ID K0NQF9_DESTT Unreviewed; 465 AA.
AC K0NQF9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Cobalamin-binding radical SAM domain protein {ECO:0000313|EMBL:CCK82393.1};
GN OrderedLocusNames=TOL2_C42370 {ECO:0000313|EMBL:CCK82393.1};
OS Desulfobacula toluolica (strain DSM 7467 / Tol2).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulfobacula.
OX NCBI_TaxID=651182 {ECO:0000313|EMBL:CCK82393.1, ECO:0000313|Proteomes:UP000007347};
RN [1] {ECO:0000313|EMBL:CCK82393.1, 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; CCK82393.1; -; Genomic_DNA.
DR RefSeq; WP_014959573.1; NC_018645.1.
DR AlphaFoldDB; K0NQF9; -.
DR STRING; 651182.TOL2_C42370; -.
DR KEGG; dto:TOL2_C42370; -.
DR HOGENOM; CLU_021572_4_3_7; -.
DR OrthoDB; 9804952at2; -.
DR Proteomes; UP000007347; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR Gene3D; 3.80.30.20; tm_1862 like domain; 1.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR036724; Cobalamin-bd_sf.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR034466; Methyltransferase_Class_B.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023404; rSAM_horseshoe.
DR PANTHER; PTHR43409:SF7; ANAEROBIC MAGNESIUM-PROTOPORPHYRIN IX MONOMETHYL ESTER CYCLASE; 1.
DR PANTHER; PTHR43409; ANAEROBIC MAGNESIUM-PROTOPORPHYRIN IX MONOMETHYL ESTER CYCLASE-RELATED; 1.
DR Pfam; PF02310; B12-binding; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDG01082; B12-binding_domain_containing; 1.
DR SFLD; SFLDG01123; methyltransferase_(Class_B); 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00022485};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00022485};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW Reference proteome {ECO:0000313|Proteomes:UP000007347}.
FT DOMAIN 12..187
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT DOMAIN 227..446
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 465 AA; 52354 MW; FE2EC7E36268094D CRC64;
MKTDSPHILC VNPWIHDFAA FDFWAKPLGL LTLAAIMREK GITVSYIDCL DRFHPREPSQ
MKVLWDGRGP FRKTQIDLPQ GLENTGKKFS RYGIKPQWFK EDLEQINKPD IIFVTSLMTY
WASGVQETIE AVKEVYPDIP VVLGGIYASL CHDHAAKNTL ADLVIKGPGE HQLKNIIQKF
TGFELDAGNL PDVNIPDVEI SGVSDVPGIS NRVNDLDDLP FPALDLQNKI VYAPVLTSRG
CPFSCEYCAS SYLEPKLRRR SPENVFKEIE HWHYSHGVKN FAFYDDALLV NAGKYAFLLF
EKIIASKMDL FFHTPNALHI REITRKAADL MFEAGFKTIR LGLETTDFSA DRSHDVKVAE
NEFFNAIAHL KAAGFEEKQI GAYLLCGLPG QNLDDVEASV QVVKHAGIIP VLAYYTPIPH
TPMWSDAVKQ SKFNLLEHPV FTNNTLFPCV NSSRDLARIS QLKNS
//
