SitesBLAST
Comparing AO356_18985 FitnessBrowser__pseudo5_N2C3_1:AO356_18985 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: 5:392/393 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 (= G191) to D: in dbSNP:rs10941112
- L201 (= L216) to S: in dbSNP:rs2287939
- M261 (≠ L273) to T: in dbSNP:rs3195678
- E277 (≠ K293) to K: in dbSNP:rs2278008
Sites not aligning to the query:
- 380:382 Microbody targeting signal
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
39% identity, 84% coverage: 1:329/393 of query aligns to 1:317/360 of O06543
- R38 (≠ S38) binding
- 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 (≠ LDLK 71:74) binding
- E82 (= E94) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ QFR 95:97) binding
- R91 (= R103) binding ; 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
- H126 (= H138) mutation to A: 4.5% of wild-type activity.
- D156 (= D168) mutation to A: 17.6 of wild-type activity.
- D190 (= D202) 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 (≠ Q324) mutation to A: 10.1% of wild-type activity.
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)
39% identity, 83% coverage: 3:329/393 of query aligns to 2:311/354 of 2gd6A
- active site: G16 (≠ L17), D121 (= D139), D150 (= D168), G213 (= G231), G214 (= G232)
- binding acetyl coenzyme *a: I15 (≠ L16), R37 (≠ S38), A53 (≠ L71), D54 (= D72), L55 (= L73), K56 (= K74), G77 (≠ Q95), Y78 (≠ F96), R79 (= R97), V82 (= V100), R85 (= R103), G119 (= G137), H120 (= H138), Y124 (= Y142), D150 (= D168), M182 (= M200)
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)
39% identity, 83% coverage: 3:329/393 of query aligns to 2:311/354 of 2gd2A
- active site: G16 (≠ L17), D121 (= D139), D150 (= D168), G213 (= G231), G214 (= G232)
- binding acetoacetyl-coenzyme a: I15 (≠ L16), R37 (≠ S38), A53 (≠ L71), L55 (= L73), K56 (= K74), G77 (≠ Q95), Y78 (≠ F96), R79 (= R97), V82 (= V100), R85 (= R103), L86 (= L104), A118 (= A136), G119 (= G137), H120 (= H138), Y124 (= Y142), D150 (= D168)
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)
39% identity, 83% coverage: 3:329/393 of query aligns to 2:311/354 of 2gd0A
- active site: G16 (≠ L17), D121 (= D139), D150 (= D168), G213 (= G231), G214 (= G232)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D43), L55 (= L73), K56 (= K74), G77 (≠ Q95), Y78 (≠ F96), R79 (= R97), V82 (= V100), R85 (= R103), L86 (= L104), G119 (= G137), H120 (= H138), D121 (= D139), Y124 (= Y142), D150 (= D168)
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)
39% identity, 83% coverage: 3:329/393 of query aligns to 2:311/354 of 2gciA
- active site: G16 (≠ L17), D121 (= D139), D150 (= D168), G213 (= G231), G214 (= G232)
- binding (r)-2-methylmyristoyl-coenzyme a: R37 (≠ S38), L55 (= L73), K56 (= K74), G77 (≠ Q95), Y78 (≠ F96), R79 (= R97), V82 (= V100), G119 (= G137), H120 (= H138), D121 (= D139), Y124 (= Y142), D150 (= D168), 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)
39% identity, 83% coverage: 3:329/393 of query aligns to 2:311/354 of 2gceA
- active site: G16 (≠ L17), D121 (= D139), D150 (= D168), G213 (= G231), G214 (= G232)
- binding (r)-ibuprofenoyl-coenzyme a: I15 (≠ L16), R37 (≠ S38), L55 (= L73), K56 (= K74), G77 (≠ Q95), Y78 (≠ F96), R79 (= R97), V82 (= V100), R85 (= R103), G119 (= G137), H120 (= H138), D121 (= D139), Y124 (= Y142), D150 (= D168), L211 (= L229), Y218 (= Y235), I234 (≠ L251)
