ID U4KQ46_9MOLU Unreviewed; 173 AA.
AC U4KQ46;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
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:CCV66652.1};
GN ORFNames=BN85316310 {ECO:0000313|EMBL:CCV66652.1};
OS Paracholeplasma brassicae.
OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC Acholeplasmataceae; Paracholeplasma.
OX NCBI_TaxID=61635 {ECO:0000313|EMBL:CCV66652.1, ECO:0000313|Proteomes:UP000032737};
RN [1] {ECO:0000313|EMBL:CCV66652.1, ECO:0000313|Proteomes:UP000032737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0502 {ECO:0000313|Proteomes:UP000032737};
RX PubMed=24158107; DOI=10.1159/000354322;
RA Kube M., Siewert C., Migdoll A.M., Duduk B., Holz S., Rabus R.,
RA Seemuller E., Mitrovic J., Muller I., Buttner C., Reinhardt R.;
RT "Analysis of the Complete Genomes of Acholeplasma brassicae , A. palmae and
RT A. laidlawii and Their Comparison to the Obligate Parasites from '
RT Candidatus Phytoplasma'.";
RL J. Mol. Microbiol. Biotechnol. 24:19-36(2013).
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; FO681348; CCV66652.1; -; Genomic_DNA.
DR RefSeq; WP_030005502.1; NC_022549.1.
DR AlphaFoldDB; U4KQ46; -.
DR STRING; 61635.BN85316310; -.
DR KEGG; abra:BN85316310; -.
DR HOGENOM; CLU_089926_0_0_14; -.
DR OrthoDB; 9782387at2; -.
DR Proteomes; UP000032737; Chromosome Acholeplasma brassicae.
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 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 Pfam; PF04055; Radical_SAM; 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:UP000032737};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 23..86
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|Pfam:PF04055"
SQ SEQUENCE 173 AA; 19411 MW; D9B14309844B4008 CRC64;
MKIRLAQIYA NSIVDGPGIR YAIYTQGCLH DCKGCHNPGT HALNQGYLMD TQAIIDEIKG
KPHLNKITFS GGEPLLQVKA INEIIEGLEP GYQIIVYTGF TYEFLISSAG GNTHLMRLLH
QIDYLIDGKF ILEQRDLTLL YRGSKNQRII DVKQSLSKRK VVTTETMKNN SSV
//