SitesBLAST
Comparing Ac3H11_3532 FitnessBrowser__acidovorax_3H11:Ac3H11_3532 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)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
32% identity, 98% coverage: 7:423/424 of query aligns to 1:427/430 of 3ubmB
- active site: Q17 (≠ L23), E140 (≠ D153), D182 (= D186), G261 (vs. gap), G262 (vs. gap)
- binding coenzyme a: V16 (= V22), R38 (= R44), L72 (≠ I85), N73 (≠ D86), T74 (≠ M87), K75 (≠ A88), N96 (= N109), F97 (= F110), R98 (≠ K111), A101 (≠ G114), R104 (≠ Q117), K125 (≠ T138), D182 (= D186), M213 (= M219)
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)
32% identity, 100% coverage: 1:424/424 of query aligns to 1:416/416 of P69902
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
32% identity, 98% coverage: 11:424/424 of query aligns to 4:427/427 of 2vjoA
- active site: A16 (≠ L23), E139 (≠ D153), D168 (= D186), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R21), A16 (≠ L23), A17 (= A24), R37 (= R44), L71 (≠ I85), M73 (= M87), N95 (= N109), F96 (= F110), G97 (≠ K111), R103 (≠ Q117), M104 (≠ Y118), K136 (≠ A150), V137 (≠ G151), Y138 (= Y152), D168 (= D186), M199 (≠ L221)
- 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)
32% identity, 98% coverage: 11:424/424 of query aligns to 4:427/427 of 2vjkA
- active site: Q16 (≠ L23), E139 (≠ D153), D168 (= D186), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R21), Q16 (≠ L23), A17 (= A24), R37 (= R44), M73 (= M87), K74 (≠ A88), N95 (= N109), F96 (= F110), G97 (≠ K111), R103 (≠ Q117), M104 (≠ Y118), K136 (≠ A150), V137 (≠ G151), Y138 (= Y152), D168 (= D186), M199 (≠ L221)
- binding magnesium ion: D293 (≠ A281), D296 (≠ N284)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
32% identity, 98% coverage: 11:424/424 of query aligns to 4:427/427 of 1t4cA
- active site: Q16 (≠ L23), E139 (≠ D153), D168 (= D186), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R21), V15 (= V22), Q16 (≠ L23), R37 (= R44), M73 (= M87), N95 (= N109), F96 (= F110), R103 (≠ Q117), M104 (≠ Y118), V137 (≠ G151), Y138 (= Y152), D168 (= D186), M199 (≠ L221)
- binding oxalic acid: G259 (vs. gap), G260 (vs. gap)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
32% identity, 98% coverage: 11:424/424 of query aligns to 5:428/428 of O06644
- Q17 (≠ L23) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (= R44) binding
- W48 (= W54) 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 (≠ Q117) binding
- D169 (= D186) 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.
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
32% identity, 98% coverage: 11:424/424 of query aligns to 4:427/427 of 1p5rA
- active site: Q16 (≠ L23), E139 (≠ D153), D168 (= D186), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R21), V15 (= V22), Q16 (≠ L23), A17 (= A24), R37 (= R44), M73 (= M87), K74 (≠ A88), N95 (= N109), F96 (= F110), A100 (≠ G114), R103 (≠ Q117), K136 (≠ A150), V137 (≠ G151), D168 (= D186), M199 (≠ L221)
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
31% identity, 100% coverage: 1:424/424 of query aligns to 1:416/417 of 1q6yA
- active site: Q17 (≠ L23), E140 (≠ D153), D169 (= D186), G248 (vs. gap), G249 (vs. gap)
- binding coenzyme a: V16 (= V22), Q17 (≠ L23), S18 (≠ A24), R38 (= R44), L72 (≠ I85), N73 (≠ D86), T74 (≠ M87), K75 (≠ A88), N96 (= N109), F97 (= F110), H98 (≠ K111), M105 (≠ Y118), I124 (≠ V137), K137 (≠ A150), A138 (≠ G151), Y139 (= Y152), D169 (= D186), M200 (vs. gap)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
