SitesBLAST
Comparing Dsui_0037 FitnessBrowser__PS:Dsui_0037 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)
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)
29% identity, 98% coverage: 11:403/403 of query aligns to 4:416/416 of P69902
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
29% identity, 98% coverage: 11:403/403 of query aligns to 4:416/417 of 1q6yA
- active site: Q17 (≠ I24), E140 (≠ G146), D169 (= D175), G248 (vs. gap), G249 (vs. gap)
- binding coenzyme a: V16 (≠ L23), Q17 (≠ I24), S18 (≠ A25), R38 (≠ S45), L72 (≠ V78), N73 (= N79), T74 (≠ L80), K75 (= K81), N96 (= N102), F97 (= F103), H98 (≠ R104), M105 (≠ L111), I124 (≠ L130), K137 (≠ P143), A138 (≠ G144), Y139 (≠ F145), D169 (= D175), M200 (≠ L207)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
29% identity, 98% coverage: 11:403/403 of query aligns to 3:415/415 of 1pt5A
- active site: Q16 (≠ I24), E139 (≠ G146), D168 (= D175), G247 (vs. gap), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (≠ L23), S17 (≠ A25), R37 (≠ S45), L71 (≠ V78), N72 (= N79), T73 (≠ L80), K74 (= K81), N95 (= N102), F96 (= F103), H97 (≠ R104), K124 (≠ S131), K136 (≠ P143), A137 (≠ G144), Y138 (≠ F145), E139 (≠ G146), D168 (= D175), M199 (≠ L207)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
29% identity, 97% coverage: 10:399/403 of query aligns to 3:424/430 of 3ubmB
- active site: Q17 (≠ I24), E140 (≠ G146), D182 (= D175), G261 (vs. gap), G262 (vs. gap)
- binding coenzyme a: V16 (≠ L23), R38 (≠ S45), L72 (≠ V78), N73 (= N79), T74 (≠ L80), K75 (= K81), N96 (= N102), F97 (= F103), R98 (= R104), A101 (≠ V107), R104 (≠ K110), K125 (≠ S131), D182 (= D175), M213 (≠ L207)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
29% identity, 98% coverage: 11:403/403 of query aligns to 4:409/410 of 1q7eA
- active site: Q17 (≠ I24), E133 (≠ G146), D162 (= D175), G241 (vs. gap), G242 (vs. gap)
- binding methionine: N96 (= N102), F97 (= F103), H98 (≠ R104), P99 (= P105), K118 (≠ S131), K130 (≠ P143), A131 (≠ G144), W246 (vs. gap), F299 (≠ D292), A303 (= A296), E306 (≠ D299)
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
26% identity, 97% coverage: 10:398/403 of query aligns to 2:422/427 of 2vjoA
- active site: A16 (≠ I24), E139 (≠ G146), D168 (= D175), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T22), A16 (≠ I24), A17 (= A25), R37 (≠ S45), L71 (≠ V78), M73 (≠ L80), N95 (= N102), F96 (= F103), G97 (≠ R104), R103 (≠ K110), M104 (≠ L111), K136 (≠ P143), V137 (≠ G144), Y138 (≠ F145), D168 (= D175), M199 (≠ L207)
- 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)
26% identity, 97% coverage: 10:398/403 of query aligns to 2:422/427 of 2vjkA
- active site: Q16 (≠ I24), E139 (≠ G146), D168 (= D175), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T22), Q16 (≠ I24), A17 (= A25), R37 (≠ S45), M73 (≠ L80), K74 (= K81), N95 (= N102), F96 (= F103), G97 (≠ R104), R103 (≠ K110), M104 (≠ L111), K136 (≠ P143), V137 (≠ G144), Y138 (≠ F145), D168 (= D175), M199 (≠ L207)
- binding magnesium ion: D293 (≠ R268), D296 (≠ G271)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
26% identity, 97% coverage: 10:398/403 of query aligns to 2:422/427 of 1t4cA
- active site: Q16 (≠ I24), E139 (≠ G146), D168 (= D175), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T22), V15 (≠ L23), Q16 (≠ I24), R37 (≠ S45), M73 (≠ L80), N95 (= N102), F96 (= F103), R103 (≠ K110), M104 (≠ L111), V137 (≠ G144), Y138 (≠ F145), D168 (= D175), M199 (≠ L207)
- binding oxalic acid: G259 (vs. gap), G260 (vs. gap)
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
26% identity, 97% coverage: 10:398/403 of query aligns to 2:422/427 of 1p5rA
- active site: Q16 (≠ I24), E139 (≠ G146), D168 (= D175), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T22), V15 (≠ L23), Q16 (≠ I24), A17 (= A25), R37 (≠ S45), M73 (≠ L80), K74 (= K81), N95 (= N102), F96 (= F103), A100 (≠ V107), R103 (≠ K110), K136 (≠ P143), V137 (≠ G144), D168 (= D175), M199 (≠ L207)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
26% identity, 97% coverage: 10:398/403 of query aligns to 3:423/428 of O06644
- Q17 (≠ I24) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ S45) binding
- W48 (= W55) 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 (≠ K110) binding
- D169 (= D175) 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.
