEYGQHLDDM NMDEMYEELL ANDNIKKKTI MSARDMLTKI AMIQLESGYP YIMNKTNANK
     NHALKDIGSV KMSNLCTEIF QLQDTSTINN YGEMDIIRRD ISCNLASLNI VNVMEQKKIR
     ESVHEGIEAI TSVSDMTAVE NAPGVQKANR ELHSVGLGAM NLHGYLAKNK IAYESEEAKD
     FARTFFMMMN FYSLEMSMEI AKERKTTFLG FEQSEYAKGT YFSKYEETDY RPRTEKVKQL
     FADMYIPTTE DWAQLKEKVQ TYGLYHAYRL AIAPTQSISY IQNATSSVMP IVEHIETRTY
     ANSTTYYPMP YLSQENYFFY KSAYVIDQFK VIDLIAEIQE HVDQGISTVL HVNSNVSTRE
     LARYYIYAAK KGLKSLYYTR TKHLTVEECI SCAV
//