SitesBLAST
Comparing GFF2916 FitnessBrowser__WCS417:GFF2916 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)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
31% identity, 99% coverage: 6:397/397 of query aligns to 3:415/415 of 1pt5A
- active site: Q16 (≠ I19), E139 (≠ D141), D168 (= D171), G247 (≠ A230), G248 (≠ H231)
- binding acetyl coenzyme *a: V15 (≠ A18), S17 (≠ A20), R37 (= R40), L71 (= L73), N72 (≠ D74), T73 (≠ L75), K74 (= K76), N95 (= N97), F96 (≠ L98), H97 (≠ A99), K124 (≠ S126), K136 (= K138), A137 (= A139), Y138 (= Y140), E139 (≠ D141), D168 (= D171), M199 (= M202)
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, 99% coverage: 6:397/397 of query aligns to 4:416/416 of P69902
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
31% identity, 99% coverage: 6:397/397 of query aligns to 4:416/417 of 1q6yA
- active site: Q17 (≠ I19), E140 (≠ D141), D169 (= D171), G248 (≠ A230), G249 (≠ H231)
- binding coenzyme a: V16 (≠ A18), Q17 (≠ I19), S18 (≠ A20), R38 (= R40), L72 (= L73), N73 (≠ D74), T74 (≠ L75), K75 (= K76), N96 (= N97), F97 (≠ L98), H98 (≠ A99), M105 (= M106), I124 (= I125), K137 (= K138), A138 (= A139), Y139 (= Y140), D169 (= D171), M200 (= M202)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
28% identity, 99% coverage: 3:396/397 of query aligns to 1:427/430 of 3ubmB
- active site: Q17 (≠ I19), E140 (≠ D141), D182 (= D171), G261 (≠ T233), G262 (vs. gap)
- binding coenzyme a: V16 (≠ A18), R38 (= R40), L72 (= L73), N73 (≠ D74), T74 (≠ L75), K75 (= K76), N96 (= N97), F97 (≠ L98), R98 (≠ A99), A101 (= A102), R104 (= R105), K125 (≠ S126), D182 (= D171), M213 (= M202)
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
29% identity, 99% coverage: 5:397/397 of query aligns to 2:427/427 of 2vjoA
- active site: A16 (≠ I19), E139 (≠ D141), D168 (= D171), G259 (≠ T233), G260 (≠ I234)
- binding coenzyme a: H14 (= H17), A16 (≠ I19), A17 (= A20), R37 (= R40), L71 (= L73), M73 (≠ L75), N95 (= N97), F96 (≠ L98), G97 (≠ A99), R103 (= R105), M104 (= M106), K136 (= K138), V137 (≠ A139), Y138 (= Y140), D168 (= D171), M199 (= M202)
- binding oxalate ion: G257 (≠ H231), G259 (≠ T233), Q261 (≠ Y235)
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
29% identity, 99% coverage: 5:397/397 of query aligns to 2:427/427 of 1p5rA
- active site: Q16 (≠ I19), E139 (≠ D141), D168 (= D171), G259 (≠ T233), G260 (≠ I234)
- binding coenzyme a: H14 (= H17), V15 (≠ A18), Q16 (≠ I19), A17 (= A20), R37 (= R40), M73 (≠ L75), K74 (= K76), N95 (= N97), F96 (≠ L98), A100 (= A102), R103 (= R105), K136 (= K138), V137 (≠ A139), D168 (= D171), M199 (= M202)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
29% identity, 99% coverage: 5:397/397 of query aligns to 3:428/428 of O06644
- Q17 (≠ I19) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (= R40) binding
- W48 (≠ Y50) 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 (= D171) 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 (≠ S232) mutation to A: 2.5-fold decrease of the catalytic effiency.
