SitesBLAST
Comparing GFF1363 FitnessBrowser__WCS417:GFF1363 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)
29% identity, 100% coverage: 1:396/397 of query aligns to 1:428/428 of O06644
- Q17 (≠ I17) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ A38) binding
- W48 (= W48) 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 (≠ K103) 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.
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
28% identity, 99% coverage: 2:396/397 of query aligns to 1:427/427 of 2vjoA
- active site: A16 (≠ I17), E139 (≠ G139), D168 (= D168), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T15), A16 (≠ I17), A17 (= A18), R37 (≠ A38), L71 (= L71), M73 (≠ L73), N95 (= N95), F96 (≠ L96), G97 (≠ R97), R103 (≠ K103), M104 (≠ L104), K136 (≠ P136), V137 (≠ G137), Y138 (≠ F138), D168 (= D168), M199 (≠ L200)
- 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)
28% identity, 99% coverage: 2:396/397 of query aligns to 1:427/427 of 2vjkA
- active site: Q16 (≠ I17), E139 (≠ G139), D168 (= D168), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T15), Q16 (≠ I17), A17 (= A18), R37 (≠ A38), M73 (≠ L73), K74 (= K74), N95 (= N95), F96 (≠ L96), G97 (≠ R97), R103 (≠ K103), M104 (≠ L104), K136 (≠ P136), V137 (≠ G137), Y138 (≠ F138), D168 (= D168), M199 (≠ L200)
- binding magnesium ion: D293 (≠ T261), D296 (≠ G264)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
28% identity, 99% coverage: 2:396/397 of query aligns to 1:427/427 of 1t4cA
- active site: Q16 (≠ I17), E139 (≠ G139), D168 (= D168), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T15), V15 (≠ L16), Q16 (≠ I17), R37 (≠ A38), M73 (≠ L73), N95 (= N95), F96 (≠ L96), R103 (≠ K103), M104 (≠ L104), V137 (≠ G137), Y138 (≠ F138), D168 (= D168), M199 (≠ L200)
- binding oxalic acid: G259 (vs. gap), G260 (vs. gap)
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
28% identity, 99% coverage: 2:396/397 of query aligns to 1:427/427 of 1p5rA
- active site: Q16 (≠ I17), E139 (≠ G139), D168 (= D168), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T15), V15 (≠ L16), Q16 (≠ I17), A17 (= A18), R37 (≠ A38), M73 (≠ L73), K74 (= K74), N95 (= N95), F96 (≠ L96), A100 (≠ G100), R103 (≠ K103), K136 (≠ P136), V137 (≠ G137), D168 (= D168), M199 (≠ L200)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
28% identity, 99% coverage: 2:396/397 of query aligns to 1:427/427 of 1t3zA
- active site: Q16 (≠ I17), E139 (≠ G139), S168 (≠ D168), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (≠ T15), V15 (≠ L16), A17 (= A18), R37 (≠ A38), K74 (= K74), N95 (= N95), F96 (≠ L96), A100 (≠ G100), R103 (≠ K103), M104 (≠ L104), K136 (≠ P136), V137 (≠ G137), Y138 (≠ F138), E139 (≠ G139), M199 (≠ L200)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
27% identity, 99% coverage: 2:396/397 of query aligns to 2:428/430 of 3ubmB
- active site: Q17 (≠ I17), E140 (≠ G139), D182 (= D168), G261 (vs. gap), G262 (vs. gap)
- binding coenzyme a: V16 (≠ L16), R38 (≠ A38), L72 (= L71), N73 (≠ D72), T74 (≠ L73), K75 (= K74), N96 (= N95), F97 (≠ L96), R98 (= R97), A101 (≠ G100), R104 (≠ K103), K125 (≠ S124), D182 (= D168), M213 (≠ L200)
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: 1:391/397 of query aligns to 1:411/416 of P69902
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
27% identity, 100% coverage: 1:397/397 of query aligns to 1:417/417 of 1q6yA
