ID A0A0Q6XLR5_9BURK Unreviewed; 943 AA.
AC A0A0Q6XLR5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=ASC87_00530 {ECO:0000313|EMBL:KQW02875.1};
OS Rhizobacter sp. Root1221.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX NCBI_TaxID=1736433 {ECO:0000313|EMBL:KQW02875.1, ECO:0000313|Proteomes:UP000051465};
RN [1] {ECO:0000313|EMBL:KQW02875.1, ECO:0000313|Proteomes:UP000051465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1221 {ECO:0000313|EMBL:KQW02875.1,
RC ECO:0000313|Proteomes:UP000051465};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW02875.1, ECO:0000313|Proteomes:UP000051465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1221 {ECO:0000313|EMBL:KQW02875.1,
RC ECO:0000313|Proteomes:UP000051465};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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}.
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:KQW02875.1}.
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DR EMBL; LMDI01000001; KQW02875.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q6XLR5; -.
DR STRING; 1736433.ASC87_00530; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000051465; Unassembled WGS sequence.
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; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000051465}.
FT DOMAIN 15..121
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 133..224
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 943 AA; 104571 MW; F9F2C8DAC5915E3F CRC64;
MESIMQMKTS ELSALSVIRR EGNVVPFDAA KIRTAIANAF LKDGAGLPRR HGGAALSASE
RAKVDRFTDE VVSAVTRRRD ATVPVRIEDI QDYVELALMR AGEHEVARGY VLFRHRRAEL
RETAKSEASS ADRTVVLVDG DNRRRIGRDD IAELVADSCR GIDGADANAI VLQALRDLPA
EVTSERVVDE ALLLAASSLI ERDPAYDRVT AQLFLRMIRR EVLGEGVTDE VMAMVYAHQL
AEMISVGIDT ERLDKRLAEF DLKRLGAAIQ PERDREFRYM GLQVLYDRYF MQVDERCIEL
PQSFFMRIAM GIALNEADRN GRAIEFYDTL STFRFMNSTP TLFNAGTVVP QLSSCYLTTV
ADDLDGIYES IKDNALLQKF AGGMGNDWTR VRALGSRIKG TNGKSQGTIP FLKVVNDTAV
AVNQGGKRKG AVCAYLETWH LDIEEFVELR KNAGDDRRRT HDMNTAHWVP DLFMKRVIAN
GEWTLFSPVD VPDLHDKYGR AFEKAYVAYE AMAADGRIKH TKTVQAVALW RKMLSMLFET
GHPWICFKDA CNVRSPQQHV GVVHSSNLCT EITLNTSDDE IAVCNLGSVN LAAHMVGGAL
DRELLRHTVR SGMRMLDNVI DLNHYAVEKA RRSNMLHRPV GLGMMGLQDA LYALQVSFAS
EEAVHFGSAA TEALCYYAYE ASSDLAAERG RYETYDRSLW NLGILPPDTV EMLHTERGGN
VDQGGETTLD WESLRKRICL QGMRNSNCVA IAPTATIASI VGINATIEPA YQNLYVKSNL
SGEFTVVNES LVRDLKALGL WDEVMVADLK YFDGSVQSID RVPAELKALY ATAFEIDARW
LIEAASARQR WIDQSQSVNL FFRAPSGATL DAAYKLAWTK GLKTTYYLRA LAATSAEKST
GRVGSLNAVS VGTPAASTEE AFATTARPMA LCALDNPECE SCQ
//
