ID G2FL04_9FIRM Unreviewed; 471 AA.
AC G2FL04;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Radical SAM superfamily protein {ECO:0000313|EMBL:EGW41673.1};
GN ORFNames=DOT_0357 {ECO:0000313|EMBL:EGW41673.1};
OS Desulfosporosinus sp. OT.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=913865 {ECO:0000313|EMBL:EGW41673.1, ECO:0000313|Proteomes:UP000004928};
RN [1] {ECO:0000313|EMBL:EGW41673.1, ECO:0000313|Proteomes:UP000004928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT {ECO:0000313|EMBL:EGW41673.1,
RC ECO:0000313|Proteomes:UP000004928};
RX PubMed=21994931; DOI=10.1128/JB.06018-11;
RA Abicht H.K., Mancini S., Karnachuk O.V., Solioz M.;
RT "Genome Sequence of Desulfosporosinus sp. OT, an Acidophilic Sulfate-
RT Reducing Bacterium from Copper Mining Waste in Norilsk, Northern Siberia.";
RL J. Bacteriol. 193:6104-6105(2011).
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};
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:EGW41673.1}.
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DR EMBL; AGAF01000020; EGW41673.1; -; Genomic_DNA.
DR RefSeq; WP_009613222.1; NZ_AGAF01000020.1.
DR AlphaFoldDB; G2FL04; -.
DR PATRIC; fig|913865.3.peg.331; -.
DR eggNOG; COG0502; Bacteria.
DR OrthoDB; 9801120at2; -.
DR Proteomes; UP000004928; Unassembled WGS sequence.
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; IPR024007; FeFe-hyd_mat_HydG.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR034428; ThiH/NoCL/HydG-like.
DR NCBIfam; TIGR03955; rSAM_HydG; 1.
DR PANTHER; PTHR43583; 2-IMINOACETATE SYNTHASE; 1.
DR PANTHER; PTHR43583:SF2; BIOTIN AND THIAMIN SYNTHESIS ASSOCIATED DOMAIN CONTAINING PROTEIN; 1.
DR Pfam; PF06968; BATS; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDF00319; Fe_hydrogenase_maturase_(HydG; 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 Coiled coil {ECO:0000256|SAM:Coils}; 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 77..309
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT COILED 102..129
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 471 AA; 53140 MW; CDA1888371EAF35E CRC64;
MQEYLAKDFI IDEEIRKSLD EGVEKAKEKD LVRAILEKAK TCQGLSHREA AVLLNINDPN
VLTEMFKTAK EIKEKIYGKR IVLFAPLYIS SYCVNGCVYC GYQACNESLK RSKLTMEQLE
EEVKILESLG HKRIVIEAGE DPINCSLDYV IECIKKIYSL KFDNGSIRRI NINVAATTVE
NYKRLKDADI GTYTLFQETY NQEVYEKMHP TGPKHNYNWH TTAMDRAMEA GIGDVGIGVL
YGLYEHKYET IAMLMHAEHL EDAFGVGPHT ISVPRLRAAE GVDLNDLPYL VTDDEFKKLV
AVLRLAVPYT GMILSTREEA GFREEVLALG ISQFSAGSCT GVGAYSKEHG IDKTVEKPQF
EVADHRSPME VIKSLCESGY IPSYCTACYR EGRTGDRFMV LAKAGQIGNV CQPNALLTFR
EFLLDYADDE MKELGKKVIE KGLMDIPKEA ARKAAEEKLK RIEAGERDLR F
//
