ID A0A1Q9JQA6_9FIRM Unreviewed; 570 AA.
AC A0A1Q9JQA6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=B12-binding domain-containing radical SAM protein {ECO:0000313|EMBL:OLR58399.1};
GN ORFNames=BHF70_01415 {ECO:0000313|EMBL:OLR58399.1};
OS Anaerostipes sp. 494a.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerostipes.
OX NCBI_TaxID=1261636 {ECO:0000313|EMBL:OLR58399.1, ECO:0000313|Proteomes:UP000242190};
RN [1] {ECO:0000313|EMBL:OLR58399.1, ECO:0000313|Proteomes:UP000242190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=494a {ECO:0000313|EMBL:OLR58399.1,
RC ECO:0000313|Proteomes:UP000242190};
RX PubMed=27613689;
RA Trachsel J., Bayles D.O., Looft T., Levine U.Y., Allen H.K.;
RT "Function and Phylogeny of Bacterial Butyryl Coenzyme A:Acetate
RT Transferases and Their Diversity in the Proximal Colon of Swine.";
RL Appl. Environ. Microbiol. 82:6788-6798(2016).
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:OLR58399.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MJIF01000001; OLR58399.1; -; Genomic_DNA.
DR RefSeq; WP_075758585.1; NZ_MJIF01000001.1.
DR AlphaFoldDB; A0A1Q9JQA6; -.
DR STRING; 1261636.BHF70_01415; -.
DR OrthoDB; 9801424at2; -.
DR Proteomes; UP000242190; 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 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:UP000242190}.
FT DOMAIN 1..134
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT DOMAIN 171..401
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 570 AA; 67552 MW; E5234C9D2BB82E02 CRC64;
MNIILTAINA KYIHSNLAVY CLRAYAKPYK EDIQIAEYTI NQQIDDMIMD LYKRKPDILC
FSCYIWNIEY VERVLREIKK LFPSLPIWLG GPEVSYDSHN VLERLPEVTG VIKGEGEQTF
LEVMGYYHGK IHDLSEIDGI TYRNQDKIIE NPWRSVIDLS SVPFVYDHME DFEHKIIYYE
SSRGCPFSCS YCLSSIDKCL RFRNLSLVKK ELQFFIDHKV PQVKFVDRTF NCNHQHALEI
WRFIKEHDNG ITNFHFEVAA DLLNEEELTL ISDMRPGLIQ LEIGVQSTNP KTINEIHRKM
DFQKVAKIVD RINAGHNIHQ HLDLIAGLPY EDLESFQKSF NDVYAVKPEQ LQLGFLKVLK
GSYMEQQKDA YGLVFKDIPP YEVLYTNWLP YDQMLILKSI ENIVEIYYNS GQFSYTMRYL
EHEFSSAFEM YRKLGEFYES EGYHKMNHSR ISRYEILFQF IKRHSSKEKL PFYQELLTFD
LYLRENIKNR PDFAGEYSIG KEELYYLYDE VLSKDPVLNV YAKKNMRKMM HIEKFHYAVH
TDGKPAETIL LFDYLERNPL NHQAKIISVK
//
