SitesBLAST
Comparing GFF2744 FitnessBrowser__Phaeo:GFF2744 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)
9br7C Succinate--hydroxymethylglutarate CoA-transferase (see paper)
39% identity, 97% coverage: 1:365/375 of query aligns to 3:369/403 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)
39% identity, 97% coverage: 1:365/375 of query aligns to 38:404/438 of Q9HAC7
- D205 (= D171) mutation to A: Loss of CoA transferase activity toward glutaryl-CoA and 3-hydroxy-3-methylglutarate substrates.
- R329 (≠ A295) to W: in GA3; severely decreased protein stability and processing; dbSNP:rs137852860
5yx6A Crystal structure of rv3272 from m. Tuberculosis orthorhombic form (see paper)
31% identity, 92% coverage: 3:348/375 of query aligns to 5:335/360 of 5yx6A
1q6yA Hypothetical protein yfdw from e. Coli bound to coenzyme a (see paper)
36% identity, 58% coverage: 2:218/375 of query aligns to 3:221/417 of 1q6yA
- active site: Q17 (≠ L16), E140 (≠ D142), D169 (= D171)
- binding coenzyme a: V16 (≠ I15), Q17 (≠ L16), S18 (≠ A17), R38 (≠ S37), L72 (≠ A74), N73 (≠ D75), T74 (≠ F76), K75 (≠ R77), N96 (= N98), F97 (= F99), H98 (≠ K100), M105 (≠ Y107), I124 (≠ V126), K137 (≠ A139), A138 (≠ G140), Y139 (= Y141), D169 (= D171), M200 (≠ L202)
Sites not aligning to the query:
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)
36% identity, 58% coverage: 2:218/375 of query aligns to 3:221/416 of P69902
1pt5A Crystal structure of gene yfdw of e. Coli (see paper)
36% identity, 58% coverage: 2:218/375 of query aligns to 2:220/415 of 1pt5A
- active site: Q16 (≠ L16), E139 (≠ D142), D168 (= D171)
- binding acetyl coenzyme *a: V15 (≠ I15), S17 (≠ A17), R37 (≠ S37), L71 (≠ A74), N72 (≠ D75), T73 (≠ F76), K74 (≠ R77), N95 (= N98), F96 (= F99), H97 (≠ K100), K124 (≠ T127), K136 (≠ A139), A137 (≠ G140), Y138 (= Y141), E139 (≠ D142), D168 (= D171), M199 (≠ L202)
Sites not aligning to the query:
O06543 Alpha-methylacyl-CoA racemase; AMACR; MtMCR; EC 5.1.99.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
32% identity, 89% coverage: 3:334/375 of query aligns to 4:317/360 of O06543
- R38 (≠ S37) binding substrate
- R52 (= R67) mutation to A: 15.7% of wild-type activity.
- I56 (≠ C71) mutation to P: 28.8% of wild-type activity.
- ADLK 59:62 (≠ ADFR 74:77) binding substrate
- E82 (= E97) mutation to A: 12.5% of wild-type activity.
- GYR 83:85 (≠ NFK 98:100) binding substrate
- R91 (≠ K106) binding substrate; mutation to A: 19.9% of wild-type activity.
- M111 (≠ V126) mutation to P: 5.2% of wild-type activity.
- GHDINY 125:130 (≠ GYDFLL 140:145) binding substrate
- H126 (≠ Y141) mutation to A: 4.5% of wild-type activity.
- D156 (= D171) mutation to A: 17.6 of wild-type activity.
- D190 (= D204) mutation to A: 3.3% of wild-type activity.
- E241 (≠ D254) mutation to A: 2.1% of wild-type activity.
- C297 (≠ P314) mutation to A: 6.2% of wild-type activity.
- H312 (≠ Q329) mutation to A: 10.1% of wild-type activity.
1p5rA Formyl-coa transferase in complex with coenzyme a (see paper)
26% identity, 97% coverage: 3:365/375 of query aligns to 3:400/427 of 1p5rA
- active site: Q16 (≠ L16), E139 (≠ D142), D168 (= D171), G259 (≠ N233), G260 (≠ I234)
- binding coenzyme a: H14 (≠ R14), V15 (≠ I15), Q16 (≠ L16), A17 (= A17), R37 (≠ S37), M73 (≠ F76), K74 (≠ R77), N95 (= N98), F96 (= F99), A100 (≠ G103), R103 (≠ K106), K136 (≠ A139), V137 (≠ G140), D168 (= D171), M199 (≠ L202)
O06644 Formyl-CoA:oxalate CoA-transferase; FCOCT; Formyl-coenzyme A transferase; EC 2.8.3.16 from Oxalobacter formigenes (see 4 papers)
26% identity, 97% coverage: 3:365/375 of query aligns to 4:401/428 of O06644
- Q17 (≠ L16) mutation to A: 45-fold decrease of the catalytic effiency.