- active site: Q17 (≠ I17), E140 (≠ G139), D169 (= D168), G248 (vs. gap), G249 (vs. gap)
- binding coenzyme a: V16 (≠ L16), Q17 (≠ I17), S18 (≠ A18), R38 (≠ A38), L72 (= L71), N73 (≠ D72), T74 (≠ L73), K75 (= K74), N96 (= N95), F97 (≠ L96), H98 (≠ R97), M105 (≠ L104), I124 (= I123), K137 (≠ P136), A138 (≠ G137), Y139 (≠ F138), D169 (= D168), M200 (≠ L200)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
28% identity, 98% coverage: 2:391/397 of query aligns to 1:410/415 of 1pt5A
- active site: Q16 (≠ I17), E139 (≠ G139), D168 (= D168), G247 (vs. gap), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (≠ L16), S17 (≠ A18), R37 (≠ A38), L71 (= L71), N72 (≠ D72), T73 (≠ L73), K74 (= K74), N95 (= N95), F96 (≠ L96), H97 (≠ R97), K124 (≠ S124), K136 (≠ P136), A137 (≠ G137), Y138 (≠ F138), E139 (≠ G139), D168 (= D168), M199 (≠ L200)
1xvtA Crystal structure of native caib in complex with coenzyme a (see paper)
28% identity, 99% coverage: 4:397/397 of query aligns to 8:399/402 of 1xvtA
- active site: I21 (= I17), N138 (≠ G139), D166 (= D168), G225 (= G227), K226 (≠ A228)
- binding coenzyme a: I21 (= I17), A22 (= A18), N42 (≠ A38), L68 (= L71), N69 (≠ D72), F71 (≠ K74), S93 (≠ L96), K94 (≠ R97), R100 (≠ K103), R101 (≠ L104), P135 (= P136), A136 (≠ G137), D166 (= D168), M197 (≠ L200)
P31572 L-carnitine CoA-transferase; Crotonobetainyl-CoA:carnitine CoA-transferase; EC 2.8.3.21 from Escherichia coli (strain K12) (see paper)
28% identity, 99% coverage: 4:397/397 of query aligns to 11:402/405 of P31572
- K97 (≠ R97) binding
- R104 (≠ L104) binding
1xvvA Crystal structure of caib mutant d169a in complex with carnitinyl-coa (see paper)
28% identity, 99% coverage: 4:397/397 of query aligns to 8:399/402 of 1xvvA
- active site: I21 (= I17), N138 (≠ G139), A166 (≠ L166), G225 (= G227), K226 (≠ A228)
- binding l-carnitinyl-coa inner salt: I19 (≠ T15), E20 (≠ L16), I21 (= I17), A22 (= A18), N69 (≠ D72), F71 (≠ K74), A92 (≠ N95), S93 (≠ L96), K94 (≠ R97), R100 (≠ K103), R101 (≠ L104), A136 (≠ G137), Y137 (≠ F138), N138 (≠ G139), Y163 (≠ G163)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
27% identity, 100% coverage: 1:397/397 of query aligns to 1:410/410 of 1q7eA
- active site: Q17 (≠ I17), E133 (≠ G139), D162 (= D168), G241 (vs. gap), G242 (vs. gap)
- binding methionine: N96 (= N95), F97 (≠ L96), H98 (≠ R97), P99 (= P98), K118 (≠ S124), K130 (≠ P136), A131 (≠ G137), W246 (vs. gap), F299 (≠ G285), A303 (= A289), E306 (≠ T292)
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
27% identity, 99% coverage: 5:397/397 of query aligns to 3:374/382 of Q9UHK6
- V9 (= V11) to M: in dbSNP:rs3195676
- S52 (= S68) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ I123) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G191) to D: in dbSNP:rs10941112
- L201 (≠ M217) to S: in dbSNP:rs2287939
- M261 (≠ H276) to T: in dbSNP:rs3195678
- E277 (vs. gap) 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, 84% coverage: 4:336/397 of query aligns to 5:324/360 of 5yx6A
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
29% identity, 90% coverage: 1:358/397 of query aligns to 1:337/360 of O06543
- R38 (≠ A38) binding
- R52 (= R64) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S68) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ LDLK 71:74) binding
- E82 (= E94) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NLR 95:97) binding
- R91 (≠ K103) binding ; mutation to A: 19.9% of wild-type activity.
