SitesBLAST
Comparing Pf6N2E2_667 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_667 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)
2og1A Crystal structure of bphd, a c-c hydrolase from burkholderia xenovorans lb400 (see paper)
30% identity, 67% coverage: 123:369/370 of query aligns to 24:284/285 of 2og1A
- active site: G41 (≠ F141), G42 (= G142), G44 (≠ D144), N110 (≠ H205), S111 (= S206), M112 (= M207), L155 (≠ A250), R189 (= R282), A207 (≠ D300), D236 (= D326), H264 (= H349), W265 (≠ M350)
- binding glycerol: Y52 (≠ H152), E184 (≠ M277)
P47229 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase; HOPDA hydrolase; 2,6-dioxo-6-phenylhexa-3-enoate hydrolase; EC 3.7.1.8 from Paraburkholderia xenovorans (strain LB400) (see paper)
30% identity, 67% coverage: 123:369/370 of query aligns to 25:285/286 of P47229
- S112 (= S206) mutation to A: Catalyzes the tautomerisation of HOPDA. Extremely low hydrolase activity; when associated with A-265.
- H265 (= H349) mutation to A: Unable to catalyze the tautomerisation of HOPDA. Extremely low hydrolase activity; when associated with A-112.
2rhwA Crystal structure of the s112a mutant of a c-c hydrolase, bphd from burkholderia xenovorans lb400, in complex with 3,10-di-fluoro hopda (see paper)
30% identity, 67% coverage: 123:369/370 of query aligns to 22:282/283 of 2rhwA
- active site: G39 (≠ F141), G40 (= G142), G42 (≠ D144), N108 (≠ H205), A109 (≠ S206), M110 (= M207), R187 (= R282), D234 (= D326), H262 (= H349), W263 (≠ M350)
- binding 3-fluoro-6-(4-fluorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid: G38 (= G140), G39 (≠ F141), G40 (= G142), A109 (≠ S206), M110 (= M207), G135 (≠ A232), I150 (≠ S241), F172 (= F263), L210 (≠ T305), F236 (≠ I328), V237 (≠ I329), H262 (= H349)
2rhtA Crystal structure of the s112a mutant of a c-c hydrolase, bphd from burkholderia xenovorans lb400, in complex with 3-cl hopda (see paper)
30% identity, 67% coverage: 123:369/370 of query aligns to 22:282/283 of 2rhtA
- active site: G39 (≠ F141), G40 (= G142), G42 (≠ D144), N108 (≠ H205), A109 (≠ S206), M110 (= M207), R187 (= R282), D234 (= D326), H262 (= H349), W263 (≠ M350)
- binding (2Z,4E)-3-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid: G38 (= G140), G39 (≠ F141), G40 (= G142), A109 (≠ S206), M110 (= M207), I150 (≠ S241), L153 (≠ Q244), F172 (= F263), R187 (= R282), F236 (≠ I328), V237 (≠ I329), H262 (= H349)
2puhA Crystal structure of the s112a mutant of a c-c hydrolase, bphd from burkholderia xenovorans lb400, in complex with its substrate hopda (see paper)
30% identity, 67% coverage: 123:369/370 of query aligns to 22:282/283 of 2puhA
- active site: G39 (≠ F141), G40 (= G142), G42 (≠ D144), N108 (≠ H205), A109 (≠ S206), M110 (= M207), R187 (= R282), D234 (= D326), H262 (= H349), W263 (≠ M350)
- binding (3e)-2,6-dioxo-6-phenylhex-3-enoate: G38 (= G140), G39 (≠ F141), G40 (= G142), N108 (≠ H205), A109 (≠ S206), M110 (= M207), I150 (≠ S241), F172 (= F263), R187 (= R282), L210 (≠ T305), W213 (≠ R308), V237 (≠ I329), H262 (= H349), W263 (≠ M350)
P77044 2-hydroxy-6-oxononadienedioate/2-hydroxy-6-oxononatrienedioate hydrolase; 2-hydroxy-6-ketonona-2,4-diene-1,9-dioic acid 5,6-hydrolase; 2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioic acid 5,6-hydrolase; 2-hydroxy-6-oxonona-2,4-diene-1,9-dioic acid 5,6-hydrolase; EC 3.7.1.14 from Escherichia coli (strain K12) (see 3 papers)
28% identity, 69% coverage: 115:369/370 of query aligns to 16:287/288 of P77044
- S44 (≠ F141) mutation to A: 2-fold decrease in catalytic efficiency and more than 5-fold increase in affinity for the natural substrate.
