SitesBLAST
Comparing SM_b21089 SM_b21089 membrane-anchored racemase 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)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
36% identity, 66% coverage: 8:241/356 of query aligns to 5:234/360 of 5yx6A
Sites not aligning to the query:
1pt8A Crystal structure of the yfdw gene product of e. Coli, in complex with oxalate and acetyl-coa (see paper)
32% identity, 67% coverage: 8:246/356 of query aligns to 4:236/416 of 1pt8A
- active site: Q17 (≠ L21), E140 (≠ D146), D169 (= D175)
- binding acetyl coenzyme *a: V16 (≠ F20), Q17 (≠ L21), S18 (= S22), E37 (= E41), R38 (= R42), L72 (≠ I78), N73 (≠ D79), T74 (≠ L80), K75 (= K81), N96 (= N102), F97 (= F103), H98 (≠ R104), A101 (≠ V107), I124 (= I130), K137 (≠ P143), A138 (≠ G144), Y139 (≠ Q145), D169 (= D175), M200 (≠ L206)
- binding oxalate ion: Q48 (≠ L52), L49 (≠ Y53), E226 (≠ S236)
Sites not aligning to the query:
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, 67% coverage: 8:246/356 of query aligns to 4:236/416 of P69902
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
32% identity, 67% coverage: 8:246/356 of query aligns to 3:235/415 of 1pt5A
- active site: Q16 (≠ L21), E139 (≠ D146), D168 (= D175)
- binding acetyl coenzyme *a: F12 (≠ M17), V15 (≠ F20), S17 (= S22), E36 (= E41), R37 (= R42), L71 (≠ I78), N72 (≠ D79), T73 (≠ L80), K74 (= K81), N95 (= N102), F96 (= F103), H97 (≠ R104), A100 (≠ V107), I123 (= I130), K124 (≠ S131), K136 (≠ P143), A137 (≠ G144), Y138 (≠ Q145), E139 (≠ D146), D168 (= D175), M199 (≠ L206)
Sites not aligning to the query:
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
32% identity, 67% coverage: 8:246/356 of query aligns to 4:236/417 of 1q6yA
- active site: Q17 (≠ L21), E140 (≠ D146), D169 (= D175)
- binding coenzyme a: F13 (≠ M17), V16 (≠ F20), Q17 (≠ L21), S18 (= S22), E37 (= E41), R38 (= R42), L72 (≠ I78), N73 (≠ D79), T74 (≠ L80), K75 (= K81), N96 (= N102), F97 (= F103), H98 (≠ R104), A101 (≠ V107), M105 (≠ L111), I124 (= I130), K125 (≠ S131), G126 (= G132), K137 (≠ P143), A138 (≠ G144), Y139 (≠ Q145), D169 (= D175), M200 (≠ L206)
Sites not aligning to the query:
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
34% identity, 58% coverage: 8:213/356 of query aligns to 3:206/427 of 1p5rA
- active site: Q16 (≠ L21), E139 (≠ D146), D168 (= D175)
- binding coenzyme a: H14 (≠ Q19), V15 (≠ F20), Q16 (≠ L21), A17 (≠ S22), E36 (= E41), R37 (= R42), L71 (≠ I78), D72 (= D79), M73 (≠ L80), K74 (= K81), N95 (= N102), F96 (= F103), A100 (≠ V107), R103 (= R110), M104 (≠ L111), V123 (≠ I130), K136 (≠ P143), V137 (≠ G144), Y138 (≠ Q145), D168 (= D175), M199 (≠ L206)
Sites not aligning to the query:
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
34% identity, 58% coverage: 8:213/356 of query aligns to 4:207/428 of O06644
- Q17 (≠ L21) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (= R42) binding
- W48 (≠ Y53) 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 (= R110) binding
- D169 (= D175) 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.
Sites not aligning to the query:
- 259 G→A: 2.5-fold decrease of the catalytic effiency.
- 260 G→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)
34% identity, 58% coverage: 8:213/356 of query aligns to 3:206/427 of 2vjkA
- active site: Q16 (≠ L21), E139 (≠ D146), D168 (= D175)
- binding coenzyme a: H14 (≠ Q19), V15 (≠ F20), Q16 (≠ L21), A17 (≠ S22), E36 (= E41), R37 (= R42), L71 (≠ I78), D72 (= D79), M73 (≠ L80), K74 (= K81), N95 (= N102), F96 (= F103), G97 (≠ R104), A100 (≠ V107), R103 (= R110), M104 (≠ L111), V123 (≠ I130), K136 (≠ P143), V137 (≠ G144), Y138 (≠ Q145), D168 (= D175), M199 (≠ L206)
Sites not aligning to the query:
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
34% identity, 58% coverage: 8:213/356 of query aligns to 3:206/427 of 2vjoA
- active site: A16 (≠ L21), E139 (≠ D146), D168 (= D175)
- binding coenzyme a: H14 (≠ Q19), V15 (≠ F20), A16 (≠ L21), A17 (≠ S22), E36 (= E41), R37 (= R42), M43 (≠ L48), L71 (≠ I78), D72 (= D79), M73 (≠ L80), K74 (= K81), N95 (= N102), F96 (= F103), G97 (≠ R104), A100 (≠ V107), R103 (= R110), M104 (≠ L111), V123 (≠ I130), K124 (≠ S131), K136 (≠ P143), V137 (≠ G144), Y138 (≠ Q145), D168 (= D175), M199 (≠ L206)
Sites not aligning to the query:
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
28% identity, 92% coverage: 7:334/356 of query aligns to 1:306/382 of Q9UHK6
- V9 (= V15) 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 (= G197) to D: in dbSNP:rs10941112
