SitesBLAST
Comparing AO356_25770 FitnessBrowser__pseudo5_N2C3_1:AO356_25770 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)
30% identity, 88% coverage: 19:262/277 of query aligns to 21:259/261 of 2xuaH
4uheA Structural studies of a thermophilic esterase from thermogutta terrifontis (malate bound) (see paper)
31% identity, 94% coverage: 2:262/277 of query aligns to 4:267/272 of 4uheA
- active site: F34 (≠ V30), L99 (≠ F94), S100 (= S95), M101 (= M96), D124 (≠ N119), E164 (≠ R158), D221 (= D216), H249 (= H244), L250 (≠ M245)
- binding d-malate: F34 (≠ V30), S100 (= S95), M101 (= M96), Y104 (≠ L99), R138 (≠ V132), H249 (= H244)
4uhdA Structural studies of a thermophilic esterase from thermogutta terrifontis (acetate bound) (see paper)
31% identity, 94% coverage: 2:262/277 of query aligns to 4:267/274 of 4uhdA
- active site: F34 (≠ V30), L99 (≠ F94), S100 (= S95), M101 (= M96), D124 (≠ N119), E164 (≠ R158), D221 (= D216), H249 (= H244), L250 (≠ M245)
- binding acetate ion: G33 (= G29), F34 (≠ V30), S100 (= S95), Y104 (≠ L99), R138 (≠ V132), H249 (= H244)
- binding magnesium ion: A233 (= A228), I236 (= I231), S239 (≠ A234)
4uhfA Structural studies of a thermophilic esterase from thermogutta terrifontis (l37a mutant with butyrate bound) (see paper)
31% identity, 94% coverage: 2:262/277 of query aligns to 4:267/278 of 4uhfA
- active site: F34 (≠ V30), L99 (≠ F94), S100 (= S95), M101 (= M96), D124 (≠ N119), E164 (≠ R158), D221 (= D216), H249 (= H244), L250 (≠ M245)
- binding butanoic acid: G33 (= G29), F34 (≠ V30), S100 (= S95), H249 (= H244)
6eb3B Structural and enzymatic characterization of an esterase from a metagenomic library
32% identity, 96% coverage: 4:270/277 of query aligns to 2:267/268 of 6eb3B
6eb3C Structural and enzymatic characterization of an esterase from a metagenomic library
31% identity, 96% coverage: 4:270/277 of query aligns to 2:261/262 of 6eb3C
6eb3A Structural and enzymatic characterization of an esterase from a metagenomic library
31% identity, 96% coverage: 4:270/277 of query aligns to 2:264/265 of 6eb3A
8pi1B Bicyclic incypro pseudomonas fluorescens esterase (see paper)
32% identity, 88% coverage: 19:262/277 of query aligns to 17:269/276 of 8pi1B
Sites not aligning to the query:
3heaA The l29p/l124i mutation of pseudomonas fluorescens esterase (see paper)
32% identity, 88% coverage: 19:262/277 of query aligns to 17:269/271 of 3heaA
- active site: W28 (≠ V30), S94 (= S95), M95 (= M96), L118 (= L118), G119 (≠ N119), D222 (= D216), H251 (= H244)
- binding ethyl acetate: G27 (= G29), W28 (≠ V30), S94 (= S95), M95 (= M96), H251 (= H244)
3hi4A Switching catalysis from hydrolysis to perhydrolysis in p. Fluorescens esterase (see paper)
32% identity, 88% coverage: 19:262/277 of query aligns to 17:269/271 of 3hi4A
3ia2A Pseudomonas fluorescens esterase complexed to the r-enantiomer of a sulfonate transition state analog (see paper)
32% identity, 88% coverage: 19:262/277 of query aligns to 17:269/271 of 3ia2A
- active site: W28 (≠ V30), S94 (= S95), M95 (= M96), G119 (≠ N119), D222 (= D216), H251 (= H244)
- binding (2R)-butane-2-sulfonate: W28 (≠ V30), S94 (= S95), M95 (= M96), F198 (= F190), I224 (≠ G218), H251 (= H244)
P22862 Arylesterase; Aryl-ester hydrolase; Carboxylic acid perhydrolase; PFE; Putative bromoperoxidase; EC 3.1.1.2; EC 1.-.-.- from Pseudomonas fluorescens (see 5 papers)
32% identity, 88% coverage: 19:262/277 of query aligns to 18:270/272 of P22862
- W29 (≠ V30) binding
- L30 (≠ G31) 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 (≠ H58) mutation to H: 50-fold increase in catalytic efficiency with acetic acid as substrate; when associated with P-30.
- Y70 (≠ L70) mutation to M: Does not affect esterase and perhydrolase activities.
- M96 (= M96) binding ; mutation to T: 4-fold decrease in esterase activity. Loss of perhydrolase activity.
- D100 (≠ L99) mutation to E: Small decrease in esterase and perhydrolase activities.
- T123 (vs. gap) mutation to P: Does not affect esterase and perhydrolase activities.
