SitesBLAST
Comparing Ac3H11_198 Hydroxymethylglutaryl-CoA lyase (EC 4.1.3.4) to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
28% identity, 97% coverage: 14:403/404 of query aligns to 3:427/427 of 1p5rA
- active site: Q16 (≠ V27), E139 (≠ D144), D168 (= D172), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (= H25), V15 (≠ M26), Q16 (≠ V27), A17 (≠ M28), R37 (≠ P48), M73 (≠ L79), K74 (≠ R80), N95 (= N101), F96 (= F102), A100 (≠ V106), R103 (≠ K109), K136 (≠ T141), V137 (≠ A142), D168 (= D172), M199 (≠ L203)
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
28% identity, 97% coverage: 14:403/404 of query aligns to 3:427/427 of 2vjoA
- active site: A16 (≠ V27), E139 (≠ D144), D168 (= D172), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (= H25), A16 (≠ V27), A17 (≠ M28), R37 (≠ P48), L71 (= L77), M73 (≠ L79), N95 (= N101), F96 (= F102), G97 (≠ K103), R103 (≠ K109), M104 (≠ Y110), K136 (≠ T141), V137 (≠ A142), Y138 (≠ L143), D168 (= D172), M199 (≠ L203)
- binding oxalate ion: G257 (vs. gap), G259 (vs. gap), Q261 (vs. gap)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
28% identity, 97% coverage: 14:403/404 of query aligns to 4:428/428 of O06644
- Q17 (≠ V27) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ P48) binding
- W48 (≠ L57) 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 (≠ K109) binding
- D169 (= D172) 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.
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
28% identity, 97% coverage: 14:403/404 of query aligns to 3:427/427 of 2vjkA
- active site: Q16 (≠ V27), E139 (≠ D144), D168 (= D172), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (= H25), Q16 (≠ V27), A17 (≠ M28), R37 (≠ P48), M73 (≠ L79), K74 (≠ R80), N95 (= N101), F96 (= F102), G97 (≠ K103), R103 (≠ K109), M104 (≠ Y110), K136 (≠ T141), V137 (≠ A142), Y138 (≠ L143), D168 (= D172), M199 (≠ L203)
- binding magnesium ion: D293 (= D264), D296 (≠ G267)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
28% identity, 97% coverage: 14:403/404 of query aligns to 3:427/427 of 1t4cA
- active site: Q16 (≠ V27), E139 (≠ D144), D168 (= D172), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (= H25), V15 (≠ M26), Q16 (≠ V27), R37 (≠ P48), M73 (≠ L79), N95 (= N101), F96 (= F102), R103 (≠ K109), M104 (≠ Y110), V137 (≠ A142), Y138 (≠ L143), D168 (= D172), M199 (≠ L203)
- binding oxalic acid: G259 (vs. gap), G260 (vs. gap)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
29% identity, 95% coverage: 14:398/404 of query aligns to 4:423/430 of 3ubmB
- active site: Q17 (≠ V27), E140 (≠ D144), D182 (= D172), G261 (≠ D230), G262 (≠ R231)
- binding coenzyme a: V16 (≠ M26), R38 (≠ P48), L72 (= L77), N73 (≠ D78), T74 (≠ L79), K75 (≠ R80), N96 (= N101), F97 (= F102), R98 (≠ K103), A101 (≠ V106), R104 (≠ K109), K125 (≠ T130), D182 (= D172), M213 (vs. gap)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
28% identity, 97% coverage: 14:403/404 of query aligns to 3:427/427 of 1t3zA
- active site: Q16 (≠ V27), E139 (≠ D144), S168 (≠ D172), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (= H25), V15 (≠ M26), A17 (≠ M28), R37 (≠ P48), K74 (≠ R80), N95 (= N101), F96 (= F102), A100 (≠ V106), R103 (≠ K109), M104 (≠ Y110), K136 (≠ T141), V137 (≠ A142), Y138 (≠ L143), E139 (≠ D144), M199 (≠ L203)
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)
