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
//