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Database: UniProt
Entry: R7I8X0_9FIRM
LinkDB: R7I8X0_9FIRM
Original site: R7I8X0_9FIRM 
ID   R7I8X0_9FIRM            Unreviewed;       269 AA.
AC   R7I8X0;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Pyruvate formate lyase activating enzyme {ECO:0000313|EMBL:CDE47946.1};
GN   ORFNames=BN770_01446 {ECO:0000313|EMBL:CDE47946.1};
OS   Faecalibacterium sp. CAG:74.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Faecalibacterium.
OX   NCBI_TaxID=1262897 {ECO:0000313|EMBL:CDE47946.1, ECO:0000313|Proteomes:UP000018328};
RN   [1] {ECO:0000313|EMBL:CDE47946.1, ECO:0000313|Proteomes:UP000018328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:74 {ECO:0000313|Proteomes:UP000018328};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycyl-[protein] + reduced [flavodoxin] + S-adenosyl-L-
CC         methionine = 5'-deoxyadenosine + glycin-2-yl radical-[protein] + H(+)
CC         + L-methionine + semiquinone [flavodoxin]; Xref=Rhea:RHEA:61976,
CC         Rhea:RHEA-COMP:10622, Rhea:RHEA-COMP:14480, Rhea:RHEA-COMP:15993,
CC         Rhea:RHEA-COMP:15994, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319,
CC         ChEBI:CHEBI:29947, ChEBI:CHEBI:32722, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:140311;
CC         Evidence={ECO:0000256|ARBA:ARBA00000544};
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|ARBA:ARBA00009777}.
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:CDE47946.1}.
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DR   EMBL; CBJB010000075; CDE47946.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7I8X0; -.
DR   Proteomes; UP000018328; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd01335; Radical_SAM; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.80.30.10; pyruvate-formate lyase- activating enzyme; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR034457; Organic_radical-activating.
DR   InterPro; IPR012839; Organic_radical_activase.
DR   InterPro; IPR001989; Radical_activat_CS.
DR   InterPro; IPR007197; rSAM.
DR   PANTHER; PTHR30352:SF13; GLYCYL-RADICAL ENZYME ACTIVATING ENZYME YJJW-RELATED; 1.
DR   PANTHER; PTHR30352; PYRUVATE FORMATE-LYASE-ACTIVATING ENZYME; 1.
DR   Pfam; PF13353; Fer4_12; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   PIRSF; PIRSF000371; PFL_act_enz; 3.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   PROSITE; PS01087; RADICAL_ACTIVATING; 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   Lyase {ECO:0000313|EMBL:CDE47946.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pyruvate {ECO:0000313|EMBL:CDE47946.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018328};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          21..265
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   269 AA;  30428 MW;  E2AC9E2FEEA15941 CRC64;
     MSNPNPDMKG RIHSFESFAL VDGPGVRCAV FLYGCALRCK FCHNPDTWCP SSISQTKEMT
     ARELFDKAIR YKPYWKNNGG ITVSGGEPLV QLGGIPVSGG NPLVQLDFVT EFFRLMKKEG
     VHTCVDTAGQ PFRRDPEWLD RFNELMSLTD LFMLDLKQFD SKLHVDLTGK DNANILDMAR
     YLSDNGKEMW IRHVLVPGVT DDENDLRKMS DFIASLKTVS RVEILPYHTL GVSKWQKLGI
     PYPLEGVPTP TDEQVKRAED ILNVTAYHK
//
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