31% identity, 95% coverage: 14:397/404 of query aligns to 4:410/416 of P69902
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
31% identity, 95% coverage: 14:397/404 of query aligns to 3:409/415 of 1pt5A
- active site: Q16 (≠ V27), E139 (≠ D144), D168 (= D172), G247 (≠ D230), G248 (≠ R231)
- binding acetyl coenzyme *a: V15 (≠ M26), S17 (≠ M28), R37 (vs. gap), L71 (= L77), N72 (≠ D78), T73 (≠ L79), K74 (≠ R80), N95 (= N101), F96 (= F102), H97 (≠ K103), K124 (≠ T130), K136 (≠ T141), A137 (= A142), Y138 (≠ L143), E139 (≠ D144), D168 (= D172), M199 (vs. gap)
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
31% identity, 95% coverage: 14:397/404 of query aligns to 4:410/417 of 1q6yA
- active site: Q17 (≠ V27), E140 (≠ D144), D169 (= D172), G248 (≠ D230), G249 (≠ R231)
- binding coenzyme a: V16 (≠ M26), Q17 (≠ V27), S18 (≠ M28), R38 (vs. gap), L72 (= L77), N73 (≠ D78), T74 (≠ L79), K75 (≠ R80), N96 (= N101), F97 (= F102), H98 (≠ K103), M105 (≠ Y110), I124 (≠ H129), K137 (≠ T141), A138 (= A142), Y139 (≠ L143), D169 (= D172), M200 (vs. gap)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
31% identity, 95% coverage: 14:397/404 of query aligns to 4:403/410 of 1q7eA
- active site: Q17 (≠ V27), E133 (≠ D144), D162 (= D172), G241 (≠ D230), G242 (≠ R231)
- binding methionine: N96 (= N101), F97 (= F102), H98 (≠ K103), P99 (= P104), K118 (≠ T130), K130 (≠ T141), A131 (= A142), W246 (= W235), F299 (≠ M291), A303 (≠ R295), E306 (≠ A299)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
32% identity, 93% coverage: 10:384/404 of query aligns to 1:360/360 of 5yx6A
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
32% identity, 84% coverage: 14:352/404 of query aligns to 4:340/360 of O06543
- R38 (vs. gap) binding
- R52 (= R70) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S74) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ LDLR 77:80) binding
- E82 (≠ Q100) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NFK 101:103) binding
- R91 (≠ K109) binding ; mutation to A: 19.9% of wild-type activity.
- M111 (≠ H129) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ ALDEVV 142:147) binding
- H126 (≠ L143) mutation to A: 4.5% of wild-type activity.
- D156 (= D172) mutation to A: 17.6 of wild-type activity.
- D190 (≠ E205) mutation to A: 3.3% of wild-type activity.
- E241 (≠ S255) mutation to A: 2.1% of wild-type activity.
- C297 (≠ P316) mutation to A: 6.2% of wild-type activity.
- H312 (= H331) 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)
32% identity, 84% coverage: 14:352/404 of query aligns to 3:335/355 of 2yimA
- active site: G16 (≠ V27), D122 (= D144), D151 (= D172), G214 (≠ R231), G215 (≠ I232)
- binding 2-methylacetoacetyl coa: I15 (≠ M26), R37 (≠ P48), A54 (≠ L77), L56 (= L79), K57 (≠ R80), G78 (≠ N101), Y79 (≠ F102), R80 (≠ K103), V83 (= V106), R86 (≠ K109), L87 (≠ Y110), A119 (≠ T141), G120 (≠ A142), H121 (≠ L143), Y125 (≠ V147), D151 (= D172)
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)
32% identity, 84% coverage: 14:352/404 of query aligns to 3:334/354 of 2gd6A
- active site: G16 (≠ V27), D121 (= D144), D150 (= D172), G213 (≠ R231), G214 (≠ I232)
- binding acetyl coenzyme *a: I15 (≠ M26), R37 (vs. gap), A53 (≠ L77), D54 (= D78), L55 (= L79), K56 (≠ R80), G77 (≠ N101), Y78 (≠ F102), R79 (≠ K103), V82 (= V106), R85 (≠ K109), G119 (≠ A142), H120 (≠ L143), Y124 (≠ V147), D150 (= D172), M182 (≠ L203)
