SitesBLAST
Comparing GFF1451 FitnessBrowser__Marino:GFF1451 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: 4:394/401 of query aligns to 4:429/430 of 3ubmB
- active site: Q17 (≠ I17), E140 (≠ D139), D182 (= D169), G261 (vs. gap), G262 (vs. gap)
- binding coenzyme a: V16 (≠ M16), R38 (≠ N38), L72 (= L71), N73 (= N72), T74 (≠ L73), K75 (= K74), N96 (= N95), F97 (= F96), R98 (= R97), A101 (≠ V100), R104 (= R103), K125 (≠ S124), D182 (= D169), 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)
33% identity, 97% coverage: 1:387/401 of query aligns to 1:410/416 of P69902
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
33% identity, 97% coverage: 1:387/401 of query aligns to 1:410/417 of 1q6yA
- active site: Q17 (≠ I17), E140 (≠ D139), D169 (= D169), G248 (vs. gap), G249 (vs. gap)
- binding coenzyme a: V16 (≠ M16), Q17 (≠ I17), S18 (= S18), R38 (≠ N38), L72 (= L71), N73 (= N72), T74 (≠ L73), K75 (= K74), N96 (= N95), F97 (= F96), H98 (≠ R97), M105 (= M104), I124 (= I123), K137 (≠ P136), A138 (≠ V137), Y139 (= Y138), D169 (= D169), M200 (= M200)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
33% identity, 96% coverage: 4:387/401 of query aligns to 3:409/415 of 1pt5A
- active site: Q16 (≠ I17), E139 (≠ D139), D168 (= D169), G247 (vs. gap), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (≠ M16), S17 (= S18), R37 (≠ N38), L71 (= L71), N72 (= N72), T73 (≠ L73), K74 (= K74), N95 (= N95), F96 (= F96), H97 (≠ R97), K124 (≠ S124), K136 (≠ P136), A137 (≠ V137), Y138 (= Y138), E139 (≠ D139), D168 (= D169), M199 (= M200)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
32% identity, 97% coverage: 1:387/401 of query aligns to 1:403/410 of 1q7eA
- active site: Q17 (≠ I17), E133 (≠ D139), D162 (= D169), G241 (vs. gap), G242 (vs. gap)
- binding methionine: N96 (= N95), F97 (= F96), H98 (≠ R97), P99 (= P98), K118 (≠ S124), K130 (≠ P136), A131 (≠ V137), W246 (vs. gap), F299 (vs. gap), A303 (≠ L285), E306 (≠ I288)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
33% identity, 93% coverage: 4:374/401 of query aligns to 5:360/360 of 5yx6A
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
28% identity, 97% coverage: 1:387/401 of query aligns to 1:422/428 of O06644
- Q17 (≠ I17) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ N38) binding
- W48 (≠ A48) 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 (= D169) 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.
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
28% identity, 96% coverage: 2:387/401 of query aligns to 1:421/427 of 2vjoA
- active site: A16 (≠ I17), E139 (≠ D139), D168 (= D169), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ A15), A16 (≠ I17), A17 (≠ S18), R37 (≠ N38), L71 (= L71), M73 (≠ L73), N95 (= N95), F96 (= F96), G97 (≠ R97), R103 (= R103), M104 (= M104), K136 (≠ P136), V137 (= V137), Y138 (= Y138), D168 (= D169), M199 (= M200)
- binding oxalate ion: G257 (vs. gap), G259 (vs. gap), Q261 (vs. gap)
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
28% identity, 96% coverage: 2:387/401 of query aligns to 1:421/427 of 1p5rA
- active site: Q16 (≠ I17), E139 (≠ D139), D168 (= D169), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ A15), V15 (≠ M16), Q16 (≠ I17), A17 (≠ S18), R37 (≠ N38), M73 (≠ L73), K74 (= K74), N95 (= N95), F96 (= F96), A100 (≠ V100), R103 (= R103), K136 (≠ P136), V137 (= V137), D168 (= D169), M199 (= M200)
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
28% identity, 96% coverage: 2:387/401 of query aligns to 1:421/427 of 2vjkA
- active site: Q16 (≠ I17), E139 (≠ D139), D168 (= D169), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ A15), Q16 (≠ I17), A17 (≠ S18), R37 (≠ N38), M73 (≠ L73), K74 (= K74), N95 (= N95), F96 (= F96), G97 (≠ R97), R103 (= R103), M104 (= M104), K136 (≠ P136), V137 (= V137), Y138 (= Y138), D168 (= D169), M199 (= M200)
- binding magnesium ion: D293 (≠ R258), D296 (= D261)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
28% identity, 96% coverage: 2:387/401 of query aligns to 1:421/427 of 1t4cA
- active site: Q16 (≠ I17), E139 (≠ D139), D168 (= D169), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ A15), V15 (≠ M16), Q16 (≠ I17), R37 (≠ N38), M73 (≠ L73), N95 (= N95), F96 (= F96), R103 (= R103), M104 (= M104), V137 (= V137), Y138 (= Y138), D168 (= D169), M199 (= M200)
- binding oxalic acid: G259 (vs. gap), G260 (vs. gap)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
28% identity, 96% coverage: 2:387/401 of query aligns to 1:421/427 of 1t3zA
