NRDG_ECOLI
ID NRDG_ECOLI Reviewed; 154 AA.
AC P0A9N8; P39329; Q2M670;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Anaerobic ribonucleoside-triphosphate reductase-activating protein {ECO:0000305};
DE EC=1.97.1.- {ECO:0000269|PubMed:9305874};
DE AltName: Full=Class III anaerobic ribonucleotide reductase small component {ECO:0000305};
GN Name=nrdG; Synonyms=yjgE; OrderedLocusNames=b4237, JW4196;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, IRON-SULFUR CLUSTER, AND
RP SUBUNIT.
RC STRAIN=K12;
RX PubMed=7852304; DOI=10.1074/jbc.270.6.2443;
RA Sun X., Eliasson R., Pontis E., Andersson J., Buist G., Sjoeberg B.-M.,
RA Reichard P.;
RT "Generation of the glycyl radical of the anaerobic Escherichia coli
RT ribonucleotide reductase requires a specific activating enzyme.";
RL J. Biol. Chem. 270:2443-2446(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, AND SUBUNIT.
RX PubMed=1460049; DOI=10.1016/s0021-9258(19)74074-5;
RA Eliasson R., Pontis E., Fontecave M., Gerez C., Harder J., Joernvall H.,
RA Krook M., Reichard P.;
RT "Characterization of components of the anaerobic ribonucleotide reductase
RT system from Escherichia coli.";
RL J. Biol. Chem. 267:25541-25547(1992).
RN [6]
RP SUBUNIT, INTERACTION WITH NRDD, AND IRON-SULFUR CLUSTER.
RX PubMed=8621608; DOI=10.1074/jbc.271.16.9410;
RA Ollagnier S., Mulliez E., Gaillard J., Eliasson R., Fontecave M.,
RA Reichard P.;
RT "The anaerobic Escherichia coli ribonucleotide reductase. Subunit structure
RT and iron sulfur center.";
RL J. Biol. Chem. 271:9410-9416(1996).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND IRON-SULFUR CLUSTER.
RX PubMed=9305874; DOI=10.1074/jbc.272.39.24216;
RA Ollagnier S., Mulliez E., Schmidt P.P., Eliasson R., Gaillard J.,
RA Deronzier C., Bergman T., Graeslund A., Reichard P., Fontecave M.;
RT "Activation of the anaerobic ribonucleotide reductase from Escherichia
RT coli. The essential role of the iron-sulfur center for S-adenosylmethionine
RT reduction.";
RL J. Biol. Chem. 272:24216-24223(1997).
RN [8]
RP IRON-SULFUR LIGANDS, AND MUTAGENESIS OF CYS-19; CYS-26; CYS-30; CYS-33 AND
RP CYS-96.
RX PubMed=10821845; DOI=10.1074/jbc.275.21.15669;
RA Tamarit J., Gerez C., Meier C., Mulliez E., Trautwein A., Fontecave M.;
RT "The activating component of the anaerobic ribonucleotide reductase from
RT Escherichia coli. An iron-sulfur center with only three cysteines.";
RL J. Biol. Chem. 275:15669-15675(2000).
RN [9]
RP INDUCTION BY HYDROXYUREA.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
RA Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
RA Walker G.C.;
RT "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia
RT coli.";
RL Mol. Cell 36:845-860(2009).
CC -!- FUNCTION: Activation of anaerobic ribonucleoside-triphosphate reductase
CC under anaerobic conditions by generation of an organic free radical,
CC using S-adenosylmethionine and reduced flavodoxin as cosubstrates to
CC produce 5'-deoxy-adenosine. {ECO:0000269|PubMed:1460049,
CC ECO:0000269|PubMed:7852304, ECO:0000269|PubMed:9305874}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycyl-[protein] + reduced [flavodoxin] + S-adenosyl-L-
CC methionine = 5'-deoxyadenosine + glycin-2-yl radical-[protein] + H(+)
CC + L-methionine + semiquinone [flavodoxin]; Xref=Rhea:RHEA:61976,
CC Rhea:RHEA-COMP:10622, Rhea:RHEA-COMP:14480, Rhea:RHEA-COMP:15993,
CC Rhea:RHEA-COMP:15994, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319,
CC ChEBI:CHEBI:29947, ChEBI:CHEBI:32722, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:140311;
CC Evidence={ECO:0000269|PubMed:9305874};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:10821845, ECO:0000269|PubMed:7852304,
CC ECO:0000269|PubMed:8621608, ECO:0000269|PubMed:9305874};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000250|UniProtKB:P0A9N4};
CC -!- SUBUNIT: Monomer or homodimer (PubMed:7852304, PubMed:1460049,
CC PubMed:8621608). Forms a tetramer composed of two NrdD and two NrdG
CC subunits (PubMed:8621608). {ECO:0000269|PubMed:1460049,
CC ECO:0000269|PubMed:7852304, ECO:0000269|PubMed:8621608}.
