ID   A2SKS8_METPP            Unreviewed;       971 AA.
AC   A2SKS8;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   24-JAN-2024, entry version 98.
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; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; 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}.
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DR   EMBL; CP000555; ABM96167.1; -; Genomic_DNA.
DR   RefSeq; WP_011830790.1; NC_008825.1.
DR   AlphaFoldDB; A2SKS8; -.
DR   STRING; 420662.Mpe_A3214; -.
DR   KEGG; mpt:Mpe_A3214; -.
DR   eggNOG; COG0209; Bacteria.
DR   HOGENOM; CLU_000404_3_0_4; -.
DR   OMA; RGSIQNI; -.
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:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
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; 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};
KW   Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
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
//