SitesBLAST
Comparing WP_052664075.1 NCBI__GCF_000969705.1:WP_052664075.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
32% identity, 94% coverage: 12:379/392 of query aligns to 3:355/360 of 5yx6A
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
29% identity, 95% coverage: 12:385/392 of query aligns to 2:410/430 of 3ubmB
- active site: Q17 (≠ L27), E140 (≠ D149), D182 (= D178), G261 (vs. gap), G262 (vs. gap)
- binding coenzyme a: V16 (≠ I26), R38 (≠ G48), L72 (= L81), N73 (= N82), T74 (≠ L83), K75 (= K84), N96 (= N105), F97 (≠ M106), R98 (= R107), A101 (≠ G110), R104 (= R113), K125 (≠ S134), D182 (= D178), M213 (≠ L209)
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
29% identity, 94% coverage: 14:383/392 of query aligns to 3:407/427 of 1p5rA
- active site: Q16 (≠ L27), E139 (≠ D149), D168 (= D178), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R25), V15 (≠ I26), Q16 (≠ L27), A17 (= A28), R37 (≠ G48), M73 (≠ L83), K74 (= K84), N95 (= N105), F96 (≠ M106), A100 (≠ G110), R103 (= R113), K136 (≠ A146), V137 (≠ G147), D168 (= D178), M199 (≠ L209)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
29% identity, 94% coverage: 14:383/392 of query aligns to 4:408/428 of O06644
- Q17 (≠ L27) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ G48) binding CoA
- W48 (= W57) 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 (= R113) binding CoA
- D169 (= D178) 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.
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
28% identity, 94% coverage: 14:383/392 of query aligns to 3:407/427 of 2vjkA
- active site: Q16 (≠ L27), E139 (≠ D149), D168 (= D178), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R25), Q16 (≠ L27), A17 (= A28), R37 (≠ G48), M73 (≠ L83), K74 (= K84), N95 (= N105), F96 (≠ M106), G97 (≠ R107), R103 (= R113), M104 (≠ F114), K136 (≠ A146), V137 (≠ G147), Y138 (= Y148), D168 (= D178), M199 (≠ L209)
- binding magnesium ion: D293 (= D269), D296 (≠ G272)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
28% identity, 94% coverage: 14:383/392 of query aligns to 3:407/427 of 1t4cA
- active site: Q16 (≠ L27), E139 (≠ D149), D168 (= D178), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R25), V15 (≠ I26), Q16 (≠ L27), R37 (≠ G48), M73 (≠ L83), N95 (= N105), F96 (≠ M106), R103 (= R113), M104 (≠ F114), V137 (≠ G147), Y138 (= Y148), D168 (= D178), M199 (≠ L209)
- 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)
28% identity, 94% coverage: 14:383/392 of query aligns to 3:407/427 of 2vjoA
- active site: A16 (≠ L27), E139 (≠ D149), D168 (= D178), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ R25), A16 (≠ L27), A17 (= A28), R37 (≠ G48), L71 (= L81), M73 (≠ L83), N95 (= N105), F96 (≠ M106), G97 (≠ R107), R103 (= R113), M104 (≠ F114), K136 (≠ A146), V137 (≠ G147), Y138 (= Y148), D168 (= D178), M199 (≠ L209)
- binding oxalate ion: G257 (vs. gap), G259 (vs. gap), Q261 (≠ A237)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
28% identity, 94% coverage: 14:383/392 of query aligns to 3:407/427 of 1t3zA
- active site: Q16 (≠ L27), E139 (≠ D149), S168 (≠ D178), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (≠ R25), V15 (≠ I26), A17 (= A28), R37 (≠ G48), K74 (= K84), N95 (= N105), F96 (≠ M106), A100 (≠ G110), R103 (= R113), M104 (≠ F114), K136 (≠ A146), V137 (≠ G147), Y138 (= Y148), E139 (≠ D149), M199 (≠ L209)
