SitesBLAST
Comparing PP_3393 FitnessBrowser__Putida:PP_3393 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)
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
31% identity, 97% coverage: 5:390/396 of query aligns to 3:427/427 of 2vjoA
- active site: A16 (≠ V18), E139 (= E136), D168 (= D163), G259 (vs. gap), G260 (≠ R222)
- binding coenzyme a: H14 (= H16), A16 (≠ V18), A17 (≠ M19), R37 (≠ P39), L71 (≠ V68), M73 (≠ V70), N95 (= N92), F96 (= F93), G97 (≠ K94), R103 (≠ K100), M104 (≠ L101), K136 (≠ A133), V137 (≠ L134), Y138 (≠ D135), D168 (= D163), M199 (≠ L194)
- binding oxalate ion: G257 (vs. gap), G259 (vs. gap), Q261 (≠ I223)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
31% identity, 97% coverage: 5:390/396 of query aligns to 4:428/428 of O06644
- Q17 (≠ V18) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ P39) binding
- W48 (≠ L48) 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 (≠ K100) binding
- D169 (= D163) 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, 97% coverage: 5:390/396 of query aligns to 3:427/427 of 1p5rA
- active site: Q16 (≠ V18), E139 (= E136), D168 (= D163), G259 (vs. gap), G260 (≠ R222)
- binding coenzyme a: H14 (= H16), V15 (≠ M17), Q16 (≠ V18), A17 (≠ M19), R37 (≠ P39), M73 (≠ V70), K74 (≠ E71), N95 (= N92), F96 (= F93), A100 (≠ R97), R103 (≠ K100), K136 (≠ A133), V137 (≠ L134), D168 (= D163), M199 (≠ L194)
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
31% identity, 97% coverage: 5:390/396 of query aligns to 3:427/427 of 2vjkA
- active site: Q16 (≠ V18), E139 (= E136), D168 (= D163), G259 (vs. gap), G260 (≠ R222)
- binding coenzyme a: H14 (= H16), Q16 (≠ V18), A17 (≠ M19), R37 (≠ P39), M73 (≠ V70), K74 (≠ E71), N95 (= N92), F96 (= F93), G97 (≠ K94), R103 (≠ K100), M104 (≠ L101), K136 (≠ A133), V137 (≠ L134), Y138 (≠ D135), D168 (= D163), M199 (≠ L194)
- binding magnesium ion: D293 (≠ R255), D296 (≠ G258)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
31% identity, 97% coverage: 5:390/396 of query aligns to 3:427/427 of 1t4cA
- active site: Q16 (≠ V18), E139 (= E136), D168 (= D163), G259 (vs. gap), G260 (≠ R222)
- binding coenzyme a: H14 (= H16), V15 (≠ M17), Q16 (≠ V18), R37 (≠ P39), M73 (≠ V70), N95 (= N92), F96 (= F93), R103 (≠ K100), M104 (≠ L101), V137 (≠ L134), Y138 (≠ D135), D168 (= D163), M199 (≠ L194)
- binding oxalic acid: G259 (vs. gap), G260 (≠ R222)
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
31% identity, 97% coverage: 5:390/396 of query aligns to 3:427/427 of 1t3zA
- active site: Q16 (≠ V18), E139 (= E136), S168 (≠ D163), G259 (vs. gap), G260 (≠ R222)
- binding oxidized coenzyme a: H14 (= H16), V15 (≠ M17), A17 (≠ M19), R37 (≠ P39), K74 (≠ E71), N95 (= N92), F96 (= F93), A100 (≠ R97), R103 (≠ K100), M104 (≠ L101), K136 (≠ A133), V137 (≠ L134), Y138 (≠ D135), E139 (= E136), M199 (≠ L194)
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
32% identity, 96% coverage: 5:384/396 of query aligns to 3:409/415 of 1pt5A
- active site: Q16 (≠ V18), E139 (≠ D135), D168 (= D163), G247 (≠ A225), G248 (≠ W226)
- binding acetyl coenzyme *a: V15 (≠ M17), S17 (≠ M19), R37 (vs. gap), L71 (≠ V68), N72 (≠ D69), T73 (≠ V70), K74 (≠ E71), N95 (= N92), F96 (= F93), H97 (≠ K94), K124 (= K121), K136 (≠ L132), A137 (= A133), Y138 (≠ L134), E139 (≠ D135), D168 (= D163), M199 (vs. gap)
