SitesBLAST
Comparing WP_043744516.1 AMB_RS13130 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)
31% identity, 100% coverage: 2:406/406 of query aligns to 3:428/428 of O06644
- Q17 (≠ L16) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ K37) 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 (≠ K110) binding
- D169 (= D179) 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)
31% identity, 100% coverage: 2:406/406 of query aligns to 2:427/427 of 1p5rA
- active site: Q16 (≠ L16), E139 (≠ D146), D168 (= D179), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R14), V15 (= V15), Q16 (≠ L16), A17 (= A17), R37 (≠ K37), M73 (= M80), K74 (≠ A81), N95 (= N102), F96 (≠ Y103), A100 (≠ G107), R103 (≠ K110), K136 (≠ A143), V137 (≠ G144), D168 (= D179), M199 (≠ L210)
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
31% identity, 100% coverage: 2:406/406 of query aligns to 2:427/427 of 2vjkA
- active site: Q16 (≠ L16), E139 (≠ D146), D168 (= D179), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R14), Q16 (≠ L16), A17 (= A17), R37 (≠ K37), M73 (= M80), K74 (≠ A81), N95 (= N102), F96 (≠ Y103), G97 (≠ K104), R103 (≠ K110), M104 (≠ Y111), K136 (≠ A143), V137 (≠ G144), Y138 (= Y145), D168 (= D179), M199 (≠ L210)
- binding magnesium ion: D293 (≠ E270), D296 (≠ G273)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
31% identity, 100% coverage: 2:406/406 of query aligns to 2:427/427 of 1t4cA
- active site: Q16 (≠ L16), E139 (≠ D146), D168 (= D179), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R14), V15 (= V15), Q16 (≠ L16), R37 (≠ K37), M73 (= M80), N95 (= N102), F96 (≠ Y103), R103 (≠ K110), M104 (≠ Y111), V137 (≠ G144), Y138 (= Y145), D168 (= D179), M199 (≠ L210)
- binding oxalic acid: G259 (vs. gap), G260 (vs. gap)
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
31% identity, 100% coverage: 2:406/406 of query aligns to 2:427/427 of 2vjoA
- active site: A16 (≠ L16), E139 (≠ D146), D168 (= D179), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R14), A16 (≠ L16), A17 (= A17), R37 (≠ K37), L71 (≠ I78), M73 (= M80), N95 (= N102), F96 (≠ Y103), G97 (≠ K104), R103 (≠ K110), M104 (≠ Y111), K136 (≠ A143), V137 (≠ G144), Y138 (= Y145), D168 (= D179), M199 (≠ L210)
- binding oxalate ion: G257 (vs. gap), G259 (vs. gap), Q261 (≠ G238)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
31% identity, 100% coverage: 2:406/406 of query aligns to 2:427/427 of 1t3zA
- active site: Q16 (≠ L16), E139 (≠ D146), S168 (≠ D179), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (≠ R14), V15 (= V15), A17 (= A17), R37 (≠ K37), K74 (≠ A81), N95 (= N102), F96 (≠ Y103), A100 (≠ G107), R103 (≠ K110), M104 (≠ Y111), K136 (≠ A143), V137 (≠ G144), Y138 (= Y145), E139 (≠ D146), M199 (≠ L210)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
29% identity, 100% coverage: 2:406/406 of query aligns to 3:428/430 of 3ubmB
- active site: Q17 (≠ L16), E140 (≠ D146), D182 (= D179), G261 (vs. gap), G262 (vs. gap)
- binding coenzyme a: V16 (= V15), R38 (≠ K37), L72 (≠ I78), N73 (≠ D79), T74 (≠ M80), K75 (≠ A81), N96 (= N102), F97 (≠ Y103), R98 (≠ K104), A101 (≠ G107), R104 (≠ K110), K125 (≠ T131), D182 (= D179), M213 (≠ L210)
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
32% identity, 95% coverage: 4:389/406 of query aligns to 5:400/417 of 1q6yA
