SitesBLAST
Comparing GFF1502 FitnessBrowser__Phaeo:GFF1502 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)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
32% identity, 97% coverage: 1:380/391 of query aligns to 1:413/428 of O06644
- Q17 (≠ L17) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (= R38) binding
- W48 (≠ F48) 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.
- 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, 97% coverage: 3:380/391 of query aligns to 2:412/427 of 1p5rA
- active site: Q16 (≠ L17), E139 (≠ D139), D168 (= D168), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (= H15), V15 (= V16), Q16 (≠ L17), A17 (= A18), R37 (= R38), M73 (≠ L73), K74 (≠ R74), N95 (= N95), F96 (= F96), A100 (≠ V100), R103 (= R103), K136 (≠ P136), V137 (≠ A137), D168 (= D168), M199 (= M199)
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
32% identity, 97% coverage: 3:380/391 of query aligns to 2:412/427 of 2vjkA
- active site: Q16 (≠ L17), E139 (≠ D139), D168 (= D168), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (= H15), Q16 (≠ L17), A17 (= A18), R37 (= R38), M73 (≠ L73), K74 (≠ R74), N95 (= N95), F96 (= F96), G97 (≠ R97), R103 (= R103), M104 (≠ L104), K136 (≠ P136), V137 (≠ A137), Y138 (= Y138), D168 (= D168), M199 (= M199)
- binding magnesium ion: D293 (≠ T259), D296 (= D262)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
32% identity, 97% coverage: 3:380/391 of query aligns to 2:412/427 of 1t4cA
- active site: Q16 (≠ L17), E139 (≠ D139), D168 (= D168), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (= H15), V15 (= V16), Q16 (≠ L17), R37 (= R38), M73 (≠ L73), N95 (= N95), F96 (= F96), R103 (= R103), M104 (≠ L104), V137 (≠ A137), Y138 (= Y138), D168 (= D168), M199 (= M199)
- 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)
32% identity, 97% coverage: 3:380/391 of query aligns to 2:412/427 of 2vjoA
- active site: A16 (≠ L17), E139 (≠ D139), D168 (= D168), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (= H15), A16 (≠ L17), A17 (= A18), R37 (= R38), L71 (= L71), M73 (≠ L73), N95 (= N95), F96 (= F96), G97 (≠ R97), R103 (= R103), M104 (≠ L104), K136 (≠ P136), V137 (≠ A137), Y138 (= Y138), D168 (= D168), M199 (= M199)
- binding oxalate ion: G257 (vs. gap), G259 (vs. gap), Q261 (vs. gap)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
31% identity, 97% coverage: 3:380/391 of query aligns to 2:412/427 of 1t3zA
- active site: Q16 (≠ L17), E139 (≠ D139), S168 (≠ D168), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (= H15), V15 (= V16), A17 (= A18), R37 (= R38), K74 (≠ R74), N95 (= N95), F96 (= F96), A100 (≠ V100), R103 (= R103), M104 (≠ L104), K136 (≠ P136), V137 (≠ A137), Y138 (= Y138), E139 (≠ D139), M199 (= M199)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
30% identity, 97% coverage: 3:380/391 of query aligns to 3:413/430 of 3ubmB
- active site: Q17 (≠ L17), E140 (≠ D139), D182 (= D168), G261 (vs. gap), G262 (vs. gap)
- binding coenzyme a: V16 (= V16), R38 (= R38), L72 (= L71), N73 (≠ D72), T74 (≠ L73), K75 (≠ R74), N96 (= N95), F97 (= F96), R98 (= R97), A101 (≠ V100), R104 (= R103), K125 (≠ S124), D182 (= D168), M213 (= M199)
