ID   G2T125_ROSHA            Unreviewed;       172 AA.
AC   G2T125;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Anaerobic ribonucleoside-triphosphate reductase-activating protein {ECO:0000256|PIRNR:PIRNR000368};
DE            EC=1.97.1.- {ECO:0000256|PIRNR:PIRNR000368};
GN   OrderedLocusNames=RHOM_04870 {ECO:0000313|EMBL:AEN96094.1};
OS   Roseburia hominis (strain DSM 16839 / JCM 17582 / NCIMB 14029 / A2-183).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX   NCBI_TaxID=585394 {ECO:0000313|EMBL:AEN96094.1, ECO:0000313|Proteomes:UP000008178};
RN   [1] {ECO:0000313|EMBL:AEN96094.1, ECO:0000313|Proteomes:UP000008178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16839 / JCM 17582 / NCIMB 14029 / A2-183
RC   {ECO:0000313|Proteomes:UP000008178};
RX   PubMed=26543119; DOI=10.1128/genomeA.01286-15;
RA   Travis A.J., Kelly D., Flint H.J., Aminov R.I.;
RT   "Complete genome sequence of the human gut symbiont Roseburia hominis.";
RL   Genome Announc. 3:E0128615-E0128615(2015).
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; CP003040; AEN96094.1; -; Genomic_DNA.
DR   RefSeq; WP_014079139.1; NC_015977.1.
DR   AlphaFoldDB; G2T125; -.
DR   STRING; 585394.RHOM_04870; -.
DR   GeneID; 77458614; -.
DR   KEGG; rho:RHOM_04870; -.
DR   eggNOG; COG0602; Bacteria.
DR   HOGENOM; CLU_089926_2_1_9; -.
DR   OrthoDB; 9782387at2; -.
DR   BioCyc; RHOM585394:G1H02-989-MONOMER; -.
DR   Proteomes; UP000008178; 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   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; SFLDF00299; anaerobic_ribonucleoside-triph; 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:UP000008178};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
SQ   SEQUENCE   172 AA;  19228 MW;  BAE75DB4942CF1E9 CRC64;
     MNYSAIKYCD IANGTGVRTV LFVSGCRNHC KDCFQPETWA FEYGNPFTGE VEDEIIASLK
     PDYIRGLTLL GGDPFEPENQ KALLPFMRRV KAECPGKDVW AYTGYVLDRD LVPGGKCCTA
     DTAELLHMID VLVDGPFVTE LHDISLLFKG SSNQRVIDCA EYCRSGEIRE LM
//