SitesBLAST
Comparing Ac3H11_369 FitnessBrowser__acidovorax_3H11:Ac3H11_369 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)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
30% identity, 89% coverage: 45:434/436 of query aligns to 5:427/430 of 3ubmB
- active site: Q17 (≠ I57), E140 (≠ G179), D182 (= D208), G261 (vs. gap), G262 (vs. gap)
- binding coenzyme a: V16 (≠ L56), R38 (≠ A78), L72 (= L111), N73 (≠ D112), T74 (≠ L113), K75 (≠ R114), N96 (= N135), F97 (= F136), R98 (= R137), A101 (≠ T140), R104 (≠ G143), K125 (≠ S164), D182 (= D208), M213 (≠ L240)
P31572 L-carnitine CoA-transferase; Crotonobetainyl-CoA:carnitine CoA-transferase; EC 2.8.3.21 from Escherichia coli (strain K12) (see paper)
29% identity, 92% coverage: 36:434/436 of query aligns to 1:400/405 of P31572
- K97 (≠ R137) binding
- R104 (≠ W144) binding
1xvtA Crystal structure of native caib in complex with coenzyme a (see paper)
29% identity, 89% coverage: 45:434/436 of query aligns to 9:397/402 of 1xvtA
- active site: I21 (= I57), N138 (≠ G179), D166 (= D208), G225 (= G266), K226 (≠ S267)
- binding coenzyme a: I21 (= I57), A22 (= A58), N42 (≠ A78), L68 (= L111), N69 (≠ D112), F71 (≠ R114), S93 (≠ F136), K94 (≠ R137), R100 (≠ G143), R101 (≠ W144), P135 (= P176), A136 (≠ G177), D166 (= D208), M197 (≠ L240)
1xvvA Crystal structure of caib mutant d169a in complex with carnitinyl-coa (see paper)
28% identity, 89% coverage: 45:434/436 of query aligns to 9:397/402 of 1xvvA
- active site: I21 (= I57), N138 (≠ G179), A166 (= A211), G225 (= G266), K226 (≠ S267)
- binding l-carnitinyl-coa inner salt: I19 (≠ Q55), E20 (≠ L56), I21 (= I57), A22 (= A58), N69 (≠ D112), F71 (≠ R114), A92 (≠ N135), S93 (≠ F136), K94 (≠ R137), R100 (≠ G143), R101 (≠ W144), A136 (≠ G177), Y137 (≠ F178), N138 (≠ G179), Y163 (≠ D208)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
29% identity, 90% coverage: 45:435/436 of query aligns to 5:428/428 of O06644
- Q17 (≠ I57) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ A78) binding
- W48 (= W88) 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 (≠ G143) binding
- D169 (= D208) 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)
29% identity, 90% coverage: 45:435/436 of query aligns to 4:427/427 of 1p5rA
- active site: Q16 (≠ I57), E139 (≠ G179), D168 (= D208), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ Q55), V15 (≠ L56), Q16 (≠ I57), A17 (= A58), R37 (≠ A78), M73 (≠ L113), K74 (≠ R114), N95 (= N135), F96 (= F136), A100 (≠ T140), R103 (≠ G143), K136 (≠ P176), V137 (≠ G177), D168 (= D208), M199 (≠ L240)
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
29% identity, 90% coverage: 45:435/436 of query aligns to 4:427/427 of 2vjoA
- active site: A16 (≠ I57), E139 (≠ G179), D168 (= D208), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ Q55), A16 (≠ I57), A17 (= A58), R37 (≠ A78), L71 (= L111), M73 (≠ L113), N95 (= N135), F96 (= F136), G97 (≠ R137), R103 (≠ G143), M104 (≠ W144), K136 (≠ P176), V137 (≠ G177), Y138 (≠ F178), D168 (= D208), M199 (≠ L240)
- binding oxalate ion: G257 (vs. gap), G259 (vs. gap), Q261 (vs. gap)
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
29% identity, 90% coverage: 45:435/436 of query aligns to 4:427/427 of 2vjkA
- active site: Q16 (≠ I57), E139 (≠ G179), D168 (= D208), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ Q55), Q16 (≠ I57), A17 (= A58), R37 (≠ A78), M73 (≠ L113), K74 (≠ R114), N95 (= N135), F96 (= F136), G97 (≠ R137), R103 (≠ G143), M104 (≠ W144), K136 (≠ P176), V137 (≠ G177), Y138 (≠ F178), D168 (= D208), M199 (≠ L240)