- active site: Q17 (≠ L16), E140 (≠ D146), D169 (= D179), G248 (≠ A241), G249 (vs. gap)
- binding coenzyme a: V16 (= V15), Q17 (≠ L16), S18 (≠ A17), R38 (≠ K37), L72 (≠ I78), N73 (≠ D79), T74 (≠ M80), K75 (≠ A81), N96 (= N102), F97 (≠ Y103), H98 (≠ K104), M105 (≠ Y111), I124 (= I130), K137 (≠ A143), A138 (≠ G144), Y139 (= Y145), D169 (= D179), M200 (≠ L210)
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, 95% coverage: 4:389/406 of query aligns to 5:400/416 of P69902
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
32% identity, 95% coverage: 4:389/406 of query aligns to 4:399/415 of 1pt5A
- active site: Q16 (≠ L16), E139 (≠ D146), D168 (= D179), G247 (≠ A241), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (= V15), S17 (≠ A17), R37 (≠ K37), L71 (≠ I78), N72 (≠ D79), T73 (≠ M80), K74 (≠ A81), N95 (= N102), F96 (≠ Y103), H97 (≠ K104), K124 (≠ T131), K136 (≠ A143), A137 (≠ G144), Y138 (= Y145), E139 (≠ D146), D168 (= D179), M199 (≠ L210)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
32% identity, 95% coverage: 2:386/406 of query aligns to 4:360/360 of 5yx6A
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
32% identity, 95% coverage: 4:389/406 of query aligns to 5:393/410 of 1q7eA
- active site: Q17 (≠ L16), E133 (≠ D146), D162 (= D179), G241 (≠ A241), G242 (vs. gap)
- binding methionine: N96 (= N102), F97 (≠ Y103), H98 (≠ Y111), P99 (≠ G112), K118 (≠ T131), K130 (≠ A143), A131 (≠ G144), W246 (vs. gap), F299 (≠ E294), A303 (≠ P298), E306 (= E301)
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
31% identity, 66% coverage: 3:268/406 of query aligns to 2:243/382 of Q9UHK6
- V9 (≠ L10) to M: in dbSNP:rs3195676
- S52 (= S75) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ I130) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G201) to D: in dbSNP:rs10941112
- L201 (≠ V227) to S: in dbSNP:rs2287939
Sites not aligning to the query:
- 261 M → T: in dbSNP:rs3195678
- 277 E → K: in dbSNP:rs2278008
- 380:382 Microbody targeting signal
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)
28% identity, 65% coverage: 4:265/406 of query aligns to 4:239/355 of 2yimA
- active site: G16 (≠ L16), D122 (= D146), D151 (= D179), G214 (≠ A241), G215 (≠ I242)
- binding 2-methylacetoacetyl coa: I15 (≠ V15), R37 (≠ K37), A54 (≠ I78), L56 (≠ M80), K57 (≠ A81), G78 (≠ N102), Y79 (= Y103), R80 (≠ K104), V83 (≠ G107), R86 (≠ K110), L87 (≠ Y111), A119 (= A143), G120 (= G144), H121 (≠ Y145), Y125 (≠ I149), D151 (= D179)
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
29% identity, 65% coverage: 4:265/406 of query aligns to 5:244/360 of O06543
- R38 (≠ K37) 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 (≠ IDMA 78:81) binding
- E82 (= E101) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NYK 102:104) binding
- R91 (≠ K110) binding ; mutation to A: 19.9% of wild-type activity.
- M111 (≠ I130) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ GYDFMI 144:149) binding
- H126 (≠ Y145) mutation to A: 4.5% of wild-type activity.
- D156 (= D179) mutation to A: 17.6 of wild-type activity.
- D190 (= D212) mutation to A: 3.3% of wild-type activity.
- E241 (≠ D262) mutation to A: 2.1% of wild-type activity.
Sites not aligning to the query:
- 297 C→A: 6.2% of wild-type activity.