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)
32% identity, 96% coverage: 5:384/396 of query aligns to 4:410/416 of P69902
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
32% identity, 96% coverage: 5:384/396 of query aligns to 4:410/417 of 1q6yA
- active site: Q17 (≠ V18), E140 (≠ D135), D169 (= D163), G248 (≠ A225), G249 (≠ W226)
- binding coenzyme a: V16 (≠ M17), Q17 (≠ V18), S18 (≠ M19), R38 (vs. gap), L72 (≠ V68), N73 (≠ D69), T74 (≠ V70), K75 (≠ E71), N96 (= N92), F97 (= F93), H98 (≠ K94), M105 (≠ L101), I124 (≠ H120), K137 (≠ L132), A138 (= A133), Y139 (≠ L134), D169 (= D163), M200 (vs. gap)
3ubmB Formyl-coa:oxalate coa-transferase from acetobacter aceti (see paper)
29% identity, 96% coverage: 5:384/396 of query aligns to 4:422/430 of 3ubmB
- active site: Q17 (≠ V18), E140 (≠ D135), D182 (vs. gap), G261 (vs. gap), G262 (≠ R222)
- binding coenzyme a: V16 (≠ M17), R38 (≠ P39), L72 (≠ V68), N73 (≠ D69), T74 (≠ V70), K75 (≠ E71), N96 (= N92), F97 (= F93), R98 (≠ K94), A101 (≠ R97), R104 (≠ K100), K125 (= K121), D182 (vs. gap), M213 (vs. gap)
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
35% identity, 76% coverage: 5:306/396 of query aligns to 5:300/360 of 5yx6A
1q7eA Crystal structure of yfdw protein from e. Coli (see paper)
31% identity, 96% coverage: 5:384/396 of query aligns to 4:403/410 of 1q7eA
- active site: Q17 (≠ V18), E133 (≠ D135), D162 (= D163), G241 (≠ A225), G242 (≠ W226)
- binding methionine: N96 (= N92), F97 (= F93), H98 (≠ K94), P99 (= P95), K118 (= K121), K130 (≠ L132), A131 (= A133), W246 (≠ D230), F299 (≠ P279), A303 (= A283), E306 (≠ A286)
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
32% identity, 91% coverage: 5:363/396 of query aligns to 4:349/360 of O06543
- R38 (vs. gap) binding
- R52 (= R61) mutation to A: 15.7% of wild-type activity.
- I56 (≠ C65) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ VDVE 68:71) binding
- E82 (= E91) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NFK 92:94) binding
- R91 (≠ K100) binding ; mutation to A: 19.9% of wild-type activity.
- M111 (≠ H120) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ ALDEVV 133:138) binding
- H126 (≠ L134) mutation to A: 4.5% of wild-type activity.
- D156 (= D163) mutation to A: 17.6 of wild-type activity.
- D190 (≠ E196) mutation to A: 3.3% of wild-type activity.
- E241 (≠ G246) mutation to A: 2.1% of wild-type activity.
- C297 (≠ P307) mutation to A: 6.2% of wild-type activity.
- H312 (= H322) 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)
32% identity, 91% coverage: 5:363/396 of query aligns to 3:343/354 of 2gd6A
- active site: G16 (≠ V18), D121 (= D135), D150 (= D163), G213 (≠ A225), G214 (≠ W226)
- binding acetyl coenzyme *a: I15 (≠ M17), R37 (vs. gap), A53 (≠ V68), D54 (= D69), L55 (≠ V70), K56 (≠ E71), G77 (≠ N92), Y78 (≠ F93), R79 (≠ K94), V82 (≠ R97), R85 (≠ K100), G119 (≠ A133), H120 (≠ L134), Y124 (≠ V138), D150 (= D163), M182 (≠ L194)
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)
32% identity, 91% coverage: 5:363/396 of query aligns to 3:343/354 of 2gd2A
- active site: G16 (≠ V18), D121 (= D135), D150 (= D163), G213 (≠ A225), G214 (≠ W226)
- binding acetoacetyl-coenzyme a: I15 (≠ M17), R37 (vs. gap), A53 (≠ V68), L55 (≠ V70), K56 (≠ E71), G77 (≠ N92), Y78 (≠ F93), R79 (≠ K94), V82 (≠ R97), R85 (≠ K100), L86 (= L101), A118 (≠ L132), G119 (≠ A133), H120 (≠ L134), Y124 (≠ V138), D150 (= D163)
