SitesBLAST
Comparing WP_086511810.1 NCBI__GCF_002151265.1:WP_086511810.1 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)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
31% identity, 99% coverage: 3:393/394 of query aligns to 4:428/428 of O06644
- Q17 (≠ M16) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ K37) binding
- W48 (vs. gap) 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 (≠ K101) binding
- D169 (= D166) 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, 99% coverage: 3:393/394 of query aligns to 3:427/427 of 1p5rA
- active site: Q16 (≠ M16), E139 (≠ D137), D168 (= D166), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ Q14), V15 (≠ I15), Q16 (≠ M16), A17 (= A17), R37 (≠ K37), M73 (≠ L71), K74 (= K72), N95 (= N93), F96 (≠ Y94), A100 (≠ V98), R103 (≠ K101), K136 (≠ G134), V137 (≠ G135), D168 (= D166), M199 (≠ I197)
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
31% identity, 99% coverage: 3:393/394 of query aligns to 3:427/427 of 2vjkA
- active site: Q16 (≠ M16), E139 (≠ D137), D168 (= D166), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ Q14), Q16 (≠ M16), A17 (= A17), R37 (≠ K37), M73 (≠ L71), K74 (= K72), N95 (= N93), F96 (≠ Y94), G97 (≠ R95), R103 (≠ K101), M104 (≠ L102), K136 (≠ G134), V137 (≠ G135), Y138 (≠ F136), D168 (= D166), M199 (≠ I197)
- binding magnesium ion: D293 (≠ E258), D296 (= D261)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
31% identity, 99% coverage: 3:393/394 of query aligns to 3:427/427 of 1t4cA
- active site: Q16 (≠ M16), E139 (≠ D137), D168 (= D166), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ Q14), V15 (≠ I15), Q16 (≠ M16), R37 (≠ K37), M73 (≠ L71), N95 (= N93), F96 (≠ Y94), R103 (≠ K101), M104 (≠ L102), V137 (≠ G135), Y138 (≠ F136), D168 (= D166), M199 (≠ I197)
- 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, 99% coverage: 3:393/394 of query aligns to 3:427/427 of 2vjoA
- active site: A16 (≠ M16), E139 (≠ D137), D168 (= D166), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ Q14), A16 (≠ M16), A17 (= A17), R37 (≠ K37), L71 (= L69), M73 (≠ L71), N95 (= N93), F96 (≠ Y94), G97 (≠ R95), R103 (≠ K101), M104 (≠ L102), K136 (≠ G134), V137 (≠ G135), Y138 (≠ F136), D168 (= D166), M199 (≠ I197)
- binding oxalate ion: G257 (vs. gap), G259 (vs. gap), Q261 (vs. gap)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
30% identity, 99% coverage: 3:393/394 of query aligns to 3:427/427 of 1t3zA
- active site: Q16 (≠ M16), E139 (≠ D137), S168 (≠ D166), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (≠ Q14), V15 (≠ I15), A17 (= A17), R37 (≠ K37), K74 (= K72), N95 (= N93), F96 (≠ Y94), A100 (≠ V98), R103 (≠ K101), M104 (≠ L102), K136 (≠ G134), V137 (≠ G135), Y138 (≠ F136), E139 (≠ D137), M199 (≠ I197)
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
30% identity, 99% coverage: 3:394/394 of query aligns to 4:417/417 of 1q6yA
- active site: Q17 (≠ M16), E140 (≠ D137), D169 (= D166), G248 (≠ R227), G249 (≠ V228)
- binding coenzyme a: V16 (≠ I15), Q17 (≠ M16), S18 (≠ A17), R38 (≠ K37), L72 (= L69), N73 (= N70), T74 (≠ L71), K75 (= K72), N96 (= N93), F97 (≠ Y94), H98 (≠ R95), M105 (≠ L102), I124 (= I121), K137 (≠ G134), A138 (≠ G135), Y139 (≠ F136), D169 (= D166), M200 (≠ I197)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
