SitesBLAST
Comparing WP_043917999.1 NCBI__GCF_000877395.1:WP_043917999.1 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: 7:369/373 of query aligns to 5:371/403 of 9br7C
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
31% identity, 97% coverage: 7:369/373 of query aligns to 5:354/360 of 5yx6A
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
29% identity, 97% coverage: 7:369/373 of query aligns to 3:402/427 of 1p5rA
- active site: Q16 (≠ L20), E139 (≠ D144), D168 (= D173), G259 (≠ S235), G260 (≠ I236)
- binding coenzyme a: H14 (≠ R18), V15 (= V19), Q16 (≠ L20), A17 (= A21), R37 (≠ A41), M73 (≠ F78), K74 (≠ R79), N95 (= N100), F96 (= F101), A100 (≠ G105), R103 (≠ K108), K136 (≠ P141), V137 (≠ G142), D168 (= D173), M199 (≠ L204)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
29% identity, 97% coverage: 7:369/373 of query aligns to 4:403/428 of O06644
- Q17 (≠ L20) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ A41) binding CoA
- W48 (= W50) 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 (≠ K108) binding CoA
- D169 (= D173) 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 (≠ P234) mutation to A: 2.5-fold decrease of the catalytic effiency.
- G260 (≠ S235) 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)
29% identity, 97% coverage: 7:369/373 of query aligns to 3:402/427 of 2vjoA
- active site: A16 (≠ L20), E139 (≠ D144), D168 (= D173), G259 (≠ S235), G260 (≠ I236)
- binding coenzyme a: H14 (≠ R18), A16 (≠ L20), A17 (= A21), R37 (≠ A41), L71 (≠ A76), M73 (≠ F78), N95 (= N100), F96 (= F101), G97 (≠ K102), R103 (≠ K108), M104 (≠ Y109), K136 (≠ P141), V137 (≠ G142), Y138 (= Y143), D168 (= D173), M199 (≠ L204)
- binding oxalate ion: G257 (≠ H233), G259 (≠ S235), Q261 (≠ A237)
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
29% identity, 97% coverage: 7:369/373 of query aligns to 3:402/427 of 2vjkA
- active site: Q16 (≠ L20), E139 (≠ D144), D168 (= D173), G259 (≠ S235), G260 (≠ I236)
- binding coenzyme a: H14 (≠ R18), Q16 (≠ L20), A17 (= A21), R37 (≠ A41), M73 (≠ F78), K74 (≠ R79), N95 (= N100), F96 (= F101), G97 (≠ K102), R103 (≠ K108), M104 (≠ Y109), K136 (≠ P141), V137 (≠ G142), Y138 (= Y143), D168 (= D173), M199 (≠ L204)
- binding magnesium ion: D293 (≠ E264), D296 (≠ E267)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
29% identity, 97% coverage: 7:369/373 of query aligns to 3:402/427 of 1t4cA
- active site: Q16 (≠ L20), E139 (≠ D144), D168 (= D173), G259 (≠ S235), G260 (≠ I236)
- binding coenzyme a: H14 (≠ R18), V15 (= V19), Q16 (≠ L20), R37 (≠ A41), M73 (≠ F78), N95 (= N100), F96 (= F101), R103 (≠ K108), M104 (≠ Y109), V137 (≠ G142), Y138 (= Y143), D168 (= D173), M199 (≠ L204)
- binding oxalic acid: G259 (≠ S235), G260 (≠ I236)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
30% identity, 90% coverage: 7:340/373 of query aligns to 4:371/430 of 3ubmB
- active site: Q17 (≠ L20), E140 (≠ D144), D182 (= D173), G261 (≠ S235), G262 (≠ I236)
- binding coenzyme a: V16 (= V19), R38 (≠ A41), L72 (≠ A76), N73 (≠ D77), T74 (≠ F78), K75 (≠ R79), N96 (= N100), F97 (= F101), R98 (≠ K102), A101 (≠ G105), R104 (≠ K108), K125 (≠ T129), D182 (= D173), M213 (≠ L204)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
29% identity, 97% coverage: 7:369/373 of query aligns to 3:402/427 of 1t3zA
- active site: Q16 (≠ L20), E139 (≠ D144), S168 (≠ D173), G259 (≠ S235), G260 (≠ I236)
- binding oxidized coenzyme a: H14 (≠ R18), V15 (= V19), A17 (= A21), R37 (≠ A41), K74 (≠ R79), N95 (= N100), F96 (= F101), A100 (≠ G105), R103 (≠ K108), M104 (≠ Y109), K136 (≠ P141), V137 (≠ G142), Y138 (= Y143), E139 (≠ D144), M199 (≠ L204)
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)
29% identity, 98% coverage: 6:369/373 of query aligns to 3:391/416 of P69902
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
29% identity, 98% coverage: 6:369/373 of query aligns to 2:390/415 of 1pt5A
- active site: Q16 (≠ L20), E139 (≠ D144), D168 (= D173), G247 (≠ S235), G248 (≠ I236)
- binding acetyl coenzyme *a: V15 (= V19), S17 (≠ A21), R37 (≠ A41), L71 (≠ A76), N72 (≠ D77), T73 (≠ F78), K74 (≠ R79), N95 (= N100), F96 (= F101), H97 (≠ K102), K124 (≠ T129), K136 (≠ P141), A137 (≠ G142), Y138 (= Y143), E139 (≠ D144), D168 (= D173), M199 (≠ L204)
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
29% identity, 98% coverage: 6:369/373 of query aligns to 3:391/417 of 1q6yA