31% identity, 98% coverage: 11:424/424 of query aligns to 4:415/415 of 1pt5A
- active site: Q16 (≠ L23), E139 (≠ D153), D168 (= D186), G247 (vs. gap), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (= V22), S17 (≠ A24), R37 (= R44), L71 (≠ I85), N72 (≠ D86), T73 (≠ M87), K74 (≠ A88), N95 (= N109), F96 (= F110), H97 (≠ K111), K124 (≠ T138), K136 (≠ A150), A137 (≠ G151), Y138 (= Y152), E139 (≠ D153), D168 (= D186), M199 (vs. gap)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
32% identity, 98% coverage: 11:424/424 of query aligns to 4:427/427 of 1t3zA
- active site: Q16 (≠ L23), E139 (≠ D153), S168 (≠ D186), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (≠ R21), V15 (= V22), A17 (= A24), R37 (= R44), K74 (≠ A88), N95 (= N109), F96 (= F110), A100 (≠ G114), R103 (≠ Q117), M104 (≠ Y118), K136 (≠ A150), V137 (≠ G151), Y138 (= Y152), E139 (≠ D153), M199 (≠ L221)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
31% identity, 100% coverage: 1:424/424 of query aligns to 1:409/410 of 1q7eA
- active site: Q17 (≠ L23), E133 (≠ D153), D162 (= D186), G241 (vs. gap), G242 (vs. gap)
- binding methionine: N96 (= N109), F97 (= F110), H98 (≠ Y118), P99 (≠ G119), K118 (≠ T138), K130 (≠ A150), A131 (≠ G151), W246 (vs. gap), F299 (≠ T305), A303 (≠ P309), E306 (= E312)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
30% identity, 93% coverage: 8:400/424 of query aligns to 3:355/360 of 5yx6A
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
28% identity, 98% coverage: 10:424/424 of query aligns to 2:373/382 of Q9UHK6
- V9 (≠ L17) to M: in dbSNP:rs3195676
- S52 (= S82) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ V137) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G212) to D: in dbSNP:rs10941112
- L201 (= L237) to S: in dbSNP:rs2287939
- M261 (≠ V301) to T: in dbSNP:rs3195678
- E277 (≠ T317) to K: in dbSNP:rs2278008
Sites not aligning to the query:
- 380:382 Microbody targeting signal
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)
31% identity, 63% coverage: 8:276/424 of query aligns to 1:239/355 of 2yimA
- active site: G16 (≠ L23), D122 (= D153), D151 (vs. gap), G214 (≠ S252), G215 (≠ L253)
- binding 2-methylacetoacetyl coa: I15 (≠ V22), R37 (= R44), A54 (≠ I85), L56 (≠ M87), K57 (≠ A88), G78 (≠ N109), Y79 (≠ F110), R80 (≠ K111), V83 (≠ G114), R86 (≠ Q117), L87 (≠ Y118), A119 (= A150), G120 (= G151), H121 (≠ Y152), Y125 (≠ V156), D151 (vs. gap)
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
31% identity, 63% coverage: 8:276/424 of query aligns to 2:244/360 of O06543
- R38 (= R44) binding
- R52 (= R78) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S82) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ IDMA 85:88) binding
- E82 (= E108) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NFK 109:111) binding
- R91 (≠ Q117) binding ; mutation to A: 19.9% of wild-type activity.
- M111 (≠ V137) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ GYDLMV 151:156) binding
- H126 (≠ Y152) mutation to A: 4.5% of wild-type activity.
- D156 (vs. gap) mutation to A: 17.6 of wild-type activity.
- D190 (= D223) mutation to A: 3.3% of wild-type activity.
- E241 (≠ D273) mutation to A: 2.1% of wild-type activity.
Sites not aligning to the query:
- 297 C→A: 6.2% of wild-type activity.
