SitesBLAST
Comparing WP_011384532.1 AMB_RS10775 CoA transferase 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)
28% identity, 99% coverage: 6:402/402 of query aligns to 3:428/428 of O06644
- Q17 (≠ I20) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ Q41) binding
- W48 (≠ S53) 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 (≠ K108) binding
- D169 (= D174) 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)
28% identity, 99% coverage: 6:402/402 of query aligns to 2:427/427 of 1p5rA
- active site: Q16 (≠ I20), E139 (≠ A144), D168 (= D174), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T18), V15 (≠ F19), Q16 (≠ I20), A17 (= A21), R37 (≠ Q41), M73 (≠ L78), K74 (≠ R79), N95 (= N100), F96 (= F101), A100 (≠ T105), R103 (≠ K108), K136 (≠ P141), V137 (≠ G142), D168 (= D174), M199 (≠ L205)
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
28% identity, 99% coverage: 6:402/402 of query aligns to 2:427/427 of 2vjoA
- active site: A16 (≠ I20), E139 (≠ A144), D168 (= D174), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T18), A16 (≠ I20), A17 (= A21), R37 (≠ Q41), L71 (= L76), M73 (≠ L78), N95 (= N100), F96 (= F101), G97 (≠ R102), R103 (≠ K108), M104 (≠ W109), K136 (≠ P141), V137 (≠ G142), Y138 (≠ F143), D168 (= D174), M199 (≠ L205)
- 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: 6:402/402 of query aligns to 2:427/427 of 2vjkA
- active site: Q16 (≠ I20), E139 (≠ A144), D168 (= D174), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T18), Q16 (≠ I20), A17 (= A21), R37 (≠ Q41), M73 (≠ L78), K74 (≠ R79), N95 (= N100), F96 (= F101), G97 (≠ R102), R103 (≠ K108), M104 (≠ W109), K136 (≠ P141), V137 (≠ G142), Y138 (≠ F143), D168 (= D174), M199 (≠ L205)
- binding magnesium ion: D293 (≠ E266), D296 (≠ E269)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
28% identity, 99% coverage: 6:402/402 of query aligns to 2:427/427 of 1t4cA
- active site: Q16 (≠ I20), E139 (≠ A144), D168 (= D174), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T18), V15 (≠ F19), Q16 (≠ I20), R37 (≠ Q41), M73 (≠ L78), N95 (= N100), F96 (= F101), R103 (≠ K108), M104 (≠ W109), V137 (≠ G142), Y138 (≠ F143), D168 (= D174), M199 (≠ L205)
- binding oxalic acid: G259 (vs. gap), G260 (vs. gap)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
27% identity, 99% coverage: 6:402/402 of query aligns to 2:427/427 of 1t3zA
- active site: Q16 (≠ I20), E139 (≠ A144), S168 (≠ D174), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (≠ T18), V15 (≠ F19), A17 (= A21), R37 (≠ Q41), K74 (≠ R79), N95 (= N100), F96 (= F101), A100 (≠ T105), R103 (≠ K108), M104 (≠ W109), K136 (≠ P141), V137 (≠ G142), Y138 (≠ F143), E139 (≠ A144), M199 (≠ L205)
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, 99% coverage: 7:402/402 of query aligns to 4:416/416 of P69902
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
28% identity, 99% coverage: 7:402/402 of query aligns to 4:416/417 of 1q6yA
- active site: Q17 (≠ I20), E140 (≠ A144), D169 (= D174), G248 (≠ N236), G249 (≠ A237)
