ID A0A0A7FTZ6_9CLOT Unreviewed; 303 AA.
AC A0A0A7FTZ6;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Radical SAM superfamily protein {ECO:0000313|EMBL:AIY82400.1};
GN ORFNames=U729_2982 {ECO:0000313|EMBL:AIY82400.1};
OS Clostridium baratii str. Sullivan.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1415775 {ECO:0000313|EMBL:AIY82400.1, ECO:0000313|Proteomes:UP000030635};
RN [1] {ECO:0000313|EMBL:AIY82400.1, ECO:0000313|Proteomes:UP000030635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sullivan {ECO:0000313|EMBL:AIY82400.1};
RX PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002;
RA Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H., Foster J.T.,
RA Johnson S.L., Chertkov O., Teshima H., Gibbons H.S., Johnsky L.A.,
RA Karavis M.A., Smith L.A.;
RT "Genomic sequences of six botulinum neurotoxin-producing strains
RT representing three clostridial species illustrate the mobility and
RT diversity of botulinum neurotoxin genes.";
RL Infect. Genet. Evol. 30:102-113(2014).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|PIRSR:PIRSR004869-50};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000256|PIRSR:PIRSR004869-50};
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DR EMBL; CP006905; AIY82400.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A7FTZ6; -.
DR STRING; 1561.NPD11_56; -.
DR KEGG; cbv:U729_2982; -.
DR eggNOG; COG1180; Bacteria.
DR HOGENOM; CLU_044176_1_0_9; -.
DR Proteomes; UP000030635; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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; IPR027596; AmmeMemoSam_rS.
DR InterPro; IPR034457; Organic_radical-activating.
DR InterPro; IPR016431; Pyrv-formate_lyase-activ_prd.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR04337; AmmeMemoSam_rS; 1.
DR PANTHER; PTHR30352; PYRUVATE FORMATE-LYASE-ACTIVATING ENZYME; 1.
DR PANTHER; PTHR30352:SF5; TRNA 4-DEMETHYLWYOSINE SYNTHASE (ADOMET-DEPENDENT); 1.
DR Pfam; PF13353; Fer4_12; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF004869; PflX_prd; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SFLD; SFLDG01101; Uncharacterised_Radical_SAM_Su; 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, ECO:0000256|PIRSR:PIRSR004869-50};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR004869-
KW 50};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR004869-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000030635};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRSR:PIRSR004869-50}.
FT DOMAIN 76..284
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT BINDING 91
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|PIRSR:PIRSR004869-50"
FT BINDING 95
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|PIRSR:PIRSR004869-50"
FT BINDING 98
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|PIRSR:PIRSR004869-50"
SQ SEQUENCE 303 AA; 34815 MW; 829EB662CDB863A9 CRC64;
MEKEEFYKEA QFYKEENGMI RCSLCPHNCL IKENEVGLCK VRKAISAFGE LKLYTLNYGN
LTSAQIDPIE KKPLSEFYPG SKILSVGSFG CNFTCSFCQN YSISQERPHT QEITPEELAN
IVCTTKDNLG VAFTYNEPSI WYEFVYETSK IIKEMDSSKK VVIVTNGYIS EEPLKKLLPF
VDAMNVDLKG DDCYYKRLCT GRISPVKNTI KLAKEFGVHV EITTLLVPGE NTNDEFLKDL
SEFIKRIDKN MPLHLSRYFP RYKMEKDLTS LSEMKEAYKS LSLNLNNIYL GNLSEGEKKY
ILN
//
