ID A2SKS8_METPP Unreviewed; 971 AA. AC A2SKS8; DT 06-MAR-2007, integrated into UniProtKB/TrEMBL. DT 06-MAR-2007, sequence version 1. DT 02-JUN-2021, entry version 91. 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 OrderedLocusNames=Mpe_A3214 {ECO:0000313|EMBL:ABM96167.1}; OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Methylibium. OX NCBI_TaxID=420662 {ECO:0000313|EMBL:ABM96167.1, ECO:0000313|Proteomes:UP000000366}; RN [1] {ECO:0000313|EMBL:ABM96167.1, ECO:0000313|Proteomes:UP000000366} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1 RC {ECO:0000313|Proteomes:UP000000366}; RX PubMed=17158667; DOI=10.1128/JB.01259-06; RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W., RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M., RA Hristova K.R.; RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta- RT proteobacterium Methylibium petroleiphilum PM1."; RL J. Bacteriol. 189:1931-1945(2007). 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 -!- PATHWAY: Genetic information processing; DNA replication. CC {ECO:0000256|ARBA:ARBA00005160, 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}. 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; CP000555; ABM96167.1; -; Genomic_DNA. DR RefSeq; WP_011830790.1; NC_008825.1. DR STRING; 420662.Mpe_A3214; -. DR EnsemblBacteria; ABM96167; ABM96167; Mpe_A3214. DR KEGG; mpt:Mpe_A3214; -. DR eggNOG; COG0209; Bacteria. DR HOGENOM; CLU_000404_3_0_4; -. DR OMA; TYKLAWL; -. DR OrthoDB; 357568at2; -. DR UniPathway; UPA00326; -. DR Proteomes; UP000000366; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway. DR InterPro; IPR005144; ATP-cone_dom. DR InterPro; IPR013346; NrdE_NrdA. DR InterPro; IPR000788; RNR_lg_C. DR InterPro; IPR013509; RNR_lsu_N. DR InterPro; IPR008926; RNR_R1-su_N. DR InterPro; IPR039718; Rrm1. DR PANTHER; PTHR11573; PTHR11573; 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; SSF48168; SSF48168; 1. DR TIGRFAMs; TIGR02506; NrdE_NrdA; 1. DR PROSITE; PS51161; ATP_CONE; 2. DR PROSITE; PS00089; RIBORED_LARGE; 1. PE 3: Inferred from homology; KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU00492}; Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW DNA replication {ECO:0000256|ARBA:ARBA00022705, KW ECO:0000256|RuleBase:RU003410}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU00492}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU003410}; KW Reference proteome {ECO:0000313|Proteomes:UP000000366}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..19 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 20..971 FT /note="Ribonucleoside-diphosphate reductase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5002646475" FT DOMAIN 36..136 FT /note="ATP-cone" FT /evidence="ECO:0000259|PROSITE:PS51161" FT DOMAIN 150..239 FT /note="ATP-cone" FT /evidence="ECO:0000259|PROSITE:PS51161" SQ SEQUENCE 971 AA; 107322 MW; 2922953B61A02799 CRC64; MQSISSSVPA AALAGGALAA TAVSRAAPGS SAYAGYQIIR RNGAVVAFEP NKIAVALMKA FLAVHGTQGA ASASVREMVD GLTESVVRAL LRSRPGGGTF HIEDVQDAVE LGLMRGGHHE IARAYVLYRE RRAQERAKQG AAPVTPAVAL HVIDRGQRVP LDTGRLQALV ESACANLGSE VQAAPILAET QRNLYDGVPI DEVYKAAILA ARTLIEKDPA YTRATARLLL HTIRREILGG EVLHEEMQQR YADYFPGFIK QGVEAELLDE RLMQYDLRRL GEALKADRDL QFDYLGLQTL YDRYFLHVRK ARIELPQAFF MRVAMGLALN EVDREARAIE FYEVLSSFDF MSSTPTLFNS GTRRSQLSSC YLTTVADDLD GIYEAIKENA LLSKFAGGLG NDWTPVRALG SHIKGTNGES QGVVPFLKVV NDTAVAVNQG GKRKGAVCAY LETWHLDIEE FLELRKNTGD DRRRTHDMNT ANWIPDLFMR RVIEGGDWTL FSPSTCPDLH DKFGIAFEQA YTAYEQKADR GELKLYKRVP AKDLWRKMLS MLFETGHPWI TFKDACNVRS PQQHVGVVHS SNLCTEITLN TNGSEIAVCN LGSVNLAQHL MHGAEGLEID HAKLRKTVST AMRMLDNVID INYYAVKKAR DSNLRHRPVG LGVMGFQDSL YQLRIAYASQ QAVEYADRSM EAVCYHAYWA STELAEERGR YSSYKGSLWD RGILPIDSLD LLAEQRGGYV DVDRSTSLDW DALRARIQQH GMRNSNCVAI APTATISNII GVDASIEPSF SNLSVKSNLS GEFTVINEYL VRDLKKLGLW DDVMVMDLKH FDGSLRRIDR VPEELKSLYA TAFEVEPTWL VEAAARRQKW IDQAQSLNIY MAGASGKKLD DTYKLAWQRG LKTTYYLRTV GATHAEKSTV KAGHLNAVSS GSGGVDAVAA AAQAQFDAAS SVPATDMKFC AIDDPTCEAC Q //