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)
32% identity, 91% coverage: 5:363/396 of query aligns to 3:343/354 of 2gd0A
- active site: G16 (≠ V18), D121 (= D135), D150 (= D163), G213 (≠ A225), G214 (≠ W226)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D43), L55 (≠ V70), K56 (≠ E71), G77 (≠ N92), Y78 (≠ F93), R79 (≠ K94), V82 (≠ R97), R85 (≠ K100), L86 (= L101), G119 (≠ A133), H120 (≠ L134), D121 (= D135), Y124 (≠ V138), D150 (= D163)
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)
32% identity, 91% coverage: 5:363/396 of query aligns to 3:343/354 of 2gciA
- active site: G16 (≠ V18), D121 (= D135), D150 (= D163), G213 (≠ A225), G214 (≠ W226)
- binding (r)-2-methylmyristoyl-coenzyme a: R37 (vs. gap), L55 (≠ V70), K56 (≠ E71), G77 (≠ N92), Y78 (≠ F93), R79 (≠ K94), V82 (≠ R97), G119 (≠ A133), H120 (≠ L134), D121 (= D135), Y124 (≠ V138), D150 (= D163), Y218 (= Y229), I234 (≠ T245), E235 (≠ G246)
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)
32% identity, 91% coverage: 5:363/396 of query aligns to 3:343/354 of 2gceA
- active site: G16 (≠ V18), D121 (= D135), D150 (= D163), G213 (≠ A225), G214 (≠ W226)
- binding (r)-ibuprofenoyl-coenzyme a: I15 (≠ M17), R37 (vs. gap), L55 (≠ V70), K56 (≠ E71), G77 (≠ N92), Y78 (≠ F93), R79 (≠ K94), V82 (≠ R97), R85 (≠ K100), G119 (≠ A133), H120 (≠ L134), D121 (= D135), Y124 (≠ V138), D150 (= D163), L211 (≠ I223), Y218 (= Y229), I234 (≠ T245)
- binding (s)-ibuprofenoyl-coenzyme a: I15 (≠ M17), G16 (≠ V18), P17 (≠ M19), R37 (vs. gap), L55 (≠ V70), K56 (≠ E71), G77 (≠ N92), Y78 (≠ F93), R79 (≠ K94), V82 (≠ R97), R85 (≠ K100), G119 (≠ A133), H120 (≠ L134), Y124 (≠ V138), D150 (= D163)
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)
32% identity, 91% coverage: 5:363/396 of query aligns to 3:344/355 of 2yimA
- active site: G16 (≠ V18), D122 (= D135), D151 (= D163), G214 (≠ A225), G215 (≠ W226)
- binding 2-methylacetoacetyl coa: I15 (≠ M17), R37 (= R41), A54 (≠ V68), L56 (≠ V70), K57 (≠ E71), G78 (≠ N92), Y79 (≠ F93), R80 (≠ K94), V83 (≠ R97), R86 (≠ K100), L87 (= L101), A119 (≠ L132), G120 (≠ A133), H121 (≠ L134), Y125 (≠ V138), D151 (= D163)
Q9UHK6 Alpha-methylacyl-CoA racemase; 2-methylacyl-CoA racemase; EC 5.1.99.4 from Homo sapiens (Human) (see 5 papers)
27% identity, 98% coverage: 4:393/396 of query aligns to 1:376/382 of Q9UHK6
- V9 (= V12) to M: in dbSNP:rs3195676
- S52 (≠ C65) to P: in AMACRD and CBAS4; inactive enzyme; dbSNP:rs121917814
- L107 (≠ H120) to P: in CBAS4; inactive enzyme; dbSNP:rs121917816
- G175 (= G185) to D: in dbSNP:rs10941112
- L201 (≠ V211) to S: in dbSNP:rs2287939
- M261 (≠ N271) to T: in dbSNP:rs3195678
- E277 (≠ P291) to K: in dbSNP:rs2278008
Sites not aligning to the query:
- 380:382 Microbody targeting signal
Query Sequence
>PP_3393 FitnessBrowser__Putida:PP_3393
MSRLPLDGIRVVEISHMVMGPTCGMILGDLGAEVIKIEPVRGDGTRRLLGAGAGFFRTFN
RNKQCIAVDVETPEGREAVLQLIDTADVFIENFKPGRMQKLGLGYDALCQRNPGLIYASH
KGFLSGPYDNRLALDEVVQMMAGLAYMTGPVGRPLRAGSSVNDIMGGMFGAIGVLAALNE
RHSTGRGREVQSALYENCVLLAAQHMQQYVVTGEAAAPMPNRISAWAIYDVFTFAGGEQM
FVAATGEGQWHALCRVLGQTALLDDPTLGSNNDRVLQRPRLLAHLAEVFAPLDAGQLALQ
LEANGIPFAPIRRPEELFEDPHLLQSGGMAELQLEDGSHTPMPLLPLSLDGQRLQPRRAI
ARIGEHTRQVMRELGYSDAHIAQLCAAGVLKTDDAA
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