SitesBLAST
Comparing WP_035703129.1 NCBI__GCF_000691145.1:WP_035703129.1 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)
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)
33% identity, 100% coverage: 1:400/400 of query aligns to 35:432/438 of Q9HAC7
- D205 (= D170) mutation to A: Loss of CoA transferase activity toward glutaryl-CoA and 3-hydroxy-3-methylglutarate substrates.
- R329 (≠ W297) to W: in GA3; severely decreased protein stability and processing; dbSNP:rs137852860
9br7C Succinate--hydroxymethylglutarate CoA-transferase (see paper)
33% identity, 100% coverage: 2:400/400 of query aligns to 1:397/403 of 9br7C
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
28% identity, 99% coverage: 6:399/400 of query aligns to 4:427/430 of 3ubmB
- active site: Q17 (≠ I19), E140 (≠ G141), D182 (= D170), G261 (vs. gap), G262 (vs. gap)
- binding coenzyme a: V16 (≠ M18), R38 (≠ I40), L72 (= L73), N73 (≠ D74), T74 (≠ L75), K75 (≠ H76), N96 (= N97), F97 (= F98), R98 (= R99), A101 (≠ T102), R104 (≠ K105), K125 (≠ S126), D182 (= D170), M213 (≠ L203)
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)
27% identity, 99% coverage: 4:400/400 of query aligns to 2:416/416 of P69902
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
27% identity, 99% coverage: 4:400/400 of query aligns to 1:415/415 of 1pt5A
- active site: Q16 (≠ I19), E139 (≠ G141), D168 (= D170), G247 (vs. gap), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (≠ M18), S17 (≠ A20), R37 (≠ I40), L71 (= L73), N72 (≠ D74), T73 (≠ L75), K74 (≠ H76), N95 (= N97), F96 (= F98), H97 (≠ R99), K124 (≠ S126), K136 (≠ A138), A137 (≠ G139), Y138 (≠ F140), E139 (≠ G141), D168 (= D170), M199 (≠ L203)
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
27% identity, 99% coverage: 4:400/400 of query aligns to 2:416/417 of 1q6yA
- active site: Q17 (≠ I19), E140 (≠ G141), D169 (= D170), G248 (vs. gap), G249 (vs. gap)
- binding coenzyme a: V16 (≠ M18), Q17 (≠ I19), S18 (≠ A20), R38 (≠ I40), L72 (= L73), N73 (≠ D74), T74 (≠ L75), K75 (≠ H76), N96 (= N97), F97 (= F98), H98 (≠ R99), M105 (≠ W106), I124 (≠ V125), K137 (≠ A138), A138 (≠ G139), Y139 (≠ F140), D169 (= D170), M200 (≠ L203)
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
27% identity, 99% coverage: 4:400/400 of query aligns to 2:409/410 of 1q7eA
- active site: Q17 (≠ I19), E133 (≠ G141), D162 (= D170), G241 (vs. gap), G242 (vs. gap)
- binding methionine: N96 (= N97), F97 (= F98), H98 (≠ R99), P99 (= P100), K118 (≠ S126), K130 (≠ A138), A131 (≠ G139), W246 (vs. gap), F299 (≠ D288), A303 (= A292), E306 (≠ S295)
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
27% identity, 99% coverage: 7:400/400 of query aligns to 3:373/382 of Q9UHK6
- V9 (≠ L13) to M: in dbSNP:rs3195676
- S52 (= S70) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ V125) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G194) to D: in dbSNP:rs10941112
- L201 (≠ D219) to S: in dbSNP:rs2287939
- M261 (≠ L284) to T: in dbSNP:rs3195678
- E277 (≠ S300) to K: in dbSNP:rs2278008
Sites not aligning to the query:
- 380:382 Microbody targeting signal
1xvtA Crystal structure of native caib in complex with coenzyme a (see paper)
28% identity, 100% coverage: 1:399/400 of query aligns to 3:397/402 of 1xvtA
- active site: I21 (= I19), N138 (≠ G141), D166 (= D170), G225 (= G230), K226 (≠ L231)
- binding coenzyme a: I21 (= I19), A22 (= A20), N42 (≠ I40), L68 (= L73), N69 (≠ D74), F71 (≠ H76), S93 (≠ F98), K94 (≠ R99), R100 (≠ K105), R101 (≠ W106), P135 (≠ A138), A136 (≠ G139), D166 (= D170), M197 (≠ L203)
P31572 L-carnitine CoA-transferase; Crotonobetainyl-CoA:carnitine CoA-transferase; EC 2.8.3.21 from Escherichia coli (strain K12) (see paper)
28% identity, 100% coverage: 1:399/400 of query aligns to 6:400/405 of P31572
- K97 (≠ R99) binding CoA
- R104 (≠ W106) binding CoA
1xvvA Crystal structure of caib mutant d169a in complex with carnitinyl-coa (see paper)
28% identity, 100% coverage: 1:399/400 of query aligns to 3:397/402 of 1xvvA
- active site: I21 (= I19), N138 (≠ G141), A166 (≠ D170), G225 (= G230), K226 (≠ L231)
- binding l-carnitinyl-coa inner salt: I19 (≠ T17), E20 (≠ M18), I21 (= I19), A22 (= A20), N69 (≠ D74), F71 (≠ H76), A92 (≠ N97), S93 (≠ F98), K94 (≠ R99), R100 (≠ K105), R101 (≠ W106), A136 (≠ G139), Y137 (≠ F140), N138 (≠ G141), Y163 (≠ L168)
Q5U921 (R)-2-hydroxy-4-methylpentanoate CoA-transferase; 2-hydroxyisocaproate-CoA transferase; EC 2.8.3.24 from Clostridioides difficile (Peptoclostridium difficile) (see paper)
28% identity, 99% coverage: 7:400/400 of query aligns to 3:397/399 of Q5U921
- D171 (= D170) mutation D->A,N: Loss of activity.
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
29% identity, 95% coverage: 2:380/400 of query aligns to 1:360/360 of 5yx6A
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
27% identity, 89% coverage: 6:361/400 of query aligns to 4:337/360 of O06543
- R38 (≠ I40) binding substrate
- R52 (= R66) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S70) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ LDLH 73:76) binding substrate
- E82 (= E96) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NFR 97:99) binding substrate
- R91 (≠ K105) binding substrate; mutation to A: 19.9% of wild-type activity.
- M111 (≠ V125) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ GFGTPA 139:144) binding substrate
- H126 (≠ F140) mutation to A: 4.5% of wild-type activity.
- D156 (= D170) mutation to A: 17.6 of wild-type activity.
- D190 (≠ E205) mutation to A: 3.3% of wild-type activity.
- E241 (≠ D256) mutation to A: 2.1% of wild-type activity.
- C297 (≠ P316) mutation to A: 6.2% of wild-type activity.
- H312 (≠ Q331) mutation to A: 10.1% of wild-type activity.
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
24% identity, 99% coverage: 6:400/400 of query aligns to 3:427/427 of 2vjoA
- active site: A16 (≠ I19), E139 (≠ G141), D168 (= D170), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T17), A16 (≠ I19), A17 (= A20), R37 (≠ I40), L71 (= L73), M73 (≠ L75), N95 (= N97), F96 (= F98), G97 (≠ R99), R103 (≠ K105), M104 (≠ W106), K136 (≠ A138), V137 (≠ G139), Y138 (≠ F140), D168 (= D170), M199 (≠ L203)
- binding oxalate ion: G257 (vs. gap), G259 (vs. gap), Q261 (vs. gap)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
24% identity, 99% coverage: 6:400/400 of query aligns to 4:428/428 of O06644
- Q17 (≠ I19) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ I40) binding CoA
- W48 (≠ P52) 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 (≠ K105) binding CoA
- D169 (= D170) 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)
24% identity, 99% coverage: 6:400/400 of query aligns to 3:427/427 of 1p5rA
- active site: Q16 (≠ I19), E139 (≠ G141), D168 (= D170), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T17), V15 (≠ M18), Q16 (≠ I19), A17 (= A20), R37 (≠ I40), M73 (≠ L75), K74 (≠ H76), N95 (= N97), F96 (= F98), A100 (≠ T102), R103 (≠ K105), K136 (≠ A138), V137 (≠ G139), D168 (= D170), M199 (≠ L203)
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
24% identity, 99% coverage: 6:400/400 of query aligns to 3:427/427 of 2vjkA
- active site: Q16 (≠ I19), E139 (≠ G141), D168 (= D170), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T17), Q16 (≠ I19), A17 (= A20), R37 (≠ I40), M73 (≠ L75), K74 (≠ H76), N95 (= N97), F96 (= F98), G97 (≠ R99), R103 (≠ K105), M104 (≠ W106), K136 (≠ A138), V137 (≠ G139), Y138 (≠ F140), D168 (= D170), M199 (≠ L203)
- binding magnesium ion: D293 (≠ E264), D296 (≠ N267)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
24% identity, 99% coverage: 6:400/400 of query aligns to 3:427/427 of 1t4cA
- active site: Q16 (≠ I19), E139 (≠ G141), D168 (= D170), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ T17), V15 (≠ M18), Q16 (≠ I19), R37 (≠ I40), M73 (≠ L75), N95 (= N97), F96 (= F98), R103 (≠ K105), M104 (≠ W106), V137 (≠ G139), Y138 (≠ F140), D168 (= D170), M199 (≠ L203)
- binding oxalic acid: G259 (vs. gap), G260 (vs. gap)
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)
26% identity, 89% coverage: 6:361/400 of query aligns to 3:331/354 of 2gd6A
- active site: G16 (≠ I19), D121 (≠ G141), D150 (= D170), G213 (≠ H234), G214 (≠ S235)
- binding acetyl coenzyme *a: I15 (≠ M18), R37 (≠ E57), A53 (≠ L73), D54 (= D74), L55 (= L75), K56 (≠ H76), G77 (≠ N97), Y78 (≠ F98), R79 (= R99), V82 (≠ T102), R85 (≠ K105), G119 (= G139), H120 (≠ F140), Y124 (≠ A144), D150 (= D170), M182 (≠ L203)
Query Sequence
>WP_035703129.1 NCBI__GCF_000691145.1:WP_035703129.1
MNKNTPLEGIKILDVSTMIAAPYGAVLLGDFGAEVIKVEIPGKGDTLRHVGPFADGEPLR
WSGLSRNKKSLTLDLHKEEAKDIFKKLAAQVDVIIENFRPGTLEKWDVGYDVLKEINPRL
IMIRVSGYGQTGPFKDKAGFGTPATAFSGFTYIQGFTDRHPVSPSFSLTDYIAGIYVAFA
TVTAMYYRDTHSEGTGQMVDLALYESVFRMLEFLVAEYDKLGKVRERSPGLSGHSSPAGT
YETKDGHYLVLVTSTDSTFNRLAEAMNRLDLLENEKFSVNAARLKHNDEMDAIVSQWIAS
KTRDDVLDILDTHGVPVSPILSIRDIFEHPQFKARENIVEVHHPRLGKVKVPGIIPKFEK
TPGRIRHIAPDLGEHNYEILTKMLGFTEEECKQLEEKGVI
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