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
26% identity, 97% coverage: 10:398/403 of query aligns to 2:422/427 of 1t3zA
- active site: Q16 (≠ I24), E139 (≠ G146), S168 (≠ D175), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (≠ T22), V15 (≠ L23), A17 (= A25), R37 (≠ S45), K74 (= K81), N95 (= N102), F96 (= F103), A100 (≠ V107), R103 (≠ K110), M104 (≠ L111), K136 (≠ P143), V137 (≠ G144), Y138 (≠ F145), E139 (≠ G146), M199 (≠ L207)
1xvvA Crystal structure of caib mutant d169a in complex with carnitinyl-coa (see paper)
28% identity, 97% coverage: 11:401/403 of query aligns to 8:396/402 of 1xvvA
- active site: I21 (= I24), N138 (≠ G146), A166 (≠ G170), G225 (≠ I235), K226 (≠ M236)
- binding l-carnitinyl-coa inner salt: I19 (≠ T22), E20 (≠ L23), I21 (= I24), A22 (= A25), N69 (= N79), F71 (≠ K81), A92 (≠ N102), S93 (≠ F103), K94 (≠ R104), R100 (≠ K110), R101 (≠ L111), A136 (≠ G144), Y137 (≠ F145), N138 (≠ G146), Y163 (≠ V167)
1xvtA Crystal structure of native caib in complex with coenzyme a (see paper)
28% identity, 97% coverage: 11:401/403 of query aligns to 8:396/402 of 1xvtA
- active site: I21 (= I24), N138 (≠ G146), D166 (≠ G170), G225 (≠ I235), K226 (≠ M236)
- binding coenzyme a: I21 (= I24), A22 (= A25), N42 (≠ S45), L68 (≠ V78), N69 (= N79), F71 (≠ K81), S93 (≠ F103), K94 (≠ R104), R100 (≠ K110), R101 (≠ L111), P135 (= P143), A136 (≠ G144), D166 (≠ G170), M197 (≠ L207)
P31572 L-carnitine CoA-transferase; Crotonobetainyl-CoA:carnitine CoA-transferase; EC 2.8.3.21 from Escherichia coli (strain K12) (see paper)
28% identity, 97% coverage: 11:401/403 of query aligns to 11:399/405 of P31572
- K97 (≠ R104) binding
- R104 (≠ L111) binding
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
30% identity, 83% coverage: 11:346/403 of query aligns to 4:323/360 of O06543
- R38 (≠ S45) binding
- R52 (= R71) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S75) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ VNLK 78:81) binding
- E82 (= E101) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NFR 102:104) binding
- R91 (≠ K110) binding ; mutation to A: 19.9% of wild-type activity.
- M111 (≠ L130) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ GFGAVG 144:149) binding
- H126 (≠ F145) mutation to A: 4.5% of wild-type activity.
- D156 (= D175) mutation to A: 17.6 of wild-type activity.
- D190 (≠ E209) mutation to A: 3.3% of wild-type activity.
- E241 (≠ G259) mutation to A: 2.1% of wild-type activity.
- C297 (≠ P320) mutation to A: 6.2% of wild-type activity.
