SitesBLAST
Comparing Ac3H11_3532 FitnessBrowser__acidovorax_3H11:Ac3H11_3532 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)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
32% identity, 98% coverage: 7:423/424 of query aligns to 1:427/430 of 3ubmB
- active site: Q17 (≠ L23), E140 (≠ D153), D182 (= D186), G261 (vs. gap), G262 (vs. gap)
- binding coenzyme a: V16 (= V22), R38 (= R44), L72 (≠ I85), N73 (≠ D86), T74 (≠ M87), K75 (≠ A88), N96 (= N109), F97 (= F110), R98 (≠ K111), A101 (≠ G114), R104 (≠ Q117), K125 (≠ T138), D182 (= D186), M213 (= M219)
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)
32% identity, 100% coverage: 1:424/424 of query aligns to 1:416/416 of P69902
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
32% identity, 98% coverage: 11:424/424 of query aligns to 4:427/427 of 2vjoA
- active site: A16 (≠ L23), E139 (≠ D153), D168 (= D186), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R21), A16 (≠ L23), A17 (= A24), R37 (= R44), L71 (≠ I85), M73 (= M87), N95 (= N109), F96 (= F110), G97 (≠ K111), R103 (≠ Q117), M104 (≠ Y118), K136 (≠ A150), V137 (≠ G151), Y138 (= Y152), D168 (= D186), M199 (≠ L221)
- 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)
32% identity, 98% coverage: 11:424/424 of query aligns to 4:427/427 of 2vjkA
- active site: Q16 (≠ L23), E139 (≠ D153), D168 (= D186), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R21), Q16 (≠ L23), A17 (= A24), R37 (= R44), M73 (= M87), K74 (≠ A88), N95 (= N109), F96 (= F110), G97 (≠ K111), R103 (≠ Q117), M104 (≠ Y118), K136 (≠ A150), V137 (≠ G151), Y138 (= Y152), D168 (= D186), M199 (≠ L221)
- binding magnesium ion: D293 (≠ A281), D296 (≠ N284)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
32% identity, 98% coverage: 11:424/424 of query aligns to 4:427/427 of 1t4cA
- active site: Q16 (≠ L23), E139 (≠ D153), D168 (= D186), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R21), V15 (= V22), Q16 (≠ L23), R37 (= R44), M73 (= M87), N95 (= N109), F96 (= F110), R103 (≠ Q117), M104 (≠ Y118), V137 (≠ G151), Y138 (= Y152), D168 (= D186), M199 (≠ L221)
- binding oxalic acid: G259 (vs. gap), G260 (vs. gap)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
32% identity, 98% coverage: 11:424/424 of query aligns to 5:428/428 of O06644
- Q17 (≠ L23) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (= R44) binding
- 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 (≠ Q117) binding
- D169 (= D186) 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.
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
32% identity, 98% coverage: 11:424/424 of query aligns to 4:427/427 of 1p5rA
- active site: Q16 (≠ L23), E139 (≠ D153), D168 (= D186), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R21), V15 (= V22), Q16 (≠ L23), A17 (= A24), R37 (= R44), M73 (= M87), K74 (≠ A88), N95 (= N109), F96 (= F110), A100 (≠ G114), R103 (≠ Q117), K136 (≠ A150), V137 (≠ G151), D168 (= D186), M199 (≠ L221)
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
31% identity, 100% coverage: 1:424/424 of query aligns to 1:416/417 of 1q6yA
- active site: Q17 (≠ L23), E140 (≠ D153), D169 (= D186), G248 (vs. gap), G249 (vs. gap)
- binding coenzyme a: V16 (= V22), Q17 (≠ L23), S18 (≠ A24), R38 (= R44), L72 (≠ I85), N73 (≠ D86), T74 (≠ M87), K75 (≠ A88), N96 (= N109), F97 (= F110), H98 (≠ K111), M105 (≠ Y118), I124 (≠ V137), K137 (≠ A150), A138 (≠ G151), Y139 (= Y152), D169 (= D186), M200 (vs. gap)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
31% identity, 98% coverage: 11:424/424 of query aligns to 4:415/415 of 1pt5A
- active site: Q16 (≠ L23), E139 (≠ D153), D168 (= D186), G247 (vs. gap), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (= V22), S17 (≠ A24), R37 (= R44), L71 (≠ I85), N72 (≠ D86), T73 (≠ M87), K74 (≠ A88), N95 (= N109), F96 (= F110), H97 (≠ K111), K124 (≠ T138), K136 (≠ A150), A137 (≠ G151), Y138 (= Y152), E139 (≠ D153), D168 (= D186), M199 (vs. gap)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
32% identity, 98% coverage: 11:424/424 of query aligns to 4:427/427 of 1t3zA
- active site: Q16 (≠ L23), E139 (≠ D153), S168 (≠ D186), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (≠ R21), V15 (= V22), A17 (= A24), R37 (= R44), K74 (≠ A88), N95 (= N109), F96 (= F110), A100 (≠ G114), R103 (≠ Q117), M104 (≠ Y118), K136 (≠ A150), V137 (≠ G151), Y138 (= Y152), E139 (≠ D153), M199 (≠ L221)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
31% identity, 100% coverage: 1:424/424 of query aligns to 1:409/410 of 1q7eA