ID A0A0K8JJY9_9FIRM Unreviewed; 317 AA.
AC A0A0K8JJY9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Glycyl-radical enzyme activating protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=P22_3966 {ECO:0000313|EMBL:CUH97820.1};
OS Propionispora sp. 2/2-37.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Propionispora.
OX NCBI_TaxID=1677858 {ECO:0000313|EMBL:CUH97820.1, ECO:0000313|Proteomes:UP000041641};
RN [1] {ECO:0000313|EMBL:CUH97820.1, ECO:0000313|Proteomes:UP000041641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2/2 {ECO:0000313|EMBL:CUH97820.1};
RA Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CYSP01000030; CUH97820.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K8JJY9; -.
DR STRING; 1677858.P22_3966; -.
DR Proteomes; UP000041641; 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; PYRUVATE FORMATE-LYASE-ACTIVATING ENZYME; 1.
DR Pfam; PF12838; Fer4_7; 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; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000041641};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 29..308
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT DOMAIN 89..118
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 317 AA; 35561 MW; 93F9C6DA697C1623 CRC64;
MPLSPVRKIP GPDMNAKGLI STIQKYSTKD GPGIRSTVFC IGCNLRCKWC SNPELMEPGI
KYMHFENRCI HCGACVSIAN NQSIKFAEEG CEIDRARCTN MDECMDICPR EAFEKVGYEI
TSEELVGKLL RDKVFYDQSA GGVTFSGGEA ALQGDFVVEA AQRLRQQGVH VALDTAGCLP
WCELKKVVET VDMVLYDIKT FDRDIHKACT GAGNETILTN ARNLARMNKE MIIRLVIVPG
WNDQFTDIKK RLNFIKELGK SVIRVDILRY HALGAGKYRR LGMEYPIRTG LECDETLLEA
TRQMAVELNL NVHLAEK
//