30% identity, 99% coverage: 3:393/394 of query aligns to 3:415/415 of 1pt5A
- active site: Q16 (≠ M16), E139 (≠ D137), D168 (= D166), G247 (≠ R227), G248 (≠ V228)
- binding acetyl coenzyme *a: V15 (≠ I15), S17 (≠ A17), R37 (≠ K37), L71 (= L69), N72 (= N70), T73 (≠ L71), K74 (= K72), N95 (= N93), F96 (≠ Y94), H97 (≠ R95), K124 (≠ S122), K136 (≠ G134), A137 (≠ G135), Y138 (≠ F136), E139 (≠ D137), D168 (= D166), M199 (≠ I197)
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)
30% identity, 99% coverage: 3:393/394 of query aligns to 4:416/416 of P69902
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
30% identity, 99% coverage: 3:394/394 of query aligns to 4:410/410 of 1q7eA
- active site: Q17 (≠ M16), E133 (≠ D137), D162 (= D166), G241 (≠ R227), G242 (≠ V228)
- binding methionine: N96 (= N93), F97 (≠ Y94), H98 (≠ R95), P99 (≠ K103), K118 (≠ S122), K130 (≠ G134), A131 (≠ G135), W246 (≠ Y232), F299 (≠ E282), A303 (= A286), E306 (= E289)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
27% identity, 99% coverage: 3:392/394 of query aligns to 4:427/430 of 3ubmB
- active site: Q17 (≠ M16), E140 (≠ D137), D182 (= D166), G261 (≠ R227), G262 (≠ V228)
- binding coenzyme a: V16 (≠ I15), R38 (≠ K37), L72 (= L69), N73 (= N70), T74 (≠ L71), K75 (= K72), N96 (= N93), F97 (≠ Y94), R98 (= R95), A101 (≠ V98), R104 (≠ K101), K125 (≠ S122), D182 (= D166), M213 (≠ I197)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
29% identity, 93% coverage: 3:369/394 of query aligns to 5:355/360 of 5yx6A
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
26% identity, 100% coverage: 2:394/394 of query aligns to 1:374/382 of Q9UHK6
- V9 (≠ L10) to M: in dbSNP:rs3195676
- S52 (= S66) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ I121) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G188) to D: in dbSNP:rs10941112
- L201 (≠ F213) to S: in dbSNP:rs2287939
- M261 (≠ G278) to T: in dbSNP:rs3195678
- E277 (≠ H294) 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)
27% identity, 87% coverage: 3:345/394 of query aligns to 3:334/355 of 2yimA
- active site: G16 (≠ M16), D122 (= D137), D151 (= D166), G214 (≠ V228), G215 (≠ S229)
- binding 2-methylacetoacetyl coa: I15 (= I15), R37 (≠ K37), A54 (≠ L69), L56 (= L71), K57 (= K72), G78 (≠ N93), Y79 (= Y94), R80 (= R95), V83 (= V98), R86 (≠ K101), L87 (= L102), A119 (≠ G134), G120 (= G135), H121 (≠ F136), Y125 (≠ A140), D151 (= D166)
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
27% identity, 87% coverage: 3:345/394 of query aligns to 4:339/360 of O06543
- R38 (≠ K37) binding
- R52 (= R62) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S66) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ LNLK 69:72) binding
- E82 (= E92) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NYR 93:95) binding
- R91 (≠ K101) binding ; mutation to A: 19.9% of wild-type activity.
- M111 (≠ I121) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ GFDLVA 135:140) binding
- H126 (≠ F136) mutation to A: 4.5% of wild-type activity.
- D156 (= D166) mutation to A: 17.6 of wild-type activity.
- D190 (≠ E199) mutation to A: 3.3% of wild-type activity.
- E241 (≠ D268) mutation to A: 2.1% of wild-type activity.
- C297 (≠ P310) mutation to A: 6.2% of wild-type activity.
