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Database: UniProt
Entry: E0NPL8_9BACT
LinkDB: E0NPL8_9BACT
Original site: E0NPL8_9BACT 
ID   E0NPL8_9BACT            Unreviewed;       169 AA.
AC   E0NPL8;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 40.
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:EFM02977.1};
GN   ORFNames=HMPREF0658_0119 {ECO:0000313|EMBL:EFM02977.1};
OS   Hoylesella marshii DSM 16973 = JCM 13450.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Hoylesella.
OX   NCBI_TaxID=862515 {ECO:0000313|EMBL:EFM02977.1, ECO:0000313|Proteomes:UP000004394};
RN   [1] {ECO:0000313|EMBL:EFM02977.1, ECO:0000313|Proteomes:UP000004394}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16973 {ECO:0000313|EMBL:EFM02977.1,
RC   ECO:0000313|Proteomes:UP000004394};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
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}.
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:EFM02977.1}.
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DR   EMBL; AEEI01000004; EFM02977.1; -; Genomic_DNA.
DR   RefSeq; WP_006947797.1; NZ_GL397214.1.
DR   AlphaFoldDB; E0NPL8; -.
DR   STRING; 862515.HMPREF0658_0119; -.
DR   eggNOG; COG0602; Bacteria.
DR   HOGENOM; CLU_089926_0_0_10; -.
DR   OrthoDB; 9782387at2; -.
DR   Proteomes; UP000004394; 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: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   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.
DR   PROSITE; PS51918; RADICAL_SAM; 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   ECO:0000313|EMBL:EFM02977.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004394};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          13..169
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   169 AA;  18946 MW;  CA5DD2DF1E920077 CRC64;
     MISILDIVHD TMVDGPGFRT SIYCAGCPNK CPGCHNPQSW DIRHGRMLET EEIMKEIVSD
     PFANVTFTGG DPMFQPEGFL ALARAIKHET GKTIWCYSGF VFEQLLNHPK QRALLNYIDV
     LVDGPFIEAR KDADLPFRGS SNQRILDVKK SLKAGKGILL NNDPQRDII
//
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