ID   NRDG_PASMU              Reviewed;         158 AA.
AC   Q9CM94;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=PM0941;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(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}.
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DR   EMBL; AE004439; AAK03025.1; -; Genomic_DNA.
DR   RefSeq; WP_010906934.1; NC_002663.1.
DR   AlphaFoldDB; Q9CM94; -.
DR   SMR; Q9CM94; -.
DR   STRING; 747.DR93_1040; -.
DR   EnsemblBacteria; AAK03025; AAK03025; PM0941.
DR   GeneID; 62224800; -.
DR   KEGG; pmu:PM0941; -.
DR   HOGENOM; CLU_089926_2_1_6; -.
DR   OMA; NQVIHYL; -.
DR   Proteomes; UP000000809; 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..158
FT                   /note="Anaerobic ribonucleoside-triphosphate reductase-
FT                   activating protein"
FT                   /id="PRO_0000200538"
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   158 AA;  18181 MW;  CBE01A6E928650FD CRC64;
     MNYVQYYPTD IVNGEGTRCT LFVSGCTHAC RGCYNKKSWS FCAGLPFDEK MEAQILQDLK
     DTRIKRQGLT LTGGDPLHPR NLAVLLPFVK RVKHECPDKD LWVWTGYTLA ELKADTLQRQ
     ILPYIDVLID GKFEQDKADP SLVWRGSANQ IIYRFTQY