SitesBLAST
Comparing Pf6N2E2_2401 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_2401 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)
2xuaH Crystal structure of the enol-lactonase from burkholderia xenovorans lb400 (see paper)
28% identity, 99% coverage: 1:267/270 of query aligns to 1:260/261 of 2xuaH
4uheA Structural studies of a thermophilic esterase from thermogutta terrifontis (malate bound) (see paper)
29% identity, 96% coverage: 11:270/270 of query aligns to 17:271/272 of 4uheA
- active site: F34 (≠ Y28), L99 (= L93), S100 (= S94), M101 (≠ V95), D124 (= D118), E164 (≠ R159), D221 (= D221), H249 (= H248), L250 (≠ I249)
- binding d-malate: F34 (≠ Y28), S100 (= S94), M101 (≠ V95), Y104 (≠ M98), R138 (≠ Y132), H249 (= H248)
4uhdA Structural studies of a thermophilic esterase from thermogutta terrifontis (acetate bound) (see paper)
29% identity, 96% coverage: 11:270/270 of query aligns to 17:271/274 of 4uhdA
- active site: F34 (≠ Y28), L99 (= L93), S100 (= S94), M101 (≠ V95), D124 (= D118), E164 (≠ R159), D221 (= D221), H249 (= H248), L250 (≠ I249)
- binding acetate ion: G33 (≠ S27), F34 (≠ Y28), S100 (= S94), Y104 (≠ M98), R138 (≠ Y132), H249 (= H248)
- binding magnesium ion: A233 (= A233), I236 (= I236), S239 (≠ C238)
4uhfA Structural studies of a thermophilic esterase from thermogutta terrifontis (l37a mutant with butyrate bound) (see paper)
29% identity, 96% coverage: 11:270/270 of query aligns to 17:271/278 of 4uhfA
- active site: F34 (≠ Y28), L99 (= L93), S100 (= S94), M101 (≠ V95), D124 (= D118), E164 (≠ R159), D221 (= D221), H249 (= H248), L250 (≠ I249)
- binding butanoic acid: G33 (≠ S27), F34 (≠ Y28), S100 (= S94), H249 (= H248)
3ia2A Pseudomonas fluorescens esterase complexed to the r-enantiomer of a sulfonate transition state analog (see paper)
29% identity, 97% coverage: 7:268/270 of query aligns to 7:271/271 of 3ia2A
- active site: W28 (≠ Y28), S94 (= S94), M95 (≠ V95), G119 (≠ D118), D222 (= D221), H251 (= H248)
- binding (2R)-butane-2-sulfonate: W28 (≠ Y28), S94 (= S94), M95 (≠ V95), F198 (= F196), I224 (≠ P223), H251 (= H248)
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, 97% coverage: 7:268/270 of query aligns to 8:272/272 of P22862
- W29 (≠ Y28) binding
- L30 (= L29) 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 (≠ H56) mutation to H: 50-fold increase in catalytic efficiency with acetic acid as substrate; when associated with P-30.
- Y70 (≠ L69) mutation to M: Does not affect esterase and perhydrolase activities.
- M96 (≠ V95) binding ; mutation to T: 4-fold decrease in esterase activity. Loss of perhydrolase activity.
- D100 (≠ W99) mutation to E: Small decrease in esterase and perhydrolase activities.
- T123 (≠ V121) mutation to P: Does not affect esterase and perhydrolase activities.
- F228 (vs. gap) 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
8pi1B Bicyclic incypro pseudomonas fluorescens esterase (see paper)
30% identity, 97% coverage: 7:268/270 of query aligns to 7:271/276 of 8pi1B
Sites not aligning to the query:
8agnAAA Alpha/beta epoxide hydrolase
26% identity, 87% coverage: 34:268/270 of query aligns to 37:287/287 of 8agnAAA
8agmAAA Alpha/beta epoxide hydrolase
26% identity, 87% coverage: 34:268/270 of query aligns to 37:287/287 of 8agmAAA
8agsAAA Alpha/beta epoxide hydrolase
26% identity, 87% coverage: 34:268/270 of query aligns to 39:289/298 of 8agsAAA
8agpAAA Alpha/beta epoxide hydrolase
26% identity, 87% coverage: 34:268/270 of query aligns to 38:288/297 of 8agpAAA
- binding (1~{S},2~{S},4~{R})-2-chloranyl-1-methyl-4-prop-1-en-2-yl-cyclohexan-1-ol: D99 (≠ S94), W100 (≠ V95), I103 (≠ M98), Y130 (= Y120), Y146 (≠ F136), Y146 (≠ F136), M171 (≠ I152), L211 (≠ I188), H268 (= H248), W269 (≠ I249)
Sites not aligning to the query:
5ng7B Novel epoxide hydrolases belonging to the alpha/beta hydrolases superfamily in metagenomes from hot environments (see paper)
