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Database: UniProt
Entry: K0NIR5_DESTT
LinkDB: K0NIR5_DESTT
Original site: K0NIR5_DESTT 
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};
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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
//
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