- 312 H→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)
28% identity, 65% coverage: 4:265/406 of query aligns to 4:238/354 of 2gd6A
- active site: G16 (≠ L16), D121 (= D146), D150 (= D179), G213 (≠ A241), G214 (≠ I242)
- binding acetyl coenzyme *a: I15 (≠ V15), R37 (≠ K37), A53 (≠ I78), D54 (= D79), L55 (≠ M80), K56 (≠ A81), G77 (≠ N102), Y78 (= Y103), R79 (≠ K104), V82 (≠ G107), R85 (≠ K110), G119 (= G144), H120 (≠ Y145), Y124 (≠ I149), D150 (= D179), M182 (≠ L210)
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)
28% identity, 65% coverage: 4:265/406 of query aligns to 4:238/354 of 2gd2A
- active site: G16 (≠ L16), D121 (= D146), D150 (= D179), G213 (≠ A241), G214 (≠ I242)
- binding acetoacetyl-coenzyme a: I15 (≠ V15), R37 (≠ K37), A53 (≠ I78), L55 (≠ M80), K56 (≠ A81), G77 (≠ N102), Y78 (= Y103), R79 (≠ K104), V82 (≠ G107), R85 (≠ K110), L86 (≠ Y111), A118 (= A143), G119 (= G144), H120 (≠ Y145), Y124 (≠ I149), D150 (= D179)
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)
28% identity, 65% coverage: 4:265/406 of query aligns to 4:238/354 of 2gd0A
- active site: G16 (≠ L16), D121 (= D146), D150 (= D179), G213 (≠ A241), G214 (≠ I242)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D42), L55 (≠ M80), K56 (≠ A81), G77 (≠ N102), Y78 (= Y103), R79 (≠ K104), V82 (≠ G107), R85 (≠ K110), L86 (≠ Y111), G119 (= G144), H120 (≠ Y145), D121 (= D146), Y124 (≠ I149), D150 (= D179)
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)
28% identity, 65% coverage: 4:265/406 of query aligns to 4:238/354 of 2gciA
- active site: G16 (≠ L16), D121 (= D146), D150 (= D179), G213 (≠ A241), G214 (≠ I242)
- binding (r)-2-methylmyristoyl-coenzyme a: R37 (≠ K37), L55 (≠ M80), K56 (≠ A81), G77 (≠ N102), Y78 (= Y103), R79 (≠ K104), V82 (≠ G107), G119 (= G144), H120 (≠ Y145), D121 (= D146), Y124 (≠ I149), D150 (= D179), Y218 (= Y245), I234 (≠ N261), E235 (≠ D262)
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)
28% identity, 65% coverage: 4:265/406 of query aligns to 4:238/354 of 2gceA
- active site: G16 (≠ L16), D121 (= D146), D150 (= D179), G213 (≠ A241), G214 (≠ I242)
- binding (r)-ibuprofenoyl-coenzyme a: I15 (≠ V15), R37 (≠ K37), L55 (≠ M80), K56 (≠ A81), G77 (≠ N102), Y78 (= Y103), R79 (≠ K104), V82 (≠ G107), R85 (≠ K110), G119 (= G144), H120 (≠ Y145), D121 (= D146), Y124 (≠ I149), D150 (= D179), L211 (≠ H239), Y218 (= Y245), I234 (≠ N261)
- binding (s)-ibuprofenoyl-coenzyme a: I15 (≠ V15), G16 (≠ L16), P17 (≠ A17), R37 (≠ K37), L55 (≠ M80), K56 (≠ A81), G77 (≠ N102), Y78 (= Y103), R79 (≠ K104), V82 (≠ G107), R85 (≠ K110), G119 (= G144), H120 (≠ Y145), Y124 (≠ I149), D150 (= D179)
Query Sequence
>WP_043744516.1 AMB_RS13130 CoA transferase
MRALDDILVLDLSRVLAGPWCTQMLSDLGAKVIKVEKPGAGDDTRGWGPPFLTDPATEEK
GDAAYYLAANRGKHSVTIDMATPEGQELIRHLAAKADVLVENYKLGGLKKYGLDYDALKA
VNPRLVYCSITGFGQTGPYAPRAGYDFMIQAMGGMMSVTGEKDALPGGGPQKAGIAIADL
STGLHAVIAILAALNQRHRTGRGQYIDLGLLDVQVSMMSNQAQTYLVGGKAPARAGNGHA
AIVPYQAFPTQDGHLIIAVGNDGQFAKLAEVLGHPEWAADQRFILNRSRVEHREVLVPLL
EAETRRFPSAHLLDALERRQIPCGPINTMDKVFDDPQAQARNLRQEVPHALAGTVPTVAS
PLRLSDSPVIYDRGPPLLGEHTEVVLGDLLGLDAPAVEALRAKGVV
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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