26% identity, 87% coverage: 34:268/270 of query aligns to 39:289/290 of 5ng7B
3hi4A Switching catalysis from hydrolysis to perhydrolysis in p. Fluorescens esterase (see paper)
29% identity, 97% coverage: 7:268/270 of query aligns to 7:271/271 of 3hi4A
3heaA The l29p/l124i mutation of pseudomonas fluorescens esterase (see paper)
29% identity, 97% coverage: 7:268/270 of query aligns to 7:271/271 of 3heaA
- active site: W28 (≠ Y28), S94 (= S94), M95 (≠ V95), L118 (≠ M117), G119 (≠ D118), D222 (= D221), H251 (= H248)
- binding ethyl acetate: G27 (≠ S27), W28 (≠ Y28), S94 (= S94), M95 (≠ V95), H251 (= H248)
4ccwA Crystal structure of naproxen esterase (carboxylesterase np) from bacillus subtilis (see paper)
24% identity, 92% coverage: 20:267/270 of query aligns to 49:285/285 of 4ccwA
- active site: A56 (≠ S27), L121 (= L93), S122 (= S94), L123 (≠ V95), E237 (≠ D200), H266 (= H248), V267 (≠ I249)
- binding (2-hydroxyethoxy)acetic acid: A56 (≠ S27), L57 (= L29), F158 (≠ Q130), A162 (≠ S134), F174 (≠ P148)
2d0dA Crystal structure of a meta-cleavage product hydrolase (cumd) a129v mutant (see paper)
27% identity, 94% coverage: 13:267/270 of query aligns to 17:269/271 of 2d0dA
- active site: S32 (= S27), G33 (≠ Y28), G35 (vs. gap), N100 (≠ L93), S101 (= S94), F102 (≠ V95), G125 (≠ D118), V140 (≠ I145), R172 (= R183), F185 (= F196), D222 (= D221), H250 (= H248), W251 (≠ I249)
- binding chloride ion: S32 (= S27), S101 (= S94), F102 (≠ V95)
1iunB Meta-cleavage product hydrolase from pseudomonas fluorescens ip01 (cumd) s103a mutant hexagonal (see paper)
27% identity, 96% coverage: 13:270/270 of query aligns to 18:273/276 of 1iunB
- active site: S33 (= S27), G34 (≠ Y28), G36 (vs. gap), N101 (≠ L93), A102 (≠ S94), F103 (≠ V95), G126 (≠ D118), V141 (≠ I145), R173 (= R183), F186 (= F196), D223 (= D221), H251 (= H248), W252 (≠ I249)
- binding acetate ion: H244 (vs. gap), R260 (≠ F257)
1ukaA Crystal structure of a meta-cleavage product hydrolase (cumd) complexed with (s)-2-methylbutyrate (see paper)
27% identity, 94% coverage: 13:267/270 of query aligns to 17:269/271 of 1ukaA
- active site: S32 (= S27), G33 (≠ Y28), G35 (vs. gap), N100 (≠ L93), A101 (≠ S94), F102 (≠ V95), G125 (≠ D118), V140 (≠ I145), R172 (= R183), F185 (= F196), D222 (= D221), H250 (= H248), W251 (≠ I249)
- binding 2-methylbutanoic acid: S32 (= S27), A101 (≠ S94), F102 (≠ V95), W141 (≠ P146), V224 (≠ P223), H250 (= H248)
1uk9A Crystal structure of a meta-cleavage product hydrolase (cumd) complexed with isovalerate (see paper)
27% identity, 94% coverage: 13:267/270 of query aligns to 17:269/271 of 1uk9A
- active site: S32 (= S27), G33 (≠ Y28), G35 (vs. gap), N100 (≠ L93), A101 (≠ S94), F102 (≠ V95), G125 (≠ D118), V140 (≠ I145), R172 (= R183), F185 (= F196), D222 (= D221), H250 (= H248), W251 (≠ I249)
- binding isovaleric acid: S32 (= S27), A101 (≠ S94), F102 (≠ V95), W141 (≠ P146), H250 (= H248)
1uk8A Crystal structure of a meta-cleavage product hydrolase (cumd) complexed with n-valerate (see paper)
27% identity, 94% coverage: 13:267/270 of query aligns to 17:269/271 of 1uk8A
- active site: S32 (= S27), G33 (≠ Y28), G35 (vs. gap), N100 (≠ L93), A101 (≠ S94), F102 (≠ V95), G125 (≠ D118), V140 (≠ I145), R172 (= R183), F185 (= F196), D222 (= D221), H250 (= H248), W251 (≠ I249)
- binding pentanoic acid: S32 (= S27), A101 (≠ S94), F102 (≠ V95), L137 (≠ S142), W141 (≠ P146), L231 (≠ R230), G234 (≠ A233), E235 (= E234), H250 (= H248)
Query Sequence
>Pf6N2E2_2401 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_2401
MPIAMIDGQPLYYLDQGQGPVVLLGGSYLWDHAMWAPQIEVLSRHYRVIAPDLWGHGQSG
QMPEGMSSLNDLARQMMELLDYLSIDCFHLVGLSVGGMWGTRLALAAPTRIQSLVLMDTY
VGVEPEQTRQYYFSLFDKIEASGSIPEPLLDIIVPIFFRPGIDPQSALYQQFRATLAALP
SDRLRASIVPLGRIIFGRDDILPRLHALDAKGTVVMCGDQDKPRPPSESREMAELIGCPH
VVIPDAGHISNLENPEFVTGALLKFLTRKH
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