- R38 (≠ S37) binding CoA
- W48 (= W46) 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 (≠ K106) binding CoA
- D169 (= D171) 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 (≠ P232) mutation to A: 2.5-fold decrease of the catalytic effiency.
- G260 (≠ N233) mutation to A: 25-fold decrease of the catalytic effiency. Reduction of the affinity binding for both formyl-CoA and oxalate.
2vjoA Formyl-coa transferase mutant variant q17a with aspartyl-coa thioester intermediates and oxalate (see paper)
26% identity, 97% coverage: 3:365/375 of query aligns to 3:400/427 of 2vjoA
- active site: A16 (≠ L16), E139 (≠ D142), D168 (= D171), G259 (≠ N233), G260 (≠ I234)
- binding coenzyme a: H14 (≠ R14), A16 (≠ L16), A17 (= A17), R37 (≠ S37), L71 (≠ A74), M73 (≠ F76), N95 (= N98), F96 (= F99), G97 (≠ K100), R103 (≠ K106), M104 (≠ Y107), K136 (≠ A139), V137 (≠ G140), Y138 (= Y141), D168 (= D171), M199 (≠ L202)
- binding oxalate ion: G257 (≠ H231), G259 (≠ N233), Q261 (≠ A235)
2vjkA Formyl-coa transferase with aspartyl-coa thioester intermediate derived from oxalyl-coa (see paper)
26% identity, 97% coverage: 3:365/375 of query aligns to 3:400/427 of 2vjkA
- active site: Q16 (≠ L16), E139 (≠ D142), D168 (= D171), G259 (≠ N233), G260 (≠ I234)
- binding coenzyme a: H14 (≠ R14), Q16 (≠ L16), A17 (= A17), R37 (≠ S37), M73 (≠ F76), K74 (≠ R77), N95 (= N98), F96 (= F99), G97 (≠ K100), R103 (≠ K106), M104 (≠ Y107), K136 (≠ A139), V137 (≠ G140), Y138 (= Y141), D168 (= D171), M199 (≠ L202)
- binding magnesium ion: D293 (≠ A262), D296 (≠ N265)
1t4cA Formyl-coa transferase in complex with oxalyl-coa (see paper)
26% identity, 97% coverage: 3:365/375 of query aligns to 3:400/427 of 1t4cA
- active site: Q16 (≠ L16), E139 (≠ D142), D168 (= D171), G259 (≠ N233), G260 (≠ I234)
- binding coenzyme a: H14 (≠ R14), V15 (≠ I15), Q16 (≠ L16), R37 (≠ S37), M73 (≠ F76), N95 (= N98), F96 (= F99), R103 (≠ K106), M104 (≠ Y107), V137 (≠ G140), Y138 (= Y141), D168 (= D171), M199 (≠ L202)
- binding oxalic acid: G259 (≠ N233), G260 (≠ I234)
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, 89% coverage: 3:334/375 of query aligns to 3:312/355 of 2yimA
- active site: G16 (≠ L16), D122 (= D142), D151 (= D171), G214 (≠ N233), G215 (≠ I234)
- binding 2-methylacetoacetyl coa: I15 (= I15), R37 (≠ S37), A54 (= A74), L56 (≠ F76), K57 (≠ R77), G78 (≠ N98), Y79 (≠ F99), R80 (≠ K100), V83 (≠ G103), R86 (≠ K106), L87 (≠ Y107), A119 (= A139), G120 (= G140), H121 (≠ Y141), Y125 (≠ L145), D151 (= D171)
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, 89% coverage: 3:334/375 of query aligns to 3:311/354 of 2gd6A
- active site: G16 (≠ L16), D121 (= D142), D150 (= D171), G213 (≠ N233), G214 (≠ I234)
- binding acetyl coenzyme *a: I15 (= I15), R37 (≠ S37), A53 (= A74), D54 (= D75), L55 (≠ F76), K56 (≠ R77), G77 (≠ N98), Y78 (≠ F99), R79 (≠ K100), V82 (≠ G103), R85 (≠ K106), G119 (= G140), H120 (≠ Y141), Y124 (≠ L145), D150 (= D171), M182 (≠ L202)
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, 89% coverage: 3:334/375 of query aligns to 3:311/354 of 2gd2A
