ID A0A1I3US21_9BACL Unreviewed; 694 AA.
AC A0A1I3US21;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=SAMN02799624_06301 {ECO:0000313|EMBL:SFJ85782.1};
OS Paenibacillus sp. UNC496MF.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1502753 {ECO:0000313|EMBL:SFJ85782.1, ECO:0000313|Proteomes:UP000198714};
RN [1] {ECO:0000313|EMBL:SFJ85782.1, ECO:0000313|Proteomes:UP000198714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UNC496MF {ECO:0000313|EMBL:SFJ85782.1,
RC ECO:0000313|Proteomes:UP000198714};
RA de Groot N.N.;
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}.
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DR EMBL; FORE01000022; SFJ85782.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3US21; -.
DR STRING; 1502753.SAMN02799624_06301; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000198714; 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:UP000198714}.
FT DOMAIN 552..574
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 694 AA; 78252 MW; F8C14746674C6F34 CRC64;
MRHIELNNLL MQRGEDGFFR LEKDREAVDA FMAEAASRSL TFASTADKLR YMIDHDYYED
VYRDYTAREV DEVFALTHGH PFRFESYMAV SKFYTDYAMK SDDKSLYLEH YPDRVAIVAL
HLGRGDAETA RKLALAMMEQ RVQPATPTFL NAGKSRRGEL VSCFLLEMDD SLNSINYVLA
TCMQLSKIGG GVAVNLSKLR GRGEPIKGVE GAAKGIMPVL KLMEDAFSYA DQMGQRKGSG
AGYYNIFGWD VMEFLDSKKI NADEKTRLKT LSIGLIVPNK FYELAERNEK LHVFGPHSVL
KAYGTHLDDM DMDEMYETLL ADGRVKKKAV LDARDMLTKI ATIQLESGYP YIMNRSNANR
GHALRGIGMI KMSNLCTEIF QFQETSEIGD YGQADVIRRD ISCNLASLNI ANVMALGKIR
ESVHEGMLAL TAVTDMTRIE NAPGVAKAND ELRSVGLGAM NLHGYLAKNR IAYESPEARD
FARTFFMTMN YHSLECSMEI ARRTGRTFAG FGKSDYASGV YFERYLETDY RPATEKVRAL
FADIAVPSPA DWARLKADVA EHGLYHAYRL AIAPTQSISY VQNSTSSVMP IVEPIETRTY
ANSTTYYPMP FLSKDNLFYY KSAYQMNQLK VIDLIAEIQT HVDQGISTIL HVNSDVSTRE
LSRYYVYAAK KGLKSLYYTR TNMLSVENCI SCAV
//
