ID RIR1_BACSU Reviewed; 700 AA. AC P50620; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 144. DE RecName: Full=Ribonucleoside-diphosphate reductase subunit alpha; DE EC=1.17.4.1; DE AltName: Full=Ribonucleotide reductase large subunit; GN Name=nrdE {ECO:0000303|PubMed:8969495}; Synonyms=nrdA; GN OrderedLocusNames=BSU17380; OS Bacillus subtilis (strain 168). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=224308; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], OPERON, DISRUPTION PHENOTYPE, AND RP MUTAGENESIS OF HIS-255. RC STRAIN=168; RX PubMed=8969495; DOI=10.1099/13500872-142-11-2995; RA Scotti C., Valbuzzi A., Perego M., Galizzi A., Albertini A.M.; RT "The Bacillus subtilis genes for ribonucleotide reductase are similar to RT the genes for the second class I NrdE/NrdF enzymes of Enterobacteriaceae."; RL Microbiology 142:2995-3004(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(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=[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 -!- INDUCTION: Part of the probable nrdI(ymaA)-nrdE-nrdF-ymaB operon. CC Expression is constitutive but low, dramatically induced by thymidine CC starvation which requires recA. {ECO:0000269|PubMed:8969495}. CC -!- DISRUPTION PHENOTYPE: Essential, at least the last 3 genes of the locus CC cannot be deleted; could be due to polar effects on downstream ymaB. CC {ECO:0000269|PubMed:8969495}. 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; Z68500; CAA92810.1; -; Genomic_DNA. DR EMBL; AL009126; CAB13622.1; -; Genomic_DNA. DR PIR; B69667; B69667. DR RefSeq; NP_389620.1; NC_000964.3. DR RefSeq; WP_003245700.1; NZ_JNCM01000035.1. DR PDB; 6CGL; X-ray; 3.20 A; A/B=1-700. DR PDB; 6CGM; X-ray; 2.00 A; A=1-700. DR PDB; 6CGN; X-ray; 2.26 A; A=1-700. DR PDB; 6MT9; X-ray; 2.50 A; A=1-700. DR PDB; 6MV9; X-ray; 2.95 A; A/B=1-700. DR PDB; 6MVE; X-ray; 2.55 A; A=1-700. DR PDB; 6MW3; EM; 4.65 A; C/D=1-700. DR PDB; 6MYX; EM; 6.00 A; C/D/I/J=1-700. DR PDBsum; 6CGL; -. DR PDBsum; 6CGM; -. DR PDBsum; 6CGN; -. DR PDBsum; 6MT9; -. DR PDBsum; 6MV9; -. DR PDBsum; 6MVE; -. DR PDBsum; 6MW3; -. DR PDBsum; 6MYX; -. DR AlphaFoldDB; P50620; -. DR EMDB; EMD-9272; -. DR EMDB; EMD-9293; -. DR SMR; P50620; -. DR STRING; 224308.BSU17380; -. DR jPOST; P50620; -. DR PaxDb; 224308-BSU17380; -. DR EnsemblBacteria; CAB13622; CAB13622; BSU_17380. DR GeneID; 940091; -. DR KEGG; bsu:BSU17380; -. DR PATRIC; fig|224308.179.peg.1884; -. DR eggNOG; COG0209; Bacteria. DR InParanoid; P50620; -. DR OrthoDB; 9762933at2; -. DR PhylomeDB; P50620; -. DR BioCyc; BSUB:BSU17380-MONOMER; -. DR Proteomes; UP000001570; 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; IMP:CACAO. 