SitesBLAST
Comparing PfGW456L13_3635 L-carnitine dehydratase/bile acid-inducible protein F 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, 96% coverage: 2:392/409 of query aligns to 3:428/428 of O06644
- Q17 (≠ L16) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ P37) binding
- W48 (= W47) 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 (≠ S102) binding
- D169 (= D167) 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, 96% coverage: 2:392/409 of query aligns to 2:427/427 of 1p5rA
- active site: Q16 (≠ L16), E139 (≠ D138), D168 (= D167), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R14), V15 (≠ A15), Q16 (≠ L16), A17 (≠ S17), R37 (≠ P37), M73 (≠ L72), K74 (≠ R73), N95 (= N94), F96 (= F95), A100 (≠ T99), R103 (≠ S102), K136 (≠ P135), V137 (≠ G136), D168 (= D167), M199 (≠ L198)
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
32% identity, 96% coverage: 2:392/409 of query aligns to 2:427/427 of 2vjoA
- active site: A16 (≠ L16), E139 (≠ D138), D168 (= D167), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R14), A16 (≠ L16), A17 (≠ S17), R37 (≠ P37), L71 (≠ I70), M73 (≠ L72), N95 (= N94), F96 (= F95), G97 (≠ K96), R103 (≠ S102), M104 (= M103), K136 (≠ P135), V137 (≠ G136), Y138 (≠ F137), D168 (= D167), M199 (≠ L198)
- 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)
32% identity, 96% coverage: 2:392/409 of query aligns to 2:427/427 of 2vjkA
- active site: Q16 (≠ L16), E139 (≠ D138), D168 (= D167), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R14), Q16 (≠ L16), A17 (≠ S17), R37 (≠ P37), M73 (≠ L72), K74 (≠ R73), N95 (= N94), F96 (= F95), G97 (≠ K96), R103 (≠ S102), M104 (= M103), K136 (≠ P135), V137 (≠ G136), Y138 (≠ F137), D168 (= D167), M199 (≠ L198)
- binding magnesium ion: D293 (≠ I258), D296 (= D261)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
32% identity, 96% coverage: 2:392/409 of query aligns to 2:427/427 of 1t4cA
- active site: Q16 (≠ L16), E139 (≠ D138), D168 (= D167), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R14), V15 (≠ A15), Q16 (≠ L16), R37 (≠ P37), M73 (≠ L72), N95 (= N94), F96 (= F95), R103 (≠ S102), M104 (= M103), V137 (≠ G136), Y138 (≠ F137), D168 (= D167), M199 (≠ L198)
- binding oxalic acid: G259 (vs. gap), G260 (vs. gap)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
32% identity, 96% coverage: 2:392/409 of query aligns to 2:427/427 of 1t3zA
- active site: Q16 (≠ L16), E139 (≠ D138), S168 (≠ D167), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (≠ R14), V15 (≠ A15), A17 (≠ S17), R37 (≠ P37), K74 (≠ R73), N95 (= N94), F96 (= F95), A100 (≠ T99), R103 (≠ S102), M104 (= M103), K136 (≠ P135), V137 (≠ G136), Y138 (≠ F137), E139 (≠ D138), M199 (≠ L198)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
30% identity, 95% coverage: 2:391/409 of query aligns to 3:427/430 of 3ubmB
- active site: Q17 (≠ L16), E140 (≠ D138), D182 (= D167), G261 (≠ S228), G262 (≠ V229)
