SitesBLAST
Comparing WP_043531944.1 NCBI__GCF_000759345.1:WP_043531944.1 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)
41% identity, 99% coverage: 3:393/394 of query aligns to 5:397/403 of 9br7C
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
31% identity, 99% coverage: 3:393/394 of query aligns to 4:428/428 of O06644
- Q17 (≠ M16) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ K37) binding CoA
- W48 (vs. gap) 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 (≠ K101) binding CoA
- D169 (= D166) 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 (≠ K238) mutation to A: 2.5-fold decrease of the catalytic effiency.
- G260 (≠ D239) 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)
31% identity, 99% coverage: 3:393/394 of query aligns to 3:427/427 of 1p5rA
- active site: Q16 (≠ M16), E139 (≠ D137), D168 (= D166), G259 (≠ D239), G260 (= G240)
- binding coenzyme a: H14 (≠ Q14), V15 (≠ I15), Q16 (≠ M16), A17 (= A17), R37 (≠ K37), M73 (≠ L71), K74 (= K72), N95 (= N93), F96 (≠ Y94), A100 (≠ V98), R103 (≠ K101), K136 (≠ G134), V137 (≠ G135), D168 (= D166), M199 (≠ I197)
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
31% identity, 99% coverage: 3:393/394 of query aligns to 3:427/427 of 2vjkA
- active site: Q16 (≠ M16), E139 (≠ D137), D168 (= D166), G259 (≠ D239), G260 (= G240)
- binding coenzyme a: H14 (≠ Q14), Q16 (≠ M16), A17 (= A17), R37 (≠ K37), M73 (≠ L71), K74 (= K72), N95 (= N93), F96 (≠ Y94), G97 (≠ R95), R103 (≠ K101), M104 (≠ L102), K136 (≠ G134), V137 (≠ G135), Y138 (≠ F136), D168 (= D166), M199 (≠ I197)
- binding magnesium ion: D293 (≠ E258), D296 (≠ N261)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
31% identity, 99% coverage: 3:393/394 of query aligns to 3:427/427 of 1t4cA
- active site: Q16 (≠ M16), E139 (≠ D137), D168 (= D166), G259 (≠ D239), G260 (= G240)
- binding coenzyme a: H14 (≠ Q14), V15 (≠ I15), Q16 (≠ M16), R37 (≠ K37), M73 (≠ L71), N95 (= N93), F96 (≠ Y94), R103 (≠ K101), M104 (≠ L102), V137 (≠ G135), Y138 (≠ F136), D168 (= D166), M199 (≠ I197)
- binding oxalic acid: G259 (≠ D239), G260 (= G240)
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
31% identity, 99% coverage: 3:393/394 of query aligns to 3:427/427 of 2vjoA
- active site: A16 (≠ M16), E139 (≠ D137), D168 (= D166), G259 (≠ D239), G260 (= G240)
- binding coenzyme a: H14 (≠ Q14), A16 (≠ M16), A17 (= A17), R37 (≠ K37), L71 (= L69), M73 (≠ L71), N95 (= N93), F96 (≠ Y94), G97 (≠ R95), R103 (≠ K101), M104 (≠ L102), K136 (≠ G134), V137 (≠ G135), Y138 (≠ F136), D168 (= D166), M199 (≠ I197)
- binding oxalate ion: G257 (≠ V237), G259 (≠ D239), Q261 (≠ Y241)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
30% identity, 99% coverage: 3:393/394 of query aligns to 3:427/427 of 1t3zA
- active site: Q16 (≠ M16), E139 (≠ D137), S168 (≠ D166), G259 (≠ D239), G260 (= G240)
- binding oxidized coenzyme a: H14 (≠ Q14), V15 (≠ I15), A17 (= A17), R37 (≠ K37), K74 (= K72), N95 (= N93), F96 (≠ Y94), A100 (≠ V98), R103 (≠ K101), M104 (≠ L102), K136 (≠ G134), V137 (≠ G135), Y138 (≠ F136), E139 (≠ D137), M199 (≠ I197)
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
29% identity, 99% coverage: 3:394/394 of query aligns to 4:417/417 of 1q6yA
- active site: Q17 (≠ M16), E140 (≠ D137), D169 (= D166), G248 (≠ R227), G249 (≠ V228)
- binding coenzyme a: V16 (≠ I15), Q17 (≠ M16), S18 (≠ A17), R38 (≠ K37), L72 (= L69), N73 (= N70), T74 (≠ L71), K75 (= K72), N96 (= N93), F97 (≠ Y94), H98 (≠ R95), M105 (≠ L102), I124 (= I121), K137 (≠ G134), A138 (≠ G135), Y139 (≠ F136), D169 (= D166), M200 (≠ I197)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
29% identity, 99% coverage: 3:393/394 of query aligns to 3:415/415 of 1pt5A
- active site: Q16 (≠ M16), E139 (≠ D137), D168 (= D166), G247 (≠ R227), G248 (≠ V228)
- binding acetyl coenzyme *a: V15 (≠ I15), S17 (≠ A17), R37 (≠ K37), L71 (= L69), N72 (= N70), T73 (≠ L71), K74 (= K72), N95 (= N93), F96 (≠ Y94), H97 (≠ R95), K124 (≠ S122), K136 (≠ G134), A137 (≠ G135), Y138 (≠ F136), E139 (≠ D137), D168 (= D166), M199 (≠ I197)
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, 99% coverage: 3:393/394 of query aligns to 4:416/416 of P69902
Q5U921 (R)-2-hydroxy-4-methylpentanoate CoA-transferase; 2-hydroxyisocaproate-CoA transferase; EC 2.8.3.24 from Clostridioides difficile (Peptoclostridium difficile) (see paper)
32% identity, 99% coverage: 4:394/394 of query aligns to 3:398/399 of Q5U921