ID   T0V8V2_9STRE            Unreviewed;       199 AA.
AC   T0V8V2;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Anaerobic ribonucleoside-triphosphate reductase-activating protein {ECO:0000256|PIRNR:PIRNR000368};
DE            EC=1.97.1.- {ECO:0000256|PIRNR:PIRNR000368};
GN   ORFNames=HSISM1_103 {ECO:0000313|EMBL:EQC75853.1};
OS   Streptococcus sp. HSISM1.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1316408 {ECO:0000313|EMBL:EQC75853.1};
RN   [1] {ECO:0000313|EMBL:EQC75853.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HSISM1 {ECO:0000313|EMBL:EQC75853.1};
RA   Van den Bogert B., Boekhorst J., Herrmann R., Smid E.J., Zoetendal E.G.,
RA   Kleerebezem M.;
RT   "Comparative Genomics Analysis of Streptococcus Isolates from the Human
RT   Small Intestine Reveals their Adaptation to a Highly Dynamic Ecosystem.";
RL   PLoS ONE 8:E83418-E83418(2013).
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:0000256|PIRNR:PIRNR000368}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SIMILARITY: Belongs to the organic radical-activating enzymes family.
CC       {ECO:0000256|PIRNR:PIRNR000368}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EQC75853.1}.
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DR   EMBL; ASKI01000088; EQC75853.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0V8V2; -.
DR   PATRIC; fig|1316408.3.peg.1953; -.
DR   eggNOG; COG0602; Bacteria.
DR   HOGENOM; CLU_089926_2_0_9; -.
DR   Proteomes; UP000015933; Chromosome.
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   CDD; cd01335; Radical_SAM; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR012837; NrdG.
DR   InterPro; IPR034457; Organic_radical-activating.
DR   NCBIfam; TIGR02491; NrdG; 1.
DR   PANTHER; PTHR30352:SF2; ANAEROBIC RIBONUCLEOSIDE-TRIPHOSPHATE REDUCTASE-ACTIVATING PROTEIN; 1.
DR   PANTHER; PTHR30352; PYRUVATE FORMATE-LYASE-ACTIVATING ENZYME; 1.
DR   Pfam; PF13353; Fer4_12; 1.
DR   PIRSF; PIRSF000368; NrdG; 1.
DR   SFLD; SFLDG01063; activating_enzymes__group_1; 1.
DR   SFLD; SFLDF00299; anaerobic_ribonucleoside-triph; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000368,
KW   ECO:0000313|EMBL:EQC75853.1};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
SQ   SEQUENCE   199 AA;  23059 MW;  C0CCE82C19B5F660 CRC64;
     MNNPKPQEWK SEELSKGRII DYKAFNFVDG EGVRNSLYVA GCMFHCEGCY NVATWSFNAG
     IPYTKELEEQ IMEDLAQPYV QGLTLLGGEP FLNTGILLPL VKRIRKELPE KDIWSWTGYT
     WEEMMLETPD KLELLSLIDI LVDGRYDKSK RNLMLQFRGS SNQRIIDVQK SLKEGKVVIW
     DKLNDGKESF EQVKRDDLL
//