- L201 (= L228) to S: in dbSNP:rs2287939
- M261 (≠ P281) to T: in dbSNP:rs3195678
- E277 (≠ A297) to K: in dbSNP:rs2278008
Sites not aligning to the query:
- 380:382 Microbody targeting signal
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
33% identity, 63% coverage: 8:230/356 of query aligns to 3:219/427 of 1t3zA
- active site: Q16 (≠ L21), E139 (≠ D146), S168 (≠ D175)
- binding oxidized coenzyme a: H14 (≠ Q19), V15 (≠ F20), Q16 (≠ L21), A17 (≠ S22), E36 (= E41), R37 (= R42), L71 (≠ I78), M73 (≠ L80), K74 (= K81), N95 (= N102), F96 (= F103), G97 (≠ R104), A100 (≠ V107), R103 (= R110), M104 (≠ L111), V123 (≠ I130), K136 (≠ P143), V137 (≠ G144), Y138 (≠ Q145), E139 (≠ D146), S168 (≠ D175), M199 (≠ L206)
Sites not aligning to the query:
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
31% identity, 67% coverage: 8:246/356 of query aligns to 4:249/430 of 3ubmB
- active site: Q17 (≠ L21), E140 (≠ D146), D182 (= D175)
- binding coenzyme a: F13 (≠ M17), V16 (≠ F20), S18 (= S22), E37 (= E41), R38 (= R42), L72 (≠ I78), N73 (≠ D79), T74 (≠ L80), K75 (= K81), N96 (= N102), F97 (= F103), R98 (= R104), A101 (≠ V107), R104 (= R110), M105 (≠ L111), V124 (≠ I130), K125 (≠ S131), G126 (= G132), A138 (≠ G144), D182 (= D175), M213 (≠ L206)
Sites not aligning to the query:
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
36% identity, 56% coverage: 8:208/356 of query aligns to 4:190/360 of O06543
- R38 (= R42) 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 (≠ IDLK 78:81) binding
- E82 (≠ Q101) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NFR 102:104) binding
- R91 (= R110) binding ; mutation to A: 19.9% of wild-type activity.
- M111 (≠ I130) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ GQDLLA 144:149) binding
- H126 (≠ Q145) mutation to A: 4.5% of wild-type activity.
- D156 (= D175) mutation to A: 17.6 of wild-type activity.
- D190 (≠ E208) mutation to A: 3.3% of wild-type activity.
Sites not aligning to the query:
- 241 E→A: 2.1% of wild-type activity.
- 297 C→A: 6.2% of wild-type activity.
- 312 H→A: 10.1% of wild-type activity.
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)
36% identity, 56% coverage: 8:208/356 of query aligns to 3:185/355 of 2yimA
- active site: G16 (≠ L21), D122 (= D146), D151 (= D175)
- binding 2-methylacetoacetyl coa: I15 (≠ F20), G16 (≠ L21), P17 (≠ S22), D36 (≠ E41), R37 (= R42), A54 (≠ I78), D55 (= D79), L56 (= L80), K57 (= K81), G78 (≠ N102), Y79 (≠ F103), R80 (= R104), V83 (= V107), R86 (= R110), L87 (= L111), T107 (≠ S131), A119 (≠ P143), G120 (= G144), H121 (≠ Q145), D122 (= D146), Y125 (≠ A149), N147 (≠ L171), D151 (= D175), M183 (≠ L206)
Sites not aligning to the query:
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)
36% identity, 56% coverage: 8:208/356 of query aligns to 3:184/354 of 2gd6A
- active site: G16 (≠ L21), D121 (= D146), D150 (= D175)
- binding acetyl coenzyme *a: I15 (≠ F20), G16 (≠ L21), P17 (≠ S22), R37 (= R42), A53 (≠ I78), D54 (= D79), L55 (= L80), K56 (= K81), G77 (≠ N102), Y78 (≠ F103), R79 (= R104), V82 (= V107), R85 (= R110), L86 (= L111), A118 (≠ P143), G119 (= G144), H120 (≠ Q145), Y124 (≠ A149), N146 (≠ L171), D150 (= D175), M182 (≠ L206)
Sites not aligning to the query:
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)
36% identity, 56% coverage: 8:208/356 of query aligns to 3:184/354 of 2gd2A
- active site: G16 (≠ L21), D121 (= D146), D150 (= D175)
- binding acetoacetyl-coenzyme a: I15 (≠ F20), G16 (≠ L21), P17 (≠ S22), D36 (≠ E41), R37 (= R42), A53 (≠ I78), D54 (= D79), L55 (= L80), K56 (= K81), G77 (≠ N102), Y78 (≠ F103), R79 (= R104), V82 (= V107), R85 (= R110), L86 (= L111), T106 (≠ S131), A118 (≠ P143), G119 (= G144), H120 (≠ Q145), D121 (= D146), Y124 (≠ A149), D150 (= D175), M182 (≠ L206)
Sites not aligning to the query:
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)
36% identity, 56% coverage: 8:208/356 of query aligns to 3:184/354 of 2gd0A
- active site: G16 (≠ L21), D121 (= D146), D150 (= D175)
- binding (s)-2-methylmyristoyl-coenzyme a: I15 (≠ F20), D36 (≠ E41), R37 (= R42), D42 (≠ H67), A53 (≠ I78), D54 (= D79), L55 (= L80), K56 (= K81), G77 (≠ N102), Y78 (≠ F103), R79 (= R104), V82 (= V107), R85 (= R110), L86 (= L111), T106 (≠ S131), A118 (≠ P143), G119 (= G144), H120 (≠ Q145), D121 (= D146), Y124 (≠ A149), N146 (≠ L171), D150 (= D175), M182 (≠ L206)
Sites not aligning to the query:
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)
36% identity, 56% coverage: 8:208/356 of query aligns to 3:184/354 of 2gciA