ID D9TFR4_CALOO Unreviewed; 300 AA.
AC D9TFR4;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Radical SAM domain protein {ECO:0000313|EMBL:ADL43034.1};
GN OrderedLocusNames=COB47_1757 {ECO:0000313|EMBL:ADL43034.1};
OS Caldicellulosiruptor obsidiansis (strain ATCC BAA-2073 / strain OB47).
OC Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales;
OC Caldicellulosiruptoraceae; Caldicellulosiruptor.
OX NCBI_TaxID=608506 {ECO:0000313|EMBL:ADL43034.1, ECO:0000313|Proteomes:UP000000347};
RN [1] {ECO:0000313|EMBL:ADL43034.1, ECO:0000313|Proteomes:UP000000347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2073 / strain OB47
RC {ECO:0000313|Proteomes:UP000000347};
RX PubMed=20851897; DOI=10.1128/JB.00950-10;
RA Elkins J.G., Lochner A., Hamilton-Brehm S.D., Davenport K.W., Podar M.,
RA Brown S.D., Land M.L., Hauser L.J., Klingeman D.M., Raman B., Goodwin L.A.,
RA Tapia R., Meincke L.J., Detter J.C., Bruce D.C., Han C.S., Palumbo A.V.,
RA Cottingham R.W., Keller M., Graham D.E.;
RT "Complete genome sequence of the cellulolytic thermophile
RT Caldicellulosiruptor obsidiansis OB47T.";
RL J. Bacteriol. 192:6099-6100(2010).
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};
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DR EMBL; CP002164; ADL43034.1; -; Genomic_DNA.
DR RefSeq; WP_013291031.1; NC_014392.1.
DR AlphaFoldDB; D9TFR4; -.
DR STRING; 608506.COB47_1757; -.
DR KEGG; cob:COB47_1757; -.
DR eggNOG; COG1313; Bacteria.
DR HOGENOM; CLU_062674_0_1_9; -.
DR OrthoDB; 9781783at2; -.
DR Proteomes; UP000000347; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01335; Radical_SAM; 1.
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; 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; 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.
PE 4: Predicted;
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 S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRSR:PIRSR004869-50}.
FT DOMAIN 59..220
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|Pfam:PF04055"
FT BINDING 64
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 68
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 71
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 300 AA; 34429 MW; 2DC4EF590B05ADD0 CRC64;
MFSQEVLRNC RICPRECGVN RIEGEMGFCK IAGGVKVAKA FLHFWEEPCI SGKNGSGTVF
FSGCNMGCVF CQNYEISQMR FGVFIDVNKL ATIFLNLQSK GAHNINLVTP TIYVPYIIEA
IDIAREKGLR IPIVYNTSSY EKPETLELLR GYVDIFLPDL KYFDDEIAKK YSNAPRYFEF
ASKSILKMVE LVGDVVIENG IMKKGVIIRH LVLPMHTNDS IKILSWIRDN LKGKVMLSLM
SQYYPMYRAK EFKEISRKIT VREYQKVVNF VIENGLDYGY IQDKESATDR YTPDFDLEGI
//