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Database: UniProt
Entry: T0MWG3_9CLOT
LinkDB: T0MWG3_9CLOT
Original site: T0MWG3_9CLOT 
ID   T0MWG3_9CLOT            Unreviewed;       428 AA.
AC   T0MWG3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EQB86984.1};
GN   ORFNames=M918_11610 {ECO:0000313|EMBL:EQB86984.1};
OS   Clostridium sp. BL8.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1354301 {ECO:0000313|EMBL:EQB86984.1, ECO:0000313|Proteomes:UP000015873};
RN   [1] {ECO:0000313|EMBL:EQB86984.1, ECO:0000313|Proteomes:UP000015873}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL8 {ECO:0000313|EMBL:EQB86984.1,
RC   ECO:0000313|Proteomes:UP000015873};
RX   PubMed=25076986; DOI=10.1186/1757-4749-6-30;
RA   Marathe N.P., Shetty S.A., Lanjekar V.B., Rasane M.H., Ranade D.R.,
RA   Shouche Y.S.;
RT   "Genome sequencing of multidrug resistant novel Clostridium sp. BL8 reveals
RT   its potential for pathogenicity.";
RL   Gut Pathog. 6:30-30(2014).
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EQB86984.1}.
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DR   EMBL; AUPA01000208; EQB86984.1; -; Genomic_DNA.
DR   RefSeq; WP_021284566.1; NZ_AUPA01000208.1.
DR   AlphaFoldDB; T0MWG3; -.
DR   STRING; 1354301.M918_11610; -.
DR   PATRIC; fig|1354301.3.peg.3454; -.
DR   OrthoDB; 9801424at2; -.
DR   Proteomes; UP000015873; Unassembled WGS sequence.
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   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; 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:SF17; MG-PROTOPORPHYRIN IX MONOMETHYL ESTER OXIDATIVE CYCLASE 66KD SUBUNIT; 1.
DR   Pfam; PF02310; B12-binding; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDG01123; methyltransferase_(Class_B); 1.
DR   SFLD; SFLDS00029; Radical_SAM; 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:UP000015873}.
FT   DOMAIN          1..138
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
FT   DOMAIN          183..398
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   428 AA;  49936 MW;  E8BD403BA6585DB7 CRC64;
     MKIMLVRTRA KSAYNFLQPI VVEPLELEYM ATILEKSGLK YFIQDEIISK KNTLNVFIEE
     KPQIVIMSGY LNNVTTILAH SIEMKKINPE VLIIVGGVHA EVNYKDFFSE GVDIVCYSGG
     FKPLEALITY KFDKSFFQNI KGICYKSFYD EWITNGREVF SPEELMAPDR SFFYKNKKSF
     KYLNLGAYAM VKTSYGCPYA CNFCYCRLLN GGAYTQRTLE SVVEEIKNIN CKNIWIIDDT
     FLISRRRLID FNEILKSHDI KKNFIVYSRA DFIVENKDLL SVMKEIGIKQ VIVGLEAVED
     LTLKEFTKGT DSNVNKKCVE LLNESGIQCV GLFVTHIDYK KEDFNKLYKW IKSVGLKLCT
     FSIYTPLPGT ELYEKHKQEL RFKNYDHMDF LHLLVKPRNL SVSKYYYYFY TMQLKIYLNS
     LKLIILGR
//
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