NRDD_SALTY
ID NRDD_SALTY Reviewed; 712 AA.
AC Q9L646;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Anaerobic ribonucleoside-triphosphate reductase {ECO:0000250|UniProtKB:P28903};
DE EC=1.1.98.6 {ECO:0000250|UniProtKB:P28903};
DE AltName: Full=Class III ribonucleoside-triphosphate reductase {ECO:0000250|UniProtKB:P28903};
GN Name=nrdD; OrderedLocusNames=STM4452;
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: Catalyzes the conversion of ribonucleotides into
CC deoxyribonucleotides, which are required for DNA synthesis and repair.
CC {ECO:0000250|UniProtKB:P28903}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + formate + H(+) = a 2'-
CC deoxyribonucleoside 5'-triphosphate + CO2 + H2O;
CC Xref=Rhea:RHEA:51476, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:16526, ChEBI:CHEBI:61557,
CC ChEBI:CHEBI:61560; EC=1.1.98.6;
CC Evidence={ECO:0000250|UniProtKB:P28903};
CC -!- ACTIVITY REGULATION: Activated under anaerobic conditions by NrdG, a
CC tightly associated activase. Activation involves the formation of a
CC glycyl radical at Gly-681. {ECO:0000250|UniProtKB:P28903}.
CC -!- SUBUNIT: Forms a tetramer composed of two NrdD and two NrdG subunits.
CC {ECO:0000250|UniProtKB:P28903}.
CC -!- SIMILARITY: Belongs to the anaerobic ribonucleoside-triphosphate
CC reductase family. {ECO:0000305}.
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DR EMBL; AF242390; AAF60351.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL23272.1; -; Genomic_DNA.
DR RefSeq; NP_463313.1; NC_003197.2.
DR RefSeq; WP_000187818.1; NC_003197.2.
DR AlphaFoldDB; Q9L646; -.
DR SMR; Q9L646; -.
DR STRING; 99287.STM4452; -.
DR PaxDb; Q9L646; -.
DR PRIDE; Q9L646; -.
DR EnsemblBacteria; AAL23272; AAL23272; STM4452.
DR GeneID; 1255978; -.
DR KEGG; stm:STM4452; -.
DR PATRIC; fig|99287.12.peg.4682; -.
DR HOGENOM; CLU_002707_2_0_6; -.
DR OMA; YSYDRVP; -.
DR PhylomeDB; Q9L646; -.
DR BioCyc; SENT99287:STM4452-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0031250; C:anaerobic ribonucleoside-triphosphate reductase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008998; F:ribonucleoside-triphosphate reductase activity; IBA:GO_Central.
DR GO; GO:0009265; P:2'-deoxyribonucleotide biosynthetic process; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd01675; RNR_III; 1.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR019777; Form_AcTrfase_GR_CS.
DR InterPro; IPR001150; Gly_radical.
DR InterPro; IPR012833; NrdD.
DR Pfam; PF03477; ATP-cone; 1.
DR Pfam; PF13597; NRDD; 1.
DR TIGRFAMs; TIGR02487; NrdD; 1.
DR PROSITE; PS51161; ATP_CONE; 1.
DR PROSITE; PS00850; GLY_RADICAL_1; 1.
DR PROSITE; PS51149; GLY_RADICAL_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Metal-binding; Nucleotide-binding; Organic radical;
KW Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..712
FT /note="Anaerobic ribonucleoside-triphosphate reductase"
FT /id="PRO_0000166685"
FT DOMAIN 3..92
FT /note="ATP-cone"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00492"
FT DOMAIN 583..708
FT /note="Glycine radical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00493"
FT BINDING 644
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P07071"
FT BINDING 647
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P07071"
FT BINDING 662
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P07071"
FT BINDING 665
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P07071"
FT MOD_RES 681
FT /note="Glycine radical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 712 AA; 79959 MW; 1D907CF6B758D7E4 CRC64;
MTPHVMKRDG CKVPFKSERI KEAILRAAKA AGVDDADYCA TVAEVVSSQM NARSQVDINE
IQTAVENQLM SGPYKQLARA YIEYRHDRDI QREKRGRLNQ EIRGLVEQTN SALLNENANK
DSKVIPTQRD LLAGIVAKHY ARQHLLPRDV VQAHERGDIH YHDLDYSPFF PMFNCMLIDL
KGMLTQGFKM GNAEIEPPKS ISTATAVTAQ IIAQVASHIY GGTTINRIDE VLAPFVTESY
NKHRKTADEW QIPDAEGYAR SRTEKECYDA FQSLEYEVNT LHTANGQTPF VTFGFGLGTS
WESRLIQASI LRNRIAGLGK NRKTAVFPKL VFAIRDGLNH KFGDPNYDIK QLALECASKR
MYPDILNYDQ VVKVTGSFKT PMGCRSFLGV WENENGEQIH DGRNNLGVIS LNLPRIALEA
KGDETAFWKL LDERLALARK ALMTRIARLE GVKARVAPIL YMEGACGVRL KADDDVSEIF
KNGRASISLG YIGIHETINA LFGGEHLYDS EQLRAKGIAI VERLRQAVDQ WKDETGYGFS
LYSTPSENLC DRFCRLDTAE FGVVPGVTDK GYYTNSFHLD VEKKVNPYDK IDFEAPYPPL
ANGGFICYGE YPNIQHNLKA LEDVWDYSYQ HVPYYGTNTP IDECYECGFT GEFECTSKGF
TCPKCGNHDA ARVSVTRRVC GYLGSPDARP FNAGKQEEVK RRVKHLGNGQ IG
