SitesBLAST
Comparing WP_234239471.1 NCBI__GCF_002151265.1:WP_234239471.1 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)
9br7C Succinate--hydroxymethylglutarate CoA-transferase (see paper)
40% identity, 99% coverage: 3:389/390 of query aligns to 9:397/403 of 9br7C
Q9HAC7 Succinyl-CoA:glutarate CoA-transferase; Dermal papilla-derived protein 13; Dicarboxyl-CoA:dicarboxylic acid coenzyme A transferase SUGCT; Succinate--hydroxymethylglutarate CoA-transferase; EC 2.8.3.-; EC 2.8.3.13 from Homo sapiens (Human) (see 3 papers)
40% identity, 99% coverage: 3:389/390 of query aligns to 44:432/438 of Q9HAC7
- D205 (= D162) mutation to A: Loss of CoA transferase activity toward glutaryl-CoA and 3-hydroxy-3-methylglutarate substrates.
- R329 (≠ I287) to W: in GA3; severely decreased protein stability and processing; dbSNP:rs137852860
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
30% identity, 99% coverage: 3:389/390 of query aligns to 7:427/427 of 1p5rA
- active site: Q16 (≠ M12), E139 (≠ D133), D168 (= D162), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ Q10), V15 (≠ I11), Q16 (≠ M12), A17 (= A13), R37 (≠ K33), M73 (≠ L67), K74 (= K68), N95 (= N89), F96 (≠ Y90), A100 (≠ V94), R103 (≠ K97), K136 (≠ G130), V137 (≠ G131), D168 (= D162), M199 (≠ I193)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
30% identity, 99% coverage: 3:389/390 of query aligns to 8:428/428 of O06644
- Q17 (≠ M12) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ K33) binding CoA
- W48 (≠ Q41) 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 (≠ K97) binding CoA
- D169 (= D162) 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)
30% identity, 99% coverage: 3:389/390 of query aligns to 7:427/427 of 2vjkA
- active site: Q16 (≠ M12), E139 (≠ D133), D168 (= D162), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ Q10), Q16 (≠ M12), A17 (= A13), R37 (≠ K33), M73 (≠ L67), K74 (= K68), N95 (= N89), F96 (≠ Y90), G97 (≠ R91), R103 (≠ K97), M104 (≠ L98), K136 (≠ G130), V137 (≠ G131), Y138 (≠ F132), D168 (= D162), M199 (≠ I193)
- binding magnesium ion: D293 (≠ E254), D296 (= D257)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
30% identity, 99% coverage: 3:389/390 of query aligns to 7:427/427 of 1t4cA
- active site: Q16 (≠ M12), E139 (≠ D133), D168 (= D162), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ Q10), V15 (≠ I11), Q16 (≠ M12), R37 (≠ K33), M73 (≠ L67), N95 (= N89), F96 (≠ Y90), R103 (≠ K97), M104 (≠ L98), V137 (≠ G131), Y138 (≠ F132), D168 (= D162), M199 (≠ I193)
- 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)
30% identity, 99% coverage: 3:389/390 of query aligns to 7:427/427 of 2vjoA
- active site: A16 (≠ M12), E139 (≠ D133), D168 (= D162), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ Q10), A16 (≠ M12), A17 (= A13), R37 (≠ K33), L71 (= L65), M73 (≠ L67), N95 (= N89), F96 (≠ Y90), G97 (≠ R91), R103 (≠ K97), M104 (≠ L98), K136 (≠ G130), V137 (≠ G131), Y138 (≠ F132), D168 (= D162), M199 (≠ I193)
- 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: 3:389/390 of query aligns to 7:427/427 of 1t3zA
- active site: Q16 (≠ M12), E139 (≠ D133), S168 (≠ D162), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (≠ Q10), V15 (≠ I11), A17 (= A13), R37 (≠ K33), K74 (= K68), N95 (= N89), F96 (≠ Y90), A100 (≠ V94), R103 (≠ K97), M104 (≠ L98), K136 (≠ G130), V137 (≠ G131), Y138 (≠ F132), E139 (≠ D133), M199 (≠ I193)
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
30% identity, 99% coverage: 3:390/390 of query aligns to 8:417/417 of 1q6yA
- active site: Q17 (≠ M12), E140 (≠ D133), D169 (= D162), G248 (≠ R223), G249 (≠ V224)
- binding coenzyme a: V16 (≠ I11), Q17 (≠ M12), S18 (≠ A13), R38 (≠ K33), L72 (= L65), N73 (= N66), T74 (≠ L67), K75 (= K68), N96 (= N89), F97 (≠ Y90), H98 (≠ R91), M105 (≠ L98), I124 (= I117), K137 (≠ G130), A138 (≠ G131), Y139 (≠ F132), D169 (= D162), M200 (≠ I193)
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: 3:389/390 of query aligns to 8:416/416 of P69902
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
30% identity, 99% coverage: 3:389/390 of query aligns to 7:415/415 of 1pt5A
- active site: Q16 (≠ M12), E139 (≠ D133), D168 (= D162), G247 (≠ R223), G248 (≠ V224)
- binding acetyl coenzyme *a: V15 (≠ I11), S17 (≠ A13), R37 (≠ K33), L71 (= L65), N72 (= N66), T73 (≠ L67), K74 (= K68), N95 (= N89), F96 (≠ Y90), H97 (≠ R91), K124 (≠ S118), K136 (≠ G130), A137 (≠ G131), Y138 (≠ F132), E139 (≠ D133), D168 (= D162), M199 (≠ I193)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
29% identity, 99% coverage: 3:390/390 of query aligns to 8:410/410 of 1q7eA
- active site: Q17 (≠ M12), E133 (≠ D133), D162 (= D162), G241 (≠ R223), G242 (≠ V224)
- binding methionine: N96 (= N89), F97 (≠ Y90), H98 (≠ R91), P99 (≠ K99), K118 (≠ S118), K130 (≠ G130), A131 (≠ G131), W246 (≠ Y228), F299 (≠ E278), A303 (= A282), E306 (= E285)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
27% identity, 99% coverage: 3:388/390 of query aligns to 8:427/430 of 3ubmB
- active site: Q17 (≠ M12), E140 (≠ D133), D182 (= D162), G261 (≠ R223), G262 (≠ V224)
- binding coenzyme a: V16 (≠ I11), R38 (≠ K33), L72 (= L65), N73 (= N66), T74 (≠ L67), K75 (= K68), N96 (= N89), F97 (≠ Y90), R98 (= R91), A101 (≠ V94), R104 (≠ K97), K125 (≠ S118), D182 (= D162), M213 (≠ I193)
Q5U921 (R)-2-hydroxy-4-methylpentanoate CoA-transferase; 2-hydroxyisocaproate-CoA transferase; EC 2.8.3.24 from Clostridioides difficile (Peptoclostridium difficile) (see paper)
30% identity, 99% coverage: 3:390/390 of query aligns to 6:398/399 of Q5U921
- D171 (= D162) mutation D->A,N: Loss of activity.
