ID A0A095WTR4_9ACTO Unreviewed; 718 AA.
AC A0A095WTR4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=HMPREF1627_02675 {ECO:0000313|EMBL:KGF01028.1};
OS Actinomyces sp. S6-Spd3.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=1284680 {ECO:0000313|EMBL:KGF01028.1, ECO:0000313|Proteomes:UP000029604};
RN [1] {ECO:0000313|EMBL:KGF01028.1, ECO:0000313|Proteomes:UP000029604}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S6-Spd3 {ECO:0000313|EMBL:KGF01028.1,
RC ECO:0000313|Proteomes:UP000029604};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGF01028.1}.
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DR EMBL; JRMV01000272; KGF01028.1; -; Genomic_DNA.
DR RefSeq; WP_034500852.1; NZ_JRMV01000272.1.
DR AlphaFoldDB; A0A095WTR4; -.
DR PATRIC; fig|1284680.3.peg.285; -.
DR eggNOG; COG0209; Bacteria.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000029604; 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:UP000029604}.
FT DOMAIN 570..592
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 718 AA; 81401 MW; 526B545F1CC97A88 CRC64;
MAENLTDTGV EPAPSPELDY HALNAQLNLY DADGKIQFEA DRQAARQYFL QHVNQNTVFF
HDLEEKMEYL VEQGYYEKHV LDQYDFQDIK DLHKQAYAHK FRFPTFLGAF KYYTSYTLKT
FDGTRYLERF EDRVVMVALY LAQGDIEMAR HLVDEMMTGR FQPATPTFLN AGKAARGELV
SCFLLRIEDN MESIARGINS ALQLSKRGGG VALQLTNLRE AGAPIKKIQN QSSGVVPVMK
LLEDSFSYAN QLGARQGAGA VYLHAHHPDI MQFLDTKREN ADEKIRIKTL SLGVVIPDIT
FELARKNEDM YLFSPYDVER VYGVPFSEIS VTEKYHEMVD DGRIHKKKIN ARRFFQTIAE
IQFESGYPYI VFEDTVNAAN PIKGRITMSN LCSEILQVSE ASTYNDDLSY SHIGKDISCN
LGSLNIAKTM DSPDFSKTIE TAIRGLTAVS DLSDIQSVPS IARGNAMSHA IGLGQMNLHG
YLAREHIYYG SEEALDFTNM YFMAVAYEAI KASCLIARER GVSFEGFEDS QYASGEYFRK
YIDQVWEPQT ERCRELLAAS TIHLPTQEDW AALAADVAQY GMYNQNLQAV PPTGSISYIN
GSTSSIHPIV SRIEIRKEGK IGRVYYPAPY MTNENLEYYQ DAYEIGPEKI IDTYAVATQH
VDQGLSLTLF YPDTVTTRDL NKSYIYAWRK GIKTLYYMRL RQMALEGTEV SGCVSCML
//
