ID A0A109IN86_9ACTN Unreviewed; 791 AA.
AC A0A109IN86;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=GA0070623_1403 {ECO:0000313|EMBL:SCG46781.1};
OS Micromonospora rifamycinica.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=291594 {ECO:0000313|EMBL:SCG46781.1, ECO:0000313|Proteomes:UP000198226};
RN [1] {ECO:0000313|EMBL:SCG46781.1, ECO:0000313|Proteomes:UP000198226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44983 {ECO:0000313|EMBL:SCG46781.1,
RC ECO:0000313|Proteomes:UP000198226};
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}.
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DR EMBL; LT607752; SCG46781.1; -; Genomic_DNA.
DR RefSeq; WP_067303618.1; NZ_LT607752.1.
DR AlphaFoldDB; A0A109IN86; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000198226; 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};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410}.
SQ SEQUENCE 791 AA; 86986 MW; FA60BAF485C1046A CRC64;
MTVVQESPPP GAGEVEPRRP VMRVRRPDGG TEPVDVDRIV TAVARWAADL DEVDPLRVAT
ATVNGLYDGA TTAEVDRLSI QTAAELIGTE PQYSRLAARL LVGFVEKEVR GQSVTSFSES
VRYAHGLGLI ADDTAAFVAR HARQLDDAVD PDGDLRFEYF GLRTVADRYL LRHPESRLVV
ETPQHWLLRV ACGLSGTPDE AVGFYRLMSS LAYLPSSPTL FNSGTRHTQM SSCFLVDSPR
DELDSIYERY HQVAKLSKFS GGIGISFTRV RGRGALIRGT NGRSNGIVPF LKTLDAGVAA
VNQGGRRKGA ACVYLEPWHP DVEEFLELRD NTGEEARRTH NLNLANWIPD EFMRRVEADA
EWSLIDPSDA PELPDLYGEA FDAAYRVAEK KAVRTVKARD LYGRMMRTLA QTGNGWMTFK
DPANRLSNQT GVPGNTIHLS NLCTEILEVN SDTETAVCNL GSVNLGAHLT GGGVDWEKLR
ATVRTAVVFL DRVIDVNYYP AEQAAASNPR WRPVGLGLMG LQDALFALRL PFDSAGAREL
STRVQEEIFL TALETSTDLA ERFGAHPAYP QTRAARGDLH PDLWGVEPAQ AGRWAALRTR
IAAHGLRNSL LVAIAPTATI ASIAGCYECI EPQVSNLFKR ETMSGEFLQI NTYLVRELKA
RGLWTPEIRD RIKRADGSVQ GIVELPAEVR ELFRTAWELP QRALIDLAAA RAPYIDQSQS
LNLFLSAPTI GKLSSMYLHA WKSGLKTTYY LRSRPATRIQ QATVTVGPAV TADAEALACS
LENPESCEAC Q
//
