SitesBLAST
Comparing YP_004142287.1 NCBI__GCF_000185905.1:YP_004142287.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
9br7C Succinate--hydroxymethylglutarate CoA-transferase (see paper)
40% identity, 98% coverage: 5:386/391 of query aligns to 5:380/403 of 9br7C
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)
28% identity, 98% coverage: 5:386/391 of query aligns to 4:400/416 of P69902
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
28% identity, 98% coverage: 5:386/391 of query aligns to 3:399/415 of 1pt5A
- active site: Q16 (≠ L18), E139 (≠ D147), D168 (= D176), G247 (vs. gap), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (≠ I17), S17 (≠ A19), R37 (≠ S39), L71 (≠ I79), N72 (≠ D80), T73 (≠ F81), K74 (≠ S82), N95 (= N103), F96 (= F104), H97 (≠ K105), K124 (≠ T132), K136 (≠ A144), A137 (≠ G145), Y138 (= Y146), E139 (≠ D147), D168 (= D176), M199 (≠ L207)
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
28% identity, 98% coverage: 5:386/391 of query aligns to 4:400/417 of 1q6yA
- active site: Q17 (≠ L18), E140 (≠ D147), D169 (= D176), G248 (vs. gap), G249 (vs. gap)
- binding coenzyme a: V16 (≠ I17), Q17 (≠ L18), S18 (≠ A19), R38 (≠ S39), L72 (≠ I79), N73 (≠ D80), T74 (≠ F81), K75 (≠ S82), N96 (= N103), F97 (= F104), H98 (≠ K105), M105 (≠ Y112), I124 (= I131), K137 (≠ A144), A138 (≠ G145), Y139 (= Y146), D169 (= D176), M200 (≠ L207)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
30% identity, 97% coverage: 5:383/391 of query aligns to 5:360/360 of 5yx6A
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
28% identity, 98% coverage: 5:386/391 of query aligns to 4:393/410 of 1q7eA
- active site: Q17 (≠ L18), E133 (≠ D147), D162 (= D176), G241 (vs. gap), G242 (vs. gap)
- binding methionine: N96 (= N103), F97 (= F104), H98 (≠ Y112), P99 (≠ G113), K118 (≠ T132), K130 (≠ A144), A131 (≠ G145), W246 (vs. gap), F299 (≠ V291), A303 (≠ E295), E306 (≠ I298)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
26% identity, 99% coverage: 5:391/391 of query aligns to 4:417/430 of 3ubmB
- active site: Q17 (≠ L18), E140 (≠ D147), D182 (= D176), G261 (vs. gap), G262 (vs. gap)
- binding coenzyme a: V16 (≠ I17), R38 (≠ S39), L72 (≠ I79), N73 (≠ D80), T74 (≠ F81), K75 (≠ S82), N96 (= N103), F97 (= F104), R98 (≠ K105), A101 (≠ G108), R104 (≠ K111), K125 (≠ T132), D182 (= D176), M213 (≠ L207)
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
27% identity, 98% coverage: 5:386/391 of query aligns to 3:411/427 of 1p5rA
- active site: Q16 (≠ L18), E139 (≠ D147), D168 (= D176), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R16), V15 (≠ I17), Q16 (≠ L18), A17 (= A19), R37 (≠ S39), M73 (≠ F81), K74 (≠ S82), N95 (= N103), F96 (= F104), A100 (≠ G108), R103 (≠ K111), K136 (≠ A144), V137 (≠ G145), D168 (= D176), M199 (≠ L207)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
27% identity, 98% coverage: 5:386/391 of query aligns to 4:412/428 of O06644
- Q17 (≠ L18) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ S39) binding CoA
- W48 (= W49) 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 (≠ K111) binding CoA
- D169 (= D176) 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)
27% identity, 98% coverage: 5:386/391 of query aligns to 3:411/427 of 2vjkA
- active site: Q16 (≠ L18), E139 (≠ D147), D168 (= D176), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R16), Q16 (≠ L18), A17 (= A19), R37 (≠ S39), M73 (≠ F81), K74 (≠ S82), N95 (= N103), F96 (= F104), G97 (≠ K105), R103 (≠ K111), M104 (≠ Y112), K136 (≠ A144), V137 (≠ G145), Y138 (= Y146), D168 (= D176), M199 (≠ L207)
- binding magnesium ion: D293 (≠ A267), D296 (≠ G270)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
27% identity, 98% coverage: 5:386/391 of query aligns to 3:411/427 of 1t4cA
- active site: Q16 (≠ L18), E139 (≠ D147), D168 (= D176), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R16), V15 (≠ I17), Q16 (≠ L18), R37 (≠ S39), M73 (≠ F81), N95 (= N103), F96 (= F104), R103 (≠ K111), M104 (≠ Y112), V137 (≠ G145), Y138 (= Y146), D168 (= D176), M199 (≠ L207)
- binding oxalic acid: G259 (vs. gap), G260 (vs. gap)
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
27% identity, 98% coverage: 5:386/391 of query aligns to 3:411/427 of 2vjoA