ID Q6YRG1_ONYPE Unreviewed; 769 AA.
AC Q6YRG1;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 109.
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=nrdA {ECO:0000313|EMBL:BAD04139.1};
GN OrderedLocusNames=PAM_054 {ECO:0000313|EMBL:BAD04139.1};
OS Onion yellows phytoplasma (strain OY-M).
OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC Acholeplasmataceae; Phytoplasma; 16SrI (Aster yellows group).
OX NCBI_TaxID=262768 {ECO:0000313|EMBL:BAD04139.1, ECO:0000313|Proteomes:UP000002523};
RN [1] {ECO:0000313|EMBL:BAD04139.1, ECO:0000313|Proteomes:UP000002523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OY-M {ECO:0000313|Proteomes:UP000002523};
RX PubMed=14661021; DOI=10.1038/ng1277;
RA Oshima K., Kakizawa S., Nishigawa H., Jung H.-Y., Wei W., Suzuki S.,
RA Arashida R., Nakata D., Miyata S., Ugaki M., Namba S.;
RT "Reductive evolution suggested from the complete genome sequence of a
RT plant-pathogenic phytoplasma.";
RL Nat. Genet. 36:27-29(2004).
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; AP006628; BAD04139.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6YRG1; -.
DR STRING; 262768.PAM_054; -.
DR KEGG; poy:PAM_054; -.
DR eggNOG; COG0209; Bacteria.
DR eggNOG; COG1780; Bacteria.
DR HOGENOM; CLU_000404_4_1_14; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000002523; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0010181; F:FMN 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 GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR CDD; cd01679; RNR_I; 1.
DR Gene3D; 1.10.1650.20; -; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR InterPro; IPR029039; Flavoprotein-like_sf.
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; IPR004465; RNR_NrdI.
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; PF07972; Flavodoxin_NdrI; 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}.
FT DOMAIN 628..650
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 769 AA; 87453 MW; C3F70034693D5504 CRC64;
MSGNKNWGKN YGKAGDTIAS TYNVPLVLKF EGSGMPEERA FLKKWLACYC NDQKLPSYQS
QTQAQLQTLT PKKTVLPPWI TLTNQIIDEQ GNIKDLNKDK EALQSFLQEG VLPKLKRFAT
LQEKLTFLQE NEYYESAFLQ KYTHSQIKEI YQIAYQKNFT FPTFMGAFKF YHDYALKTRD
KQHYLETYED RLSVNALYHA KGDFEIAKRL IVSLINQDFT PATPTLLNTG KKHRGEFVSC
FLLEAGDSLN DIARINEFSM QLSKIGGGVS INITNLRAKG ESIKGIKGVC KGVVGVCKLL
DHSFRYADQI GLRTGAGAVY LNVFHSDIID FLSTKKLSAD EDVRVKTLSL GVVVPNKMIE
LARNNEVMYT FFPHTVFLEY GKNFADIAVD MDYWYDILVA NPKVQKKAIN PRQLLELIAH
MQGESGYPYL MFCDNTNQAN TSDLKVKFSN LCTEILQPTI TSHYKDYHQT QQDEIGMDVS
CNLASGHMGN MITNNTIQET VFMAMEVMNC VSENTNISYV PAVAKANFIN RSVGFGIMGH
HGFLAQNYIA FGSEENKDLI DVFFNAVNFY SLLHSCNKAK TTGKKFYRFE QSKYADGSYF
DNRGEILPKT AKIKKMFQNI TLPTQKDWHQ LKQDVMQFGL YNSHRLAVAP NGSIGYIMGA
TPSLTPVKQL VEERTYGNSK TYCPMPALKQ TSFMYTTAYK MNKYDLIDVI AIAQKHVDQG
ISFELGITSD ITTRELQKYY LYAHHKKIKT LYYTRTQKLK IDECEACGV
//
