ID A0A1J0GCD8_9CLOT Unreviewed; 172 AA.
AC A0A1J0GCD8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Anaerobic ribonucleoside-triphosphate reductase-activating protein {ECO:0000256|PIRNR:PIRNR000368};
DE EC=1.97.1.- {ECO:0000256|PIRNR:PIRNR000368};
GN ORFNames=A7L45_02375 {ECO:0000313|EMBL:APC38991.1};
OS Clostridium estertheticum subsp. estertheticum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1552 {ECO:0000313|EMBL:APC38991.1, ECO:0000313|Proteomes:UP000182569};
RN [1] {ECO:0000313|Proteomes:UP000182569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8809 {ECO:0000313|Proteomes:UP000182569};
RX PubMed=27891116;
RA Yu Z., Gunn L., Brennan E., Reid R., Wall P.G., Gaora O.P., Hurley D.,
RA Bolton D., Fanning S.;
RT "Complete Genome Sequence of Clostridium estertheticum DSM 8809, a Microbe
RT Identified in Spoiled Vacuum Packed Beef.";
RL Front. Microbiol. 7:1764-1764(2016).
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 -!- SIMILARITY: Belongs to the organic radical-activating enzymes family.
CC {ECO:0000256|PIRNR:PIRNR000368}.
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DR EMBL; CP015756; APC38991.1; -; Genomic_DNA.
DR RefSeq; WP_071611288.1; NZ_CP015756.1.
DR AlphaFoldDB; A0A1J0GCD8; -.
DR STRING; 1552.A7L45_02375; -.
DR KEGG; ceu:A7L45_02375; -.
DR OrthoDB; 9782387at2; -.
DR Proteomes; UP000182569; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
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 Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR012837; NrdG.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR02491; NrdG; 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.
PE 3: Inferred from homology;
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:UP000182569};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
SQ SEQUENCE 172 AA; 19556 MW; 1448ACBF6790B252 CRC64;
MNYASIFFDD TVNGIGFRTS LFVSGCAKTP PCKGCWSPEA RQFDYGVPFT KYVKTSILES
LKHPYVKGLS ILGGEPMDNL CGGALLDLVK TIKINFPHKT IFCWSGYTFE ELIKNPIRLE
FLQYIDMLRD GEFIEGLKDI TQYLSGSKNQ RMIAVRESLD QNRIIKYSVL DN
//
