NRDG_SALTY
ID NRDG_SALTY Reviewed; 154 AA.
AC Q9L645;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Anaerobic ribonucleoside-triphosphate reductase-activating protein {ECO:0000250|UniProtKB:P0A9N8};
DE EC=1.97.1.- {ECO:0000250|UniProtKB:P0A9N8};
DE AltName: Full=Class III anaerobic ribonucleotide reductase small component {ECO:0000250|UniProtKB:P0A9N8};
GN Name=nrdG; OrderedLocusNames=STM4451;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Ng W., Wong K., Kwan H.;
RT "Genetic regulation and mutant characterization of anaerobic ribonucleotide
RT reductase in Salmonella typhimurium.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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:0000250|UniProtKB:P0A9N8}.
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:0000250|UniProtKB:P0A9N8};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P0A9N8};
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: Forms a tetramer composed of two NrdD and two NrdG subunits.
CC {ECO:0000250|UniProtKB:P0A9N8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A9N8}.
CC -!- SIMILARITY: Belongs to the organic radical-activating enzymes family.
CC {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; AF242390; AAF60352.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL23271.1; -; Genomic_DNA.
DR RefSeq; NP_463312.1; NC_003197.2.
DR RefSeq; WP_001268859.1; NC_003197.2.
DR AlphaFoldDB; Q9L645; -.
DR SMR; Q9L645; -.
DR STRING; 99287.STM4451; -.
DR PaxDb; Q9L645; -.
DR DNASU; 1255977; -.
DR EnsemblBacteria; AAL23271; AAL23271; STM4451.
DR GeneID; 1255977; -.
DR KEGG; stm:STM4451; -.
DR PATRIC; fig|99287.12.peg.4681; -.
DR HOGENOM; CLU_089926_2_1_6; -.
DR OMA; NQVIHYL; -.
DR PhylomeDB; Q9L645; -.
DR BioCyc; SENT99287:STM4451-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0043365; F:[formate-C-acetyltransferase]-activating enzyme activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 PANTHER; PTHR30352; PTHR30352; 1.
DR PANTHER; PTHR30352:SF2; PTHR30352:SF2; 1.
DR PIRSF; PIRSF000368; NrdG; 1.
DR SFLD; SFLDF00299; anaerobic_ribonucleoside-triph; 1.
DR TIGRFAMs; TIGR02491; NrdG; 1.
DR PROSITE; PS01087; RADICAL_ACTIVATING; 1.
PE 3: Inferred from homology;
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_0000200540"
FT BINDING 26
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT BINDING 30
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:P0A9N4"
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:0000250|UniProtKB:P0A9N4"
FT BINDING 74
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT CONFLICT 111
FT /note="E -> K (in Ref. 1; AAF60352)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="D -> N (in Ref. 1; AAF60352)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 154 AA; 17434 MW; 10EC587571006593 CRC64;
MRYHQYYPVD IVNGPGTRCT LFVSGCVHEC PGCYNKSTWR LNSGQPFTKE MEDKIIADLN
DTRIHRQGIS LSGGDPLHPQ NVPDILALVQ RIHAECPGKD IWVWTGYKLD ELNAAQMQVV
DLINVLVDGK FVQDLKDPAL IWRGSSNQVV HHLR
