SitesBLAST
Comparing WP_073038547.1 NCBI__GCF_900129305.1:WP_073038547.1 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)
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
38% identity, 99% coverage: 5:392/392 of query aligns to 3:373/382 of Q9UHK6
- V9 (≠ L11) to M: in dbSNP:rs3195676
- S52 (= S68) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ I123) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G190) to D: in dbSNP:rs10941112
- L201 (= L215) to S: in dbSNP:rs2287939
- M261 (≠ P276) to T: in dbSNP:rs3195678
- E277 (≠ G293) to K: in dbSNP:rs2278008
Sites not aligning to the query:
- 380:382 Microbody targeting signal
9br7C Succinate--hydroxymethylglutarate CoA-transferase (see paper)
35% identity, 99% coverage: 4:392/392 of query aligns to 5:397/403 of 9br7C
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
37% identity, 91% coverage: 1:355/392 of query aligns to 1:338/360 of O06543
- R38 (≠ D38) binding substrate
- R52 (= R64) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S68) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ LNLK 71:74) binding substrate
- E82 (= E94) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ GFR 95:97) binding substrate
- R91 (= R103) binding substrate; mutation to A: 19.9% of wild-type activity.
- M111 (≠ I123) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (= GHDINY 137:142) binding substrate
- H126 (= H138) mutation to A: 4.5% of wild-type activity.
- D156 (= D167) mutation to A: 17.6 of wild-type activity.
- D190 (= D201) mutation to A: 3.3% of wild-type activity.
- E241 (= E252) mutation to A: 2.1% of wild-type activity.
- C297 (= C309) mutation to A: 6.2% of wild-type activity.
- H312 (≠ A324) mutation to A: 10.1% of wild-type activity.
2yimA The enolisation chemistry of a thioester-dependent racemase: the 1.4 a crystal structure of a complex with a planar reaction intermediate analogue (see paper)
36% identity, 90% coverage: 2:355/392 of query aligns to 1:333/355 of 2yimA
- active site: G16 (≠ L17), D122 (= D139), D151 (= D167), G214 (≠ H230), G215 (= G231)
- binding 2-methylacetoacetyl coa: I15 (≠ L16), R37 (≠ D38), A54 (≠ L71), L56 (= L73), K57 (= K74), G78 (= G95), Y79 (≠ F96), R80 (= R97), V83 (= V100), R86 (= R103), L87 (= L104), A119 (= A136), G120 (= G137), H121 (= H138), Y125 (= Y142), D151 (= D167)
2gd6A The 1,1-proton transfer reaction mechanism by alpha-methylacyl-coa racemase is catalyzed by an aspartate/histidine pair and involves a smooth, methionine-rich surface for binding the fatty acyl moiety (see paper)
37% identity, 90% coverage: 2:355/392 of query aligns to 1:332/354 of 2gd6A
- active site: G16 (≠ L17), D121 (= D139), D150 (= D167), G213 (≠ H230), G214 (= G231)
- binding acetyl coenzyme *a: I15 (≠ L16), R37 (≠ D38), A53 (≠ L71), D54 (≠ N72), L55 (= L73), K56 (= K74), G77 (= G95), Y78 (≠ F96), R79 (= R97), V82 (= V100), R85 (= R103), G119 (= G137), H120 (= H138), Y124 (= Y142), D150 (= D167), M182 (= M199)
2gd2A The 1,1-proton transfer reaction mechanism by alpha-methylacyl-coa racemase is catalyzed by an aspartate/histidine pair and involves a smooth, methionine-rich surface for binding the fatty acyl moiety (see paper)
37% identity, 90% coverage: 2:355/392 of query aligns to 1:332/354 of 2gd2A
- active site: G16 (≠ L17), D121 (= D139), D150 (= D167), G213 (≠ H230), G214 (= G231)