- N113 (≠ H205) mutation to A: 200-fold decrease in catalytic activity and almost 2-fold increase in affinity.; mutation to H: 350-fold decrease in catalytic activity and almost 2-fold increase in affinity.
- S114 (= S206) Transition state stabilizer; mutation to A: Weakly active. 3-fold decrease in affinity. Fast ketonisation and slow C-C cleavage.; mutation to G: Weakly active. 3-fold decrease in affinity. Fast ketonisation and slow C-C cleavage.
- H118 (≠ A210) mutation to A: More than 2-fold decrease in catalytic efficiency and 3-fold increase affinity.
- F177 (≠ E267) mutation to D: 100-fold decrease in catalytic activity.; mutation to G: 4-fold and 8-fold decrease in catalytic activity and affinity, respectively.
- R192 (= R282) Catalytic role in ketonization of the dienol substrate (substrate destabilization); mutation to K: 40-fold and 5-fold decrease in catalytic activity and affinity, respectively.; mutation to Q: 280-fold and 10-fold decrease in catalytic activity and affinity, respectively.
- C265 (≠ Q347) mutation to A: 2-fold decrease in catalytic activity and almost 2-fold increase in affinity.
- H267 (= H349) active site, Proton acceptor; mutation to A: Weakly active, 1000-fold decrease in catalytic efficiency. Very slow ketonisation and C-C cleavage.
- W268 (≠ M350) mutation to G: 10-fold and 20-fold decrease in catalytic activity and affinity, respectively.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2pujA Crystal structure of the s112a/h265a double mutant of a c-c hydrolase, bphd from burkholderia xenovorans lb400, in complex with its substrate hopda (see paper)
29% identity, 67% coverage: 123:369/370 of query aligns to 22:282/283 of 2pujA
- active site: G39 (≠ F141), G40 (= G142), G42 (≠ D144), N108 (≠ H205), A109 (≠ S206), M110 (= M207), R187 (= R282), D234 (= D326), A262 (≠ H349), W263 (≠ M350)
- binding (2e,4e)-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid: G38 (= G140), G39 (≠ F141), G40 (= G142), A109 (≠ S206), M110 (= M207), G135 (≠ A232), I150 (≠ V247), L153 (≠ A250), F172 (= F263), R187 (= R282), V237 (≠ I329)
6i8wB Crystal structure of a membrane phospholipase a, a novel bacterial virulence factor (see paper)
29% identity, 69% coverage: 114:367/370 of query aligns to 43:304/310 of 6i8wB
Sites not aligning to the query:
Q8R2Y0 Monoacylglycerol lipase ABHD6; 2-arachidonoylglycerol hydrolase; Abhydrolase domain-containing protein 6; EC 3.1.1.23 from Mus musculus (Mouse) (see paper)
28% identity, 67% coverage: 119:367/370 of query aligns to 57:324/336 of Q8R2Y0
- S148 (= S206) mutation to A: Loss of the lipid hydrolase activity.
