ID D3QC28_STANL Unreviewed; 184 AA.
AC D3QC28;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE RecName: Full=Anaerobic ribonucleoside-triphosphate reductase-activating protein {ECO:0000256|PIRNR:PIRNR000368};
DE EC=1.97.1.- {ECO:0000256|PIRNR:PIRNR000368};
GN OrderedLocusNames=Snas_5283 {ECO:0000313|EMBL:ADD44917.1};
OS Stackebrandtia nassauensis (strain DSM 44728 / CIP 108903 / NRRL B-16338 /
OS NBRC 102104 / LLR-40K-21).
OC Bacteria; Actinomycetota; Actinomycetes; Glycomycetales; Glycomycetaceae;
OC Stackebrandtia.
OX NCBI_TaxID=446470 {ECO:0000313|EMBL:ADD44917.1, ECO:0000313|Proteomes:UP000000844};
RN [1] {ECO:0000313|EMBL:ADD44917.1, ECO:0000313|Proteomes:UP000000844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44728 / CIP 108903 / NRRL B-16338 / NBRC 102104 /
RC LLR-40K-21 {ECO:0000313|Proteomes:UP000000844};
RX PubMed=21304662; DOI=10.4056/sigs.47643;
RA Munk C., Lapidus A., Copeland A., Jando M., Mayilraj S.,
RA Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., Cheng J.F.,
RA Han C., Detter J.C., Bruce D., Goodwin L., Chain P., Pitluck S., Goker M.,
RA Ovchinikova G., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Stackebrandtia nassauensis type strain (LLR-
RT 40K-21).";
RL Stand. Genomic Sci. 1:292-299(2009).
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}.
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DR EMBL; CP001778; ADD44917.1; -; Genomic_DNA.
DR RefSeq; WP_013020488.1; NC_013947.1.
DR AlphaFoldDB; D3QC28; -.
DR STRING; 446470.Snas_5283; -.
DR KEGG; sna:Snas_5283; -.
DR eggNOG; COG0602; Bacteria.
DR HOGENOM; CLU_089926_1_0_11; -.
DR OMA; EVNGPGC; -.
DR Proteomes; UP000000844; 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 InterPro; IPR007197; rSAM.
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 Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF000368; NrdG; 1.
DR SFLD; SFLDG01063; activating_enzymes__group_1; 1.
DR SFLD; SFLDS00029; Radical_SAM; 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 Reference proteome {ECO:0000313|Proteomes:UP000000844};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 25..123
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|Pfam:PF04055"
SQ SEQUENCE 184 AA; 19730 MW; A4DD5FF9ECFDB710 CRC64;
MTSTVRVHAT LSDSRANGPG ERFVVWFQGC SLACPGCFNP ETHGPDAEEL SVAELAGRVL
ARADRWEGIT LTGGEPLQQP EAVAELCRRI REGSRLGVLI LTGYTRGEIE ADPARLAAVA
DADLVIAGRY NAGLRLGTGL RGSSNKTYWW LTDRYREADL AAVPEAEVRI GADGTLIFTG
MEAA
//