ID B7MUS2_ECO81 Unreviewed; 385 AA.
AC B7MUS2;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Radical SAM core domain-containing protein {ECO:0000259|PROSITE:PS51918};
GN Name=ydeM {ECO:0000313|EMBL:CAR07838.2};
GN OrderedLocusNames=ECED1_1641 {ECO:0000313|EMBL:CAR07838.2};
OS Escherichia coli O81 (strain ED1a).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585397 {ECO:0000313|EMBL:CAR07838.2, ECO:0000313|Proteomes:UP000000748};
RN [1] {ECO:0000313|Proteomes:UP000000748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ED1a {ECO:0000313|Proteomes:UP000000748};
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Anaerobic
CC sulfatase-maturating enzyme family. {ECO:0000256|ARBA:ARBA00023601}.
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DR EMBL; CU928162; CAR07838.2; -; Genomic_DNA.
DR RefSeq; WP_001468160.1; NC_011745.1.
DR AlphaFoldDB; B7MUS2; -.
DR KEGG; ecq:ECED1_1641; -.
DR HOGENOM; CLU_009273_10_0_6; -.
DR Proteomes; UP000000748; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
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; cd21120; SPASM_anSME; 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; IPR034491; Anaerob_Ser_sulfatase-maturase.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR047207; SPASM_anSME.
DR InterPro; IPR023867; Sulphatase_maturase_rSAM.
DR NCBIfam; TIGR04085; rSAM_more_4Fe4S; 1.
DR NCBIfam; TIGR03942; sulfatase_rSAM; 1.
DR PANTHER; PTHR43273; ANAEROBIC SULFATASE-MATURATING ENZYME HOMOLOG ASLB-RELATED; 1.
DR PANTHER; PTHR43273:SF3; ANAEROBIC SULFATASE-MATURATING ENZYME HOMOLOG ASLB-RELATED; 1.
DR Pfam; PF13353; Fer4_12; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF13186; SPASM; 1.
DR SFLD; SFLDF00285; anaerobic_Ser-type_sulfatase-m; 1.
DR SFLD; SFLDG01386; main_SPASM_domain-containing; 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 S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 1..231
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 385 AA; 44564 MW; 97B88450062891CC CRC64;
MHVTAKPSSF QCNLKCDYCF YLEKESQFTH EKWMDDSTLK EFIKQYIAAS GNQVYFTWQG
GEPTLAGLDF FRKVIHYQQR YAGQKRIFNA LQTNGILLNN EWCAFLKEHE FLVGISIDGP
QELHDRYRRS NSGNGTFAKV IAAIERLKSY QIEFNTLTVI NNINVHYPLE VYHFLKSIGS
KHMQFIELLE TGTPNIDFSG HSENTFRIID FSVPPTAYGK FMSTIFMRWV KNDVGEIFIR
QFESFVSRFL GNGHTSCIFQ ESCKDNLVVE SNGDIYECDH FVYPQYKIGN INKSELKTMN
SVQLTAQKKR ISAKCQQCAY KPICNGGCPK HRITKVNNET VSYFCEGYKI LFSTMVPYMN
AMVELAKNRV PLYHIMDVAK QMENN
//
