ID A0A162J142_9MICO Unreviewed; 711 AA.
AC A0A162J142;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 Name=nrdE2 {ECO:0000313|EMBL:KZX20677.1};
GN ORFNames=ACH61_02212 {ECO:0000313|EMBL:KZX20677.1}, EV639_10211
GN {ECO:0000313|EMBL:TCO38374.1};
OS Rathayibacter tanaceti.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Rathayibacter.
OX NCBI_TaxID=1671680 {ECO:0000313|EMBL:KZX20677.1, ECO:0000313|Proteomes:UP000076717};
RN [1] {ECO:0000313|EMBL:TCO38374.1, ECO:0000313|Proteomes:UP000295366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM Ac-2596 {ECO:0000313|EMBL:TCO38374.1,
RC ECO:0000313|Proteomes:UP000295366};
RX PubMed=26203337; DOI=.1186/s40793-015-0017-x;
RA Whitman W.B., Woyke T., Klenk H.P., Zhou Y., Lilburn T.G., Beck B.J.,
RA De Vos P., Vandamme P., Eisen J.A., Garrity G., Hugenholtz P.,
RA Kyrpides N.C.;
RT "Genomic Encyclopedia of Bacterial and Archaeal Type Strains, Phase III:
RT the genomes of soil and plant-associated and newly described type
RT strains.";
RL Stand. Genomic Sci. 10:26-26(2015).
RN [2] {ECO:0000313|EMBL:KZX20677.1, ECO:0000313|Proteomes:UP000076717}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM Ac-2596 {ECO:0000313|EMBL:KZX20677.1,
RC ECO:0000313|Proteomes:UP000076717};
RA Vasilenko O.V., Starodumova I.P., Tarlachkov S.V., Dorofeeva L.V.,
RA Evtushenko L.I.;
RT "Draft Genome Sequence of Rathayibacter sp. Strain VKM Ac-2596 Isolated
RT from Leaf Gall Induced by Plant-Parasitic Nematodes.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:TCO38374.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VKM Ac-2596 {ECO:0000313|EMBL:TCO38374.1};
RA Whitman W., Huntemann M., Clum A., Pillay M., Palaniappan K., Varghese N.,
RA Mikhailova N., Stamatis D., Reddy T., Daum C., Shapiro N., Ivanova N.,
RA Kyrpides N., Woyke T.;
RL Submitted (MAR-2019) 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:KZX20677.1}.
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DR EMBL; LIIN01000080; KZX20677.1; -; Genomic_DNA.
DR EMBL; SLWP01000002; TCO38374.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162J142; -.
DR PATRIC; fig|1671680.3.peg.2358; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000076717; Unassembled WGS sequence.
DR Proteomes; UP000295366; 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:UP000076717}.
FT DOMAIN 563..585
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 711 AA; 80482 MW; D1DFC4F0A9A8A01E CRC64;
MIDAPRDAAQ MDYHSLNAML NLYGPNGEIQ FDKDREAARE FFLQHVNQNT VFFHTLRERL
DYLVEKEYYE QAVLDQYSFE FIQQLNDLAY SKKFRFATFL GAFKYYTSYT LKTFDGKRYL
ERFEDRVVMT ALGLAQGDEK LATALVEEIV AGRFQPATPT FLNTGKAQRG ELVSCFLLRI
EDNMESIARG INSALQLSKR GGGVALSLSN IREAGAPIKQ IENQSSGIIP VMKLLEDSFS
YANQLGARQG AGAVYLSAHH PDILRFLDTK RENADEKIRI KTLSLGVVVP DITFELAKNN
EDMYLFSPYD VERVYGIPFG DLSISEKYRE MVDDPRIKKT KISAREFFQT IAEIQFESGY
PYIVFEDTVN QANPIKGRIN MSNLCSEILQ VNTPTTYNED LSYAQIGKDI SCNLGSLNIA
LTMDSPDFGR TIETAIRGLT SVSDQSHITS VRSIEDGNDK SHAIGLGQMN LHGYLARERI
HYGSEEGIDF TNIYFYSVLF HALRASNNLS IERGTTFEGF ADSKYASGEF FDTYTEKEWA
PATERVARLF EGAGIAVPSQ DDWRALKASV MEHGIYNQNL QAVPPTGSIS YINNSTSSIH
PIASKIEIRK EGKLGRVYYP APFMTNDNLE YYQDAYEIGY EKIIDTYAAA TQHVDQGLSL
TLFFKDTATT RDINRAQIYA WRKGIKTIYY IRIRQMALEG TELDQCVSCM L
//