- binding coenzyme a: V16 (≠ F19), Q17 (≠ I20), S18 (≠ A21), R38 (≠ Q41), L72 (= L76), N73 (≠ D77), T74 (≠ L78), K75 (≠ R79), N96 (= N100), F97 (= F101), H98 (≠ R102), M105 (≠ W109), I124 (= I128), K137 (≠ P141), A138 (≠ G142), Y139 (≠ F143), D169 (= D174), M200 (≠ L205)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
28% identity, 99% coverage: 7:402/402 of query aligns to 3:415/415 of 1pt5A
- active site: Q16 (≠ I20), E139 (≠ A144), D168 (= D174), G247 (≠ N236), G248 (≠ A237)
- binding acetyl coenzyme *a: V15 (≠ F19), S17 (≠ A21), R37 (≠ Q41), L71 (= L76), N72 (≠ D77), T73 (≠ L78), K74 (≠ R79), N95 (= N100), F96 (= F101), H97 (≠ R102), K124 (≠ S129), K136 (≠ P141), A137 (≠ G142), Y138 (≠ F143), E139 (≠ A144), D168 (= D174), M199 (≠ L205)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
27% identity, 99% coverage: 6:401/402 of query aligns to 3:427/430 of 3ubmB
- active site: Q17 (≠ I20), E140 (≠ A144), D182 (= D174), G261 (≠ N236), G262 (≠ A237)
- binding coenzyme a: V16 (≠ F19), R38 (≠ Q41), L72 (= L76), N73 (≠ D77), T74 (≠ L78), K75 (≠ R79), N96 (= N100), F97 (= F101), R98 (= R102), A101 (≠ T105), R104 (≠ K108), K125 (≠ S129), D182 (= D174), M213 (≠ L205)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
28% identity, 99% coverage: 7:402/402 of query aligns to 4:409/410 of 1q7eA
- active site: Q17 (≠ I20), E133 (≠ A144), D162 (= D174), G241 (≠ N236), G242 (≠ A237)
- binding methionine: N96 (= N100), F97 (= F101), H98 (≠ R102), P99 (= P103), K118 (≠ S129), K130 (≠ P141), A131 (≠ G142), W246 (≠ G241), F299 (≠ A290), A303 (= A294), E306 (≠ G297)
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
31% identity, 84% coverage: 7:342/402 of query aligns to 4:321/360 of O06543
- R38 (≠ Q41) binding
- R52 (= R69) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S73) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ LDLR 76:79) binding
- E82 (= E99) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NFR 100:102) binding
- R91 (≠ K108) binding ; mutation to A: 19.9% of wild-type activity.
- M111 (≠ I128) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ GFARIA 142:147) binding
- H126 (≠ F143) mutation to A: 4.5% of wild-type activity.
- D156 (= D174) mutation to A: 17.6 of wild-type activity.
- D190 (≠ E207) mutation to A: 3.3% of wild-type activity.
- E241 (≠ T257) mutation to A: 2.1% of wild-type activity.
- C297 (= C312) mutation to A: 6.2% of wild-type activity.
- H312 (≠ Q333) mutation to A: 10.1% of wild-type activity.
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
31% identity, 94% coverage: 3:379/402 of query aligns to 1:357/360 of 5yx6A
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)
31% identity, 84% coverage: 7:342/402 of query aligns to 3:316/355 of 2yimA
- active site: G16 (≠ I20), D122 (≠ A144), D151 (= D174), G214 (vs. gap), G215 (vs. gap)
- binding 2-methylacetoacetyl coa: I15 (≠ F19), R37 (≠ Q41), A54 (≠ L76), L56 (= L78), K57 (≠ R79), G78 (≠ N100), Y79 (≠ F101), R80 (= R102), V83 (≠ T105), R86 (≠ K108), L87 (≠ W109), A119 (≠ P141), G120 (= G142), H121 (≠ F143), Y125 (≠ A147), D151 (= D174)
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, 84% coverage: 7:342/402 of query aligns to 3:315/354 of 2gd6A
- active site: G16 (≠ I20), D121 (≠ A144), D150 (= D174), G213 (vs. gap), G214 (vs. gap)
