ID J4W201_9FIRM Unreviewed; 173 AA.
AC J4W201;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Anaerobic ribonucleoside-triphosphate reductase-activating protein {ECO:0000256|PIRNR:PIRNR000368};
DE EC=1.97.1.- {ECO:0000256|PIRNR:PIRNR000368};
GN Name=nrdG {ECO:0000313|EMBL:EJU20241.1};
GN ORFNames=HMPREF1152_0150 {ECO:0000313|EMBL:EJU20241.1};
OS Mogibacterium sp. CM50.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Eubacteriales Family XIII. Incertae Sedis; Mogibacterium.
OX NCBI_TaxID=936375 {ECO:0000313|EMBL:EJU20241.1, ECO:0000313|Proteomes:UP000003142};
RN [1] {ECO:0000313|EMBL:EJU20241.1, ECO:0000313|Proteomes:UP000003142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM50 {ECO:0000313|EMBL:EJU20241.1,
RC ECO:0000313|Proteomes:UP000003142};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
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:EJU20241.1}.
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DR EMBL; ALNL01000039; EJU20241.1; -; Genomic_DNA.
DR RefSeq; WP_009644273.1; NZ_ALNL01000039.1.
DR AlphaFoldDB; J4W201; -.
DR STRING; 936375.HMPREF1152_0150; -.
DR PATRIC; fig|936375.3.peg.1249; -.
DR eggNOG; COG0602; Bacteria.
DR OrthoDB; 9782387at2; -.
DR Proteomes; UP000003142; Unassembled WGS sequence.
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:EJU20241.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003142};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
SQ SEQUENCE 173 AA; 19766 MW; 5956A150D028B5A0 CRC64;
MNYGEIKDCD VANGVGVRIS LFVSGCTNRC PGCFQPQTWD FNYGQEFTRK TEDKIIEMMR
PGYINGLTVL GGEPFEPGNQ QVLMPFLRRV KASYPDKTIW AFTGFVLEDL MKEGAHCHTD
VTEEMLGMLD VLIDGRFEQG LKNIQLRFRG SENQRLIDMN KTREAGKIVL WDE
//