- binding (s)-ibuprofenoyl-coenzyme a: I15 (≠ L16), G16 (≠ L17), P17 (= P18), R37 (≠ S38), L55 (= L73), K56 (= K74), G77 (≠ Q95), Y78 (≠ F96), R79 (= R97), V82 (= V100), R85 (= R103), G119 (= G137), H120 (= H138), Y124 (= Y142), D150 (= D168)
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)
39% identity, 83% coverage: 3:329/393 of query aligns to 2:312/355 of 2yimA
- active site: G16 (≠ L17), D122 (= D139), D151 (= D168), G214 (= G231), G215 (= G232)
- binding 2-methylacetoacetyl coa: I15 (≠ L16), R37 (≠ S38), A54 (≠ L71), L56 (= L73), K57 (= K74), G78 (≠ Q95), Y79 (≠ F96), R80 (= R97), V83 (= V100), R86 (= R103), L87 (= L104), A119 (= A136), G120 (= G137), H121 (= H138), Y125 (= Y142), D151 (= D168)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
30% identity, 99% coverage: 4:392/393 of query aligns to 4:428/430 of 3ubmB
- active site: Q17 (≠ L17), E140 (≠ D139), D182 (≠ G171), G261 (vs. gap), G262 (vs. gap)
- binding coenzyme a: V16 (≠ L16), R38 (≠ S38), L72 (= L71), N73 (≠ D72), T74 (≠ L73), K75 (= K74), N96 (≠ Q95), F97 (= F96), R98 (= R97), A101 (≠ V100), R104 (= R103), K125 (≠ T124), D182 (≠ G171), M213 (= M200)
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: 1:392/393 of query aligns to 1:416/416 of P69902
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
30% identity, 99% coverage: 4:392/393 of query aligns to 3:415/415 of 1pt5A
- active site: Q16 (≠ L17), E139 (≠ D139), D168 (= D168), G247 (vs. gap), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (≠ L16), S17 (≠ P18), R37 (≠ S38), L71 (= L71), N72 (≠ D72), T73 (≠ L73), K74 (= K74), N95 (≠ Q95), F96 (= F96), H97 (≠ R97), K124 (≠ T124), K136 (≠ A136), A137 (≠ G137), Y138 (≠ H138), E139 (≠ D139), D168 (= D168), M199 (= M200)
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
30% identity, 100% coverage: 1:392/393 of query aligns to 1:416/417 of 1q6yA
- active site: Q17 (≠ L17), E140 (≠ D139), D169 (= D168), G248 (vs. gap), G249 (vs. gap)
- binding coenzyme a: V16 (≠ L16), Q17 (≠ L17), S18 (≠ P18), R38 (≠ S38), L72 (= L71), N73 (≠ D72), T74 (≠ L73), K75 (= K74), N96 (≠ Q95), F97 (= F96), H98 (≠ R97), M105 (≠ L104), I124 (= I123), K137 (≠ A136), A138 (≠ G137), Y139 (≠ H138), D169 (= D168), M200 (= M200)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
29% identity, 100% coverage: 1:392/393 of query aligns to 1:409/410 of 1q7eA
- active site: Q17 (≠ L17), E133 (≠ D139), D162 (= D168), G241 (vs. gap), G242 (vs. gap)
- binding methionine: N96 (≠ Q95), F97 (= F96), H98 (≠ R97), P99 (= P98), K118 (≠ T124), K130 (≠ A136), A131 (≠ G137), W246 (≠ Q227), F299 (≠ Q285), A303 (≠ T289), E306 (= E292)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
34% identity, 67% coverage: 4:268/393 of query aligns to 5:256/360 of 5yx6A
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
33% identity, 53% coverage: 1:207/393 of query aligns to 1:207/428 of O06644
- Q17 (≠ L17) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ S38) binding
- W48 (≠ L48) 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
- D169 (= D168) 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.
Sites not aligning to the query:
- 259 G→A: 2.5-fold decrease of the catalytic effiency.
