SitesBLAST
Comparing Ga0059261_2666 FitnessBrowser__Korea:Ga0059261_2666 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)
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: 1:393/397 of query aligns to 1:428/428 of O06644
- Q17 (≠ M17) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ P38) binding
- W48 (≠ A52) 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 (= R105) binding
- D169 (= D170) 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)
31% identity, 99% coverage: 2:393/397 of query aligns to 1:427/427 of 1p5rA
- active site: Q16 (≠ M17), E139 (≠ D141), D168 (= D170), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ I15), V15 (≠ A16), Q16 (≠ M17), A17 (= A18), R37 (≠ P38), M73 (≠ L75), K74 (= K76), N95 (= N97), F96 (≠ Y98), A100 (≠ V102), R103 (= R105), K136 (≠ P138), V137 (≠ G139), D168 (= D170), M199 (= M201)
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
31% identity, 99% coverage: 2:393/397 of query aligns to 1:427/427 of 2vjkA
- active site: Q16 (≠ M17), E139 (≠ D141), D168 (= D170), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ I15), Q16 (≠ M17), A17 (= A18), R37 (≠ P38), M73 (≠ L75), K74 (= K76), N95 (= N97), F96 (≠ Y98), G97 (≠ R99), R103 (= R105), M104 (≠ L106), K136 (≠ P138), V137 (≠ G139), Y138 (≠ Q140), D168 (= D170), M199 (= M201)
- binding magnesium ion: D293 (≠ E261), D296 (≠ E264)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
31% identity, 99% coverage: 2:393/397 of query aligns to 1:427/427 of 1t4cA
- active site: Q16 (≠ M17), E139 (≠ D141), D168 (= D170), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ I15), V15 (≠ A16), Q16 (≠ M17), R37 (≠ P38), M73 (≠ L75), N95 (= N97), F96 (≠ Y98), R103 (= R105), M104 (≠ L106), V137 (≠ G139), Y138 (≠ Q140), D168 (= D170), M199 (= M201)
- binding oxalic acid: G259 (vs. gap), G260 (vs. gap)
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
31% identity, 99% coverage: 2:393/397 of query aligns to 1:427/427 of 2vjoA
- active site: A16 (≠ M17), E139 (≠ D141), D168 (= D170), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ I15), A16 (≠ M17), A17 (= A18), R37 (≠ P38), L71 (≠ V73), M73 (≠ L75), N95 (= N97), F96 (≠ Y98), G97 (≠ R99), R103 (= R105), M104 (≠ L106), K136 (≠ P138), V137 (≠ G139), Y138 (≠ Q140), D168 (= D170), M199 (= M201)
- binding oxalate ion: G257 (vs. gap), G259 (vs. gap), Q261 (vs. gap)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
31% identity, 99% coverage: 2:393/397 of query aligns to 1:427/427 of 1t3zA
- active site: Q16 (≠ M17), E139 (≠ D141), S168 (≠ D170), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (≠ I15), V15 (≠ A16), A17 (= A18), R37 (≠ P38), K74 (= K76), N95 (= N97), F96 (≠ Y98), A100 (≠ V102), R103 (= R105), M104 (≠ L106), K136 (≠ P138), V137 (≠ G139), Y138 (≠ Q140), E139 (≠ D141), M199 (= M201)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
31% identity, 93% coverage: 5:374/397 of query aligns to 6:360/360 of 5yx6A
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
28% identity, 98% coverage: 5:393/397 of query aligns to 4:415/415 of 1pt5A
