ID A0A1Y4L1E9_9FIRM Unreviewed; 302 AA.
AC A0A1Y4L1E9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Radical SAM protein {ECO:0000313|EMBL:OUP50633.1};
GN ORFNames=B5F18_03085 {ECO:0000313|EMBL:OUP50633.1};
OS Lachnoclostridium sp. An181.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1965575 {ECO:0000313|EMBL:OUP50633.1, ECO:0000313|Proteomes:UP000242090};
RN [1] {ECO:0000313|Proteomes:UP000242090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An181 {ECO:0000313|Proteomes:UP000242090};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|PIRSR:PIRSR004869-50};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000256|PIRSR:PIRSR004869-50};
CC -!- SIMILARITY: Belongs to the organic radical-activating enzymes family.
CC {ECO:0000256|ARBA:ARBA00009777}.
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:OUP50633.1}.
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DR EMBL; NFKJ01000003; OUP50633.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4L1E9; -.
DR OrthoDB; 9781783at2; -.
DR Proteomes; UP000242090; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 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:UniProtKB-KW.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR040085; MJ0674-like.
DR InterPro; IPR016431; Pyrv-formate_lyase-activ_prd.
DR InterPro; IPR001989; Radical_activat_CS.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR43075; FORMATE LYASE ACTIVATING ENZYME, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G15630)-RELATED; 1.
DR PANTHER; PTHR43075:SF1; FORMATE LYASE ACTIVATING ENZYME, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G15630)-RELATED; 1.
DR Pfam; PF13353; Fer4_12; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF004869; PflX_prd; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SFLD; SFLDG01099; Uncharacterised_Radical_SAM_Su; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS01087; RADICAL_ACTIVATING; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR004869-50};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR004869-
KW 50};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR004869-50};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000242090};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRSR:PIRSR004869-50}.
FT DOMAIN 57..225
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|Pfam:PF04055"
FT BINDING 62
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|PIRSR:PIRSR004869-50"
FT BINDING 66
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|PIRSR:PIRSR004869-50"
FT BINDING 69
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|PIRSR:PIRSR004869-50"
SQ SEQUENCE 302 AA; 34043 MW; 926F2CC944BB237C CRC64;
MKKPFQSCVI CPRNCRVDRT AGQKGFCGMS DRLVAARAAL HMWEEPCISG TKGSGTVFFS
GCSMGCVYCQ NQKIAKAEIG KQISVSRLAR IFCNLQDQGA ANINLVTPGH FVYQVLEALK
LAKQKGLDIP IVYNSSGYEK AETIRILEGY VDVYLPDFKY WEKESARRYS SAPDYRAYAI
ESLKEMVRQA GKPVFDGDGY MRRGVIVRHL VLPGHVEEAK KIIRYLYETY GDDIYISIMN
QYTPLSWVED YPEINRKLTE EEYEAVVDAA IDLGVENGFV QEGETAKESF IPDFALQGIE
KV
//