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)
32% identity, 84% coverage: 14:352/404 of query aligns to 3:334/354 of 2gd2A
- active site: G16 (≠ V27), D121 (= D144), D150 (= D172), G213 (≠ R231), G214 (≠ I232)
- binding acetoacetyl-coenzyme a: I15 (≠ M26), R37 (vs. gap), A53 (≠ L77), L55 (= L79), K56 (≠ R80), G77 (≠ N101), Y78 (≠ F102), R79 (≠ K103), V82 (= V106), R85 (≠ K109), L86 (≠ Y110), A118 (≠ T141), G119 (≠ A142), H120 (≠ L143), Y124 (≠ V147), D150 (= D172)
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)
32% identity, 84% coverage: 14:352/404 of query aligns to 3:334/354 of 2gd0A
- active site: G16 (≠ V27), D121 (= D144), D150 (= D172), G213 (≠ R231), G214 (≠ I232)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D52), L55 (= L79), K56 (≠ R80), G77 (≠ N101), Y78 (≠ F102), R79 (≠ K103), V82 (= V106), R85 (≠ K109), L86 (≠ Y110), G119 (≠ A142), H120 (≠ L143), D121 (= D144), Y124 (≠ V147), D150 (= D172)
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)
32% identity, 84% coverage: 14:352/404 of query aligns to 3:334/354 of 2gciA
- active site: G16 (≠ V27), D121 (= D144), D150 (= D172), G213 (≠ R231), G214 (≠ I232)
- binding (r)-2-methylmyristoyl-coenzyme a: R37 (vs. gap), L55 (= L79), K56 (≠ R80), G77 (≠ N101), Y78 (≠ F102), R79 (≠ K103), V82 (= V106), G119 (≠ A142), H120 (≠ L143), D121 (= D144), Y124 (≠ V147), D150 (= D172), Y218 (= Y238), I234 (≠ V254), E235 (≠ S255)
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)
32% identity, 84% coverage: 14:352/404 of query aligns to 3:334/354 of 2gceA
- active site: G16 (≠ V27), D121 (= D144), D150 (= D172), G213 (≠ R231), G214 (≠ I232)
- binding (r)-ibuprofenoyl-coenzyme a: I15 (≠ M26), R37 (vs. gap), L55 (= L79), K56 (≠ R80), G77 (≠ N101), Y78 (≠ F102), R79 (≠ K103), V82 (= V106), R85 (≠ K109), G119 (≠ A142), H120 (≠ L143), D121 (= D144), Y124 (≠ V147), D150 (= D172), L211 (≠ P229), Y218 (= Y238), I234 (≠ V254)
- binding (s)-ibuprofenoyl-coenzyme a: I15 (≠ M26), G16 (≠ V27), P17 (≠ M28), R37 (vs. gap), L55 (= L79), K56 (≠ R80), G77 (≠ N101), Y78 (≠ F102), R79 (≠ K103), V82 (= V106), R85 (≠ K109), G119 (≠ A142), H120 (≠ L143), Y124 (≠ V147), D150 (= D172)
8apqB Camct - mesaconyl-coa c1:c4 coa transferase of chloroflexus aurantiacus (see paper)
30% identity, 97% coverage: 15:404/404 of query aligns to 5:403/406 of 8apqB
- binding coenzyme a: F16 (≠ M26), V17 (= V27), A18 (≠ M28), P38 (= P48), I74 (≠ L79), N100 (≠ G105), F101 (≠ V106), L124 (≠ H129), V125 (≠ T130), G126 (= G131), D165 (= D172)
- binding (2e)-2-methylbut-2-enedioic acid: V17 (= V27), R47 (= R55), D165 (= D172)
- binding Mesaconyl Coenzme A: T249 (≠ S255), L251 (≠ A257)
Query Sequence
>Ac3H11_198 Hydroxymethylglutaryl-CoA lyase (EC 4.1.3.4)
MHDTSASPSSPRLPLEGLRVVEFTHMVMGPTCGMVLADLGAEVIKVEPVDGDRTRHLLGA
GAGFFPMFNRNKKSIALDLRSPEGLAAARKLAASADVVAQNFKPGVMTKYGLDYAALSQI
NPRLIYVNHTGFLPGPYEHRTALDEVVQMMGGLAYMTGRPGDPLRAGSSVNDIMGGMFGA
IGAMAALMQRGITGRGQEVDSALFENNVFLVGQHMMQYAVTGKPAAPMPDRISSWAVYDV
FSVKDGGQIFLAAVSDAQWQTFCDAMGYADLKADTSLATNNDRVRARPTLMPVLRERLAQ
HTADELAAVFERHGLPFAPIRRPEELFDDPHLQATGGLADITLPDGERAGQTAQITLLPL
RLDGQRLDVRCDPPRLGQHTAELLQGLGYTADEVAALHAAGTIA
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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