- binding acetyl coenzyme *a: I15 (≠ F19), R37 (≠ Q41), A53 (≠ L76), D54 (= D77), L55 (= L78), K56 (≠ R79), G77 (≠ N100), Y78 (≠ F101), R79 (= R102), V82 (≠ T105), R85 (≠ K108), G119 (= G142), H120 (≠ F143), Y124 (≠ A147), D150 (= D174), M182 (≠ L205)
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, 84% coverage: 7:342/402 of query aligns to 3:315/354 of 2gd2A
- active site: G16 (≠ I20), D121 (≠ A144), D150 (= D174), G213 (vs. gap), G214 (vs. gap)
- binding acetoacetyl-coenzyme a: I15 (≠ F19), R37 (≠ Q41), A53 (≠ L76), L55 (= L78), K56 (≠ R79), G77 (≠ N100), Y78 (≠ F101), R79 (= R102), V82 (≠ T105), R85 (≠ K108), L86 (≠ W109), A118 (≠ P141), G119 (= G142), H120 (≠ F143), Y124 (≠ A147), D150 (= D174)
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, 84% coverage: 7:342/402 of query aligns to 3:315/354 of 2gd0A
- active site: G16 (≠ I20), D121 (≠ A144), D150 (= D174), G213 (vs. gap), G214 (vs. gap)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D46), L55 (= L78), K56 (≠ R79), G77 (≠ N100), Y78 (≠ F101), R79 (= R102), V82 (≠ T105), R85 (≠ K108), L86 (≠ W109), G119 (= G142), H120 (≠ F143), D121 (≠ A144), Y124 (≠ A147), D150 (= D174)
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, 84% coverage: 7:342/402 of query aligns to 3:315/354 of 2gciA
- active site: G16 (≠ I20), D121 (≠ A144), D150 (= D174), G213 (vs. gap), G214 (vs. gap)
- binding (r)-2-methylmyristoyl-coenzyme a: R37 (≠ Q41), L55 (= L78), K56 (≠ R79), G77 (≠ N100), Y78 (≠ F101), R79 (= R102), V82 (≠ T105), G119 (= G142), H120 (≠ F143), D121 (≠ A144), Y124 (≠ A147), D150 (= D174), Y218 (≠ H240), I234 (≠ T256), E235 (≠ T257)
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, 84% coverage: 7:342/402 of query aligns to 3:315/354 of 2gceA
- active site: G16 (≠ I20), D121 (≠ A144), D150 (= D174), G213 (vs. gap), G214 (vs. gap)
- binding (r)-ibuprofenoyl-coenzyme a: I15 (≠ F19), R37 (≠ Q41), L55 (= L78), K56 (≠ R79), G77 (≠ N100), Y78 (≠ F101), R79 (= R102), V82 (≠ T105), R85 (≠ K108), G119 (= G142), H120 (≠ F143), D121 (≠ A144), Y124 (≠ A147), D150 (= D174), L211 (≠ V235), Y218 (≠ H240), I234 (≠ T256)
- binding (s)-ibuprofenoyl-coenzyme a: I15 (≠ F19), G16 (≠ I20), P17 (≠ A21), R37 (≠ Q41), L55 (= L78), K56 (≠ R79), G77 (≠ N100), Y78 (≠ F101), R79 (= R102), V82 (≠ T105), R85 (≠ K108), G119 (= G142), H120 (≠ F143), Y124 (≠ A147), D150 (= D174)
P31572 L-carnitine CoA-transferase; Crotonobetainyl-CoA:carnitine CoA-transferase; EC 2.8.3.21 from Escherichia coli (strain K12) (see paper)
30% identity, 98% coverage: 7:401/402 of query aligns to 11:400/405 of P31572
- K97 (≠ R102) binding
- R104 (≠ W109) binding
Query Sequence
>WP_011384532.1 AMB_RS10775 CoA transferase
MAHPKRPLDGIRVLDIATFIAAPYAAAILGEFGAEVIKVEQPGGGDTFRRFGSITERDGD
SLMWLSEARNKNSVTLDLRKPEGRELFLKLVARTDVIAENFRPGTLEKWGLGWEELRRVN
PGLILLRISGYGQTGPYKDRPGFARIAHAFGGLSYLAGMPGDVPVTPGSTSLADYMSGLY
GAIGVLLALRHRDATGEGQVIDLALYESVFRALDEIAPAFAMFGKVREREGAGTVNACPH
GHFRCGDGKWVALACTTDRMFARLAEAMERPELADGAKWGLLRNRLAERADVDALVGHWA
ATRPRETVMELCLDFEVPAAPLNTIADIFEDPQFQARGNLLEVADAVLGGVVVPGVVPKL
SATPGRVDHLGPRLGEDNARVYGGLLGLGEAEIAELKSKGVI
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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