ID A0A1C4Y658_9ACTN Unreviewed; 799 AA.
AC A0A1C4Y658;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=GA0070607_6305 {ECO:0000313|EMBL:SCF16192.1};
OS Micromonospora coriariae.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=285665 {ECO:0000313|EMBL:SCF16192.1, ECO:0000313|Proteomes:UP000198243};
RN [1] {ECO:0000313|EMBL:SCF16192.1, ECO:0000313|Proteomes:UP000198243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44875 {ECO:0000313|EMBL:SCF16192.1,
RC ECO:0000313|Proteomes:UP000198243};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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; LT607412; SCF16192.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C4Y658; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000198243; Chromosome i.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 3.20.70.20; -; 1.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR013346; NrdE_NrdA_C.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR Pfam; PF03477; ATP-cone; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 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; PS51161; ATP_CONE; 1.
DR PROSITE; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410}.
FT DOMAIN 23..112
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 799 AA; 88533 MW; 3A99EC596C481BE9 CRC64;
MTVTQVVPTG GDTAVPGRRR TQMHVRKRDG ASEQVDVNKI VRAVERWTDD LTDVDPLRVA
TRTISGLYDG ATTAELDRLS IQTAAEMIGE EPQYSRLAAR LLAGYVDKEV RRQGITSFST
AIRMGHAEGL IGDETAAFVA AHARTLDDAV DPDGDRRFEY FGLRTVYDRY LLRHPTSRLV
LETPQYWLLR VACGLSRTPD EAVDFYRLMS SLAYLPSSPT LFNSGTRHTQ MSSCYLVDSP
RDELDSIYQR YAQVANLSKF AGGIGIAYSR VRSRGALIRG TNGQSNGIVP WLRTLDASVA
AVNQGGRRKG AACVYLEPWH PDVEEFLQLR DNTGEDARRT HNLNLANWIP DEFMRRVEAD
EVWSLFDPHE VPELPDLWGD EFDVAYRAAE AQGRYVRQVP ARELYGKMMR TLAQTGNGWM
TFKDAANRLC NQTAEPRNVV HLSNLCTEII EVSSDAETAV CNLGSVNLAA HLADGAIDWQ
RLRATVRTAV TFLDRVIDIN YYPTAEAAAS NPRWRPVGLG LMGLQDVFFA LRLPFDSPAA
RELSTRVSEE LYLTALETSA ELARRFGAHP AYPQTRVARG QLQPDLWGVE GTQTARWAAL
RERVEAYGLR NSLLVAVAPT ATIASIVGCY ECVEPQVSNL FKRETLSGEF LQVNTALVRE
LKARGLWTEP VRSAIKRAEG SVQDIAELPA AVRELFRTAW ELPQRALIDL AAARAPFIDQ
SQSLNLFLAS PTIGKLSSMY LYAWKAGLKT TYYLRSRPAT RIQQATVAPA AVALAAPVAS
APEALACSLE NPESCEACQ
//