- 312 H→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)
31% identity, 63% coverage: 8:276/424 of query aligns to 1:238/354 of 2gd6A
- active site: G16 (≠ L23), D121 (= D153), D150 (vs. gap), G213 (≠ S252), G214 (≠ L253)
- binding acetyl coenzyme *a: I15 (≠ V22), R37 (= R44), A53 (≠ I85), D54 (= D86), L55 (≠ M87), K56 (≠ A88), G77 (≠ N109), Y78 (≠ F110), R79 (≠ K111), V82 (≠ G114), R85 (≠ Q117), G119 (= G151), H120 (≠ Y152), Y124 (≠ V156), D150 (vs. gap), M182 (≠ L221)
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)
31% identity, 63% coverage: 8:276/424 of query aligns to 1:238/354 of 2gd2A
- active site: G16 (≠ L23), D121 (= D153), D150 (vs. gap), G213 (≠ S252), G214 (≠ L253)
- binding acetoacetyl-coenzyme a: I15 (≠ V22), R37 (= R44), A53 (≠ I85), L55 (≠ M87), K56 (≠ A88), G77 (≠ N109), Y78 (≠ F110), R79 (≠ K111), V82 (≠ G114), R85 (≠ Q117), L86 (≠ Y118), A118 (= A150), G119 (= G151), H120 (≠ Y152), Y124 (≠ V156), D150 (vs. gap)
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)
31% identity, 63% coverage: 8:276/424 of query aligns to 1:238/354 of 2gd0A
- active site: G16 (≠ L23), D121 (= D153), D150 (vs. gap), G213 (≠ S252), G214 (≠ L253)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D49), L55 (≠ M87), K56 (≠ A88), G77 (≠ N109), Y78 (≠ F110), R79 (≠ K111), V82 (≠ G114), R85 (≠ Q117), L86 (≠ Y118), G119 (= G151), H120 (≠ Y152), D121 (= D153), Y124 (≠ V156), D150 (vs. gap)
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)
31% identity, 63% coverage: 8:276/424 of query aligns to 1:238/354 of 2gciA
- active site: G16 (≠ L23), D121 (= D153), D150 (vs. gap), G213 (≠ S252), G214 (≠ L253)
- binding (r)-2-methylmyristoyl-coenzyme a: R37 (= R44), L55 (≠ M87), K56 (≠ A88), G77 (≠ N109), Y78 (≠ F110), R79 (≠ K111), V82 (≠ G114), G119 (= G151), H120 (≠ Y152), D121 (= D153), Y124 (≠ V156), D150 (vs. gap), Y218 (≠ Q257), I234 (≠ N272), E235 (≠ D273)
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)
31% identity, 63% coverage: 8:276/424 of query aligns to 1:238/354 of 2gceA
- active site: G16 (≠ L23), D121 (= D153), D150 (vs. gap), G213 (≠ S252), G214 (≠ L253)
- binding (r)-ibuprofenoyl-coenzyme a: I15 (≠ V22), R37 (= R44), L55 (≠ M87), K56 (≠ A88), G77 (≠ N109), Y78 (≠ F110), R79 (≠ K111), V82 (≠ G114), R85 (≠ Q117), G119 (= G151), H120 (≠ Y152), D121 (= D153), Y124 (≠ V156), D150 (vs. gap), L211 (≠ H250), Y218 (≠ Q257), I234 (≠ N272)
- binding (s)-ibuprofenoyl-coenzyme a: I15 (≠ V22), G16 (≠ L23), P17 (≠ A24), R37 (= R44), L55 (≠ M87), K56 (≠ A88), G77 (≠ N109), Y78 (≠ F110), R79 (≠ K111), V82 (≠ G114), R85 (≠ Q117), G119 (= G151), H120 (≠ Y152), Y124 (≠ V156), D150 (vs. gap)
Query Sequence
>Ac3H11_3532 FitnessBrowser__acidovorax_3H11:Ac3H11_3532
MSTPSSNAGALAGIKVLDLSRVLAGPWCTQVLADLGADVVKVERPGVGDDTRQWGPPFLK
DAEGNDTNQASYYTACNRNKRSVTIDMASPDGQALIRQMAQEADIVVENFKVGGLKQYGL
DHESLRALNPRLIYCSVTGFGQDGPYAERAGYDLMVQAMTGLMSITGQADTEPGGGPMRV
GVAVIDLFTGLYASNAILAALHVRDNAATGTGQGQHIDMALLDVGMAVLANQASGFLATG
KAPGRMGNSHPSLAPYQDFPTQDGNMLLAIGNDGQFQRFCAAANQPQWASDPRFATNTLR
VQNRTDLIPAMEAVTRTRTTADWIALLEDKAVPCGPINTIAQAFDDAQVQARGLAVTLPR
WKDGEAATDKVQQITGVASPLRLSATPPVLRNAPPALGQHTDEVLAEMGLDAARIAALRA
QGVV
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