- binding magnesium ion: D293 (≠ T300), D296 (≠ G303)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
29% identity, 90% coverage: 45:435/436 of query aligns to 4:427/427 of 1t4cA
- active site: Q16 (≠ I57), E139 (≠ G179), D168 (= D208), G259 (vs. gap), G260 (vs. gap)
- binding coenzyme a: H14 (≠ Q55), V15 (≠ L56), Q16 (≠ I57), R37 (≠ A78), M73 (≠ L113), N95 (= N135), F96 (= F136), R103 (≠ G143), M104 (≠ W144), V137 (≠ G177), Y138 (≠ F178), D168 (= D208), M199 (≠ L240)
- binding oxalic acid: G259 (vs. gap), G260 (vs. gap)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
28% identity, 90% coverage: 45:435/436 of query aligns to 4:427/427 of 1t3zA
- active site: Q16 (≠ I57), E139 (≠ G179), S168 (≠ D208), G259 (vs. gap), G260 (vs. gap)
- binding oxidized coenzyme a: H14 (≠ Q55), V15 (≠ L56), A17 (= A58), R37 (≠ A78), K74 (≠ R114), N95 (= N135), F96 (= F136), A100 (≠ T140), R103 (≠ G143), M104 (≠ W144), K136 (≠ P176), V137 (≠ G177), Y138 (≠ F178), E139 (≠ G179), M199 (≠ L240)
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
27% identity, 90% coverage: 45:436/436 of query aligns to 5:417/417 of 1q6yA
- active site: Q17 (≠ I57), E140 (≠ G179), D169 (= D208), G248 (vs. gap), G249 (vs. gap)
- binding coenzyme a: V16 (≠ L56), Q17 (≠ I57), S18 (≠ A58), R38 (≠ A78), L72 (= L111), N73 (≠ D112), T74 (≠ L113), K75 (≠ R114), N96 (= N135), F97 (= F136), H98 (≠ R137), M105 (≠ W144), I124 (= I163), K137 (≠ P176), A138 (≠ G177), Y139 (≠ F178), D169 (= D208), M200 (≠ L240)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
28% identity, 90% coverage: 45:435/436 of query aligns to 4:415/415 of 1pt5A
- active site: Q16 (≠ I57), E139 (≠ G179), D168 (= D208), G247 (= G271), G248 (≠ I272)
- binding acetyl coenzyme *a: V15 (≠ L56), S17 (≠ A58), R37 (≠ A78), L71 (= L111), N72 (≠ D112), T73 (≠ L113), K74 (≠ R114), N95 (= N135), F96 (= F136), H97 (≠ R137), K124 (≠ S164), K136 (≠ P176), A137 (≠ G177), Y138 (≠ F178), E139 (≠ G179), D168 (= D208), M199 (≠ L240)
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, 90% coverage: 45:435/436 of query aligns to 5:416/416 of P69902
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
28% identity, 90% coverage: 45:436/436 of query aligns to 5:410/410 of 1q7eA
- active site: Q17 (≠ I57), E133 (≠ G179), D162 (= D208), G241 (= G271), G242 (≠ I272)
- binding methionine: N96 (= N135), F97 (= F136), H98 (≠ R137), P99 (= P138), K118 (≠ S164), K130 (≠ P176), A131 (≠ G177), W246 (≠ N276), F299 (≠ G324), A303 (≠ T328), E306 (≠ G331)
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
28% identity, 90% coverage: 44:436/436 of query aligns to 2:374/382 of Q9UHK6
- V9 (≠ I51) to M: in dbSNP:rs3195676
- S52 (= S108) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ I163) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G231) to D: in dbSNP:rs10941112
- L201 (≠ Y255) to S: in dbSNP:rs2287939
- M261 (≠ V320) to T: in dbSNP:rs3195678
- E277 (≠ A336) to K: in dbSNP:rs2278008
Sites not aligning to the query:
- 380:382 Microbody targeting signal
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
28% identity, 76% coverage: 45:375/436 of query aligns to 6:324/360 of 5yx6A
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
28% identity, 86% coverage: 45:418/436 of query aligns to 5:357/360 of O06543
- R38 (≠ A78) binding
- R52 (= R104) mutation to A: 15.7% of wild-type activity.