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; 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 1: Evidence at protein level; KW 3D-structure; Allosteric enzyme; ATP-binding; KW Deoxyribonucleotide synthesis; Disulfide bond; Nucleotide-binding; KW Oxidoreductase; Reference proteome. FT CHAIN 1..700 FT /note="Ribonucleoside-diphosphate reductase subunit alpha" FT /id="PRO_0000187209" FT ACT_SITE 380 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 382 FT /note="Cysteine radical intermediate" FT /evidence="ECO:0000250" FT ACT_SITE 384 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 153 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 169..170 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 198 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 380..384 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 580..584 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 170 FT /note="Important for hydrogen atom transfer" FT /evidence="ECO:0000250" FT SITE 177 FT /note="Allosteric effector binding" FT /evidence="ECO:0000250" FT SITE 207 FT /note="Allosteric effector binding" FT /evidence="ECO:0000250" FT SITE 409 FT /note="Important for hydrogen atom transfer" FT /evidence="ECO:0000250" FT SITE 683 FT /note="Important for electron transfer" FT /evidence="ECO:0000250" FT SITE 684 FT /note="Important for electron transfer" FT /evidence="ECO:0000250" FT SITE 695 FT /note="Interacts with thioredoxin/glutaredoxin" FT /evidence="ECO:0000250" FT SITE 698 FT /note="Interacts with thioredoxin/glutaredoxin" FT /evidence="ECO:0000250" FT DISULFID 170..409 FT /note="Redox-active" FT /evidence="ECO:0000250" FT MUTAGEN 255 FT /note="H->Y: In ts-A 73; temperature-sensitive lethal FT mutation." FT /evidence="ECO:0000269|PubMed:8969495" FT HELIX 8..14 FT /evidence="ECO:0007829|PDB:6CGM" FT HELIX 15..17 FT /evidence="ECO:0007829|PDB:6CGM" FT STRAND 20..23 FT /evidence="ECO:0007829|PDB:6MT9" FT HELIX 28..39 FT /evidence="ECO:0007829|PDB:6CGM" FT TURN 40..44 FT /evidence="ECO:0007829|PDB:6CGM" FT HELIX 51..60 FT /evidence="ECO:0007829|PDB:6CGM" FT HELIX 67..70 FT /evidence="ECO:0007829|PDB:6CGM" FT HELIX 74..86 FT /evidence="ECO:0007829|PDB:6CGM" FT HELIX 94..103 FT /evidence="ECO:0007829|PDB:6CGM" FT STRAND 111..114 FT /evidence="ECO:0007829|PDB:6CGN" FT HELIX 118..130 FT /evidence="ECO:0007829|PDB:6CGM" FT HELIX 134..145 FT /evidence="ECO:0007829|PDB:6CGM" FT STRAND 148..151 FT /evidence="ECO:0007829|PDB:6CGM" FT HELIX 153..158 FT /evidence="ECO:0007829|PDB:6CGM" FT STRAND 161..163 FT /evidence="ECO:0007829|PDB:6CGN" FT STRAND 170..174 FT /evidence="ECO:0007829|PDB:6CGM" FT HELIX 179..193 FT /evidence="ECO:0007829|PDB:6CGM" FT TURN 194..196 FT /evidence="ECO:0007829|PDB:6MV9" FT STRAND 198..202 FT /evidence="ECO:0007829|PDB:6CGM" FT STRAND 214..218 FT /evidence="ECO:0007829|PDB:6CGN" FT HELIX 219..222 FT /evidence="ECO:0007829|PDB:6CGN" FT HELIX 223..233 FT /evidence="ECO:0007829|PDB:6CGM" FT TURN 239..241 FT /evidence="ECO:0007829|PDB:6MV9" FT STRAND 246..252 FT /evidence="ECO:0007829|PDB:6CGM" FT HELIX 258..263 FT /evidence="ECO:0007829|PDB:6CGM" FT