- G260 (≠ T233) 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)
29% identity, 99% coverage: 5:397/397 of query aligns to 2:427/427 of 2vjkA
- active site: Q16 (≠ I19), E139 (≠ D141), D168 (= D171), G259 (≠ T233), G260 (≠ I234)
- binding coenzyme a: H14 (= H17), Q16 (≠ I19), A17 (= A20), R37 (= R40), M73 (≠ L75), K74 (= K76), N95 (= N97), F96 (≠ L98), G97 (≠ A99), R103 (= R105), M104 (= M106), K136 (= K138), V137 (≠ A139), Y138 (= Y140), D168 (= D171), M199 (= M202)
- binding magnesium ion: D293 (= D263), D296 (≠ L267)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
29% identity, 99% coverage: 5:397/397 of query aligns to 2:427/427 of 1t4cA
- active site: Q16 (≠ I19), E139 (≠ D141), D168 (= D171), G259 (≠ T233), G260 (≠ I234)
- binding coenzyme a: H14 (= H17), V15 (≠ A18), Q16 (≠ I19), R37 (= R40), M73 (≠ L75), N95 (= N97), F96 (≠ L98), R103 (= R105), M104 (= M106), V137 (≠ A139), Y138 (= Y140), D168 (= D171), M199 (= M202)
- binding oxalic acid: G259 (≠ T233), G260 (≠ I234)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
29% identity, 99% coverage: 5:397/397 of query aligns to 2:427/427 of 1t3zA
- active site: Q16 (≠ I19), E139 (≠ D141), S168 (≠ D171), G259 (≠ T233), G260 (≠ I234)
- binding oxidized coenzyme a: H14 (= H17), V15 (≠ A18), A17 (= A20), R37 (= R40), K74 (= K76), N95 (= N97), F96 (≠ L98), A100 (= A102), R103 (= R105), M104 (= M106), K136 (= K138), V137 (≠ A139), Y138 (= Y140), E139 (≠ D141), M199 (= M202)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
30% identity, 99% coverage: 6:397/397 of query aligns to 4:409/410 of 1q7eA
- active site: Q17 (≠ I19), E133 (≠ D141), D162 (= D171), G241 (≠ A230), G242 (≠ H231)
- binding methionine: N96 (= N97), F97 (≠ L98), H98 (≠ A99), P99 (= P100), K118 (≠ S126), K130 (= K138), A131 (= A139), W246 (vs. gap), F299 (≠ V295), A303 (= A299), E306 (vs. gap)
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
28% identity, 98% coverage: 7:397/397 of query aligns to 3:373/382 of Q9UHK6
- V9 (= V13) to M: in dbSNP:rs3195676
- S52 (= S70) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ I125) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G193) to D: in dbSNP:rs10941112
- L201 (≠ D219) to S: in dbSNP:rs2287939
- M261 (≠ S284) to T: in dbSNP:rs3195678
- E277 (≠ Q300) to K: in dbSNP:rs2278008
Sites not aligning to the query:
- 380:382 Microbody targeting signal
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
29% identity, 95% coverage: 3:378/397 of query aligns to 1:360/360 of 5yx6A
1xvtA Crystal structure of native caib in complex with coenzyme a (see paper)
27% identity, 98% coverage: 6:396/397 of query aligns to 8:397/402 of 1xvtA
- active site: I21 (= I19), N138 (≠ D141), D166 (= D171), G225 (≠ A230), K226 (≠ H231)
- binding coenzyme a: I21 (= I19), A22 (= A20), N42 (≠ R40), L68 (= L73), N69 (≠ D74), F71 (≠ K76), S93 (≠ L98), K94 (≠ A99), R100 (= R105), R101 (≠ M106), P135 (≠ K138), A136 (= A139), D166 (= D171), M197 (= M202)
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: 6:396/397 of query aligns to 11:400/405 of P31572
- K97 (≠ A99) binding
- R104 (≠ M106) binding
1xvvA Crystal structure of caib mutant d169a in complex with carnitinyl-coa (see paper)
27% identity, 98% coverage: 6:396/397 of query aligns to 8:397/402 of 1xvvA
- active site: I21 (= I19), N138 (≠ D141), A166 (≠ D171), G225 (≠ A230), K226 (≠ H231)
- binding l-carnitinyl-coa inner salt: I19 (≠ H17), E20 (≠ A18), I21 (= I19), A22 (= A20), N69 (≠ D74), F71 (≠ K76), A92 (≠ N97), S93 (≠ L98), K94 (≠ A99), R100 (= R105), R101 (≠ M106), A136 (= A139), Y137 (= Y140), N138 (≠ D141), Y163 (≠ S168)
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
26% identity, 90% coverage: 6:363/397 of query aligns to 4:343/360 of O06543
- R38 (= R40) binding
- R52 (≠ T64) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S70) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ LDLK 73:76) binding
- E82 (≠ Q96) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NLA 97:99) binding
- R91 (= R105) binding ; mutation to A: 19.9% of wild-type activity.
