SitesBLAST
Comparing Ga0059261_2807 Ga0059261_2807 Predicted acyl-CoA transferases/carnitine dehydratase 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)
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
30% identity, 98% coverage: 8:402/403 of query aligns to 2:416/417 of 1q6yA
- active site: Q17 (≠ L23), E140 (≠ D146), D169 (= D175), G248 (vs. gap), G249 (vs. gap)
- binding coenzyme a: F13 (≠ L19), V16 (= V22), Q17 (≠ L23), S18 (≠ A24), E37 (= E43), R38 (≠ H44), L72 (= L78), N73 (≠ D79), T74 (≠ I80), K75 (≠ S81), N96 (= N102), F97 (≠ Y103), H98 (≠ K104), A101 (≠ G107), M105 (≠ F111), I124 (= I130), K125 (≠ S131), G126 (= G132), K137 (≠ P143), A138 (≠ G144), Y139 (= Y145), D169 (= D175), M200 (≠ L206)
1pt8A Crystal structure of the yfdw gene product of e. Coli, in complex with oxalate and acetyl-coa (see paper)
30% identity, 98% coverage: 8:402/403 of query aligns to 2:416/416 of 1pt8A
- active site: Q17 (≠ L23), E140 (≠ D146), D169 (= D175), G248 (vs. gap), G249 (vs. gap)
- binding acetyl coenzyme *a: V16 (= V22), Q17 (≠ L23), S18 (≠ A24), E37 (= E43), R38 (≠ H44), L72 (= L78), N73 (≠ D79), T74 (≠ I80), K75 (≠ S81), N96 (= N102), F97 (≠ Y103), H98 (≠ K104), A101 (≠ G107), I124 (= I130), K137 (≠ P143), A138 (≠ G144), Y139 (= Y145), D169 (= D175), M200 (≠ L206), G248 (vs. gap), G249 (vs. gap), Q273 (≠ D258)
- binding oxalate ion: Q48 (≠ W54), L49 (≠ G55), E226 (= E227), G249 (vs. gap), Q250 (vs. gap), P251 (≠ H235)
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: 8:402/403 of query aligns to 2:416/416 of P69902
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
30% identity, 98% coverage: 8:402/403 of query aligns to 1:415/415 of 1pt5A
- active site: Q16 (≠ L23), E139 (≠ D146), D168 (= D175), G247 (vs. gap), G248 (vs. gap)
- binding acetyl coenzyme *a: F12 (≠ L19), V15 (= V22), S17 (≠ A24), E36 (= E43), R37 (≠ H44), L71 (= L78), N72 (≠ D79), T73 (≠ I80), K74 (≠ S81), N95 (= N102), F96 (≠ Y103), H97 (≠ K104), A100 (≠ G107), I123 (= I130), K124 (≠ S131), K136 (≠ P143), A137 (≠ G144), Y138 (= Y145), E139 (≠ D146), D168 (= D175), M199 (≠ L206)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
28% identity, 97% coverage: 8:396/403 of query aligns to 2:422/430 of 3ubmB
- active site: Q17 (≠ L23), E140 (≠ D146), D182 (= D175), G261 (vs. gap), G262 (vs. gap)
- binding coenzyme a: F13 (≠ L19), V16 (= V22), S18 (≠ A24), E37 (= E43), R38 (≠ H44), L72 (= L78), N73 (≠ D79), T74 (≠ I80), K75 (≠ S81), N96 (= N102), F97 (≠ Y103), R98 (≠ K104), A101 (≠ G107), R104 (≠ K110), M105 (≠ F111), V124 (≠ I130), K125 (≠ S131), G126 (= G132), A138 (≠ G144), D182 (= D175), M213 (≠ L206)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
29% identity, 98% coverage: 8:402/403 of query aligns to 2:409/410 of 1q7eA
- active site: Q17 (≠ L23), E133 (≠ D146), D162 (= D175), G241 (vs. gap), G242 (vs. gap)
- binding methionine: N96 (= N102), F97 (≠ Y103), H98 (≠ K104), P99 (≠ G112), I117 (= I130), K118 (≠ S131), G119 (= G132), K130 (≠ P143), A131 (≠ G144), M193 (≠ L206), W246 (≠ T237), F299 (≠ D291), F302 (≠ L294), A303 (= A295), E306 (≠ M298)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
29% identity, 98% coverage: 10:402/403 of query aligns to 4:428/428 of O06644
- Q17 (≠ L23) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ H44) 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 (≠ K110) binding
- D169 (= D175) 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)
29% identity, 98% coverage: 10:402/403 of query aligns to 3:427/427 of 1p5rA
- active site: Q16 (≠ L23), E139 (≠ D146), D168 (= D175), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R21), V15 (= V22), Q16 (≠ L23), A17 (= A24), E36 (= E43), R37 (≠ H44), L71 (= L78), D72 (= D79), M73 (≠ I80), K74 (≠ S81), N95 (= N102), F96 (≠ Y103), A100 (≠ G107), R103 (≠ K110), M104 (≠ F111), V123 (≠ I130), K136 (≠ P143), V137 (≠ G144), Y138 (= Y145), D168 (= D175), M199 (≠ L206)
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
29% identity, 98% coverage: 10:402/403 of query aligns to 3:427/427 of 2vjoA
- active site: A16 (≠ L23), E139 (≠ D146), D168 (= D175), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R21), V15 (= V22), A16 (≠ L23), A17 (= A24), E36 (= E43), R37 (≠ H44), M43 (≠ D50), L71 (= L78), D72 (= D79), M73 (≠ I80), K74 (≠ S81), N95 (= N102), F96 (≠ Y103), G97 (≠ K104), A100 (≠ G107), R103 (≠ K110), M104 (≠ F111), V123 (≠ I130), K124 (≠ S131), K136 (≠ P143), V137 (≠ G144), Y138 (= Y145), D168 (= D175), M199 (≠ L206)
- binding oxalate ion: G257 (vs. gap), G258 (vs. gap), G259 (vs. gap), G260 (vs. gap), Q261 (vs. gap)
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
29% identity, 98% coverage: 10:402/403 of query aligns to 3:427/427 of 2vjkA
- active site: Q16 (≠ L23), E139 (≠ D146), D168 (= D175), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R21), V15 (= V22), Q16 (≠ L23), A17 (= A24), E36 (= E43), R37 (≠ H44), L71 (= L78), D72 (= D79), M73 (≠ I80), K74 (≠ S81), N95 (= N102), F96 (≠ Y103), G97 (≠ K104), A100 (≠ G107), R103 (≠ K110), M104 (≠ F111), V123 (≠ I130), K136 (≠ P143), V137 (≠ G144), Y138 (= Y145), D168 (= D175), M199 (≠ L206), G259 (vs. gap), G260 (vs. gap)
- binding magnesium ion: D293 (≠ R267), D296 (= D270)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
30% identity, 93% coverage: 8:383/403 of query aligns to 3:360/360 of 5yx6A