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, 93% coverage: 14:379/392 of query aligns to 4:392/416 of P69902
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
28% identity, 93% coverage: 14:379/392 of query aligns to 4:392/417 of 1q6yA
- active site: Q17 (≠ L27), E140 (≠ D149), D169 (= D178), G248 (vs. gap), G249 (vs. gap)
- binding coenzyme a: V16 (≠ I26), Q17 (≠ L27), S18 (≠ A28), R38 (≠ G48), L72 (= L81), N73 (= N82), T74 (≠ L83), K75 (= K84), N96 (= N105), F97 (≠ M106), H98 (≠ R107), M105 (≠ F114), I124 (= I133), K137 (≠ A146), A138 (≠ G147), Y139 (= Y148), D169 (= D178), M200 (≠ L209)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
28% identity, 93% coverage: 14:379/392 of query aligns to 3:391/415 of 1pt5A
- active site: Q16 (≠ L27), E139 (≠ D149), D168 (= D178), G247 (vs. gap), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (≠ I26), S17 (≠ A28), R37 (≠ G48), L71 (= L81), N72 (= N82), T73 (≠ L83), K74 (= K84), N95 (= N105), F96 (≠ M106), H97 (≠ R107), K124 (≠ S134), K136 (≠ A146), A137 (≠ G147), Y138 (= Y148), E139 (≠ D149), D168 (= D178), M199 (≠ L209)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
27% identity, 93% coverage: 14:379/392 of query aligns to 4:385/410 of 1q7eA
- active site: Q17 (≠ L27), E133 (≠ D149), D162 (= D178), G241 (vs. gap), G242 (vs. gap)
- binding methionine: N96 (= N105), F97 (≠ M106), H98 (≠ R107), P99 (= P108), K118 (≠ S134), K130 (≠ A146), A131 (≠ G147), W246 (vs. gap), F299 (≠ D293), A303 (≠ P297), E306 (≠ V300)
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)
31% identity, 78% coverage: 12:315/392 of query aligns to 1:285/354 of 2gd6A
- active site: G16 (≠ L27), D121 (= D149), D150 (= D178), G213 (≠ S240), G214 (≠ L241)
- binding acetyl coenzyme *a: I15 (= I26), R37 (≠ G48), A53 (≠ L81), D54 (≠ N82), L55 (= L83), K56 (= K84), G77 (≠ N105), Y78 (≠ M106), R79 (= R107), V82 (≠ G110), R85 (= R113), G119 (= G147), H120 (≠ Y148), Y124 (≠ V152), D150 (= D178), M182 (≠ L209)
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)
31% identity, 78% coverage: 12:315/392 of query aligns to 1:285/354 of 2gd2A
- active site: G16 (≠ L27), D121 (= D149), D150 (= D178), G213 (≠ S240), G214 (≠ L241)
- binding acetoacetyl-coenzyme a: I15 (= I26), R37 (≠ G48), A53 (≠ L81), L55 (= L83), K56 (= K84), G77 (≠ N105), Y78 (≠ M106), R79 (= R107), V82 (≠ G110), R85 (= R113), L86 (≠ F114), A118 (= A146), G119 (= G147), H120 (≠ Y148), Y124 (≠ V152), D150 (= D178)
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)
31% identity, 78% coverage: 12:315/392 of query aligns to 1:285/354 of 2gd0A
- active site: G16 (≠ L27), D121 (= D149), D150 (= D178), G213 (≠ S240), G214 (≠ L241)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D53), L55 (= L83), K56 (= K84), G77 (≠ N105), Y78 (≠ M106), R79 (= R107), V82 (≠ G110), R85 (= R113), L86 (≠ F114), G119 (= G147), H120 (≠ Y148), D121 (= D149), Y124 (≠ V152), D150 (= D178)
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)
31% identity, 78% coverage: 12:315/392 of query aligns to 1:285/354 of 2gciA
- active site: G16 (≠ L27), D121 (= D149), D150 (= D178), G213 (≠ S240), G214 (≠ L241)
