SitesBLAST
Comparing WP_073037622.1 NCBI__GCF_900129305.1:WP_073037622.1 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)
46% identity, 99% coverage: 5:399/400 of query aligns to 4:397/403 of 9br7C
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
35% identity, 98% coverage: 6:395/400 of query aligns to 3:411/415 of 1pt5A
- active site: Q16 (≠ L19), E139 (≠ D142), D168 (= D171), G247 (vs. gap), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (= V18), S17 (≠ A20), R37 (= R40), L71 (≠ V74), N72 (≠ D75), T73 (≠ L76), K74 (= K77), N95 (= N98), F96 (≠ Y99), H97 (≠ K100), K124 (≠ T127), K136 (≠ P139), A137 (≠ G140), Y138 (= Y141), E139 (≠ D142), D168 (= D171), M199 (≠ L202)
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
35% identity, 98% coverage: 6:395/400 of query aligns to 4:412/417 of 1q6yA
- active site: Q17 (≠ L19), E140 (≠ D142), D169 (= D171), G248 (vs. gap), G249 (vs. gap)
- binding coenzyme a: V16 (= V18), Q17 (≠ L19), S18 (≠ A20), R38 (= R40), L72 (≠ V74), N73 (≠ D75), T74 (≠ L76), K75 (= K77), N96 (= N98), F97 (≠ Y99), H98 (≠ K100), M105 (= M107), I124 (= I126), K137 (≠ P139), A138 (≠ G140), Y139 (= Y141), D169 (= D171), M200 (≠ L202)
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)
35% identity, 98% coverage: 6:395/400 of query aligns to 4:412/416 of P69902
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
34% identity, 98% coverage: 6:395/400 of query aligns to 4:405/410 of 1q7eA
- active site: Q17 (≠ L19), E133 (≠ D142), D162 (= D171), G241 (vs. gap), G242 (vs. gap)
- binding methionine: N96 (= N98), F97 (≠ Y99), H98 (≠ K100), P99 (≠ V101), K118 (≠ T127), K130 (≠ P139), A131 (≠ G140), W246 (vs. gap), F299 (≠ D287), A303 (≠ P291), E306 (≠ A294)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
33% identity, 98% coverage: 4:395/400 of query aligns to 2:424/430 of 3ubmB
- active site: Q17 (≠ L19), E140 (≠ D142), D182 (= D171), G261 (vs. gap), G262 (vs. gap)
- binding coenzyme a: V16 (= V18), R38 (= R40), L72 (≠ V74), N73 (≠ D75), T74 (≠ L76), K75 (= K77), N96 (= N98), F97 (≠ Y99), R98 (≠ K100), A101 (≠ T103), R104 (≠ K106), K125 (≠ T127), D182 (= D171), M213 (≠ L202)
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
31% identity, 99% coverage: 5:399/400 of query aligns to 2:427/427 of 1p5rA
- active site: Q16 (≠ L19), E139 (≠ D142), D168 (= D171), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R17), V15 (= V18), Q16 (≠ L19), A17 (= A20), R37 (= R40), M73 (≠ L76), K74 (= K77), N95 (= N98), F96 (≠ Y99), A100 (≠ T103), R103 (≠ K106), K136 (≠ P139), V137 (≠ G140), D168 (= D171), M199 (≠ L202)
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: 5:399/400 of query aligns to 3:428/428 of O06644
- Q17 (≠ L19) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (= R40) binding CoA
- W48 (= W50) 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 (≠ K106) binding CoA
- D169 (= D171) 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.
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
31% identity, 99% coverage: 5:399/400 of query aligns to 2:427/427 of 2vjoA
- active site: A16 (≠ L19), E139 (≠ D142), D168 (= D171), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R17), A16 (≠ L19), A17 (= A20), R37 (= R40), L71 (≠ V74), M73 (≠ L76), N95 (= N98), F96 (≠ Y99), G97 (≠ K100), R103 (≠ K106), M104 (= M107), K136 (≠ P139), V137 (≠ G140), Y138 (= Y141), D168 (= D171), M199 (≠ L202)
- binding oxalate ion: G257 (vs. gap), G259 (vs. gap), Q261 (vs. gap)
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
31% identity, 99% coverage: 5:399/400 of query aligns to 2:427/427 of 2vjkA
- active site: Q16 (≠ L19), E139 (≠ D142), D168 (= D171), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R17), Q16 (≠ L19), A17 (= A20), R37 (= R40), M73 (≠ L76), K74 (= K77), N95 (= N98), F96 (≠ Y99), G97 (≠ K100), R103 (≠ K106), M104 (= M107), K136 (≠ P139), V137 (≠ G140), Y138 (= Y141), D168 (= D171), M199 (≠ L202)
- binding magnesium ion: D293 (≠ R263), D296 (≠ G266)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
31% identity, 99% coverage: 5:399/400 of query aligns to 2:427/427 of 1t4cA