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, 97% coverage: 1:380/391 of query aligns to 1:401/416 of P69902
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
31% identity, 96% coverage: 4:380/391 of query aligns to 4:401/417 of 1q6yA
- active site: Q17 (≠ L17), E140 (≠ D139), D169 (= D168), G248 (≠ P229), G249 (≠ S230)
- binding coenzyme a: V16 (= V16), Q17 (≠ L17), S18 (≠ A18), R38 (= R38), L72 (= L71), N73 (≠ D72), T74 (≠ L73), K75 (≠ R74), N96 (= N95), F97 (= F96), H98 (≠ R97), M105 (≠ L104), I124 (≠ V123), K137 (≠ P136), A138 (= A137), Y139 (= Y138), D169 (= D168), M200 (= M199)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
31% identity, 96% coverage: 4:380/391 of query aligns to 3:400/415 of 1pt5A
- active site: Q16 (≠ L17), E139 (≠ D139), D168 (= D168), G247 (≠ P229), G248 (≠ S230)
- binding acetyl coenzyme *a: V15 (= V16), S17 (≠ A18), R37 (= R38), L71 (= L71), N72 (≠ D72), T73 (≠ L73), K74 (≠ R74), N95 (= N95), F96 (= F96), H97 (≠ R97), K124 (≠ S124), K136 (≠ P136), A137 (= A137), Y138 (= Y138), E139 (≠ D139), D168 (= D168), M199 (= M199)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
31% identity, 96% coverage: 4:380/391 of query aligns to 4:394/410 of 1q7eA
- active site: Q17 (≠ L17), E133 (≠ D139), D162 (= D168), G241 (≠ P229), G242 (≠ S230)
- binding methionine: N96 (= N95), F97 (= F96), H98 (≠ R97), P99 (= P98), K118 (≠ S124), K130 (≠ P136), A131 (= A137), W246 (vs. gap), F299 (≠ R282), A303 (≠ R286), E306 (= E289)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
32% identity, 96% coverage: 3:376/391 of query aligns to 4:360/360 of 5yx6A
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
28% identity, 97% coverage: 1:380/391 of query aligns to 1:360/360 of O06543
- R38 (= R38) binding
- R52 (≠ K52) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S68) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ LDLR 71:74) binding
- E82 (= E94) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NFR 95:97) binding
- R91 (= R103) binding ; mutation to A: 19.9% of wild-type activity.
- M111 (≠ V123) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ AYDMVV 137:142) binding
- H126 (≠ Y138) mutation to A: 4.5% of wild-type activity.
- D156 (= D168) mutation to A: 17.6 of wild-type activity.
- D190 (= D201) mutation to A: 3.3% of wild-type activity.
- E241 (≠ N250) mutation to A: 2.1% of wild-type activity.
- C297 (≠ P310) 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, 96% coverage: 4:380/391 of query aligns to 3:355/355 of 2yimA
- active site: G16 (≠ L17), D122 (= D139), D151 (= D168), G214 (≠ P229), G215 (≠ S230)
- binding 2-methylacetoacetyl coa: I15 (≠ V16), R37 (= R38), A54 (≠ L71), L56 (= L73), K57 (≠ R74), G78 (≠ N95), Y79 (≠ F96), R80 (= R97), V83 (= V100), R86 (= R103), L87 (= L104), A119 (≠ P136), G120 (≠ A137), H121 (≠ Y138), Y125 (≠ V142), D151 (= D168)
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, 96% coverage: 4:380/391 of query aligns to 3:354/354 of 2gd6A
- active site: G16 (≠ L17), D121 (= D139), D150 (= D168), G213 (≠ P229), G214 (≠ S230)
- binding acetyl coenzyme *a: I15 (≠ V16), R37 (= R38), A53 (≠ L71), D54 (= D72), L55 (= L73), K56 (≠ R74), G77 (≠ N95), Y78 (≠ F96), R79 (= R97), V82 (= V100), R85 (= R103), G119 (≠ A137), H120 (≠ Y138), Y124 (≠ V142), D150 (= D168), 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)
