ID J4J2S1_9FIRM Unreviewed; 175 AA.
AC J4J2S1;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Anaerobic ribonucleoside-triphosphate reductase-activating protein {ECO:0000256|ARBA:ARBA00014281, ECO:0000256|PIRNR:PIRNR000368};
DE EC=1.97.1.- {ECO:0000256|PIRNR:PIRNR000368};
GN Name=nrdG {ECO:0000313|EMBL:EJO22419.1};
GN ORFNames=HMPREF1148_0306 {ECO:0000313|EMBL:EJO22419.1};
OS Selenomonas sp. FOBRC6.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=936572 {ECO:0000313|EMBL:EJO22419.1, ECO:0000313|Proteomes:UP000006984};
RN [1] {ECO:0000313|EMBL:EJO22419.1, ECO:0000313|Proteomes:UP000006984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FOBRC6 {ECO:0000313|EMBL:EJO22419.1,
RC ECO:0000313|Proteomes:UP000006984};
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|ARBA:ARBA00003852,
CC ECO:0000256|PIRNR:PIRNR000368}.
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:0000256|ARBA:ARBA00000544};
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|ARBA:ARBA00009777, 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:EJO22419.1}.
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DR EMBL; ALKG01000101; EJO22419.1; -; Genomic_DNA.
DR RefSeq; WP_009656408.1; NZ_ALKG01000101.1.
DR AlphaFoldDB; J4J2S1; -.
DR STRING; 936572.HMPREF1148_0306; -.
DR PATRIC; fig|936572.3.peg.1406; -.
DR eggNOG; COG0602; Bacteria.
DR Proteomes; UP000006984; 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 InterPro; IPR001989; Radical_activat_CS.
DR InterPro; IPR007197; rSAM.
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.
DR PROSITE; PS01087; RADICAL_ACTIVATING; 1.
DR PROSITE; PS51918; RADICAL_SAM; 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|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000368};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 22..175
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 175 AA; 18986 MW; F4028008E008A11C CRC64;
MSASSTDSTE IHISGIARDS IVDGEGIRLT VFTQGCPRRC PGCHNPDTQP LVGGRMTTVG
AVLAELDENP LLTGLTLSGG EPFLQPAALL PLARGAHARG LDVWSYTGYT LEELRAQENP
AVDALLDELD VLVDGDYREE ERDLTLHFRG SRNQRVIDLA ATRATGTLRL LYKDE
//
