ID RIR1_SYNY3 Reviewed; 767 AA. AC P74240; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 27-MAR-2024, entry version 148. DE RecName: Full=Ribonucleoside-diphosphate reductase subunit alpha; DE EC=1.17.4.1; DE AltName: Full=Ribonucleotide reductase; GN Name=nrdA; OrderedLocusNames=slr1164; OS Synechocystis sp. (strain PCC 6803 / Kazusa). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae; OC Synechocystis. OX NCBI_TaxID=1111708; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 6803 / Kazusa; RX PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire RT genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). 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=[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 -!- ACTIVITY REGULATION: Under complex allosteric control mediated by CC deoxynucleoside triphosphates and ATP binding. The type of nucleotide CC bound 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 (By similarity). {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; BA000022; BAA18334.1; -; Genomic_DNA. DR PIR; S75875; S75875. DR AlphaFoldDB; P74240; -. DR SMR; P74240; -. DR IntAct; P74240; 3. DR STRING; 1148.gene:10499210; -. DR PaxDb; 1148-1653420; -. DR EnsemblBacteria; BAA18334; BAA18334; BAA18334. DR KEGG; syn:slr1164; -. DR eggNOG; COG0209; Bacteria. DR InParanoid; P74240; -. DR PhylomeDB; P74240; -. DR Proteomes; UP000001425; 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 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; 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..767 FT /note="Ribonucleoside-diphosphate reductase subunit alpha" FT /id="PRO_0000187222" FT DOMAIN 31..120 FT /note="ATP-cone" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00492" FT REGION 1..30 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..29 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 460 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 462 FT /note="Cysteine radical intermediate" FT /evidence="ECO:0000250" FT ACT_SITE 464 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 228 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 243..244 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 272 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 460..464 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 631..635 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 244 FT /note="Important for hydrogen atom transfer" FT /evidence="ECO:0000250" FT SITE 251 FT /note="Allosteric effector binding" FT /evidence="ECO:0000250" FT SITE 281 FT /note="Allosteric effector binding" FT /evidence="ECO:0000250" FT SITE 478 FT /note="Important for hydrogen atom transfer" FT /evidence="ECO:0000250" FT SITE 745 FT /note="Important for electron transfer" FT /evidence="ECO:0000250" FT SITE 746 FT /note="Important for electron transfer" FT /evidence="ECO:0000250" FT SITE 762 FT /note="Interacts with thioredoxin/glutaredoxin" FT /evidence="ECO:0000250" FT SITE 765 FT /note="Interacts with thioredoxin/glutaredoxin" FT /evidence="ECO:0000250" FT DISULFID 244..478 FT /note="Redox-active" FT /evidence="ECO:0000250" SQ SEQUENCE 767 AA; 85637 MW; 147151C406A082C5 CRC64; MHPTLISAPI SSSANDAHAG TSQGSHQGHR IQVIRRDGSS TPLNIGKIRA VVDWACLGLE VNSIALEAGL TTRLREGIST REIQDNLISC ALEMCSPNEP DWRYVAGRLH VWSLWKDTLV RRGYQYGQYL RTVQTKVTNG EYDSRILTYS EGELQEAGCW INSDWDTDYD YAGAVLLTSR YLLPNELPQE ALLTCALLLA SVEAPDRRLQ WARRFYESIA ARRISLATPI LANLRVPGGS LTSCFIVAME DNLESIFGEI TNAARISKNG GGVGVNVSRI RATGSWVMGK PNASGGVIPW TKLLNDTAIA VNQGGRRAGA VTVGLDVWHL DVPEFLEMQA ENGDQRRKAY DIFPQLILPD EFMRRVINKE DWTLVDPYEV REKMGIELAE LWGEQFEGAY REIESNLDTT ITLYKRINAR ELFKQIMRTQ VETGMPYLSF KDTINKANPN KHLGYIPGTN LCCESFSNVT PGQDAHCCNL VSLNLANLDL QDIAGVSQIA VRMLDNTIEL TAPPFADAKS HNNKYRTIGV GAMGLADWLA KRRLNYDELA DINRLFEEIG YWCTQSSMEL AKERGAYPAF PGSDWQKGLL IGSKPVSWFQ ANAAKPERWE KLSNDIQTHG IRNSHITAIA PNTSSSLVQG CTASILPVYS RFFYDKWAKG TVPIAPPFIG NCFWFYPENK TMDQRKVVKA VAAIQQWTDT GISMELLFNL NAGIYFPEEP ERSLNAKDIF DTLVMAWEAG CKAIYYIRTV QKDDFKDSSD GCVACAN //