ID K0NIR5_DESTT Unreviewed; 316 AA.
AC K0NIR5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Radical SAM domain protein {ECO:0000313|EMBL:CCK79703.1};
GN OrderedLocusNames=TOL2_C15400 {ECO:0000313|EMBL:CCK79703.1};
OS Desulfobacula toluolica (strain DSM 7467 / Tol2).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulfobacula.
OX NCBI_TaxID=651182 {ECO:0000313|EMBL:CCK79703.1, ECO:0000313|Proteomes:UP000007347};
RN [1] {ECO:0000313|EMBL:CCK79703.1, ECO:0000313|Proteomes:UP000007347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7467 / Tol2 {ECO:0000313|Proteomes:UP000007347};
RX PubMed=23088741; DOI=10.1111/j.1462-2920.2012.02885.x;
RA Wohlbrand L., Jacob J.H., Kube M., Mussmann M., Jarling R., Beck A.,
RA Amann R., Wilkes H., Reinhardt R., Rabus R.;
RT "Complete genome, catabolic sub-proteomes and key-metabolites of
RT Desulfobacula toluolica Tol2, a marine, aromatic compound-degrading,
RT sulfate-reducing bacterium.";
RL Environ. Microbiol. 15:1334-55(2013).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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; FO203503; CCK79703.1; -; Genomic_DNA.
DR RefSeq; WP_014957047.1; NC_018645.1.
DR AlphaFoldDB; K0NIR5; -.
DR STRING; 651182.TOL2_C15400; -.
DR KEGG; dto:TOL2_C15400; -.
DR PATRIC; fig|651182.5.peg.1849; -.
DR HOGENOM; CLU_058377_0_0_7; -.
DR OrthoDB; 9800840at2; -.
DR Proteomes; UP000007347; 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 CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR040084; GTPase_Obg.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR43787; FEMO COFACTOR BIOSYNTHESIS PROTEIN NIFB-RELATED; 1.
DR PANTHER; PTHR43787:SF11; UPF0026 PROTEIN SLR1464; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SFLD; SFLDG01083; Uncharacterised_Radical_SAM_Su; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000007347};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 13..247
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 316 AA; 35723 MW; AA0DA192C1C5EB6E CRC64;
MNSKTVFGPV PSRRLGKSVG INNIPPKICT YSCVYCQLGK TQKMIVYRCV FHDPDRLVEE
TKTKLINAQS NNESIDYLTI VSDGEPTLDA KLGLLIDRLR PLGIKIAVIT NSSLLHRIDV
RHDLCKADWV SVKIDTLDEK TWRKIDRPHN GIKFDVMLDG ISSFAKKFTG RLVTETMLIK
GLNDDRQNIE KTADFILGID CATAYLSIPT RPPAQKWVKP PGEQALNQAY HVFDDRGINT
EYLIGYEGNQ FAFTGNIEDD ILSITSVHPM RKDAVAGYLK KAGSDFSVIE KLLEENKLKV
SEYQNEQFYI RKLPVI
//