ID RIR1_HELPY Reviewed; 788 AA. AC P55982; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 04-NOV-2026, entry version 142. DE RecName: Full=Ribonucleoside-diphosphate reductase subunit alpha; DE EC=1.17.4.1; DE AltName: Full=Ribonucleotide reductase; GN Name=nrdA; OrderedLocusNames=HP_0680; OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori). OC Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria; OC Campylobacterales; Helicobacteraceae; Helicobacter. OX NCBI_TaxID=85962; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700392 / 26695; RX PubMed=9252185; DOI=10.1038/41483; RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A., RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.; RT "The complete genome sequence of the gastric pathogen Helicobacter RT pylori."; RL Nature 388:539-547(1997). CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis. CC Catalyzes the biosynthesis of deoxyribonucleotides from the CC corresponding ribonucleotides (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + [thioredoxin]- CC disulfide + H2O = a ribonucleoside 5'-diphosphate + [thioredoxin]- CC dithiol; 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 -!- ACTIVITY REGULATION: Under complex allosteric control mediated by CC deoxynucleoside triphosphates and ATP binding to separate specificity CC and activation sites on the alpha subunit. The type of nucleotide bound CC at the specificity site determines substrate preference. It seems CC probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP CC reduction and dTTP favors GDP reduction. Stimulated by ATP and CC inhibited by dATP binding to the activity site (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large CC chain family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE000511; AAD14884.1; -; Genomic_DNA. DR PIR; H64604; H64604. DR RefSeq; WP_000633984.1; NC_018939.1. DR AlphaFoldDB; P55982; -. DR SMR; P55982; -. DR DIP; DIP-3151N; -. DR FunCoup; P55982; 77. DR IntAct; P55982; 6. DR STRING; 85962.HP_0680; -. DR PaxDb; 85962-HP_0680; -. DR EnsemblBacteria; AAD14884; AAD14884; HP_0680. DR KEGG; heo:C694_03505; -. DR KEGG; hpy:HP_0680; -. DR PATRIC; fig|85962.47.peg.728; -. DR eggNOG; COG0209; Bacteria. DR InParanoid; P55982; -. DR OMA; AACAWNP; -. DR OrthoDB; 9762933at2; -. DR PhylomeDB; P55982; -. DR Proteomes; UP000000429; Chromosome. DR GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IBA:GO_Central. DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IBA:GO_Central. DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IBA:GO_Central. 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 NCBIfam; NF006279; PRK08447.1; 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; ATP-binding; Deoxyribonucleotide synthesis; KW Disulfide bond; Nucleotide-binding; Oxidoreductase; Reference proteome. FT CHAIN 1..788 FT /note="Ribonucleoside-diphosphate reductase subunit alpha" FT /id="PRO_0000187215" FT DOMAIN 2..92 FT /note="ATP-cone" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00492" FT ACT_SITE 424 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 426 FT /note="Cysteine radical intermediate" FT /evidence="ECO:0000250" FT ACT_SITE 428 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 6 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250|UniProtKB:P00452" FT BINDING 12..18 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250|UniProtKB:P00452" FT BINDING 52 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250|UniProtKB:P00452" FT BINDING 200 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:P00452" FT BINDING 223..225 FT /ligand="dTTP" FT /ligand_id="ChEBI:CHEBI:37568" FT /ligand_note="allosteric effector that controls substrate FT specificity" FT /evidence="ECO:0000250|UniProtKB:P00452" FT BINDING 253 FT /ligand="dTTP" FT /ligand_id="ChEBI:CHEBI:37568" FT /ligand_note="allosteric effector that controls substrate FT specificity" FT /evidence="ECO:0000250|UniProtKB:P00452" FT BINDING 424 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:P00452" FT BINDING 428 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:P00452" FT BINDING 661..663 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:P00452" FT SITE 216 FT /note="Important for hydrogen atom transfer" FT /evidence="ECO:0000250" FT SITE 497 FT /note="Important for hydrogen atom transfer" FT /evidence="ECO:0000250" FT SITE 763 FT /note="Important for electron transfer" FT /evidence="ECO:0000250" FT SITE 764 FT /note="Important for electron transfer" FT /evidence="ECO:0000250" FT SITE 784 FT /note="Interacts with thioredoxin/glutaredoxin" FT /evidence="ECO:0000250" FT SITE 787 FT /note="Interacts with thioredoxin/glutaredoxin" FT /evidence="ECO:0000250" FT DISULFID 216..497 FT /note="Redox-active" FT /evidence="ECO:0000250" SQ SEQUENCE 788 AA; 90160 MW; BF22559D3D3796D4 CRC64; MITVVKRNGR IEPLDITKIQ KYTKDATDNL EGVSQSELEV DARLQFRDKI TTEEIQQTLI KTAVDKIDID TPNWSFVASR LFLYDLYHKV SGFTGYRHLK EYFENAEEKG RILKGFKEKF DLEFLNSQIK PERDFQFNYL GIKTLYDRYL LKDANNNPIE LPQHMFMSIA MFLAQNEQEP NKIALEFYEV LSKFEAMCAT PTLANARTTK HQLSSCYIGS TPDNIEGIFD SYKEMALLSK YGGGIGWDFS LVRSIGSYID GHKNASAGTI PFLKIANDVA IAVDQLGTRK GAIAVYLEIW HIDVMEFIDL RKNSGDERRR AHDLFPALWV CDLFLKRVLE DAMWTLFDPY ECKDLTELYG QDFEKRYLEY EKDPKIIKEY INAKDLWKKI LMNYFEAGLP FLAFKDNANR CNPNAHAGII RSSNLCTEIF QNTAPNHYYM QIEYTDGTIE FFEEKELVTT DSNITKCANK LTSTDILKGK PIYIATKVAK DGQTAVCNLA SINLSKINTE EDIKRVVPIM VRLLDNVIDL NFYPNRKVKA TNLQNRAIGL GVMGEAQMLA EHQIAWGSKE HLEKIDALME QISYHAIDTS ANLAKEKGVY KDFENSEWSK GIFPIDKANN EALKLTEKGL FNHACDWQGL REKVKANGMR NGYLMAIAPT SSISILVGTT QTIEPIYKKK WFEENLSGLI PVVVPNLNVE TWNFYTSAYD IDAKDLIKAA AVRQKWIDQG QSLNVFLRIE NASGKTLHDI YTLAWKLGLK STYYLRSESP SIDEKSVLDR SVECFNCQ //