- I56 (≠ S108) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ LDLR 111:114) binding
- E82 (= E134) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NFR 135:137) binding
- R91 (≠ G143) binding ; mutation to A: 19.9% of wild-type activity.
- M111 (≠ I163) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ GFGVIG 177:182) binding
- H126 (≠ F178) mutation to A: 4.5% of wild-type activity.
- D156 (= D208) mutation to A: 17.6 of wild-type activity.
- D190 (≠ E242) mutation to A: 3.3% of wild-type activity.
- E241 (≠ G291) mutation to A: 2.1% of wild-type activity.
- C297 (≠ P352) mutation to A: 6.2% of wild-type activity.
- H312 (= H367) 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)
28% identity, 86% coverage: 45:418/436 of query aligns to 4:351/354 of 2gd6A
- active site: G16 (≠ I57), D121 (≠ G179), D150 (= D208), G213 (= G271), G214 (≠ I272)
- binding acetyl coenzyme *a: I15 (≠ L56), R37 (≠ A78), A53 (≠ L111), D54 (= D112), L55 (= L113), K56 (≠ R114), G77 (≠ N135), Y78 (≠ F136), R79 (= R137), V82 (≠ T140), R85 (≠ G143), G119 (= G177), H120 (≠ F178), Y124 (≠ G182), D150 (= D208), M182 (≠ L240)
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)
28% identity, 86% coverage: 45:418/436 of query aligns to 4:351/354 of 2gd2A
- active site: G16 (≠ I57), D121 (≠ G179), D150 (= D208), G213 (= G271), G214 (≠ I272)
- binding acetoacetyl-coenzyme a: I15 (≠ L56), R37 (≠ A78), A53 (≠ L111), L55 (= L113), K56 (≠ R114), G77 (≠ N135), Y78 (≠ F136), R79 (= R137), V82 (≠ T140), R85 (≠ G143), L86 (≠ W144), A118 (≠ P176), G119 (= G177), H120 (≠ F178), Y124 (≠ G182), D150 (= D208)
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)
28% identity, 86% coverage: 45:418/436 of query aligns to 4:351/354 of 2gd0A
- active site: G16 (≠ I57), D121 (≠ G179), D150 (= D208), G213 (= G271), G214 (≠ I272)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D83), L55 (= L113), K56 (≠ R114), G77 (≠ N135), Y78 (≠ F136), R79 (= R137), V82 (≠ T140), R85 (≠ G143), L86 (≠ W144), G119 (= G177), H120 (≠ F178), D121 (≠ G179), Y124 (≠ G182), D150 (= D208)
Query Sequence
>Ac3H11_369 FitnessBrowser__acidovorax_3H11:Ac3H11_369
MLDCDGGLLLERFAGGRRVRIIAPQHYRLHETNRSMDSTASPAALQGVRVIEMGQLIAGP
FCGKTLGEFGADVIKIEAPETGDPLRNWRLIKGGTSVWWQVQSRNKRSVALDLRQKEGQA
IARQLIAEADVLVENFRPGTLEGWGMSPDELHALNPGLVILRISGYGQTGPYRDLPGFGV
IGEAMGGLRHLTAEPGRVPVRVGVSIGDTLAALHGTIGVLTALYHRKVNGGKGQVIDVAL
HEAVFNVMESLIPEYSAFGAVREAAGSALPGIAPSNAYPCQDGWVLVAGNGDSIFKRLMT
AIGRQDLADAPDLGSNTGRVARVGEIDTAIGAWTAARSVQQVMETLGAARVPAGKVYTAK
DIAEDPHYRARDMLLTQETRDGYSVEVPGIVPKLSGTPGSIRRSAPHLGDDTDAVLAEAG
LTAEQIALLRSKGVIQ
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