ID A0A239QQZ5_9MICO Unreviewed; 717 AA.
AC A0A239QQZ5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=SAMN06298212_10646 {ECO:0000313|EMBL:SNU01044.1};
OS Ruaniaceae bacterium KH17.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Ruaniaceae.
OX NCBI_TaxID=1945888 {ECO:0000313|EMBL:SNU01044.1, ECO:0000313|Proteomes:UP000214750};
RN [1] {ECO:0000313|EMBL:SNU01044.1, ECO:0000313|Proteomes:UP000214750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH17 {ECO:0000313|EMBL:SNU01044.1,
RC ECO:0000313|Proteomes:UP000214750};
RA Sun Z.S., Albrecht U., Echele G., Lee C.C.;
RL Submitted (JUL-2017) 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; FZQV01000006; SNU01044.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239QQZ5; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000214750; 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:UP000214750}.
FT DOMAIN 569..591
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 717 AA; 81304 MW; DA3FA92BB534DE69 CRC64;
MAETLTDIGL ETTPDSLELD YHSLNAMLNL YDADGNIQFD KDRAAARQYF LQHVNQNTVF
FHNLKEKLDY LVTEGYYESE VLDKYDYEFI KSVFKFAYSF KFRFPTFLGA FKYYTSYTLK
TFDGKRYLER FEDRVSMVAL SLADGDRDFA LKLVEEIITG RFQPATPTFL NAGKKQRGEA
VSCFLLRIED NMESIARGIN SALQLSKRGG GVALLLTNLR EAGAPIKKIQ NQSSGVIPVM
KLLEDSFSYA NQLGARQGAG AVYLNAHHPD IESFLDTKRE NADEKIRIKT LSLGVVIPDI
TFELARKNED MYLFSPYDVE RIYGVPFSDI SVTEKYHEMV DNKQIRKKKI NARQFFQMLA
EIQFESGYPY IMFEDTVNRA NPVAGKVVMS NLCSEILQVS SPSVYNDDLS YKEIGKDISC
NLGSMNIAKS MESPDLGRTV GTAIRALTAV SDQTSIDSVP SIVKGNNESH AIGLGQMNLH
GYLAKERIYY GSEEGLDFTN IYFYTVLFHA LTESNKLAIE RGQAFGGFEN SKYASGEFFE
KYVDQVWEPK TARVRELFEG IHIPTQADWA ALRDSVMEHG IYNQNLQAVP PTGSISYINH
STSSIHPIVS KIEIRKEGKI GRVYYPAPYM TNENLEYYQD AYEIGYEKII DTYAEATQHV
DQGLSLTLFF PSTATTRDIN KAQIYAWKKG IKTLYYIRLR QMALEGTEVE GCVSCML
//