- binding coenzyme a: V16 (≠ A15), R38 (≠ P37), L72 (≠ I70), N73 (≠ D71), T74 (≠ L72), K75 (≠ R73), N96 (= N94), F97 (= F95), R98 (≠ K96), A101 (≠ T99), R104 (≠ S102), K125 (≠ N123), D182 (= D167), M213 (≠ L198)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
32% identity, 94% coverage: 4:386/409 of query aligns to 4:409/415 of 1pt5A
- active site: Q16 (≠ L16), E139 (≠ D138), D168 (= D167), G247 (≠ S228), G248 (≠ V229)
- binding acetyl coenzyme *a: V15 (≠ A15), S17 (= S17), R37 (≠ P37), L71 (≠ I70), N72 (≠ D71), T73 (≠ L72), K74 (≠ R73), N95 (= N94), F96 (= F95), H97 (≠ K96), K124 (≠ N123), K136 (≠ P135), A137 (≠ G136), Y138 (≠ F137), E139 (≠ D138), D168 (= D167), M199 (≠ L198)
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)
32% identity, 94% coverage: 4:386/409 of query aligns to 5:410/416 of P69902
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
32% identity, 94% coverage: 4:386/409 of query aligns to 5:410/417 of 1q6yA
- active site: Q17 (≠ L16), E140 (≠ D138), D169 (= D167), G248 (≠ S228), G249 (≠ V229)
- binding coenzyme a: V16 (≠ A15), Q17 (≠ L16), S18 (= S17), R38 (≠ P37), L72 (≠ I70), N73 (≠ D71), T74 (≠ L72), K75 (≠ R73), N96 (= N94), F97 (= F95), H98 (≠ K96), M105 (= M103), I124 (= I122), K137 (≠ P135), A138 (≠ G136), Y139 (≠ F137), D169 (= D167), M200 (≠ L198)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
33% identity, 91% coverage: 2:373/409 of query aligns to 4:360/360 of 5yx6A
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
31% identity, 94% coverage: 4:386/409 of query aligns to 5:403/410 of 1q7eA
- active site: Q17 (≠ L16), E133 (≠ D138), D162 (= D167), G241 (≠ S228), G242 (≠ V229)
- binding methionine: N96 (= N94), F97 (= F95), H98 (≠ K96), P99 (= P97), K118 (≠ N123), K130 (≠ P135), A131 (≠ G136), W246 (≠ Y233), F299 (≠ D282), A303 (≠ E286), E306 (= E289)
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
28% identity, 96% coverage: 3:396/409 of query aligns to 2:377/382 of Q9UHK6
- V9 (= V10) to M: in dbSNP:rs3195676
- S52 (≠ G67) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ I122) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G189) to D: in dbSNP:rs10941112
- L201 (= L214) to S: in dbSNP:rs2287939
- M261 (≠ V278) to T: in dbSNP:rs3195678
- E277 (≠ T294) to K: in dbSNP:rs2278008
Sites not aligning to the query:
- 380:382 Microbody targeting signal
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
27% identity, 88% coverage: 4:362/409 of query aligns to 5:345/360 of O06543
- R38 (vs. gap) binding
- R52 (= R63) mutation to A: 15.7% of wild-type activity.
- I56 (≠ G67) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ IDLR 70:73) binding
- E82 (= E93) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NFK 94:96) binding
- R91 (≠ S102) binding ; mutation to A: 19.9% of wild-type activity.
- M111 (≠ I122) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ GFDQIA 136:141) binding
- H126 (≠ F137) mutation to A: 4.5% of wild-type activity.
- D156 (= D167) mutation to A: 17.6 of wild-type activity.
- D190 (≠ A200) mutation to A: 3.3% of wild-type activity.
- E241 (≠ T249) 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.
