ID A0A0U5NS23_9CLOT Unreviewed; 465 AA.
AC A0A0U5NS23;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Radical SAM core domain-containing protein {ECO:0000259|PROSITE:PS51918};
GN ORFNames=BN3456_01931 {ECO:0000313|EMBL:CUX38854.1};
OS Clostridium sp. C105KSO13.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1776045 {ECO:0000313|EMBL:CUX38854.1, ECO:0000313|Proteomes:UP000198973};
RN [1] {ECO:0000313|EMBL:CUX38854.1, ECO:0000313|Proteomes:UP000198973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C105KSO131 {ECO:0000313|EMBL:CUX38854.1};
RA McClelland M., Jain A., Saraogi P., Mendelson R., Westerman R.,
RA SanMiguel P., Csonka L.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Anaerobic
CC sulfatase-maturating enzyme family. {ECO:0000256|ARBA:ARBA00023601}.
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DR EMBL; FBWL01000167; CUX38854.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U5NS23; -.
DR STRING; 1776045.BN3456_01931; -.
DR OrthoDB; 9808591at2; -.
DR Proteomes; UP000198973; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-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:InterPro.
DR CDD; cd01335; Radical_SAM; 1.
DR CDD; cd21124; SPASM_CteB-like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR023885; 4Fe4S-binding_SPASM_dom.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR024025; SCIFF_rSAM_maturase.
DR InterPro; IPR047602; SPASM_CteB-like.
DR InterPro; IPR023867; Sulphatase_maturase_rSAM.
DR NCBIfam; TIGR04085; rSAM_more_4Fe4S; 1.
DR NCBIfam; TIGR03974; rSAM_six_Cys; 1.
DR PANTHER; PTHR43273; ANAEROBIC SULFATASE-MATURATING ENZYME HOMOLOG ASLB-RELATED; 1.
DR PANTHER; PTHR43273:SF8; RADICAL SAM PROTEIN-RELATED; 1.
DR Pfam; PF13353; Fer4_12; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF13186; SPASM; 1.
DR SFLD; SFLDG01072; dehydrogenase_like; 1.
DR SFLD; SFLDG01384; thioether_bond_formation_requi; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000198973};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 102..327
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 465 AA; 53531 MW; 0CE11FF134E146AC CRC64;
MIHQYQNNGY NIVLDVNSGA VHVVDKIAYD VMEALETMNS FHTPQTLKDE DTYRYLLEHF
GQVYSEEDLK DVLEAVIELT EAGRLFTRDI YEDYIDEVKQ RKTVVKALCL HIAHDCNLAC
RYCFAEEGEY HGRRALMSYE VGKKALDFLI ASSGSRRNLE VDFFGGEPLM NWKVVKELVA
YGREQEKLYN KHFRFTLTTN GVLLNDEVQE FVNREMDNVV LSLDGRREVN DKMRPFRNGK
GSYDLIVPKF QKLAESRNQQ KYYIRGTFTR DNLDFSNDVM HFADLGFEQI SIEPVVGEET
DPYAIRESDL PQIFHEYDVL AKTMVERERK GEGFTFFHFM LDLEGGPCVA KRLSGCGSGT
EYLAVTPWGD LYPCHQFVGQ DEFLMGNVDE GIVKPEIADE FRGCSVYSKD KCRNCFARFY
CSGGCMANSY KFNGTINNTY DVSCEMERKR VECAIMIKAA LADRL
//