NRDG_HAEIN
ID NRDG_HAEIN Reviewed; 155 AA.
AC P45080;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 120.
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=HI_1155;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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}.
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DR EMBL; L42023; AAC22810.1; -; Genomic_DNA.
DR PIR; E64168; E64168.
DR RefSeq; NP_439313.1; NC_000907.1.
DR RefSeq; WP_005693470.1; NC_000907.1.
DR AlphaFoldDB; P45080; -.
DR SMR; P45080; -.
DR STRING; 71421.HI_1155; -.
DR EnsemblBacteria; AAC22810; AAC22810; HI_1155.
DR KEGG; hin:HI_1155; -.
DR PATRIC; fig|71421.8.peg.1206; -.
DR eggNOG; COG0602; Bacteria.
DR HOGENOM; CLU_089926_2_1_6; -.
DR OMA; EVNGPGC; -.
DR PhylomeDB; P45080; -.
DR BioCyc; HINF71421:G1GJ1-1188-MON; -.
DR Proteomes; UP000000579; 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 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 3: Inferred from homology;
KW 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..155
FT /note="Anaerobic ribonucleoside-triphosphate reductase-
FT activating protein"
FT /id="PRO_0000200537"
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"
SQ SEQUENCE 155 AA; 17856 MW; 4CB5A1D44260C7EC CRC64;
MNYLQYYPTD VINGEGTRCT LFVSGCTHAC KGCYNQKSWS FSAGVLFDDV MEQQIINDLK
DTRIKRQGLT LSGGDPLHPL NVETLLPFVQ RVKRECPDKD IWVWTGYKLD ELDKQQRAML
PYIDVLIDGK FIQEQADPSL VWRGSANQII HRFKL
