ID A0A0D5NGL8_9BACL Unreviewed; 694 AA.
AC A0A0D5NGL8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=VN24_04900 {ECO:0000313|EMBL:AJY74063.1};
OS Paenibacillus beijingensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1126833 {ECO:0000313|EMBL:AJY74063.1, ECO:0000313|Proteomes:UP000032633};
RN [1] {ECO:0000313|EMBL:AJY74063.1, ECO:0000313|Proteomes:UP000032633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24997 {ECO:0000313|EMBL:AJY74063.1,
RC ECO:0000313|Proteomes:UP000032633};
RX PubMed=25937453; DOI=10.1016/j.jbiotec.2015.04.015;
RA Kwak Y., Shin J.H.;
RT "Complete genome sequence of Paenibacillus beijingensis 7188(T) (=DSM
RT 24997(T)), a novel rhizobacterium from jujube garden soil.";
RL J. Biotechnol. 206:75-76(2015).
RN [2] {ECO:0000313|Proteomes:UP000032633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24997 {ECO:0000313|Proteomes:UP000032633};
RA Kwak Y., Shin J.-H.;
RT "Genome sequence of Paenibacillus beijingensis strain DSM 24997T.";
RL Submitted (MAR-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; CP011058; AJY74063.1; -; Genomic_DNA.
DR RefSeq; WP_045669499.1; NZ_CP011058.1.
DR AlphaFoldDB; A0A0D5NGL8; -.
DR STRING; 1126833.VN24_04900; -.
DR KEGG; pbj:VN24_04900; -.
DR PATRIC; fig|1126833.4.peg.1084; -.
DR HOGENOM; CLU_000404_4_1_9; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000032633; 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:UP000032633}.
FT DOMAIN 552..574
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 694 AA; 78639 MW; D4F8424893A2C850 CRC64;
MRHIELNNEL MQRGADGFFR LEKDREAVAA FMEEVRAKSV SFASHREKID YLVQGDYYED
VYNRYSPEDA VSVFELTHGM EFTFPSYMAA SKFYTDYAMK SNDRSQYLEH YPDRVAIVAL
HLGQGDTQLA KSLAVSMMEQ RLQPATPTFL NAGKSRRGEM VSCFLLEMDD SLNSINYCLS
TCMQLSKIGG GVAVNLSKLR GRGEPIKGVE GAAKGIMPVL KLMEDAFSYA DQMGQRKGSG
AAYYNIFGWD VMEFLDSKKI NADEKSRLKT LSIGLIVPDK FYKLAENNQP LTVFAPFSVY
KEYGIHLDDM NLDEMYEELL ANDKVVRKVV MSARDMLVKI ATIQLESGYP YIMNKSNANA
GHALKDIGSV KMSNLCTEIY QLQETSEIGD FGQPSTIRRD ISCNLASLNI TNVMEHGKIR
ETVHEGIAAL TAVSDMTRVS NAPGVVKANE EMHSVGLGAM NLHGYLTKNK IAYESAEAKD
FARTFFMMLN YYSLDKSADI AQAKNKRFRD YERSEYAKGT YFDRYIETDY RPQTERVKEL
FAGMDIPSPQ DWASLKEKVA RQGLYHAYRL AIAPTQSISY VQNATSSVMP IVEQIETRTY
ANSTTYYPMP YLSQDNFFYY KSAYQMDQFK VIDLIAEIQS HVDQGISTVL HVNSNVTTRE
LARYYLYAAK KGLKSLYYTR TNHLSVEECI SCAV
//
