ID Q189Q5_CLOD6 Unreviewed; 584 AA.
AC Q189Q5;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=Radical SAM domain-containing protein {ECO:0000313|EMBL:CAJ67546.1};
GN OrderedLocusNames=CD630_07130 {ECO:0000313|EMBL:CAJ67546.1};
OS Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=272563 {ECO:0000313|EMBL:CAJ67546.1, ECO:0000313|Proteomes:UP000001978};
RN [1] {ECO:0000313|EMBL:CAJ67546.1, ECO:0000313|Proteomes:UP000001978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=630 {ECO:0000313|EMBL:CAJ67546.1,
RC ECO:0000313|Proteomes:UP000001978};
RX PubMed=16804543; DOI=10.1038/ng1830;
RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA Price C., Rabbinowitsch R., Sharp S., Simmonds M., Steven K., Unwin L.,
RA Whithead S., Dupuy B., Dougan G., Barrell B.and.Parkhill.J.;
RT "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT mobile, mosaic genome.";
RL Nat. Genet. 38:779-786(2006).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; AM180355; CAJ67546.1; -; Genomic_DNA.
DR RefSeq; WP_011860933.1; NZ_JAUPES010000005.1.
DR RefSeq; YP_001087189.1; NC_009089.1.
DR AlphaFoldDB; Q189Q5; -.
DR STRING; 272563.CD630_07130; -.
DR EnsemblBacteria; CAJ67546; CAJ67546; CD630_07130.
DR KEGG; cdf:CD630_07130; -.
DR KEGG; pdc:CDIF630_00829; -.
DR PATRIC; fig|272563.120.peg.734; -.
DR eggNOG; COG1032; Bacteria.
DR OrthoDB; 9801424at2; -.
DR PhylomeDB; Q189Q5; -.
DR BioCyc; PDIF272563:G12WB-824-MONOMER; -.
DR Proteomes; UP000001978; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01335; Radical_SAM; 1.
DR CDD; cd02068; radical_SAM_B12_BD; 1.
DR Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR Gene3D; 3.80.30.20; tm_1862 like domain; 1.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR036724; Cobalamin-bd_sf.
DR InterPro; IPR025288; DUF4080.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR034466; Methyltransferase_Class_B.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023404; rSAM_horseshoe.
DR PANTHER; PTHR43409; ANAEROBIC MAGNESIUM-PROTOPORPHYRIN IX MONOMETHYL ESTER CYCLASE-RELATED; 1.
DR PANTHER; PTHR43409:SF18; RADICAL SAM SUPERFAMILY PROTEIN; 1.
DR Pfam; PF02310; B12-binding; 1.
DR Pfam; PF13311; DUF4080; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDG01082; B12-binding_domain_containing; 1.
DR SFLD; SFLDG01123; methyltransferase_(Class_B); 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00022485};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00022485};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001978}.
FT DOMAIN 1..133
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT DOMAIN 172..402
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 584 AA; 69217 MW; 1F7412871A91032C CRC64;
MKILLTTLNS KFIHTNLAIR YLKEFVRDLI EVNMKEYTIN NDLDYILKDI YKNEYDIILF
STYIWNVGDI VKLCDNLKKI RPNTKIALGG PEVSYDSYEA MKKYDFVDYI LYGEGELIFR
DLVLHLQGKM EINDVNGLVY RQGNEIIVNK PMELLQDLDE IPSPYENLNP KEYENRIVYY
ESSRGCPFNC QYCLSSTIPG LRYFSLDRIK SDLKALIDAR VSQIKFIDRT FNANRKVAME
IMDFLMKNDN GYTTYHFEVT AYLIDDKMLE FLADCKEGLF QFEIGVQSTN EKTLDAVGRR
DDFKKLSHVV QTVASYRNIH QHLDLIAGLP YEDYKSFENS FNDVFNLGIE HLQLGFLKMI
KGTGMRKVAD EHGFKYKDYA PYEFLYNNYI SYEETLKLKD IEDILERYYN SKNFVLSMRY
IIGRFYKKSP FKFFEVFAKY FDENGYFDLA QGKNQLYKIL MDFYNEKINI DNDVFNDILK
YDYISLGKTS NIPQFFNKLD VDDFKNKCHV FLQDNDNLST YLPSFVDKPA KHIIKYVHFE
PFRFNVVDLK NDINTEIREV ENVVLFEYDD KKIFEKSKTH KVEI
//
