SitesBLAST
Comparing HSERO_RS18350 FitnessBrowser__HerbieS:HSERO_RS18350 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
9br7C Succinate--hydroxymethylglutarate CoA-transferase (see paper)
29% identity, 98% coverage: 10:415/415 of query aligns to 5:397/403 of 9br7C
P69902 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; Formyl-CoA transferase; EC 2.8.3.16 from Escherichia coli (strain K12) (see paper)
28% identity, 98% coverage: 10:415/415 of query aligns to 4:416/416 of P69902
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
28% identity, 98% coverage: 10:415/415 of query aligns to 4:416/417 of 1q6yA
- active site: Q17 (≠ I23), E140 (≠ G145), D169 (= D174), G248 (vs. gap), G249 (vs. gap)
- binding coenzyme a: V16 (≠ L22), Q17 (≠ I23), S18 (≠ A24), R38 (≠ A44), L72 (= L77), N73 (= N78), T74 (≠ M79), K75 (= K80), N96 (= N101), F97 (≠ Y102), H98 (≠ R103), M105 (≠ W110), I124 (≠ L129), K137 (≠ P142), A138 (≠ G143), Y139 (≠ F144), D169 (= D174), M200 (≠ L219)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
28% identity, 98% coverage: 10:415/415 of query aligns to 3:415/415 of 1pt5A
- active site: Q16 (≠ I23), E139 (≠ G145), D168 (= D174), G247 (vs. gap), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (≠ L22), S17 (≠ A24), R37 (≠ A44), L71 (= L77), N72 (= N78), T73 (≠ M79), K74 (= K80), N95 (= N101), F96 (≠ Y102), H97 (≠ R103), K124 (≠ S130), K136 (≠ P142), A137 (≠ G143), Y138 (≠ F144), E139 (≠ G145), D168 (= D174), M199 (≠ L219)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
28% identity, 98% coverage: 10:415/415 of query aligns to 4:409/410 of 1q7eA
- active site: Q17 (≠ I23), E133 (≠ G145), D162 (= D174), G241 (vs. gap), G242 (vs. gap)
- binding methionine: N96 (= N101), F97 (≠ Y102), H98 (≠ R103), P99 (= P104), K118 (≠ S130), K130 (≠ P142), A131 (≠ G143), W246 (vs. gap), F299 (≠ E304), A303 (= A308), E306 (≠ Q311)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
27% identity, 98% coverage: 10:415/415 of query aligns to 4:428/430 of 3ubmB
- active site: Q17 (≠ I23), E140 (≠ G145), D182 (= D174), G261 (vs. gap), G262 (vs. gap)
- binding coenzyme a: V16 (≠ L22), R38 (≠ A44), L72 (= L77), N73 (= N78), T74 (≠ M79), K75 (= K80), N96 (= N101), F97 (≠ Y102), R98 (= R103), A101 (≠ V106), R104 (≠ K109), K125 (≠ S130), D182 (= D174), M213 (≠ L219)
Q5U921 (R)-2-hydroxy-4-methylpentanoate CoA-transferase; 2-hydroxyisocaproate-CoA transferase; EC 2.8.3.24 from Clostridioides difficile (Peptoclostridium difficile) (see paper)
29% identity, 98% coverage: 11:415/415 of query aligns to 3:397/399 of Q5U921
- D171 (= D174) mutation D->A,N: Loss of activity.
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
27% identity, 98% coverage: 10:415/415 of query aligns to 3:427/427 of 1p5rA
- active site: Q16 (≠ I23), E139 (≠ G145), D168 (= D174), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T21), V15 (≠ L22), Q16 (≠ I23), A17 (= A24), R37 (≠ A44), M73 (= M79), K74 (= K80), N95 (= N101), F96 (≠ Y102), A100 (≠ V106), R103 (≠ K109), K136 (≠ P142), V137 (≠ G143), D168 (= D174), M199 (≠ L219)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
27% identity, 98% coverage: 10:415/415 of query aligns to 4:428/428 of O06644
- Q17 (≠ I23) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ A44) binding CoA
- W48 (= W54) mutation to F: Little change in the affinity binding and catalytic efficiency, and it does not display major structural changes.; mutation to P: Little change in the affinity binding and catalytic efficiency. It exhibits substrate inhibition with oxalate. It does not display major structural changes.
- R104 (≠ K109) binding CoA
- D169 (= D174) active site, Nucleophile; mutation to A: Loss of CoA-transferase activity.; mutation to E: Loss of CoA-transferase activity.; mutation to S: Loss of CoA-transferase activity.
- G259 (vs. gap) mutation to A: 2.5-fold decrease of the catalytic effiency.
- G260 (vs. gap) mutation to A: 25-fold decrease of the catalytic effiency. Reduction of the affinity binding for both formyl-CoA and oxalate.
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
27% identity, 98% coverage: 10:415/415 of query aligns to 3:427/427 of 2vjoA
- active site: A16 (≠ I23), E139 (≠ G145), D168 (= D174), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T21), A16 (≠ I23), A17 (= A24), R37 (≠ A44), L71 (= L77), M73 (= M79), N95 (= N101), F96 (≠ Y102), G97 (≠ R103), R103 (≠ K109), M104 (≠ W110), K136 (≠ P142), V137 (≠ G143), Y138 (≠ F144), D168 (= D174), M199 (≠ L219)
- binding oxalate ion: G257 (vs. gap), G259 (vs. gap), Q261 (vs. gap)
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
27% identity, 98% coverage: 10:415/415 of query aligns to 3:427/427 of 2vjkA