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Database: UniProt
Entry: G5SNB4_9BACT
LinkDB: G5SNB4_9BACT
Original site: G5SNB4_9BACT 
ID   G5SNB4_9BACT            Unreviewed;       162 AA.
AC   G5SNB4;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Anaerobic ribonucleoside-triphosphate reductase-activating protein {ECO:0000256|PIRNR:PIRNR000368};
DE            EC=1.97.1.- {ECO:0000256|PIRNR:PIRNR000368};
GN   ORFNames=HMPREF9441_00843 {ECO:0000313|EMBL:EHH01180.1};
OS   Paraprevotella clara YIT 11840.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Paraprevotella.
OX   NCBI_TaxID=762968 {ECO:0000313|EMBL:EHH01180.1, ECO:0000313|Proteomes:UP000003598};
RN   [1] {ECO:0000313|EMBL:EHH01180.1, ECO:0000313|Proteomes:UP000003598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIT 11840 {ECO:0000313|EMBL:EHH01180.1,
RC   ECO:0000313|Proteomes:UP000003598};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (MAR-2011) 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:EHH01180.1}.
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DR   EMBL; AFFY01000015; EHH01180.1; -; Genomic_DNA.
DR   RefSeq; WP_008618171.1; NZ_JH376591.1.
DR   AlphaFoldDB; G5SNB4; -.
DR   STRING; 762968.HMPREF9441_00843; -.
DR   GeneID; 78582035; -.
DR   PATRIC; fig|762968.3.peg.752; -.
DR   eggNOG; COG0602; Bacteria.
DR   HOGENOM; CLU_089926_0_0_10; -.
DR   OrthoDB; 9782387at2; -.
DR   Proteomes; UP000003598; 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   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          13..162
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   162 AA;  18284 MW;  39C80FDB359D9D27 CRC64;
     MISVIKIVED TTVDGPGFRT TVYAAGCPNA CPGCHNPQSW DIEAGTLMTT EEIMQVIRAD
     EFADVTFSGG DPMFQPEGFA ELAEAVKRET GKNIWCYTGY KFERLRHDRR QAELLQYIDV
     LVDGPYVESL RDRDVLFRGS RNQRLIDVQA SLREGEVVLY AQ
//
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