- active site: Q16 (≠ I17), E139 (≠ D139), S168 (≠ D169), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (≠ A15), V15 (≠ M16), A17 (≠ S18), R37 (≠ N38), K74 (= K74), N95 (= N95), F96 (= F96), A100 (≠ V100), R103 (= R103), M104 (= M104), K136 (≠ P136), V137 (= V137), Y138 (= Y138), E139 (≠ D139), M199 (= M200)
1xvtA Crystal structure of native caib in complex with coenzyme a (see paper)
27% identity, 98% coverage: 3:395/401 of query aligns to 7:400/402 of 1xvtA
- active site: I21 (= I17), N138 (≠ D139), D166 (= D169), G225 (≠ S221), K226 (≠ E222)
- binding coenzyme a: I21 (= I17), A22 (≠ S18), N42 (= N38), L68 (= L71), N69 (= N72), F71 (≠ K74), S93 (≠ F96), K94 (≠ R97), R100 (= R103), R101 (≠ M104), P135 (= P136), A136 (≠ V137), D166 (= D169), M197 (= M200)
P31572 L-carnitine CoA-transferase; Crotonobetainyl-CoA:carnitine CoA-transferase; EC 2.8.3.21 from Escherichia coli (strain K12) (see paper)
27% identity, 98% coverage: 3:395/401 of query aligns to 10:403/405 of P31572
- K97 (≠ R97) binding
- R104 (≠ M104) binding
1xvvA Crystal structure of caib mutant d169a in complex with carnitinyl-coa (see paper)
27% identity, 98% coverage: 3:395/401 of query aligns to 7:400/402 of 1xvvA
- active site: I21 (= I17), N138 (≠ D139), A166 (≠ L167), G225 (≠ S221), K226 (≠ E222)
- binding l-carnitinyl-coa inner salt: I19 (≠ A15), E20 (≠ M16), I21 (= I17), A22 (≠ S18), N69 (= N72), F71 (≠ K74), A92 (≠ N95), S93 (≠ F96), K94 (≠ R97), R100 (= R103), R101 (≠ M104), A136 (≠ V137), Y137 (= Y138), N138 (≠ D139), Y163 (≠ R164)
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
29% identity, 82% coverage: 1:327/401 of query aligns to 1:314/360 of O06543
- R38 (≠ N38) binding
- R52 (= R51) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S68) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ LNLK 71:74) binding
- E82 (≠ Q94) 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 (≠ I123) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ VYDPLI 137:142) binding
- H126 (≠ Y138) mutation to A: 4.5% of wild-type activity.
- D156 (≠ V174) mutation to A: 17.6 of wild-type activity.
- D190 (= D202) mutation to A: 3.3% of wild-type activity.
- E241 (≠ S249) 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, 81% coverage: 3:327/401 of query aligns to 2:309/355 of 2yimA
- active site: G16 (≠ I17), D122 (= D139), D151 (≠ V174), G214 (≠ E227), G215 (≠ A228)
- binding 2-methylacetoacetyl coa: I15 (≠ M16), R37 (≠ N38), A54 (≠ L71), L56 (= L73), K57 (= K74), G78 (≠ N95), Y79 (≠ F96), R80 (= R97), V83 (= V100), R86 (= R103), L87 (≠ M104), A119 (≠ P136), G120 (≠ V137), H121 (≠ Y138), Y125 (≠ I142), D151 (≠ V174)
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, 81% coverage: 3:327/401 of query aligns to 2:308/354 of 2gd6A
- active site: G16 (≠ I17), D121 (= D139), D150 (≠ V174), G213 (≠ E227), G214 (≠ A228)
- binding acetyl coenzyme *a: I15 (≠ M16), R37 (≠ N38), A53 (≠ L71), D54 (≠ N72), L55 (= L73), K56 (= K74), G77 (≠ N95), Y78 (≠ F96), R79 (= R97), V82 (= V100), R85 (= R103), G119 (≠ V137), H120 (≠ Y138), Y124 (≠ I142), D150 (≠ V174), 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)
28% identity, 81% coverage: 3:327/401 of query aligns to 2:308/354 of 2gd2A
- active site: G16 (≠ I17), D121 (= D139), D150 (≠ V174), G213 (≠ E227), G214 (≠ A228)
- binding acetoacetyl-coenzyme a: I15 (≠ M16), R37 (≠ N38), A53 (≠ L71), L55 (= L73), K56 (= K74), G77 (≠ N95), Y78 (≠ F96), R79 (= R97), V82 (= V100), R85 (= R103), L86 (≠ M104), A118 (≠ P136), G119 (≠ V137), H120 (≠ Y138), Y124 (≠ I142), D150 (≠ V174)
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, 81% coverage: 3:327/401 of query aligns to 2:308/354 of 2gd0A
- active site: G16 (≠ I17), D121 (= D139), D150 (≠ V174), G213 (≠ E227), G214 (≠ A228)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (≠ S47), L55 (= L73), K56 (= K74), G77 (≠ N95), Y78 (≠ F96), R79 (= R97), V82 (= V100), R85 (= R103), L86 (≠ M104), G119 (≠ V137), H120 (≠ Y138), D121 (= D139), Y124 (≠ I142), D150 (≠ V174)
Query Sequence
>GFF1451 FitnessBrowser__Marino:GFF1451
MTGPLDGIRIIDLTAMISGPLATMILADQGAEVIKIENPAGGDFTRSAANRQGDMSALYL
NNNRNKKSVALNLKKKAGRDALLRLVASADVFVQNFRPGVIERMGLGEEQLRKVAPNLVM
VSISGFGDTGPYSQRPVYDPLIQGLSGLATVQAGADELRPQLVRTILPDKLTGVTAAQAI
TAALFARERTGESQHVRLSMLDAIIAFLWSSDMGSQTFVHSEVPQQEAASLQDLIYETTT
GYITIAVQSDREWQALIRAVDRPEWAEDPRFLTARLRQENIDARLELIQSVIKTDTAEHW
LARLEAEQVPCAPVLTRTQVLDHPQVLANDLLSHYDHPQAGRLRQARAPSRFSAAPEQHW
QGAPRLGEQTGELLAECGYSAEEIQAMCDSGIAAIAATNIF
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