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Database: UniProt
Entry: U4KQ46_9MOLU
LinkDB: U4KQ46_9MOLU
Original site: U4KQ46_9MOLU 
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
//
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