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)
27% identity, 88% coverage: 4:362/409 of query aligns to 4:339/354 of 2gd6A
- active site: G16 (≠ L16), D121 (= D138), D150 (= D167), G213 (≠ V229), G214 (≠ I230)
- binding acetyl coenzyme *a: I15 (≠ A15), R37 (= R52), A53 (≠ I70), D54 (= D71), L55 (= L72), K56 (≠ R73), G77 (≠ N94), Y78 (≠ F95), R79 (≠ K96), V82 (≠ T99), R85 (≠ S102), G119 (= G136), H120 (≠ F137), Y124 (≠ A141), D150 (= D167), M182 (≠ L198)
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)
27% identity, 88% coverage: 4:362/409 of query aligns to 4:339/354 of 2gd2A
- active site: G16 (≠ L16), D121 (= D138), D150 (= D167), G213 (≠ V229), G214 (≠ I230)
- binding acetoacetyl-coenzyme a: I15 (≠ A15), R37 (= R52), A53 (≠ I70), L55 (= L72), K56 (≠ R73), G77 (≠ N94), Y78 (≠ F95), R79 (≠ K96), V82 (≠ T99), R85 (≠ S102), L86 (≠ M103), A118 (≠ P135), G119 (= G136), H120 (≠ F137), Y124 (≠ A141), D150 (= D167)
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)
27% identity, 88% coverage: 4:362/409 of query aligns to 4:339/354 of 2gd0A
- active site: G16 (≠ L16), D121 (= D138), D150 (= D167), G213 (≠ V229), G214 (≠ I230)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (≠ Y57), L55 (= L72), K56 (≠ R73), G77 (≠ N94), Y78 (≠ F95), R79 (≠ K96), V82 (≠ T99), R85 (≠ S102), L86 (≠ M103), G119 (= G136), H120 (≠ F137), D121 (= D138), Y124 (≠ A141), D150 (= D167)
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)
27% identity, 88% coverage: 4:362/409 of query aligns to 4:339/354 of 2gciA
- active site: G16 (≠ L16), D121 (= D138), D150 (= D167), G213 (≠ V229), G214 (≠ I230)
- binding (r)-2-methylmyristoyl-coenzyme a: R37 (= R52), L55 (= L72), K56 (≠ R73), G77 (≠ N94), Y78 (≠ F95), R79 (≠ K96), V82 (≠ T99), G119 (= G136), H120 (≠ F137), D121 (= D138), Y124 (≠ A141), D150 (= D167), Y218 (= Y233), I234 (= I248), E235 (≠ T249)
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)
27% identity, 88% coverage: 4:362/409 of query aligns to 4:339/354 of 2gceA
- active site: G16 (≠ L16), D121 (= D138), D150 (= D167), G213 (≠ V229), G214 (≠ I230)
- binding (r)-ibuprofenoyl-coenzyme a: I15 (≠ A15), R37 (= R52), L55 (= L72), K56 (≠ R73), G77 (≠ N94), Y78 (≠ F95), R79 (≠ K96), V82 (≠ T99), R85 (≠ S102), G119 (= G136), H120 (≠ F137), D121 (= D138), Y124 (≠ A141), D150 (= D167), L211 (≠ H227), Y218 (= Y233), I234 (= I248)
- binding (s)-ibuprofenoyl-coenzyme a: I15 (≠ A15), G16 (≠ L16), P17 (≠ S17), R37 (= R52), L55 (= L72), K56 (≠ R73), G77 (≠ N94), Y78 (≠ F95), R79 (≠ K96), V82 (≠ T99), R85 (≠ S102), G119 (= G136), H120 (≠ F137), Y124 (≠ A141), D150 (= D167)
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)
27% identity, 88% coverage: 4:362/409 of query aligns to 4:340/355 of 2yimA
- active site: G16 (≠ L16), D122 (= D138), D151 (= D167), G214 (≠ V229), G215 (≠ I230)
- binding 2-methylacetoacetyl coa: I15 (≠ A15), R37 (≠ T40), A54 (≠ I70), L56 (= L72), K57 (≠ R73), G78 (≠ N94), Y79 (≠ F95), R80 (≠ K96), V83 (≠ T99), R86 (≠ S102), L87 (≠ M103), A119 (≠ P135), G120 (= G136), H121 (≠ F137), Y125 (≠ A141), D151 (= D167)
Query Sequence
>PfGW456L13_3635 L-carnitine dehydratase/bile acid-inducible protein F
MQAMQGVKIVDLSRALSGPFCTMVLADLGADVIKIEPGPTGDMSRTWGPFDRGVSTYYLS
CNRNKRGMCIDLRTPEGLTTIQQLIDDADVVIENFKPGTLESMGLGYEVLSARNPRLVLG
SINAFGADGPMSSWPGFDQIAQGYSGLMSLTGFVDGDPTRTGTAIGDLTSGMWLVTAVLA
ALLERERTGRGQHVSTSLLASLVGLLSVHGQRYLSLGDVPRRTGNAHSVIAPYGVFQTKD
GPLNLAPITSAMWGRLCILLDLPELPDDSRFATNEARVERRDELREILESRLKTRSKREW
TSLFVDAGLPAGPINTLDEVFDDPQVLHSQLTETLTHPTLGALRQVVTPVFCANDSVVSR
PPPLLGEHTVEVLREAGFDAASINALLAAKIVFQNSDDMTGAQSTGAAQ
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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