3heaA The l29p/l124i mutation of pseudomonas fluorescens esterase (see paper)
29% identity, 69% coverage: 116:369/370 of query aligns to 4:271/271 of 3heaA
- active site: W28 (≠ F141), S94 (= S206), M95 (= M207), L118 (≠ I229), G119 (= G230), D222 (= D326), H251 (= H349)
- binding ethyl acetate: G27 (= G140), W28 (≠ F141), S94 (= S206), M95 (= M207), H251 (= H349)
3hi4A Switching catalysis from hydrolysis to perhydrolysis in p. Fluorescens esterase (see paper)
29% identity, 69% coverage: 116:369/370 of query aligns to 4:271/271 of 3hi4A
P22862 Arylesterase; Aryl-ester hydrolase; Carboxylic acid perhydrolase; PFE; Putative bromoperoxidase; EC 3.1.1.2; EC 1.-.-.- from Pseudomonas fluorescens (see 5 papers)
29% identity, 69% coverage: 116:369/370 of query aligns to 5:272/272 of P22862
- W29 (≠ F141) binding
- L30 (≠ G142) mutation to I: 125-fold increase in catalytic efficiency for perhydrolase activity with acetic acid as substrate. 2-fold decrease in catalytic efficiency for perhydrolase activity with ethyl acetate as substrate. 1.5-fold increase in catalytic efficiency for hydrolase activity with ethyl acetate as substrate. 2.4-fold increase in kcat for hydrolysis of peracetic acid.; mutation to P: Shows faster acetyl-enzyme formation. Tenfold more efficient at hydrolysis than perhydrolysis with methyl acetate as substrate. 3-fold decrease in catalytic efficiency for hydrolase activity with methyl acetate as substrate. 15-fold decrease in catalytic efficiency for perhydrolase activity with methyl acetate as substrate (PubMed:22618813). 100-fold decrease in hydrolase activity with 4-nitrophenyl acetate as substrate. 28-fold increase in perhydrolase activity with acetate as substrate (PubMed:15803517). 100-fold increase in catalytic efficiency with acetic acid as substrate. 50-fold increase in catalytic efficiency with acetic acid as substrate; when associated with H-58 (PubMed:20112920).
- F58 (≠ H169) mutation to H: 50-fold increase in catalytic efficiency with acetic acid as substrate; when associated with P-30.
- Y70 (≠ L181) mutation to M: Does not affect esterase and perhydrolase activities.
- M96 (= M207) binding ; mutation to T: 4-fold decrease in esterase activity. Loss of perhydrolase activity.
- D100 (vs. gap) mutation to E: Small decrease in esterase and perhydrolase activities.
- T123 (≠ G233) mutation to P: Does not affect esterase and perhydrolase activities.
- F228 (≠ V331) mutation to I: 3-fold increase in esterase activity. No change in perhydrolase activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
3ia2A Pseudomonas fluorescens esterase complexed to the r-enantiomer of a sulfonate transition state analog (see paper)
29% identity, 69% coverage: 116:369/370 of query aligns to 4:271/271 of 3ia2A
- active site: W28 (≠ F141), S94 (= S206), M95 (= M207), G119 (= G230), D222 (= D326), H251 (= H349)
- binding (2R)-butane-2-sulfonate: W28 (≠ F141), S94 (= S206), M95 (= M207), F198 (= F298), I224 (= I328), H251 (= H349)
1iunB Meta-cleavage product hydrolase from pseudomonas fluorescens ip01 (cumd) s103a mutant hexagonal (see paper)
27% identity, 68% coverage: 120:369/370 of query aligns to 13:271/276 of 1iunB
- active site: S33 (≠ F141), G34 (= G142), G36 (≠ D144), N101 (≠ H205), A102 (≠ S206), F103 (≠ M207), G126 (= G230), V141 (≠ L243), R173 (= R282), F186 (≠ S294), D223 (= D326), H251 (= H349), W252 (≠ M350)
- binding acetate ion: H244 (≠ E342), R260 (≠ Q358)