- active site: Q16 (≠ M17), E139 (≠ D141), D168 (= D170), G247 (vs. gap), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (≠ A16), S17 (≠ A18), R37 (vs. gap), L71 (≠ V73), N72 (≠ D74), T73 (≠ L75), K74 (= K76), N95 (= N97), F96 (≠ Y98), H97 (≠ R99), K124 (≠ S126), K136 (≠ P138), A137 (≠ G139), Y138 (≠ Q140), E139 (≠ D141), D168 (= D170), M199 (= M201)
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)
28% identity, 98% coverage: 5:393/397 of query aligns to 5:416/416 of P69902
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
28% identity, 98% coverage: 5:393/397 of query aligns to 5:416/417 of 1q6yA
- active site: Q17 (≠ M17), E140 (≠ D141), D169 (= D170), G248 (vs. gap), G249 (vs. gap)
- binding coenzyme a: V16 (≠ A16), Q17 (≠ M17), S18 (≠ A18), R38 (vs. gap), L72 (≠ V73), N73 (≠ D74), T74 (≠ L75), K75 (= K76), N96 (= N97), F97 (≠ Y98), H98 (≠ R99), M105 (≠ L106), I124 (≠ M125), K137 (≠ P138), A138 (≠ G139), Y139 (≠ Q140), D169 (= D170), M200 (= M201)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
29% identity, 98% coverage: 5:393/397 of query aligns to 5:428/430 of 3ubmB
- active site: Q17 (≠ M17), E140 (≠ D141), D182 (= D170), G261 (≠ I249), G262 (≠ T250)
- binding coenzyme a: V16 (≠ A16), R38 (≠ P38), L72 (≠ V73), N73 (≠ D74), T74 (≠ L75), K75 (= K76), N96 (= N97), F97 (≠ Y98), R98 (= R99), A101 (≠ V102), R104 (= R105), K125 (≠ S126), D182 (= D170), M213 (= M201)
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
29% identity, 98% coverage: 5:394/397 of query aligns to 3:379/382 of Q9UHK6
- V9 (≠ L11) to M: in dbSNP:rs3195676
- S52 (= S70) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ M125) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G192) to D: in dbSNP:rs10941112
- L201 (= L213) to S: in dbSNP:rs2287939
- M261 (vs. gap) to T: in dbSNP:rs3195678
- E277 (≠ A294) to K: in dbSNP:rs2278008
Sites not aligning to the query:
- 380:382 Microbody targeting signal
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
28% identity, 98% coverage: 5:393/397 of query aligns to 5:409/410 of 1q7eA
- active site: Q17 (≠ M17), E133 (≠ D141), D162 (= D170), G241 (vs. gap), G242 (vs. gap)
- binding methionine: N96 (= N97), F97 (≠ Y98), H98 (≠ R99), P99 (= P100), K118 (≠ S126), K130 (≠ P138), A131 (≠ G139), W246 (vs. gap), F299 (vs. gap), A303 (= A286), E306 (≠ R289)
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
29% identity, 90% coverage: 5:361/397 of query aligns to 5:343/360 of O06543
- R38 (= R45) binding
- R52 (= R66) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S70) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ VDLK 73:76) binding
- E82 (≠ Q96) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NYR 97:99) binding
- R91 (= R105) binding ; mutation to A: 19.9% of wild-type activity.
- M111 (= M125) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ GQDLLL 139:144) binding
- H126 (≠ Q140) mutation to A: 4.5% of wild-type activity.
- D156 (≠ A171) mutation to A: 17.6 of wild-type activity.
- D190 (= D203) mutation to A: 3.3% of wild-type activity.
- E241 (≠ S255) mutation to A: 2.1% of wild-type activity.
- C297 (≠ W310) mutation to A: 6.2% of wild-type activity.