- binding (r)-2-methylmyristoyl-coenzyme a: R37 (≠ G48), L55 (= L83), K56 (= K84), G77 (≠ N105), Y78 (≠ M106), R79 (= R107), V82 (≠ G110), G119 (= G147), H120 (≠ Y148), D121 (= D149), Y124 (≠ V152), D150 (= D178), Y218 (= Y244), I234 (≠ N260), E235 (≠ N261)
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)
31% identity, 78% coverage: 12:315/392 of query aligns to 1:285/354 of 2gceA
- active site: G16 (≠ L27), D121 (= D149), D150 (= D178), G213 (≠ S240), G214 (≠ L241)
- binding (r)-ibuprofenoyl-coenzyme a: I15 (= I26), R37 (≠ G48), L55 (= L83), K56 (= K84), G77 (≠ N105), Y78 (≠ M106), R79 (= R107), V82 (≠ G110), R85 (= R113), G119 (= G147), H120 (≠ Y148), D121 (= D149), Y124 (≠ V152), D150 (= D178), L211 (≠ H238), Y218 (= Y244), I234 (≠ N260)
- binding (s)-ibuprofenoyl-coenzyme a: I15 (= I26), G16 (≠ L27), P17 (≠ A28), R37 (≠ G48), L55 (= L83), K56 (= K84), G77 (≠ N105), Y78 (≠ M106), R79 (= R107), V82 (≠ G110), R85 (= R113), G119 (= G147), H120 (≠ Y148), Y124 (≠ V152), D150 (= D178)
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
31% identity, 78% coverage: 12:315/392 of query aligns to 2:291/360 of O06543
- R38 (≠ S58) binding substrate
- R52 (= R74) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S78) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ LNLK 81:84) binding substrate
- E82 (= E104) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NMR 105:107) binding substrate
- R91 (= R113) binding substrate; mutation to A: 19.9% of wild-type activity.
- M111 (≠ I133) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ GYDLMV 147:152) binding substrate
- H126 (≠ Y148) mutation to A: 4.5% of wild-type activity.
- D156 (= D178) mutation to A: 17.6 of wild-type activity.
- D190 (≠ S211) mutation to A: 3.3% of wild-type activity.
- E241 (≠ N261) 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.
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
29% identity, 81% coverage: 15:332/392 of query aligns to 3:304/382 of Q9UHK6
- V9 (≠ A21) to M: in dbSNP:rs3195676
- S52 (= S78) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ I133) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G200) to D: in dbSNP:rs10941112
- L201 (≠ A224) to S: in dbSNP:rs2287939
- M261 (≠ T289) to T: in dbSNP:rs3195678
- E277 (≠ G305) to K: in dbSNP:rs2278008
Sites not aligning to the query:
- 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)
31% identity, 78% coverage: 12:315/392 of query aligns to 1:286/355 of 2yimA
- active site: G16 (≠ L27), D122 (= D149), D151 (= D178), G214 (≠ S240), G215 (≠ L241)
- binding 2-methylacetoacetyl coa: I15 (= I26), R37 (≠ G48), A54 (≠ L81), L56 (= L83), K57 (= K84), G78 (≠ N105), Y79 (≠ M106), R80 (= R107), V83 (≠ G110), R86 (= R113), L87 (≠ F114), A119 (= A146), G120 (= G147), H121 (≠ Y148), Y125 (≠ V152), D151 (= D178)
Query Sequence
>WP_052664075.1 NCBI__GCF_000969705.1:WP_052664075.1
MATEIHASPHEAGPLDGLLIADFSRILAGPYATMLLADFGADVIKVEGPLGDDTRTWSPP
VRDGVSTYYLGINRNKRSIALNLKDPGDLATARELASRADVLIENMRPGGMARFGLDFDG
VRATNPGVVYASISGFGTTPEGAALAGYDLMVQGISGLMSLTGDPEGEAFRAGISVFDVM
AGMHATIGILSALNHRHATGAGQHVEVNLLSSALSGLVNQASAAVAGGITPFRMGNAHPS
LFPYEPLPTADGAIIVIAGNNGQFATLCDVLGVPELAEDARFASNEDRTANRDQLGPLLV
DALAGDTTDEWFARFRAKGLPGGPVNTVPEGVAFAEAIGLEPVVEVGDGDRAIPSVRNPI
SFSDTQASYRYAPPGLDEHGDEIRAWLRAPRD
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