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Database: UniProt
Entry: F7KCV2_9FIRM
LinkDB: F7KCV2_9FIRM
Original site: F7KCV2_9FIRM 
ID   F7KCV2_9FIRM            Unreviewed;       303 AA.
AC   F7KCV2;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Glycyl-radical enzyme activating protein family {ECO:0000313|EMBL:EGN38962.1};
GN   ORFNames=HMPREF0994_03681 {ECO:0000313|EMBL:EGN38962.1};
OS   Lachnospiraceae bacterium 3_1_57FAA_CT1.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=658086 {ECO:0000313|EMBL:EGN38962.1, ECO:0000313|Proteomes:UP000003336};
RN   [1] {ECO:0000313|Proteomes:UP000003336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3_1_57FAA_CT1 {ECO:0000313|Proteomes:UP000003336};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA   Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA   MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Lachnospiraceae bacterium 2_1_58FAA.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EGN38962.1, ECO:0000313|Proteomes:UP000003336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3_1_57FAA_CT1 {ECO:0000313|EMBL:EGN38962.1,
RC   ECO:0000313|Proteomes:UP000003336};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA   Allen-Vercoe E., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Haas B., Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M.,
RA   Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J.,
RA   McCowan C., Murphy C., Pearson M., Poon T.W., Priest M., Roberts A.,
RA   Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Lachnospiraceae bacterium 3-1-57FAA CT1.";
RL   Submitted (APR-2013) 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:EGN38962.1}.
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DR   EMBL; ACTP02000012; EGN38962.1; -; Genomic_DNA.
DR   AlphaFoldDB; F7KCV2; -.
DR   STRING; 658086.HMPREF0994_03681; -.
DR   PATRIC; fig|658086.3.peg.4016; -.
DR   eggNOG; COG1180; Bacteria.
DR   HOGENOM; CLU_058969_0_0_9; -.
DR   Proteomes; UP000003336; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; 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; 3.30.70.20; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR040074; BssD/PflA/YjjW.
DR   InterPro; IPR034457; Organic_radical-activating.
DR   InterPro; IPR012839; Organic_radical_activase.
DR   InterPro; IPR001989; Radical_activat_CS.
DR   InterPro; IPR007197; rSAM.
DR   NCBIfam; TIGR02494; PFLE_PFLC; 1.
DR   PANTHER; PTHR30352:SF4; PYRUVATE FORMATE-LYASE 2-ACTIVATING ENZYME; 1.
DR   PANTHER; PTHR30352; PYRUVATE FORMATE-LYASE-ACTIVATING ENZYME; 1.
DR   Pfam; PF13187; Fer4_9; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   PIRSF; PIRSF000371; PFL_act_enz; 1.
DR   SFLD; SFLDG01118; activating_enzymes__group_2; 1.
DR   SFLD; SFLDG01066; organic_radical-activating_enz; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003336};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          15..297
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   DOMAIN          46..75
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          76..104
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   303 AA;  34151 MW;  5C99B55D588A28A3 CRC64;
     MELPLITNIQ KYAIHDGRGI RTTVFFKGCP LACRWCHNPE TQVYGKELIF YEERCTGCGE
     CVKECRNGAV TAADGKAFTD RELCAGCGEC VDGCMRNARQ LCGRSYTVGE LTEELLKDRA
     FYETSGGGVT LSGGEPLAQD MDYLEKLMGT LCRRGISLNV DTCGAVAFER LERVMPFTDR
     FLFDLKLLDE DKHREYTGRD NKLILENLKL LSGKGARIWI RIPVIGGVND EEEELERMAG
     FLSENVRAEQ INLIPYHNTG SGKYGHLNRE YQGGMFYAPP KERMQELQRL MERKNIAPVF
     IGG
//
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