SitesBLAST
Comparing WP_110207561.1 NCBI__GCF_003194585.1:WP_110207561.1 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)
27% identity, 96% coverage: 15:415/416 of query aligns to 6:397/403 of 9br7C
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
26% identity, 96% coverage: 15:414/416 of query aligns to 5:427/430 of 3ubmB
- active site: Q17 (≠ V27), E140 (≠ G154), D182 (vs. gap), G261 (≠ H245), G262 (≠ L246)
- binding coenzyme a: V16 (= V26), R38 (= R51), L72 (= L86), N73 (≠ D87), T74 (≠ L88), K75 (= K89), N96 (≠ S110), F97 (= F111), R98 (≠ S112), A101 (≠ Q115), R104 (≠ K118), K125 (≠ S139), D182 (vs. gap), M213 (≠ Q214)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
24% identity, 95% coverage: 15:409/416 of query aligns to 5:422/428 of O06644
- Q17 (≠ V27) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ S48) binding CoA
- W48 (≠ G64) 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 (≠ K118) binding CoA
- D169 (= D183) 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 (≠ P244) mutation to A: 2.5-fold decrease of the catalytic effiency.
- G260 (≠ H245) mutation to A: 25-fold decrease of the catalytic effiency. Reduction of the affinity binding for both formyl-CoA and oxalate.
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
25% identity, 95% coverage: 15:409/416 of query aligns to 4:421/427 of 2vjoA
- active site: A16 (≠ V27), E139 (≠ G154), D168 (= D183), G259 (≠ A256), G260 (≠ V257)
- binding coenzyme a: H14 (≠ W25), A16 (≠ V27), A17 (= A28), R37 (≠ S48), L71 (= L86), M73 (≠ L88), N95 (≠ S110), F96 (= F111), G97 (≠ S112), R103 (≠ K118), M104 (≠ W119), K136 (≠ A151), V137 (≠ G152), Y138 (≠ F153), D168 (= D183), M199 (≠ Q214)
- binding oxalate ion: G257 (≠ A254), G259 (≠ A256), Q261 (≠ D258)
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
24% identity, 95% coverage: 15:409/416 of query aligns to 4:421/427 of 1p5rA
- active site: Q16 (≠ V27), E139 (≠ G154), D168 (= D183), G259 (≠ H245), G260 (≠ L246)
- binding coenzyme a: H14 (≠ W25), V15 (= V26), Q16 (≠ V27), A17 (= A28), R37 (≠ S48), M73 (≠ L88), K74 (= K89), N95 (≠ S110), F96 (= F111), A100 (≠ Q115), R103 (≠ K118), K136 (≠ A151), V137 (≠ G152), D168 (= D183), M199 (≠ Q214)
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
24% identity, 95% coverage: 15:409/416 of query aligns to 4:421/427 of 2vjkA
- active site: Q16 (≠ V27), E139 (≠ G154), D168 (= D183), G259 (≠ H245), G260 (≠ L246)
- binding coenzyme a: H14 (≠ W25), Q16 (≠ V27), A17 (= A28), R37 (≠ S48), M73 (≠ L88), K74 (= K89), N95 (≠ S110), F96 (= F111), G97 (≠ S112), R103 (≠ K118), M104 (≠ W119), K136 (≠ A151), V137 (≠ G152), Y138 (≠ F153), D168 (= D183), M199 (≠ Q214)
- binding magnesium ion: D293 (≠ R279), D296 (≠ G282)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
24% identity, 95% coverage: 15:409/416 of query aligns to 4:421/427 of 1t4cA
- active site: Q16 (≠ V27), E139 (≠ G154), D168 (= D183), G259 (≠ H245), G260 (≠ L246)
- binding coenzyme a: H14 (≠ W25), V15 (= V26), Q16 (≠ V27), R37 (≠ S48), M73 (≠ L88), N95 (≠ S110), F96 (= F111), R103 (≠ K118), M104 (≠ W119), V137 (≠ G152), Y138 (≠ F153), D168 (= D183), M199 (≠ Q214)
- binding oxalic acid: G259 (≠ H245), G260 (≠ L246)
Q5U921 (R)-2-hydroxy-4-methylpentanoate CoA-transferase; 2-hydroxyisocaproate-CoA transferase; EC 2.8.3.24 from Clostridioides difficile (Peptoclostridium difficile) (see paper)
24% identity, 97% coverage: 15:416/416 of query aligns to 3:398/399 of Q5U921
- D171 (= D183) mutation D->A,N: Loss of activity.
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
24% identity, 95% coverage: 15:409/416 of query aligns to 4:421/427 of 1t3zA
- active site: Q16 (≠ V27), E139 (≠ G154), S168 (≠ D183), G259 (≠ H245), G260 (≠ L246)
- binding oxidized coenzyme a: H14 (≠ W25), V15 (= V26), A17 (= A28), R37 (≠ S48), K74 (= K89), N95 (≠ S110), F96 (= F111), A100 (≠ Q115), R103 (≠ K118), M104 (≠ W119), K136 (≠ A151), V137 (≠ G152), Y138 (≠ F153), E139 (≠ G154), M199 (≠ Q214)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
29% identity, 82% coverage: 15:356/416 of query aligns to 6:326/360 of 5yx6A
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
25% identity, 97% coverage: 10:412/416 of query aligns to 1:412/415 of 1pt5A