28% identity, 96% coverage: 4:380/391 of query aligns to 3:354/354 of 2gd2A
- active site: G16 (≠ L17), D121 (= D139), D150 (= D168), G213 (≠ P229), G214 (≠ S230)
- binding acetoacetyl-coenzyme a: I15 (≠ V16), R37 (= R38), A53 (≠ L71), L55 (= L73), K56 (≠ R74), G77 (≠ N95), Y78 (≠ F96), R79 (= R97), V82 (= V100), R85 (= R103), L86 (= L104), A118 (≠ P136), G119 (≠ A137), H120 (≠ Y138), Y124 (≠ V142), 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)
28% identity, 96% coverage: 4:380/391 of query aligns to 3:354/354 of 2gd0A
- active site: G16 (≠ L17), D121 (= D139), D150 (= D168), G213 (≠ P229), G214 (≠ S230)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D43), L55 (= L73), K56 (≠ R74), G77 (≠ N95), Y78 (≠ F96), R79 (= R97), V82 (= V100), R85 (= R103), L86 (= L104), G119 (≠ A137), H120 (≠ Y138), D121 (= D139), Y124 (≠ V142), 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)
28% identity, 96% coverage: 4:380/391 of query aligns to 3:354/354 of 2gciA
- active site: G16 (≠ L17), D121 (= D139), D150 (= D168), G213 (≠ P229), G214 (≠ S230)
- binding (r)-2-methylmyristoyl-coenzyme a: R37 (= R38), L55 (= L73), K56 (≠ R74), G77 (≠ N95), Y78 (≠ F96), R79 (= R97), V82 (= V100), G119 (≠ A137), H120 (≠ Y138), D121 (= D139), Y124 (≠ V142), D150 (= D168), Y218 (≠ F234), I234 (≠ G249), E235 (≠ N250)
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, 96% coverage: 4:380/391 of query aligns to 3:354/354 of 2gceA
- active site: G16 (≠ L17), D121 (= D139), D150 (= D168), G213 (≠ P229), G214 (≠ S230)
- binding (r)-ibuprofenoyl-coenzyme a: I15 (≠ V16), R37 (= R38), L55 (= L73), K56 (≠ R74), G77 (≠ N95), Y78 (≠ F96), R79 (= R97), V82 (= V100), R85 (= R103), G119 (≠ A137), H120 (≠ Y138), D121 (= D139), Y124 (≠ V142), D150 (= D168), L211 (vs. gap), Y218 (≠ F234), I234 (≠ G249)
- binding (s)-ibuprofenoyl-coenzyme a: I15 (≠ V16), G16 (≠ L17), P17 (≠ A18), R37 (= R38), L55 (= L73), K56 (≠ R74), G77 (≠ N95), Y78 (≠ F96), R79 (= R97), V82 (= V100), R85 (= R103), G119 (≠ A137), H120 (≠ Y138), Y124 (≠ V142), D150 (= D168)
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
27% identity, 96% coverage: 5:380/391 of query aligns to 3:358/382 of Q9UHK6
- V9 (≠ L11) to M: in dbSNP:rs3195676
- S52 (= S68) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ V123) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (≠ A190) to D: in dbSNP:rs10941112
- L201 (≠ V216) to S: in dbSNP:rs2287939
- M261 (≠ C278) to T: in dbSNP:rs3195678
- E277 (≠ D294) to K: in dbSNP:rs2278008
Sites not aligning to the query:
- 380:382 Microbody targeting signal
Query Sequence
>GFF1502 FitnessBrowser__Phaeo:GFF1502
MIRPLSDIVVLDLTHVLAGPYASMTLRDLGARVIKVERPGHGDDTRAFPPFKDGDSAYFS
TINHGKESIALDLRAEEDRGIFEQLLTQADVILENFRPGVMERLGYGWEALHARFPKLVY
GAVSGFGHTGPDRLRPAYDMVVQARGGVMSITGERDREPVRVGASIGDIAAGMFLCQGVL
AALYAVRGGAPGQKVDIAMLDSQLALLEHAVAITSVTGEAPRPSGARHPSITPFETFHAS
DGLFVIAAGNDTLFATLCTALDLPLATDARFASNQARCENARLLKRLIEAVTLDQPASHW
IDRLQRAGVPTGPIQSVAEVMRDPQILARNMLVDVCDQEGTPRFKAAGNPVKLSALPDET
TRPPAPMLDEHRAQILNWLGEIASGPPVNDT
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