- H312 (≠ Q335) mutation to 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)
30% identity, 83% coverage: 11:345/403 of query aligns to 3:316/354 of 2gd6A
- active site: G16 (≠ I24), D121 (≠ G146), D150 (= D175), G213 (= G238), G214 (≠ I239)
- binding acetyl coenzyme *a: I15 (≠ L23), R37 (≠ S45), A53 (≠ V78), D54 (≠ N79), L55 (= L80), K56 (= K81), G77 (≠ N102), Y78 (≠ F103), R79 (= R104), V82 (= V107), R85 (≠ K110), G119 (= G144), H120 (≠ F145), Y124 (≠ G149), D150 (= D175), M182 (≠ L207)
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)
30% identity, 83% coverage: 11:345/403 of query aligns to 3:316/354 of 2gd2A
- active site: G16 (≠ I24), D121 (≠ G146), D150 (= D175), G213 (= G238), G214 (≠ I239)
- binding acetoacetyl-coenzyme a: I15 (≠ L23), R37 (≠ S45), A53 (≠ V78), L55 (= L80), K56 (= K81), G77 (≠ N102), Y78 (≠ F103), R79 (= R104), V82 (= V107), R85 (≠ K110), L86 (= L111), A118 (≠ P143), G119 (= G144), H120 (≠ F145), Y124 (≠ G149), D150 (= D175)
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)
30% identity, 83% coverage: 11:345/403 of query aligns to 3:316/354 of 2gd0A
- active site: G16 (≠ I24), D121 (≠ G146), D150 (= D175), G213 (= G238), G214 (≠ I239)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D50), L55 (= L80), K56 (= K81), G77 (≠ N102), Y78 (≠ F103), R79 (= R104), V82 (= V107), R85 (≠ K110), L86 (= L111), G119 (= G144), H120 (≠ F145), D121 (≠ G146), Y124 (≠ G149), D150 (= D175)
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)
30% identity, 83% coverage: 11:345/403 of query aligns to 3:316/354 of 2gciA
- active site: G16 (≠ I24), D121 (≠ G146), D150 (= D175), G213 (= G238), G214 (≠ I239)
- binding (r)-2-methylmyristoyl-coenzyme a: R37 (≠ S45), L55 (= L80), K56 (= K81), G77 (≠ N102), Y78 (≠ F103), R79 (= R104), V82 (= V107), G119 (= G144), H120 (≠ F145), D121 (≠ G146), Y124 (≠ G149), D150 (= D175), Y218 (≠ S242), I234 (≠ N258), E235 (≠ G259)
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)
30% identity, 83% coverage: 11:345/403 of query aligns to 3:316/354 of 2gceA
- active site: G16 (≠ I24), D121 (≠ G146), D150 (= D175), G213 (= G238), G214 (≠ I239)
- binding (r)-ibuprofenoyl-coenzyme a: I15 (≠ L23), R37 (≠ S45), L55 (= L80), K56 (= K81), G77 (≠ N102), Y78 (≠ F103), R79 (= R104), V82 (= V107), R85 (≠ K110), G119 (= G144), H120 (≠ F145), D121 (≠ G146), Y124 (≠ G149), D150 (= D175), L211 (≠ M236), Y218 (≠ S242), I234 (≠ N258)
- binding (s)-ibuprofenoyl-coenzyme a: I15 (≠ L23), G16 (≠ I24), P17 (≠ A25), R37 (≠ S45), L55 (= L80), K56 (= K81), G77 (≠ N102), Y78 (≠ F103), R79 (= R104), V82 (= V107), R85 (≠ K110), G119 (= G144), H120 (≠ F145), Y124 (≠ G149), D150 (= D175)
Query Sequence
>Dsui_0037 FitnessBrowser__PS:Dsui_0037
MSPAASCPPKPLAGLKVVELGTLIAGPFASRLLAEFGAEVVKIESPDGGDPLRKWRKLYE
GTSLWWFVQSRNKQSVTVNLKHPQGRDIVRKLVAEADIVVENFRPGVMEKLGLSWEELSA
LNPGLVMLRLSGFGQTGPYKDQPGFGAVGESMGGLRYITGFADRPPVRTGISIGDSIAAL
WGVFGTLMALRHKEVQGGKGQVVDVALYEAIFAMMESLVPEFDVFGFVRERTGNIMPGIT
PSNTHKTRDGKFVTIGANGDAIFQRLMRALGREDLATDPGLADNAGRDGRRDEVYALIDA
WVAGLDEAELLAKLEAAEVPASRVYSVADMFADPQFLAREMIQSARLPDGKDFKVPGIVP
KLSATPGGTEWLGPGLGEHTEAVLTRLGYDAEAIAALREAGAI
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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