- binding acetoacetyl-coenzyme a: I15 (≠ L16), R37 (≠ D38), A53 (≠ L71), L55 (= L73), K56 (= K74), G77 (= G95), Y78 (≠ F96), R79 (= R97), V82 (= V100), R85 (= R103), L86 (= L104), A118 (= A136), G119 (= G137), H120 (= H138), Y124 (= Y142), D150 (= D167)
2gd0A The 1,1-proton transfer reaction mechanism by alpha-methylacyl-coa racemase is catalyzed by an aspartate/histidine pair and involves a smooth, methionine-rich surface for binding the fatty acyl moiety (see paper)
37% identity, 90% coverage: 2:355/392 of query aligns to 1:332/354 of 2gd0A
- active site: G16 (≠ L17), D121 (= D139), D150 (= D167), G213 (≠ H230), G214 (= G231)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D43), L55 (= L73), K56 (= K74), G77 (= G95), Y78 (≠ F96), R79 (= R97), V82 (= V100), R85 (= R103), L86 (= L104), G119 (= G137), H120 (= H138), D121 (= D139), Y124 (= Y142), D150 (= D167)
2gciA The 1,1-proton transfer reaction mechanism by alpha-methylacyl-coa racemase is catalyzed by an asparte/histidine pair and involves a smooth, methionine-rich surface for binding the fatty acyl moiety (see paper)
37% identity, 90% coverage: 2:355/392 of query aligns to 1:332/354 of 2gciA
- active site: G16 (≠ L17), D121 (= D139), D150 (= D167), G213 (≠ H230), G214 (= G231)
- binding (r)-2-methylmyristoyl-coenzyme a: R37 (≠ D38), L55 (= L73), K56 (= K74), G77 (= G95), Y78 (≠ F96), R79 (= R97), V82 (= V100), G119 (= G137), H120 (= H138), D121 (= D139), Y124 (= Y142), D150 (= D167), Y218 (= Y235), I234 (≠ L251), E235 (= E252)
2gceA The 1,1-proton transfer reaction mechanism by alpha-methylacyl-coa racemase is catalyzed by an aspartate/histidine pair and involves a smooth, methionine-rich surface for binding the fatty acyl moiety (see paper)
37% identity, 90% coverage: 2:355/392 of query aligns to 1:332/354 of 2gceA
- active site: G16 (≠ L17), D121 (= D139), D150 (= D167), G213 (≠ H230), G214 (= G231)
- binding (r)-ibuprofenoyl-coenzyme a: I15 (≠ L16), R37 (≠ D38), L55 (= L73), K56 (= K74), G77 (= G95), Y78 (≠ F96), R79 (= R97), V82 (= V100), R85 (= R103), G119 (= G137), H120 (= H138), D121 (= D139), Y124 (= Y142), D150 (= D167), L211 (= L228), Y218 (= Y235), I234 (≠ L251)
- binding (s)-ibuprofenoyl-coenzyme a: I15 (≠ L16), G16 (≠ L17), P17 (= P18), R37 (≠ D38), L55 (= L73), K56 (= K74), G77 (= G95), Y78 (≠ F96), R79 (= R97), V82 (= V100), R85 (= R103), G119 (= G137), H120 (= H138), Y124 (= Y142), D150 (= D167)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
32% identity, 100% coverage: 2:392/392 of query aligns to 2:428/430 of 3ubmB
- active site: Q17 (≠ L17), E140 (≠ D139), D182 (vs. gap), G261 (≠ N229), G262 (≠ H230)
- binding coenzyme a: V16 (≠ L16), R38 (≠ D38), L72 (= L71), N73 (= N72), T74 (≠ L73), K75 (= K74), N96 (≠ G95), F97 (= F96), R98 (= R97), A101 (≠ V100), R104 (= R103), K125 (≠ T124), D182 (vs. gap), M213 (= M199)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
29% identity, 100% coverage: 1:392/392 of query aligns to 1:428/428 of O06644
- Q17 (≠ L17) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ D38) binding CoA
- W48 (= W47) 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 (= R103) binding CoA
- D169 (= D167) 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.
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)
30% identity, 100% coverage: 1:392/392 of query aligns to 1:416/416 of P69902