- active site: G16 (≠ L16), D121 (= D142), D150 (= D171), G213 (≠ N233), G214 (≠ I234)
- binding acetoacetyl-coenzyme a: I15 (= I15), R37 (≠ S37), A53 (= A74), L55 (≠ F76), K56 (≠ R77), G77 (≠ N98), Y78 (≠ F99), R79 (≠ K100), V82 (≠ G103), R85 (≠ K106), L86 (≠ Y107), A118 (= A139), G119 (= G140), H120 (≠ Y141), Y124 (≠ L145), D150 (= D171)
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, 89% coverage: 3:334/375 of query aligns to 3:311/354 of 2gd0A
- active site: G16 (≠ L16), D121 (= D142), D150 (= D171), G213 (≠ N233), G214 (≠ I234)
- binding (s)-2-methylmyristoyl-coenzyme a: D42 (= D54), L55 (≠ F76), K56 (≠ R77), G77 (≠ N98), Y78 (≠ F99), R79 (≠ K100), V82 (≠ G103), R85 (≠ K106), L86 (≠ Y107), G119 (= G140), H120 (≠ Y141), D121 (= D142), Y124 (≠ L145), D150 (= D171)
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, 89% coverage: 3:334/375 of query aligns to 3:311/354 of 2gciA
- active site: G16 (≠ L16), D121 (= D142), D150 (= D171), G213 (≠ N233), G214 (≠ I234)
- binding (r)-2-methylmyristoyl-coenzyme a: R37 (≠ S37), L55 (≠ F76), K56 (≠ R77), G77 (≠ N98), Y78 (≠ F99), R79 (≠ K100), V82 (≠ G103), G119 (= G140), H120 (≠ Y141), D121 (= D142), Y124 (≠ L145), D150 (= D171), Y218 (= Y237), I234 (≠ N253), E235 (≠ D254)
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, 89% coverage: 3:334/375 of query aligns to 3:311/354 of 2gceA
- active site: G16 (≠ L16), D121 (= D142), D150 (= D171), G213 (≠ N233), G214 (≠ I234)
- binding (r)-ibuprofenoyl-coenzyme a: I15 (= I15), R37 (≠ S37), L55 (≠ F76), K56 (≠ R77), G77 (≠ N98), Y78 (≠ F99), R79 (≠ K100), V82 (≠ G103), R85 (≠ K106), G119 (= G140), H120 (≠ Y141), D121 (= D142), Y124 (≠ L145), D150 (= D171), L211 (≠ H231), Y218 (= Y237), I234 (≠ N253)
- binding (s)-ibuprofenoyl-coenzyme a: I15 (= I15), G16 (≠ L16), P17 (≠ A17), R37 (≠ S37), L55 (≠ F76), K56 (≠ R77), G77 (≠ N98), Y78 (≠ F99), R79 (≠ K100), V82 (≠ G103), R85 (≠ K106), G119 (= G140), H120 (≠ Y141), Y124 (≠ L145), D150 (= D171)
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, 87% coverage: 4:329/375 of query aligns to 3:329/399 of Q5U921
- D171 (= D171) mutation D->A,N: Loss of activity.
1t3zA Formyl-coa tranferase mutant asp169 to ser (see paper)
25% identity, 97% coverage: 3:365/375 of query aligns to 3:400/427 of 1t3zA
- active site: Q16 (≠ L16), E139 (≠ D142), S168 (≠ D171), G259 (≠ N233), G260 (≠ I234)
- binding oxidized coenzyme a: H14 (≠ R14), V15 (≠ I15), A17 (= A17), R37 (≠ S37), K74 (≠ R77), N95 (= N98), F96 (= F99), A100 (≠ G103), R103 (≠ K106), M104 (≠ Y107), K136 (≠ A139), V137 (≠ G140), Y138 (= Y141), E139 (≠ D142), M199 (≠ L202)
Query Sequence
>GFF2744 FitnessBrowser__Phaeo:GFF2744
MTPLAGLKVVELARILAGPWIGQSLADLGAEVIKVESPEGDDTRRWGPPFIERDGDKTAA
YYYAANRGKSCVTADFRTKDGKQTVLELIRDADILIENFKVGGLAKYGLDYDSLKAVNPR
LIYCSVTGFGQDGPYAARAGYDFLLQGMSGLMSITGAPEGEPQKVGVAITDIVTGLYGTI
GILAAVEQRHSTGRGQHIDMSLLDCATAVLANQNMNYLATGTSPTRMGNEHPNIAPYQVM
AVRDGHVILAVGNDGQFARLCAVLNMAGLADDPRFASNQLRVANRVELTPMLAAALAQWG
QADLLAALEAATVPAGPINTIGQAFDDPQIKHRQMQIAPEDVPGVRGPWVFSDAELALEK
SAPILPVAQDMSQGD
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