SitesBLAST
Comparing WP_076582976.1 NCBI__GCF_001971705.1:WP_076582976.1 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)
35% identity, 98% coverage: 6:402/404 of query aligns to 4:401/403 of 9br7C
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
28% identity, 98% coverage: 5:400/404 of query aligns to 2:430/430 of 3ubmB
- active site: Q17 (≠ V20), E140 (≠ D143), D182 (= D172), G261 (= G228), G262 (≠ T229)
- binding coenzyme a: V16 (≠ F19), R38 (≠ Q41), L72 (= L75), N73 (≠ D76), T74 (≠ L77), K75 (= K78), N96 (= N99), F97 (= F100), R98 (= R101), A101 (≠ T104), R104 (= R107), K125 (≠ S128), D182 (= D172), M213 (= M203)
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)
27% identity, 96% coverage: 8:394/404 of query aligns to 5:412/416 of P69902
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
27% identity, 96% coverage: 8:394/404 of query aligns to 4:411/415 of 1pt5A
- active site: Q16 (≠ V20), E139 (≠ D143), D168 (= D172), G247 (= G228), G248 (≠ T229)
- binding acetyl coenzyme *a: V15 (≠ F19), S17 (≠ T21), R37 (≠ Q41), L71 (= L75), N72 (≠ D76), T73 (≠ L77), K74 (= K78), N95 (= N99), F96 (= F100), H97 (≠ R101), K124 (≠ S128), K136 (≠ A140), A137 (≠ G141), Y138 (= Y142), E139 (≠ D143), D168 (= D172), M199 (= M203)
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
27% identity, 96% coverage: 8:394/404 of query aligns to 5:412/417 of 1q6yA
- active site: Q17 (≠ V20), E140 (≠ D143), D169 (= D172), G248 (= G228), G249 (≠ T229)
- binding coenzyme a: V16 (≠ F19), Q17 (≠ V20), S18 (≠ T21), R38 (≠ Q41), L72 (= L75), N73 (≠ D76), T74 (≠ L77), K75 (= K78), N96 (= N99), F97 (= F100), H98 (≠ R101), M105 (≠ L108), I124 (= I127), K137 (≠ A140), A138 (≠ G141), Y139 (= Y142), D169 (= D172), M200 (= M203)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
30% identity, 92% coverage: 6:375/404 of query aligns to 4:356/360 of 5yx6A
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
27% identity, 96% coverage: 8:394/404 of query aligns to 5:405/410 of 1q7eA
- active site: Q17 (≠ V20), E133 (≠ D143), D162 (= D172), G241 (= G228), G242 (≠ T229)
- binding methionine: N96 (= N99), F97 (= F100), H98 (≠ R101), P99 (= P102), K118 (≠ S128), K130 (≠ A140), A131 (≠ G141), W246 (≠ V233), F299 (≠ D286), A303 (= A290), E306 (= E293)
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
26% identity, 97% coverage: 6:397/404 of query aligns to 2:426/427 of 2vjoA
- active site: A16 (≠ V20), E139 (≠ D143), D168 (= D172), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T18), A16 (≠ V20), A17 (≠ T21), R37 (≠ Q41), L71 (= L75), M73 (≠ L77), N95 (= N99), F96 (= F100), G97 (≠ R101), R103 (= R107), M104 (≠ L108), K136 (≠ A140), V137 (≠ G141), Y138 (= Y142), D168 (= D172), M199 (= M203)
- binding oxalate ion: G257 (vs. gap), G259 (vs. gap), Q261 (vs. gap)
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
26% identity, 97% coverage: 6:397/404 of query aligns to 2:426/427 of 1p5rA
- active site: Q16 (≠ V20), E139 (≠ D143), D168 (= D172), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T18), V15 (≠ F19), Q16 (≠ V20), A17 (≠ T21), R37 (≠ Q41), M73 (≠ L77), K74 (= K78), N95 (= N99), F96 (= F100), A100 (≠ T104), R103 (= R107), K136 (≠ A140), V137 (≠ G141), D168 (= D172), M199 (= M203)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
26% identity, 97% coverage: 6:397/404 of query aligns to 3:427/428 of O06644
- Q17 (≠ V20) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ Q41) binding CoA
- W48 (≠ S51) 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 (= R107) binding CoA
- D169 (= D172) 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.
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
26% identity, 97% coverage: 6:397/404 of query aligns to 2:426/427 of 2vjkA