- M111 (≠ I123) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ GFGAIG 137:142) binding
- H126 (≠ F138) mutation to A: 4.5% of wild-type activity.
- D156 (≠ V164) mutation to A: 17.6 of wild-type activity.
- D190 (≠ E202) mutation to A: 3.3% of wild-type activity.
- E241 (≠ S252) mutation to A: 2.1% of wild-type activity.
- C297 (≠ P313) mutation to A: 6.2% of wild-type activity.
- H312 (= H328) 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)
29% identity, 89% coverage: 4:358/397 of query aligns to 3:331/354 of 2gd6A
- active site: G16 (≠ I17), D121 (≠ G139), D150 (≠ V164), G213 (= G231), G214 (≠ I232)
- binding acetyl coenzyme *a: I15 (≠ L16), R37 (= R49), A53 (≠ L71), D54 (= D72), L55 (= L73), K56 (= K74), G77 (≠ N95), Y78 (≠ L96), R79 (= R97), V82 (≠ G100), R85 (≠ K103), G119 (= G137), H120 (≠ F138), Y124 (≠ G142), D150 (≠ V164), M182 (≠ L200)
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)
29% identity, 89% coverage: 4:358/397 of query aligns to 3:331/354 of 2gd2A
- active site: G16 (≠ I17), D121 (≠ G139), D150 (≠ V164), G213 (= G231), G214 (≠ I232)
- binding acetoacetyl-coenzyme a: I15 (≠ L16), R37 (= R49), A53 (≠ L71), L55 (= L73), K56 (= K74), G77 (≠ N95), Y78 (≠ L96), R79 (= R97), V82 (≠ G100), R85 (≠ K103), L86 (= L104), A118 (≠ P136), G119 (= G137), H120 (≠ F138), Y124 (≠ G142), D150 (≠ V164)
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)
29% identity, 89% coverage: 4:358/397 of query aligns to 3:331/354 of 2gd0A
- active site: G16 (≠ I17), D121 (≠ G139), D150 (≠ V164), G213 (= G231), G214 (≠ I232)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (≠ G54), L55 (= L73), K56 (= K74), G77 (≠ N95), Y78 (≠ L96), R79 (= R97), V82 (≠ G100), R85 (≠ K103), L86 (= L104), G119 (= G137), H120 (≠ F138), D121 (≠ G139), Y124 (≠ G142), D150 (≠ V164)
Query Sequence
>GFF1363 FitnessBrowser__WCS417:GFF1363
MTAPLSGIKVVEIGTLIAAPFAARMMAEFGAEVIKIEAMGQGDPLRKWRKLHEGTSLWWY
LQSRNKKSLALDLKSPEGLDLIKQLLGDADVLIENLRPGGLEKLGLGWDVLHALNPKLTL
VRISGYGQTGPYRDRPGFGAIGEAMGGIRYTTGNPDSPPARVGVSLGDSLASLHGVIGAL
MSLLRVKTGQGDGQIVDVSLAESVFNLMESLVPEYDMLGHVRERSGGALPGIAPSNTYLT
ADGAYVVIAGNSDPIYKRLMTTIGRADLAEAPEFVHNDGRAAKSGLLDAAITHWTSSRPI
EQVLSALEAAEVPAGRIYSVADIVSDPHYQARDMLLNAELPGGVSVKMPGIVPKLSETPG
GVNWQGPTLGQHTDDILGSLGLTGADIQRLKTAGVVQ
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