- 260 G→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)
33% identity, 52% coverage: 4:207/393 of query aligns to 3:206/427 of 2vjoA
- active site: A16 (≠ L17), E139 (vs. gap), D168 (= D168)
- binding coenzyme a: H14 (≠ T15), A16 (≠ L17), A17 (≠ P18), R37 (≠ S38), L71 (= L71), M73 (≠ L73), N95 (≠ Q95), F96 (= F96), G97 (≠ R97), R103 (= R103), M104 (≠ L104), K136 (≠ A144), V137 (≠ L145), Y138 (vs. gap), D168 (= D168), M199 (= M200)
Sites not aligning to the query:
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
33% identity, 52% coverage: 4:207/393 of query aligns to 3:206/427 of 1p5rA
- active site: Q16 (≠ L17), E139 (vs. gap), D168 (= D168)
- binding coenzyme a: H14 (≠ T15), V15 (≠ L16), Q16 (≠ L17), A17 (≠ P18), R37 (≠ S38), M73 (≠ L73), K74 (= K74), N95 (≠ Q95), F96 (= F96), A100 (≠ V100), R103 (= R103), K136 (≠ A144), V137 (≠ L145), D168 (= D168), M199 (= M200)
Sites not aligning to the query:
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
33% identity, 52% coverage: 4:207/393 of query aligns to 3:206/427 of 2vjkA
- active site: Q16 (≠ L17), E139 (vs. gap), D168 (= D168)
- binding coenzyme a: H14 (≠ T15), Q16 (≠ L17), A17 (≠ P18), R37 (≠ S38), M73 (≠ L73), K74 (= K74), N95 (≠ Q95), F96 (= F96), G97 (≠ R97), R103 (= R103), M104 (≠ L104), K136 (≠ A144), V137 (≠ L145), Y138 (vs. gap), D168 (= D168), M199 (= M200)
Sites not aligning to the query:
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
33% identity, 52% coverage: 4:207/393 of query aligns to 3:206/427 of 1t4cA
- active site: Q16 (≠ L17), E139 (vs. gap), D168 (= D168)
- binding coenzyme a: H14 (≠ T15), V15 (≠ L16), Q16 (≠ L17), R37 (≠ S38), M73 (≠ L73), N95 (≠ Q95), F96 (= F96), R103 (= R103), M104 (≠ L104), V137 (≠ L145), Y138 (vs. gap), D168 (= D168), M199 (= M200)
Sites not aligning to the query:
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
33% identity, 52% coverage: 4:207/393 of query aligns to 3:206/427 of 1t3zA
- active site: Q16 (≠ L17), E139 (vs. gap), S168 (≠ I169)
- binding oxidized coenzyme a: H14 (≠ T15), V15 (≠ L16), A17 (≠ P18), R37 (≠ S38), K74 (= K74), N95 (≠ Q95), F96 (= F96), A100 (≠ V100), R103 (= R103), M104 (≠ L104), K136 (≠ A144), V137 (≠ L145), Y138 (vs. gap), E139 (vs. gap), M199 (= M200)
Sites not aligning to the query:
Query Sequence
>AO356_18985 FitnessBrowser__pseudo5_N2C3_1:AO356_18985
MQGPLASLKVLDFSTLLPGPFASLLLADMGAEVLRIESPTRQDLLRVLPPHDQGVSASHA
YLNRNKRSLALDLKQPEALEVVTQLLGDYDILLEQFRPGVMERLGLGYEALKAINPRLIY
VSITGYGQTGPYKDRAGHDINYLALAGLASHTGRADSGPLPLGIQAADIAGGSLHGVIGL
LAAVIARQQTGQGQHLDVSMTDCVFSLNAMAGAGYLACGVEPGWENQMLNGGGFYDYYRT
RDGRWMSVGSLEPAFMQALCEALGRPELAAQGLSPKPEQQQALKQALQTEFEKHDFAELC
DVFAGIDACVEPVLSLEEAVRHPQLQARELVKQVPRGDGSSQAQMACPLRFSDGLPEPRH
IGVELGAHTDQVLGALGFSALRIAELRRSGVVL
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory