SitesBLAST
Comparing Dsui_1115 FitnessBrowser__PS:Dsui_1115 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)
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
35% identity, 99% coverage: 6:388/388 of query aligns to 3:373/382 of Q9UHK6
- V9 (≠ L12) to M: in dbSNP:rs3195676
- S52 (≠ G69) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ I124) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G192) to D: in dbSNP:rs10941112
- L201 (≠ G218) to S: in dbSNP:rs2287939
- M261 (≠ G278) to T: in dbSNP:rs3195678
- E277 (≠ S294) to K: in dbSNP:rs2278008
Sites not aligning to the query:
- 380:382 Microbody targeting signal
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
38% identity, 95% coverage: 5:372/388 of query aligns to 4:358/360 of O06543
- R38 (≠ G52) binding
- R52 (= R65) mutation to A: 15.7% of wild-type activity.
- I56 (≠ G69) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ LDLK 72:75) binding
- E82 (= E95) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ SFR 96:98) binding
- R91 (≠ K104) binding ; mutation to A: 19.9% of wild-type activity.
- M111 (≠ I124) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ GHDLNY 138:143) binding
- H126 (= H139) mutation to A: 4.5% of wild-type activity.
- D156 (= D169) mutation to A: 17.6 of wild-type activity.
- D190 (= D203) mutation to A: 3.3% of wild-type activity.
- E241 (= E254) mutation to A: 2.1% of wild-type activity.
- C297 (= C310) mutation to A: 6.2% of wild-type activity.
- H312 (= H325) mutation to 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)
38% identity, 95% coverage: 5:372/388 of query aligns to 3:353/355 of 2yimA
- active site: G16 (≠ L18), D122 (= D140), D151 (= D169), G214 (= G232), G215 (= G233)
- binding 2-methylacetoacetyl coa: I15 (≠ L17), R37 (≠ G52), A54 (≠ L72), L56 (= L74), K57 (= K75), G78 (≠ S96), Y79 (≠ F97), R80 (= R98), V83 (= V101), R86 (≠ K104), L87 (= L105), A119 (= A137), G120 (= G138), H121 (= H139), Y125 (= Y143), D151 (= D169)
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)
37% identity, 95% coverage: 5:372/388 of query aligns to 3:352/354 of 2gd6A
- active site: G16 (≠ L18), D121 (= D140), D150 (= D169), G213 (= G232), G214 (= G233)
- binding acetyl coenzyme *a: I15 (≠ L17), R37 (≠ D39), A53 (≠ L72), D54 (= D73), L55 (= L74), K56 (= K75), G77 (≠ S96), Y78 (≠ F97), R79 (= R98), V82 (= V101), R85 (≠ K104), G119 (= G138), H120 (= H139), Y124 (= Y143), D150 (= D169), M182 (= M201)
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)
37% identity, 95% coverage: 5:372/388 of query aligns to 3:352/354 of 2gd2A
- active site: G16 (≠ L18), D121 (= D140), D150 (= D169), G213 (= G232), G214 (= G233)
- binding acetoacetyl-coenzyme a: I15 (≠ L17), R37 (≠ D39), A53 (≠ L72), L55 (= L74), K56 (= K75), G77 (≠ S96), Y78 (≠ F97), R79 (= R98), V82 (= V101), R85 (≠ K104), L86 (= L105), A118 (= A137), G119 (= G138), H120 (= H139), Y124 (= Y143), D150 (= D169)
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)
37% identity, 95% coverage: 5:372/388 of query aligns to 3:352/354 of 2gd0A
- active site: G16 (≠ L18), D121 (= D140), D150 (= D169), G213 (= G232), G214 (= G233)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D44), L55 (= L74), K56 (= K75), G77 (≠ S96), Y78 (≠ F97), R79 (= R98), V82 (= V101), R85 (≠ K104), L86 (= L105), G119 (= G138), H120 (= H139), D121 (= D140), Y124 (= Y143), D150 (= D169)
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)
37% identity, 95% coverage: 5:372/388 of query aligns to 3:352/354 of 2gciA
- active site: G16 (≠ L18), D121 (= D140), D150 (= D169), G213 (= G232), G214 (= G233)
- binding (r)-2-methylmyristoyl-coenzyme a: R37 (≠ D39), L55 (= L74), K56 (= K75), G77 (≠ S96), Y78 (≠ F97), R79 (= R98), V82 (= V101), G119 (= G138), H120 (= H139), D121 (= D140), Y124 (= Y143), D150 (= D169), Y218 (= Y237), I234 (≠ L253), E235 (= E254)
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)
37% identity, 95% coverage: 5:372/388 of query aligns to 3:352/354 of 2gceA
- active site: G16 (≠ L18), D121 (= D140), D150 (= D169), G213 (= G232), G214 (= G233)
- binding (r)-ibuprofenoyl-coenzyme a: I15 (≠ L17), R37 (≠ D39), L55 (= L74), K56 (= K75), G77 (≠ S96), Y78 (≠ F97), R79 (= R98), V82 (= V101), R85 (≠ K104), G119 (= G138), H120 (= H139), D121 (= D140), Y124 (= Y143), D150 (= D169), L211 (= L230), Y218 (= Y237), I234 (≠ L253)
- binding (s)-ibuprofenoyl-coenzyme a: I15 (≠ L17), G16 (≠ L18), P17 (= P19), R37 (≠ D39), L55 (= L74), K56 (= K75), G77 (≠ S96), Y78 (≠ F97), R79 (= R98), V82 (= V101), R85 (≠ K104), G119 (= G138), H120 (= H139), Y124 (= Y143), D150 (= D169)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
29% identity, 99% coverage: 3:388/388 of query aligns to 2:428/430 of 3ubmB
- active site: Q17 (≠ L18), E140 (≠ D140), D182 (vs. gap), G261 (= G232), G262 (= G233)
- binding coenzyme a: V16 (≠ L17), R38 (≠ D39), L72 (= L72), N73 (≠ D73), T74 (≠ L74), K75 (= K75), N96 (≠ S96), F97 (= F97), R98 (= R98), A101 (≠ V101), R104 (≠ K104), K125 (≠ T125), D182 (vs. gap), M213 (= M201)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
28% identity, 98% coverage: 3:384/388 of query aligns to 1:411/415 of 1pt5A
- active site: Q16 (≠ L18), E139 (≠ D140), D168 (= D169), G247 (vs. gap), G248 (vs. gap)
- binding acetyl coenzyme *a: V15 (≠ L17), S17 (≠ P19), R37 (≠ D39), L71 (= L72), N72 (≠ D73), T73 (≠ L74), K74 (= K75), N95 (≠ S96), F96 (= F97), H97 (≠ R98), K124 (≠ T125), K136 (≠ A137), A137 (≠ G138), Y138 (≠ H139), E139 (≠ D140), D168 (= D169), M199 (= M201)
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, 98% coverage: 3:384/388 of query aligns to 2:412/416 of P69902
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
28% identity, 98% coverage: 3:384/388 of query aligns to 2:412/417 of 1q6yA
- active site: Q17 (≠ L18), E140 (≠ D140), D169 (= D169), G248 (vs. gap), G249 (vs. gap)
- binding coenzyme a: V16 (≠ L17), Q17 (≠ L18), S18 (≠ P19), R38 (≠ D39), L72 (= L72), N73 (≠ D73), T74 (≠ L74), K75 (= K75), N96 (≠ S96), F97 (= F97), H98 (≠ R98), M105 (≠ L105), I124 (= I124), K137 (≠ A137), A138 (≠ G138), Y139 (≠ H139), D169 (= D169), M200 (= M201)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
30% identity, 95% coverage: 3:369/388 of query aligns to 3:360/360 of 5yx6A
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
37% identity, 53% coverage: 3:206/388 of query aligns to 1:204/427 of 2vjkA
- active site: Q16 (≠ L18), E139 (≠ I144), D168 (= D169)
- binding coenzyme a: H14 (≠ R16), Q16 (≠ L18), A17 (≠ P19), R37 (≠ D39), M73 (≠ L74), K74 (= K75), N95 (≠ S96), F96 (= F97), G97 (≠ R98), R103 (≠ K104), M104 (≠ L105), K136 (≠ L141), V137 (≠ N142), Y138 (= Y143), D168 (= D169), M199 (= M201)
Sites not aligning to the query:
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
37% identity, 53% coverage: 3:206/388 of query aligns to 1:204/427 of 1t4cA
- active site: Q16 (≠ L18), E139 (≠ I144), D168 (= D169)
- binding coenzyme a: H14 (≠ R16), V15 (≠ L17), Q16 (≠ L18), R37 (≠ D39), M73 (≠ L74), N95 (≠ S96), F96 (= F97), R103 (≠ K104), M104 (≠ L105), V137 (≠ N142), Y138 (= Y143), D168 (= D169), M199 (= M201)
Sites not aligning to the query:
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
37% identity, 53% coverage: 3:206/388 of query aligns to 1:204/427 of 2vjoA
- active site: A16 (≠ L18), E139 (≠ I144), D168 (= D169)
- binding coenzyme a: H14 (≠ R16), A16 (≠ L18), A17 (≠ P19), R37 (≠ D39), L71 (= L72), M73 (≠ L74), N95 (≠ S96), F96 (= F97), G97 (≠ R98), R103 (≠ K104), M104 (≠ L105), K136 (≠ L141), V137 (≠ N142), Y138 (= Y143), D168 (= D169), M199 (= M201)
Sites not aligning to the query:
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
37% identity, 53% coverage: 3:206/388 of query aligns to 1:204/427 of 1p5rA
- active site: Q16 (≠ L18), E139 (≠ I144), D168 (= D169)
- binding coenzyme a: H14 (≠ R16), V15 (≠ L17), Q16 (≠ L18), A17 (≠ P19), R37 (≠ D39), M73 (≠ L74), K74 (= K75), N95 (≠ S96), F96 (= F97), A100 (≠ V101), R103 (≠ K104), K136 (≠ L141), V137 (≠ N142), D168 (= D169), M199 (= M201)
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)
37% identity, 53% coverage: 3:206/388 of query aligns to 2:205/428 of O06644
- Q17 (≠ L18) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ D39) binding
- W48 (≠ T48) 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 (≠ K104) binding
- D169 (= D169) 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.
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
37% identity, 53% coverage: 3:206/388 of query aligns to 1:204/427 of 1t3zA
- active site: Q16 (≠ L18), E139 (≠ I144), S168 (≠ D169)
- binding oxidized coenzyme a: H14 (≠ R16), V15 (≠ L17), A17 (≠ P19), R37 (≠ D39), K74 (= K75), N95 (≠ S96), F96 (= F97), A100 (≠ V101), R103 (≠ K104), M104 (≠ L105), K136 (≠ L141), V137 (≠ N142), Y138 (= Y143), E139 (≠ I144), M199 (= M201)
Sites not aligning to the query:
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
27% identity, 98% coverage: 3:384/388 of query aligns to 2:405/410 of 1q7eA
- active site: Q17 (≠ L18), E133 (≠ D140), D162 (= D169), G241 (vs. gap), G242 (vs. gap)
- binding methionine: N96 (≠ S96), F97 (= F97), H98 (≠ R98), P99 (= P99), K118 (≠ T125), K130 (≠ A137), A131 (≠ G138), W246 (vs. gap), F299 (vs. gap), A303 (= A286), E306 (= E289)
Query Sequence
>Dsui_1115 FitnessBrowser__PS:Dsui_1115
MASKPLQGVRILDLTRLLPGPVATLHLADLGADVIKIEDHGAGDYARTMGDGPEGVSVFY
RAVNRNKRGLRLDLKNPEGAALFRRLAAEADVVIESFRPGVMDKLGVGYEALCSLNPRLV
FCAITGYGQSGPLALAAGHDLNYIGYAGILDQIGVDGGQPAIPNLQIGDLLGGAMSAVMG
ILAALFDARRSGQGRFVDVSMSDAALAHNLFPLFALQGGAGVAERGRDMLSGGDAGYGVY
ATADGRYMAVAPLERKFWDLFCDTLGQPRWKARHGATGAEARAMRAELETLFASQPQSYW
TEKFARVDCCVTPVLTVAEALAHPHFQARGMGFQADGITQYGPPVRLSDMPVEPVRPAPA
PGEHGQAILAEFGVTAEELQRLQNLGVV
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