1ukaA Crystal structure of a meta-cleavage product hydrolase (cumd) complexed with (s)-2-methylbutyrate (see paper)
27% identity, 68% coverage: 120:369/370 of query aligns to 12:270/271 of 1ukaA
- active site: S32 (≠ F141), G33 (= G142), G35 (≠ D144), N100 (≠ H205), A101 (≠ S206), F102 (≠ M207), G125 (= G230), V140 (≠ L243), R172 (= R282), F185 (≠ S294), D222 (= D326), H250 (= H349), W251 (≠ M350)
- binding 2-methylbutanoic acid: S32 (≠ F141), A101 (≠ S206), F102 (≠ M207), W141 (≠ Q244), V224 (≠ I328), H250 (= H349)
1uk9A Crystal structure of a meta-cleavage product hydrolase (cumd) complexed with isovalerate (see paper)
27% identity, 68% coverage: 120:369/370 of query aligns to 12:270/271 of 1uk9A
- active site: S32 (≠ F141), G33 (= G142), G35 (≠ D144), N100 (≠ H205), A101 (≠ S206), F102 (≠ M207), G125 (= G230), V140 (≠ L243), R172 (= R282), F185 (≠ S294), D222 (= D326), H250 (= H349), W251 (≠ M350)
- binding isovaleric acid: S32 (≠ F141), A101 (≠ S206), F102 (≠ M207), W141 (≠ Q244), H250 (= H349)
1uk8A Crystal structure of a meta-cleavage product hydrolase (cumd) complexed with n-valerate (see paper)
27% identity, 68% coverage: 120:369/370 of query aligns to 12:270/271 of 1uk8A
- active site: S32 (≠ F141), G33 (= G142), G35 (≠ D144), N100 (≠ H205), A101 (≠ S206), F102 (≠ M207), G125 (= G230), V140 (≠ L243), R172 (= R282), F185 (≠ S294), D222 (= D326), H250 (= H349), W251 (≠ M350)
- binding pentanoic acid: S32 (≠ F141), A101 (≠ S206), F102 (≠ M207), L137 (vs. gap), W141 (≠ Q244), L231 (≠ E335), G234 (vs. gap), E235 (vs. gap), H250 (= H349)
1uk7A Crystal structure of a meta-cleavage product hydrolase (cumd) complexed with n-butyrate (see paper)
27% identity, 68% coverage: 120:369/370 of query aligns to 12:270/271 of 1uk7A
- active site: S32 (≠ F141), G33 (= G142), G35 (≠ D144), N100 (≠ H205), A101 (≠ S206), F102 (≠ M207), G125 (= G230), V140 (≠ L243), R172 (= R282), F185 (≠ S294), D222 (= D326), H250 (= H349), W251 (≠ M350)
- binding butanoic acid: S32 (≠ F141), A101 (≠ S206), F102 (≠ M207), L137 (vs. gap), H250 (= H349)
1iupA Meta-cleavage product hydrolase from pseudomonas fluorescens ip01 (cumd) s103a mutant complexed with isobutyrates (see paper)
27% identity, 68% coverage: 120:369/370 of query aligns to 12:270/271 of 1iupA
- active site: S32 (≠ F141), G33 (= G142), G35 (≠ D144), N100 (≠ H205), A101 (≠ S206), F102 (≠ M207), G125 (= G230), V140 (≠ L243), R172 (= R282), F185 (≠ S294), D222 (= D326), H250 (= H349), W251 (≠ M350)
- binding 2-methyl-propionic acid: S32 (≠ F141), A40 (vs. gap), N41 (= N147), Y74 (vs. gap), W79 (≠ L184), A101 (≠ S206), F102 (≠ M207), L137 (vs. gap), W141 (≠ Q244), R172 (= R282), M188 (≠ L297), W196 (vs. gap), V224 (≠ I328), H250 (= H349), W251 (≠ M350)
8pi1B Bicyclic incypro pseudomonas fluorescens esterase (see paper)
29% identity, 69% coverage: 116:369/370 of query aligns to 4:271/276 of 8pi1B
Sites not aligning to the query:
Query Sequence
>Pf6N2E2_667 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_667
MSQIHTLTMPKWGLSMTEGRVDAWLKEEGQVITKGDEVMDVETDKISSSVEAPFSGVLRR
QIARQDETLAVGALLGIVVDGEASDAEIDAVIEQFQSTFVPGDTADEDSGPKPQKVELDG
RLIRYFERGEGGTPLLLVHGFGGDLNNWLFNHEALAAGRRVIALDLPGHGESGKVLQRGD
LDELSGVVLALLDHLDINAVHLVGHSMGGAVSLNTARLAPRRVRSLTLIGSAGLGSEING
SYLQGFVEAANRNALKPQLVQLFSNAELVNRQMLDDMLKYKRLEGVDAALQQLSSRLFAD
GRQQTDLREVVQAGQVPTLVVWGSDDAIIPVTHSEGLSAQVEVLPGQGHMVQMEAAEQVN
SLILAFIQQH
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