ID C7NCG6_LEPBD Unreviewed; 272 AA.
AC C7NCG6;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Glycyl-radical enzyme activating protein family {ECO:0000313|EMBL:ACV39812.1};
DE EC=1.97.1.4 {ECO:0000313|EMBL:ACV39812.1};
GN OrderedLocusNames=Lebu_1949 {ECO:0000313|EMBL:ACV39812.1};
OS Leptotrichia buccalis (strain ATCC 14201 / DSM 1135 / JCM 12969 / NCTC
OS 10249 / C-1013-b).
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Leptotrichia.
OX NCBI_TaxID=523794 {ECO:0000313|EMBL:ACV39812.1, ECO:0000313|Proteomes:UP000001910};
RN [1] {ECO:0000313|EMBL:ACV39812.1, ECO:0000313|Proteomes:UP000001910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14201 / DSM 1135 / JCM 12969 / NCTC 10249 / C-1013-b
RC {ECO:0000313|Proteomes:UP000001910};
RX PubMed=21304648; DOI=10.4056/sigs.1854;
RA Ivanova N., Gronow S., Lapidus A., Copeland A., Glavina Del Rio T.,
RA Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E., Bruce D.,
RA Goodwin L., Brettin T., Detter J.C., Han C., Pitluck S., Mikhailova N.,
RA Pati A., Mavrommatis K., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Chain P., Rohde C., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Leptotrichia buccalis type strain (C-1013-
RT b).";
RL Stand. Genomic Sci. 1:126-132(2009).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001685; ACV39812.1; -; Genomic_DNA.
DR RefSeq; WP_015770150.1; NC_013192.1.
DR AlphaFoldDB; C7NCG6; -.
DR STRING; 523794.Lebu_1949; -.
DR KEGG; lba:Lebu_1949; -.
DR eggNOG; COG1180; Bacteria.
DR HOGENOM; CLU_058969_0_0_0; -.
DR OrthoDB; 9782387at2; -.
DR Proteomes; UP000001910; Chromosome.
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:UniProtKB-EC.
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; IPR040074; BssD/PflA/YjjW.
DR InterPro; IPR034457; Organic_radical-activating.
DR InterPro; IPR012839; Organic_radical_activase.
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; PF13353; Fer4_12; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF000371; PFL_act_enz; 2.
DR SFLD; SFLDG01118; activating_enzymes__group_2; 1.
DR SFLD; SFLDG01066; organic_radical-activating_enz; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 4: Predicted;
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:0000313|EMBL:ACV39812.1};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 14..267
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 272 AA; 31162 MW; 1220D6D81B7940FF CRC64;
MRALVTDIER GATFDGPGIR TVVYFKGCPL RCLWCSNPET QKLENEFWDY DGSLYKGNKT
SCSGCPAANT LKQVAKDMTL EEVFAIVMKD ENFYRNSGGG VTLSGGEILV NSAFAIELFE
KLKEEYINTA IETTGYGNYK DFEKLAKLTD TILFDIKHMD NEKHKKYTAV SNEIILKNLT
KLSEWHKRII MRFPFIKGIN DDEKNIHETA KFLKKLNLLE VNILPYHTMG LEKYKKLGRE
YPMKTLEKHT QDELNNALNI MKSYGLQAKL NG
//