CC -!- INTERACTION:
CC P0A9N8; P28903: nrdD; NbExp=3; IntAct=EBI-1135026, EBI-370011;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: Induced 2-fold by hydroxyurea.
CC {ECO:0000269|PubMed:20005847}.
CC -!- SIMILARITY: Belongs to the organic radical-activating enzymes family.
CC {ECO:0000305}.
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DR EMBL; Z46865; CAA86937.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97134.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77194.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78236.1; -; Genomic_DNA.
DR PIR; A55692; A55692.
DR RefSeq; NP_418658.1; NC_000913.3.
DR RefSeq; WP_001106233.1; NZ_LN832404.1.
DR AlphaFoldDB; P0A9N8; -.
DR SMR; P0A9N8; -.
DR BioGRID; 4259317; 14.
DR BioGRID; 853046; 3.
DR ComplexPortal; CPX-3821; nrdDG class III anaerobic ribonucleotide reductase activation complex.
DR DIP; DIP-48068N; -.
DR IntAct; P0A9N8; 4.
DR STRING; 511145.b4237; -.
DR jPOST; P0A9N8; -.
DR PaxDb; P0A9N8; -.
DR PRIDE; P0A9N8; -.
DR DNASU; 948757; -.
DR EnsemblBacteria; AAC77194; AAC77194; b4237.
DR EnsemblBacteria; BAE78236; BAE78236; BAE78236.
DR GeneID; 67414860; -.
DR GeneID; 948757; -.
DR KEGG; ecj:JW4196; -.
DR KEGG; eco:b4237; -.
DR PATRIC; fig|1411691.4.peg.2465; -.
DR EchoBASE; EB2414; -.
DR eggNOG; COG0602; Bacteria.
DR HOGENOM; CLU_089926_2_1_6; -.
DR InParanoid; P0A9N8; -.
DR OMA; NQVIHYL; -.
DR PhylomeDB; P0A9N8; -.
DR BioCyc; EcoCyc:RNTRACTIV-MON; -.
DR BioCyc; MetaCyc:RNTRACTIV-MON; -.
DR PRO; PR:P0A9N8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0031250; C:anaerobic ribonucleoside-triphosphate reductase complex; IMP:EcoliWiki.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0043365; F:[formate-C-acetyltransferase]-activating enzyme activity; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IDA:EcoliWiki.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009265; P:2'-deoxyribonucleotide biosynthetic process; IC:ComplexPortal.
DR GO; GO:0015949; P:nucleobase-containing small molecule interconversion; IMP:EcoliWiki.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR012837; NrdG.
DR InterPro; IPR034457; Organic_radical-activating.
DR InterPro; IPR001989; Radical_activat_CS.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR30352; PTHR30352; 1.
DR PANTHER; PTHR30352:SF2; PTHR30352:SF2; 1.
DR PIRSF; PIRSF000368; NrdG; 1.
DR SFLD; SFLDF00299; anaerobic_ribonucleoside-triph; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR TIGRFAMs; TIGR02491; NrdG; 1.
DR PROSITE; PS01087; RADICAL_ACTIVATING; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..154
FT /note="Anaerobic ribonucleoside-triphosphate reductase-
FT activating protein"
FT /id="PRO_0000200535"
FT BINDING 26
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000305|PubMed:10821845"
FT BINDING 30
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000305|PubMed:10821845"
FT BINDING 32..34
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT BINDING 33
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000305|PubMed:10821845"
FT BINDING 74
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT MUTAGEN 19
FT /note="C->A: No change in activity. Does not affect iron
FT and sulfide content."
FT /evidence="ECO:0000269|PubMed:10821845"
FT MUTAGEN 26
FT /note="C->A: Loss of activity. Decrease in iron and sulfide
FT content."
FT /evidence="ECO:0000269|PubMed:10821845"
FT MUTAGEN 30
FT /note="C->A: Loss of activity. Decrease in iron and sulfide
FT content."
FT /evidence="ECO:0000269|PubMed:10821845"
FT MUTAGEN 33
FT /note="C->A: Loss of activity. Decrease in iron and sulfide
FT content."
FT /evidence="ECO:0000269|PubMed:10821845"
FT MUTAGEN 96
FT /note="C->A: No change in activity. Does not affect iron
FT and sulfide content."
FT /evidence="ECO:0000269|PubMed:10821845"
SQ SEQUENCE 154 AA; 17446 MW; 3BB3E9FACC782FD5 CRC64;
MNYHQYYPVD IVNGPGTRCT LFVSGCVHEC PGCYNKSTWR VNSGQPFTKA MEDQIINDLN
DTRIKRQGIS LSGGDPLHPQ NVPDILKLVQ RIRAECPGKD IWVWTGYKLD ELNAAQMQVV
DLINVLVDGK FVQDLKDPSL IWRGSSNQVV HHLR
