ID A0A1Q9NKF2_9ARCH Unreviewed; 146 AA.
AC A0A1Q9NKF2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Anaerobic ribonucleoside-triphosphate reductase-activating protein {ECO:0000256|ARBA:ARBA00014281};
DE AltName: Full=Class III anaerobic ribonucleotide reductase small component {ECO:0000256|ARBA:ARBA00033436};
GN Name=pflA_2 {ECO:0000313|EMBL:OLS22512.1};
GN ORFNames=HeimC3_30530 {ECO:0000313|EMBL:OLS22512.1};
OS Candidatus Heimdallarchaeota archaeon LC_3.
OC Archaea; Asgard group; Candidatus Heimdallarchaeota.
OX NCBI_TaxID=1841598 {ECO:0000313|EMBL:OLS22512.1, ECO:0000313|Proteomes:UP000186063};
RN [1] {ECO:0000313|EMBL:OLS22512.1, ECO:0000313|Proteomes:UP000186063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC_3 {ECO:0000313|EMBL:OLS22512.1};
RX PubMed=28077874; DOI=10.1038/nature21031;
RA Zaremba-Niedzwiedzka K., Caceres E.F., Saw J.H., Backstrom D.,
RA Juzokaite L., Vancaester E., Seitz K.W., Anantharaman K., Starnawski P.,
RA Kjeldsen K.U., Scott M.B., Nunoura T., Banfield J.F., Schramm A.,
RA Baker B.J., Spang A., Ettema T.J.G.;
RT "Asgard archaea illuminate the origin of eukaryotic cellular complexity.";
RL Nature 541:353-358(2017).
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 -!- 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}.
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:OLS22512.1}.
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DR EMBL; MDVS01000050; OLS22512.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q9NKF2; -.
DR Proteomes; UP000186063; 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:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 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; SFLDF00299; anaerobic_ribonucleoside-triph; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS01087; RADICAL_ACTIVATING; 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 Lyase {ECO:0000313|EMBL:OLS22512.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:OLS22512.1}; Pyruvate {ECO:0000313|EMBL:OLS22512.1};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
SQ SEQUENCE 146 AA; 16678 MW; B36A6E6CE668DEA8 CRC64;
MKIKINSIDY SGSIVDGPGL RTVLFVQGCE KKCKGCHNQG AWDYSKGTEI DIDDLVEELN
KKCLNKKLTI SGGEPLHQYE SLLVLLNKLQ DYNLILYTGN EMEEVPKTIL EYLDYIKVGR
FIEEEKGSTI PYVGSKNQQF IRLKER
//