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
29% identity, 93% coverage: 3:365/390 of query aligns to 9:355/360 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, 99% coverage: 3:390/390 of query aligns to 6:374/382 of Q9UHK6
- V9 (≠ L6) to M: in dbSNP:rs3195676
- S52 (= S62) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ I117) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G184) to D: in dbSNP:rs10941112
- L201 (≠ F209) to S: in dbSNP:rs2287939
- M261 (≠ G274) to T: in dbSNP:rs3195678
- E277 (≠ H290) 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: 3:341/390 of query aligns to 7:334/355 of 2yimA
- active site: G16 (≠ M12), D122 (= D133), D151 (= D162), G214 (≠ V224), G215 (≠ S225)
- binding 2-methylacetoacetyl coa: I15 (= I11), R37 (≠ K33), A54 (≠ L65), L56 (= L67), K57 (= K68), G78 (≠ N89), Y79 (= Y90), R80 (= R91), V83 (= V94), R86 (≠ K97), L87 (= L98), A119 (≠ G130), G120 (= G131), H121 (≠ F132), Y125 (≠ A136), D151 (= D162)
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: 3:341/390 of query aligns to 8:339/360 of O06543
- R38 (≠ K33) binding substrate
- R52 (= R58) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S62) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ LNLK 65:68) binding substrate
- E82 (= E88) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NYR 89:91) binding substrate
- R91 (≠ K97) binding substrate; mutation to A: 19.9% of wild-type activity.
- M111 (≠ I117) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ GFDLVA 131:136) binding substrate
- H126 (≠ F132) mutation to A: 4.5% of wild-type activity.
- D156 (= D162) mutation to A: 17.6 of wild-type activity.
- D190 (≠ E195) mutation to A: 3.3% of wild-type activity.
- E241 (≠ D264) mutation to A: 2.1% of wild-type activity.
- C297 (≠ P306) mutation to A: 6.2% of wild-type activity.
- H312 (= H321) 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: 3:341/390 of query aligns to 7:333/354 of 2gd6A
- active site: G16 (≠ M12), D121 (= D133), D150 (= D162), G213 (≠ V224), G214 (≠ S225)
- binding acetyl coenzyme *a: I15 (= I11), R37 (≠ K33), A53 (≠ L65), D54 (≠ N66), L55 (= L67), K56 (= K68), G77 (≠ N89), Y78 (= Y90), R79 (= R91), V82 (= V94), R85 (≠ K97), G119 (= G131), H120 (≠ F132), Y124 (≠ A136), D150 (= D162), M182 (≠ I193)
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: 3:341/390 of query aligns to 7:333/354 of 2gd2A
- active site: G16 (≠ M12), D121 (= D133), D150 (= D162), G213 (≠ V224), G214 (≠ S225)
- binding acetoacetyl-coenzyme a: I15 (= I11), R37 (≠ K33), A53 (≠ L65), L55 (= L67), K56 (= K68), G77 (≠ N89), Y78 (= Y90), R79 (= R91), V82 (= V94), R85 (≠ K97), L86 (= L98), A118 (≠ G130), G119 (= G131), H120 (≠ F132), Y124 (≠ A136), D150 (= D162)
Query Sequence
>WP_234239471.1 NCBI__GCF_002151265.1:WP_234239471.1
MKMKVLDISQIMAGPYCTMVLGDLGADVIKVEKNGGDDSRQMGPYVNEESTCFAQINRNK
KSISLNLKEEEGREIFYRLAKEADVIVENYRTGVAKKLKVDYETIKAINPGIIYCSISGY
GQTGPYSHKGGFDLVAQGMTGLMSMTGEPGRRPLKTGIAVYDIGAGITAVYSILAAYIHK
LGTGEGQHVDVAIAECGLPWFTWEAAAFFAEGTVPEPTGWRHRVSAPYQAIKVSDGYIML
GCANQRNWERLCHEVIDRPDLLQDPRFVSNHLRGQNVEALEAVLEEIFVHDTREAWLAKC
DQAGVPAGPINDFAQALDDPHYQARGMVQEMEHPVIGRMKTIGFASKLSGTPPQIRRPAP
LYAQHTDEIMAELGLDEARCEELRRKGVIK
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