ID B0K3U6_THEPX Unreviewed; 345 AA.
AC B0K3U6;
DT 18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT 18-MAR-2008, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Radical SAM domain protein {ECO:0000313|EMBL:ABY91871.1};
GN OrderedLocusNames=Teth514_0563 {ECO:0000313|EMBL:ABY91871.1};
OS Thermoanaerobacter sp. (strain X514).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=399726 {ECO:0000313|EMBL:ABY91871.1, ECO:0000313|Proteomes:UP000002155};
RN [1] {ECO:0000313|EMBL:ABY91871.1, ECO:0000313|Proteomes:UP000002155}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X514 {ECO:0000313|EMBL:ABY91871.1,
RC ECO:0000313|Proteomes:UP000002155};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Hemme C., Fields M.W., He Z., Zhou J., Richardson P.;
RT "Complete sequence of Thermoanaerobacter sp. X514.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; CP000923; ABY91871.1; -; Genomic_DNA.
DR AlphaFoldDB; B0K3U6; -.
DR KEGG; tex:Teth514_0563; -.
DR HOGENOM; CLU_033172_0_1_9; -.
DR Proteomes; UP000002155; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044271; P:cellular nitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProt.
DR GO; GO:0042364; P:water-soluble vitamin biosynthetic process; IEA:UniProt.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR010722; BATS_dom.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR024021; FeFe-hyd_HydE_rSAM.
DR InterPro; IPR034422; HydE/PylB-like.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR03956; rSAM_HydE; 1.
DR PANTHER; PTHR43726; 3-METHYLORNITHINE SYNTHASE; 1.
DR PANTHER; PTHR43726:SF1; BIOTIN SYNTHASE; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF004762; CHP00423; 1.
DR SFLD; SFLDG01082; B12-binding_domain_containing; 1.
DR SFLD; SFLDF00348; FeFe_hydrogenase_maturase_(Hyd; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00876; BATS; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 46..265
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 345 AA; 39301 MW; 4F71C125586CEF90 CRC64;
MLELIKKAEK THSLTKKEIV ELLKDDQYND ELFKAADRVR KKYVGDEVHL RGLIEFSNIC
KQNCLYCGLR RDNKNIKRYR LKPEQIINFA KNARNLGYRT VVLQSGEDDF FNVERMTKII
KSIKQLDIAI TLSIGEKTRE EYKAYKEAGA DRYLLRIETT DKELYEKLDP NMSHENRKRC
LKDLKELGYE VGTGCLIGLP GQTIESIADD ILFFKEIDAD MIGVGPFIPN PDTPLKNEKG
GTFELSLKVM AITRLLMPDI NIPATTAMET LNVNGRLIAL RSGANVVMPN VTEGEYRKLY
ALYPGKICIN DTPAHCFSCI TGKINSIGRP IAKDYGYRKN VMSKK
//