- H312 (≠ Q325) 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)
28% identity, 90% coverage: 5:361/397 of query aligns to 4:338/355 of 2yimA
- active site: G16 (≠ M17), D122 (= D141), D151 (≠ A171), G214 (≠ H232), G215 (≠ S233)
- binding 2-methylacetoacetyl coa: I15 (≠ A16), R37 (≠ K56), A54 (≠ V73), L56 (= L75), K57 (= K76), G78 (≠ N97), Y79 (= Y98), R80 (= R99), V83 (= V102), R86 (= R105), L87 (= L106), A119 (≠ P138), G120 (= G139), H121 (≠ Q140), Y125 (≠ L144), D151 (≠ A171)
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)
28% identity, 90% coverage: 5:361/397 of query aligns to 4:337/354 of 2gd6A
- active site: G16 (≠ M17), D121 (= D141), D150 (≠ A171), G213 (≠ H232), G214 (≠ S233)
- binding acetyl coenzyme *a: I15 (≠ A16), R37 (≠ P38), A53 (≠ V73), D54 (= D74), L55 (= L75), K56 (= K76), G77 (≠ N97), Y78 (= Y98), R79 (= R99), V82 (= V102), R85 (= R105), G119 (= G139), H120 (≠ Q140), Y124 (≠ L144), D150 (≠ A171), M182 (= M201)
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)
28% identity, 90% coverage: 5:361/397 of query aligns to 4:337/354 of 2gd2A
- active site: G16 (≠ M17), D121 (= D141), D150 (≠ A171), G213 (≠ H232), G214 (≠ S233)
- binding acetoacetyl-coenzyme a: I15 (≠ A16), R37 (≠ P38), A53 (≠ V73), L55 (= L75), K56 (= K76), G77 (≠ N97), Y78 (= Y98), R79 (= R99), V82 (= V102), R85 (= R105), L86 (= L106), A118 (≠ P138), G119 (= G139), H120 (≠ Q140), Y124 (≠ L144), D150 (≠ A171)
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)
28% identity, 90% coverage: 5:361/397 of query aligns to 4:337/354 of 2gd0A
- active site: G16 (≠ M17), D121 (= D141), D150 (≠ A171), G213 (≠ H232), G214 (≠ S233)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (≠ L62), L55 (= L75), K56 (= K76), G77 (≠ N97), Y78 (= Y98), R79 (= R99), V82 (= V102), R85 (= R105), L86 (= L106), G119 (= G139), H120 (≠ Q140), D121 (= D141), Y124 (≠ L144), D150 (≠ A171)
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)
28% identity, 90% coverage: 5:361/397 of query aligns to 4:337/354 of 2gciA
- active site: G16 (≠ M17), D121 (= D141), D150 (≠ A171), G213 (≠ H232), G214 (≠ S233)
- binding (r)-2-methylmyristoyl-coenzyme a: R37 (≠ P38), L55 (= L75), K56 (= K76), G77 (≠ N97), Y78 (= Y98), R79 (= R99), V82 (= V102), G119 (= G139), H120 (≠ Q140), D121 (= D141), Y124 (≠ L144), D150 (≠ A171), Y218 (= Y239), I234 (≠ A254), 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)
28% identity, 90% coverage: 5:361/397 of query aligns to 4:337/354 of 2gceA
- active site: G16 (≠ M17), D121 (= D141), D150 (≠ A171), G213 (≠ H232), G214 (≠ S233)
- binding (r)-ibuprofenoyl-coenzyme a: I15 (≠ A16), R37 (≠ P38), L55 (= L75), K56 (= K76), G77 (≠ N97), Y78 (= Y98), R79 (= R99), V82 (= V102), R85 (= R105), G119 (= G139), H120 (≠ Q140), D121 (= D141), Y124 (≠ L144), D150 (≠ A171), L211 (≠ H230), Y218 (= Y239), I234 (≠ A254)
- binding (s)-ibuprofenoyl-coenzyme a: I15 (≠ A16), G16 (≠ M17), P17 (≠ A18), R37 (≠ P38), L55 (= L75), K56 (= K76), G77 (≠ N97), Y78 (= Y98), R79 (= R99), V82 (= V102), R85 (= R105), G119 (= G139), H120 (≠ Q140), Y124 (≠ L144), D150 (≠ A171)
Query Sequence
>Ga0059261_2666 FitnessBrowser__Korea:Ga0059261_2666
VTNILSGIRVLDCSIAMAGPFAAQRMGDMGADVVKVEPTSGEWQRHASAGGANGNKINVS
FLSLNRNKRSLAVDLKAPEGKALLLELVKDADVFLQNYRPGVAERLGVDYATLSAINPSL
VYVSMSGYGEDGPYRNYPGQDLLLQGMSGAMMSTGAEGAPPSAAGQYLVDAVTAYSAFEG
ALAALFHRERTGEGQLVQVNMLDAITTIQMQELSVFTVGEKPQARSAEPHAHSYIRAPYG
VFATADGYITVAMASLKKLGELFEDSFFEGLDDERDSWALRDQIFAKVREHLPARTSAQW
LEAMRARDIWAGPVYGYADLVEDPQIKHNGTFVEYDHPTEGRVKAPGFPIRFSKTPSTVA
RGAPLVGEHSRELLREAGLDGKAIEALIESGVVRQHA
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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