SitesBLAST
Comparing WP_015887432.1 NCBI__GCF_000018545.1:WP_015887432.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
9br7C Succinate--hydroxymethylglutarate CoA-transferase (see paper)
41% identity, 97% coverage: 4:386/395 of query aligns to 5:380/403 of 9br7C
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
33% identity, 96% coverage: 4:383/395 of query aligns to 5:360/360 of 5yx6A
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)
30% identity, 98% coverage: 1:387/395 of query aligns to 1:401/416 of P69902
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
30% identity, 98% coverage: 1:387/395 of query aligns to 1:401/417 of 1q6yA
- active site: Q17 (≠ L17), E140 (≠ D145), D169 (= D174), G248 (vs. gap), G249 (vs. gap)
- binding coenzyme a: V16 (≠ I16), Q17 (≠ L17), S18 (≠ A18), R38 (≠ S38), L72 (= L77), N73 (≠ D78), T74 (≠ F79), K75 (≠ T80), N96 (= N101), F97 (= F102), H98 (≠ K103), M105 (≠ Y110), I124 (≠ V129), K137 (≠ A142), A138 (≠ G143), Y139 (= Y144), D169 (= D174), M200 (≠ L205)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
30% identity, 97% coverage: 3:387/395 of query aligns to 2:400/415 of 1pt5A
- active site: Q16 (≠ L17), E139 (≠ D145), D168 (= D174), G247 (vs. gap), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (≠ I16), S17 (≠ A18), R37 (≠ S38), L71 (= L77), N72 (≠ D78), T73 (≠ F79), K74 (≠ T80), N95 (= N101), F96 (= F102), H97 (≠ K103), K124 (≠ T130), K136 (≠ A142), A137 (≠ G143), Y138 (= Y144), E139 (≠ D145), D168 (= D174), M199 (≠ L205)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
29% identity, 99% coverage: 1:392/395 of query aligns to 1:418/428 of O06644
- Q17 (≠ L17) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ S38) binding CoA
- W48 (= W47) 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 (≠ H234) mutation to A: 2.5-fold decrease of the catalytic effiency.
- G260 (≠ P235) mutation to A: 25-fold decrease of the catalytic effiency. Reduction of the affinity binding for both formyl-CoA and oxalate.
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
29% identity, 98% coverage: 4:392/395 of query aligns to 3:417/427 of 1p5rA
- active site: Q16 (≠ L17), E139 (≠ D145), D168 (= D174), G259 (≠ P235), G260 (≠ N236)
- binding coenzyme a: H14 (≠ R15), V15 (≠ I16), Q16 (≠ L17), A17 (= A18), R37 (≠ S38), M73 (≠ F79), K74 (≠ T80), N95 (= N101), F96 (= F102), A100 (≠ G106), R103 (≠ K109), K136 (≠ A142), V137 (≠ G143), D168 (= D174), M199 (≠ L205)
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
29% identity, 98% coverage: 4:392/395 of query aligns to 3:417/427 of 2vjoA
- active site: A16 (≠ L17), E139 (≠ D145), D168 (= D174), G259 (≠ P235), G260 (≠ N236)
- binding coenzyme a: H14 (≠ R15), A16 (≠ L17), A17 (= A18), R37 (≠ S38), L71 (= L77), M73 (≠ F79), N95 (= N101), F96 (= F102), G97 (≠ K103), R103 (≠ K109), M104 (≠ Y110), K136 (≠ A142), V137 (≠ G143), Y138 (= Y144), D168 (= D174), M199 (≠ L205)
- binding oxalate ion: G257 (≠ A233), G259 (≠ P235), Q261 (≠ I237)
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
29% identity, 98% coverage: 4:392/395 of query aligns to 3:417/427 of 2vjkA
- active site: Q16 (≠ L17), E139 (≠ D145), D168 (= D174), G259 (≠ P235), G260 (≠ N236)
- binding coenzyme a: H14 (≠ R15), Q16 (≠ L17), A17 (= A18), R37 (≠ S38), M73 (≠ F79), K74 (≠ T80), N95 (= N101), F96 (= F102), G97 (≠ K103), R103 (≠ K109), M104 (≠ Y110), K136 (≠ A142), V137 (≠ G143), Y138 (= Y144), D168 (= D174), M199 (≠ L205)
- binding magnesium ion: D293 (= D265), D296 (≠ G268)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
29% identity, 98% coverage: 4:392/395 of query aligns to 3:417/427 of 1t4cA
- active site: Q16 (≠ L17), E139 (≠ D145), D168 (= D174), G259 (≠ P235), G260 (≠ N236)
- binding coenzyme a: H14 (≠ R15), V15 (≠ I16), Q16 (≠ L17), R37 (≠ S38), M73 (≠ F79), N95 (= N101), F96 (= F102), R103 (≠ K109), M104 (≠ Y110), V137 (≠ G143), Y138 (= Y144), D168 (= D174), M199 (≠ L205)
- binding oxalic acid: G259 (≠ P235), G260 (≠ N236)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
28% identity, 98% coverage: 4:392/395 of query aligns to 3:417/427 of 1t3zA