TURN 271..273 FT /evidence="ECO:0007829|PDB:6CGN" FT STRAND 279..284 FT /evidence="ECO:0007829|PDB:6CGM" FT HELIX 286..293 FT /evidence="ECO:0007829|PDB:6CGM" FT STRAND 298..301 FT /evidence="ECO:0007829|PDB:6CGM" FT HELIX 303..310 FT /evidence="ECO:0007829|PDB:6CGM" FT HELIX 314..316 FT /evidence="ECO:0007829|PDB:6CGM" FT HELIX 319..328 FT /evidence="ECO:0007829|PDB:6CGM" FT STRAND 334..337 FT /evidence="ECO:0007829|PDB:6CGM" FT HELIX 339..353 FT /evidence="ECO:0007829|PDB:6CGM" FT STRAND 357..360 FT /evidence="ECO:0007829|PDB:6CGM" FT HELIX 361..365 FT /evidence="ECO:0007829|PDB:6CGM" FT TURN 369..373 FT /evidence="ECO:0007829|PDB:6CGM" FT STRAND 397..399 FT /evidence="ECO:0007829|PDB:6MV9" FT STRAND 407..415 FT /evidence="ECO:0007829|PDB:6CGM" FT HELIX 416..422 FT /evidence="ECO:0007829|PDB:6CGM" FT HELIX 425..442 FT /evidence="ECO:0007829|PDB:6CGM" FT HELIX 449..458 FT /evidence="ECO:0007829|PDB:6CGM" FT STRAND 461..466 FT /evidence="ECO:0007829|PDB:6CGM" FT HELIX 468..474 FT /evidence="ECO:0007829|PDB:6CGM" FT HELIX 482..510 FT /evidence="ECO:0007829|PDB:6CGM" FT HELIX 517..519 FT /evidence="ECO:0007829|PDB:6CGM" FT HELIX 521..524 FT /evidence="ECO:0007829|PDB:6CGM" FT HELIX 526..528 FT /evidence="ECO:0007829|PDB:6CGM" FT HELIX 529..533 FT /evidence="ECO:0007829|PDB:6CGM" FT HELIX 541..546 FT /evidence="ECO:0007829|PDB:6CGM" FT TURN 547..549 FT /evidence="ECO:0007829|PDB:6CGM" FT HELIX 555..568 FT /evidence="ECO:0007829|PDB:6CGM" FT HELIX 584..587 FT /evidence="ECO:0007829|PDB:6CGM" FT STRAND 600..606 FT /evidence="ECO:0007829|PDB:6CGM" FT STRAND 609..614 FT /evidence="ECO:0007829|PDB:6CGM" FT HELIX 620..625 FT /evidence="ECO:0007829|PDB:6CGM" FT HELIX 629..631 FT /evidence="ECO:0007829|PDB:6CGM" FT HELIX 634..645 FT /evidence="ECO:0007829|PDB:6CGM" FT STRAND 656..658 FT /evidence="ECO:0007829|PDB:6CGM" FT HELIX 664..676 FT /evidence="ECO:0007829|PDB:6CGM" FT STRAND 681..684 FT /evidence="ECO:0007829|PDB:6MT9" FT STRAND 685..687 FT /evidence="ECO:0007829|PDB:6CGM" FT HELIX 696..698 FT /evidence="ECO:0007829|PDB:6MT9" SQ SEQUENCE 700 AA; 80689 MW; D2D4B914B97BBFA6 CRC64; MSQNQVPKWI QLNNEIMIQK DGKFQFDKDK EAVHSYFVDY INQNTVFFHN LKEKLDYLVE NQYYEEEFLS LYSFEDIKEV FKTAYAKKFR FPSFMSAFKF YNDYALKTND KKKILERYED RISIVALFFA NGDTEKAKEY VNLMINQEYQ PSTPTFLNAG RKRRGELVSC FLLEVNDSLN DISRAIDISM QLSKLGGGVS LNLSKLRAKG EAIKDVENAT KGVVGVMKLL DNAFRYADQM GQRQGSGAAY LNIFHRDIND FLDTKKISAD EDVRVKTLSI GVVIPDKFVE LAREDKAAYV FYPHTIYKEY GQHMDEMDMN EMYDKFVDNP RVKKEKINPR KLLEKLAMLR SESGYPYIMF QDNVNKVHAN NHISKVKFSN LCSEVLQASQ VSSYTDYDEE DEIGLDISCN LGSLNILNVM EHKSIEKTVK LATDSLTHVS ETTDIRNAPA VRRANKAMKS IGLGAMNLHG YLAQNGIAYE SPEARDFANT FFMMVNFYSI QRSAEIAKEK GETFDQYEGS TYATGEYFDK YVSTDFSPKY EKIANLFEGM HIPTTEDWKK LKAFVAEHGM YHSYRLCIAP TGSISYVQSS TASVMPIMER IEERTYGNSK TYYPMPGLAS NNWFFYKEAY DMDMFKVVDM IATIQQHIDQ GISFTLFLKD TMTTRDLNRI DLYAHHRGIK TIYYARTKDT GQDSCLSCVV //