- M111 (≠ I125) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ AYDLLI 139:144) binding
- H126 (≠ Y140) mutation to A: 4.5% of wild-type activity.
- D156 (= D171) mutation to A: 17.6 of wild-type activity.
- D190 (≠ E204) mutation to A: 3.3% of wild-type activity.
- E241 (≠ N254) mutation to A: 2.1% of wild-type activity.
- C297 (≠ A316) mutation to A: 6.2% of wild-type activity.
- H312 (≠ Q331) 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)
26% identity, 90% coverage: 6:363/397 of query aligns to 3:337/354 of 2gd6A
- active site: G16 (≠ I19), D121 (= D141), D150 (= D171), G213 (≠ T233), G214 (≠ I234)
- binding acetyl coenzyme *a: I15 (≠ A18), R37 (= R40), A53 (≠ L73), D54 (= D74), L55 (= L75), K56 (= K76), G77 (≠ N97), Y78 (≠ L98), R79 (≠ A99), V82 (≠ A102), R85 (= R105), G119 (≠ A139), H120 (≠ Y140), Y124 (≠ I144), D150 (= D171), M182 (= M202)
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)
26% identity, 90% coverage: 6:363/397 of query aligns to 3:337/354 of 2gd2A
- active site: G16 (≠ I19), D121 (= D141), D150 (= D171), G213 (≠ T233), G214 (≠ I234)
- binding acetoacetyl-coenzyme a: I15 (≠ A18), R37 (= R40), A53 (≠ L73), L55 (= L75), K56 (= K76), G77 (≠ N97), Y78 (≠ L98), R79 (≠ A99), V82 (≠ A102), R85 (= R105), L86 (≠ M106), A118 (≠ K138), G119 (≠ A139), H120 (≠ Y140), Y124 (≠ I144), D150 (= D171)
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)
26% identity, 90% coverage: 6:363/397 of query aligns to 3:337/354 of 2gd0A
- active site: G16 (≠ I19), D121 (= D141), D150 (= D171), G213 (≠ T233), G214 (≠ I234)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D45), L55 (= L75), K56 (= K76), G77 (≠ N97), Y78 (≠ L98), R79 (≠ A99), V82 (≠ A102), R85 (= R105), L86 (≠ M106), G119 (≠ A139), H120 (≠ Y140), D121 (= D141), Y124 (≠ I144), D150 (= D171)
Query Sequence
>GFF2916 FitnessBrowser__WCS417:GFF2916
MTNPRPLDGITVVSLEHAIAAPFCTRQLADLGARVIKVERPGAGDFARGYDERVRGLASH
FVWTNRSKESLTLDLKQEEAGTILDTLLADADVLVQNLAPGAAARMGLSFEALHERFPRL
IVCDISGYGEGGPYEKKKAYDLLIQSEGGFLSVTGGPGEDQMAKAGCSIADISAGMYAYS
GILSALLLRGKTGKGSRIDVSMLESLVEWMGYPMYYAFDGAPQPPRAGAAHSTIYPYGPF
PTGDGGTVMLGLQNEREWAAFCDKVLLTPALATDERFSANFKRSANREVLRQIIVDSFAQ
LDAEAVIQRLESAQIASARVNDMQGVWDHPQLKARDSWRAVDSPAGPLPALLPPARNAAF
TPRMDGVPGLGQHSQGILDGLGYSTDAIDGLRARGVI
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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