- H312 (= H325) 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, 87% coverage: 3:345/394 of query aligns to 3:333/354 of 2gd6A
- active site: G16 (≠ M16), D121 (= D137), D150 (= D166), G213 (≠ V228), G214 (≠ S229)
- binding acetyl coenzyme *a: I15 (= I15), R37 (≠ K37), A53 (≠ L69), D54 (≠ N70), L55 (= L71), K56 (= K72), G77 (≠ N93), Y78 (= Y94), R79 (= R95), V82 (= V98), R85 (≠ K101), G119 (= G135), H120 (≠ F136), Y124 (≠ A140), D150 (= D166), M182 (≠ I197)
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, 87% coverage: 3:345/394 of query aligns to 3:333/354 of 2gd2A
- active site: G16 (≠ M16), D121 (= D137), D150 (= D166), G213 (≠ V228), G214 (≠ S229)
- binding acetoacetyl-coenzyme a: I15 (= I15), R37 (≠ K37), A53 (≠ L69), L55 (= L71), K56 (= K72), G77 (≠ N93), Y78 (= Y94), R79 (= R95), V82 (= V98), R85 (≠ K101), L86 (= L102), A118 (≠ G134), G119 (= G135), H120 (≠ F136), Y124 (≠ A140), D150 (= D166)
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, 87% coverage: 3:345/394 of query aligns to 3:333/354 of 2gd0A
- active site: G16 (≠ M16), D121 (= D137), D150 (= D166), G213 (≠ V228), G214 (≠ S229)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D42), L55 (= L71), K56 (= K72), G77 (≠ N93), Y78 (= Y94), R79 (= R95), V82 (= V98), R85 (≠ K101), L86 (= L102), G119 (= G135), H120 (≠ F136), D121 (= D137), Y124 (≠ A140), D150 (= D166)
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, 87% coverage: 3:345/394 of query aligns to 3:333/354 of 2gciA
- active site: G16 (≠ M16), D121 (= D137), D150 (= D166), G213 (≠ V228), G214 (≠ S229)
- binding (r)-2-methylmyristoyl-coenzyme a: R37 (≠ K37), L55 (= L71), K56 (= K72), G77 (≠ N93), Y78 (= Y94), R79 (= R95), V82 (= V98), G119 (= G135), H120 (≠ F136), D121 (= D137), Y124 (≠ A140), D150 (= D166), Y218 (= Y232), I234 (≠ A247), E235 (≠ D268)
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, 87% coverage: 3:345/394 of query aligns to 3:333/354 of 2gceA
- active site: G16 (≠ M16), D121 (= D137), D150 (= D166), G213 (≠ V228), G214 (≠ S229)
- binding (r)-ibuprofenoyl-coenzyme a: I15 (= I15), R37 (≠ K37), L55 (= L71), K56 (= K72), G77 (≠ N93), Y78 (= Y94), R79 (= R95), V82 (= V98), R85 (≠ K101), G119 (= G135), H120 (≠ F136), D121 (= D137), Y124 (≠ A140), D150 (= D166), L211 (vs. gap), Y218 (= Y232), I234 (≠ A247)
- binding (s)-ibuprofenoyl-coenzyme a: I15 (= I15), G16 (≠ M16), P17 (≠ A17), R37 (≠ K37), L55 (= L71), K56 (= K72), G77 (≠ N93), Y78 (= Y94), R79 (= R95), V82 (= V98), R85 (≠ K101), G119 (= G135), H120 (≠ F136), Y124 (≠ A140), D150 (= D166)
Query Sequence
>WP_086511810.1 NCBI__GCF_002151265.1:WP_086511810.1
MLPLMKMKVLDISQIMAGPYCTMVLGDLGADVIKVEKNGGDDSRQMGPYVNEESTCFAQI
NRNKKSISLNLKEEEGREIFYRLAKEADVIVENYRTGVAKKLKVDYETIKAINPGIIYCS
ISGYGQTGPYSHKGGFDLVAQGMTGLMSMTGEPGRRPLKTGIAVYDIGAGITAVYSILAA
YIHKLGTGEGQHVDVAIAECGLPWFTWEAAAFFAEGTVPEPTGWRHRVSAPYQAIKVSDG
YIMLGCANQRNWERLCHEVIDRPDLLQDPRFVSNHLRGQNVEALEAVLEEIFVHDTREAW
LAKCDQAGVPAGPINDFAQALDDPHYQARGMVQEMEHPVIGRMKTIGFASKLSGTPPQIR
RPAPLYAQHTDEIMAELGLDEARCEELRRKGVIK
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