- F228 (≠ P221) 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
5aljA Ligand complex structure of soluble epoxide hydrolase (see paper)
26% identity, 90% coverage: 15:264/277 of query aligns to 238:520/523 of 5aljA
- active site: F253 (≠ V30), H320 (≠ F94), D321 (≠ S95), W322 (≠ M96), N345 (= N119), Y363 (≠ A137), Y442 (= Y187), D472 (= D216), H500 (= H244)
- binding 2-(3-fluoro-4-methyl-anilino)-4-methyl-quinolin-5-ol: F253 (≠ V30), D321 (≠ S95), W322 (≠ M96), F361 (≠ R135), Q364 (= Q138), Y442 (= Y187), M445 (≠ F190)
5fp0A Ligand complex structure of soluble epoxide hydrolase (see paper)
26% identity, 90% coverage: 15:264/277 of query aligns to 251:540/543 of 5fp0A
- active site: F266 (≠ V30), H333 (≠ F94), D334 (≠ S95), W335 (≠ M96), N358 (= N119), N374 (≠ A130), Y379 (≠ R135), Y462 (≠ T192), D492 (= D216), H520 (= H244)
- binding N-cyclopentyl-2-[4-(trifluoromethyl)phenyl]-3H-benzimidazole-4-sulfonamide: F266 (≠ V30), D334 (≠ S95), W335 (≠ M96), M338 (≠ L99), Y379 (≠ R135), Q380 (≠ T136), Y462 (≠ T192), M499 (= M223), H520 (= H244)
5am2A Ligand complex structure of soluble epoxide hydrolase (see paper)
26% identity, 90% coverage: 15:264/277 of query aligns to 246:534/537 of 5am2A
- active site: F261 (≠ V30), H328 (≠ F94), D329 (≠ S95), W330 (≠ M96), N353 (= N119), N372 (≠ R135), Y377 (vs. gap), Y456 (= Y187), D486 (= D216), H514 (= H244)
- binding 7-methyl-2h-isoquinolin-1-one: F261 (≠ V30), W330 (≠ M96), M333 (≠ L99), Y337 (≠ A103), I357 (vs. gap), S368 (≠ G131), Y377 (vs. gap), F381 (≠ E141), L402 (≠ E159), L418 (= L175), M459 (≠ F190), N462 (≠ Q193), D486 (= D216), F487 (≠ P217), V488 (≠ G218), H514 (= H244), W515 (≠ M245)
5alvA Ligand complex structure of soluble epoxide hydrolase (see paper)
26% identity, 90% coverage: 15:264/277 of query aligns to 246:534/537 of 5alvA
- active site: F261 (≠ V30), H328 (≠ F94), D329 (≠ S95), W330 (≠ M96), N353 (= N119), N372 (≠ R135), Y377 (vs. gap), Y456 (= Y187), D486 (= D216), H514 (= H244)
- binding 3-(3-fluorophenyl)-1H-pyrazole: D329 (≠ S95), W330 (≠ M96), M333 (≠ L99), T354 (≠ S120), Y377 (vs. gap), Q378 (= Q138), Y456 (= Y187)
1iunB Meta-cleavage product hydrolase from pseudomonas fluorescens ip01 (cumd) s103a mutant hexagonal (see paper)
26% identity, 92% coverage: 13:266/277 of query aligns to 16:273/276 of 1iunB
- active site: S33 (≠ V30), G34 (= G31), G36 (≠ N33), N101 (≠ F94), A102 (≠ S95), F103 (≠ M96), G126 (≠ N119), V141 (≠ A139), R173 (= R172), F186 (≠ L175), D223 (= D216), H251 (= H244), W252 (≠ M245)
- binding acetate ion: H244 (≠ A237), R260 (≠ L253)
2d0dA Crystal structure of a meta-cleavage product hydrolase (cumd) a129v mutant (see paper)
26% identity, 91% coverage: 13:265/277 of query aligns to 15:271/271 of 2d0dA
- active site: S32 (≠ V30), G33 (= G31), G35 (≠ N33), N100 (≠ F94), S101 (= S95), F102 (≠ M96), G125 (≠ N119), V140 (≠ A139), R172 (= R172), F185 (≠ L175), D222 (= D216), H250 (= H244), W251 (≠ M245)
- binding chloride ion: S32 (≠ V30), S101 (= S95), F102 (≠ M96)
1ukaA Crystal structure of a meta-cleavage product hydrolase (cumd) complexed with (s)-2-methylbutyrate (see paper)
26% identity, 91% coverage: 13:265/277 of query aligns to 15:271/271 of 1ukaA
- active site: S32 (≠ V30), G33 (= G31), G35 (≠ N33), N100 (≠ F94), A101 (≠ S95), F102 (≠ M96), G125 (≠ N119), V140 (≠ A139), R172 (= R172), F185 (≠ L175), D222 (= D216), H250 (= H244), W251 (≠ M245)
- binding 2-methylbutanoic acid: S32 (≠ V30), A101 (≠ S95), F102 (≠ M96), W141 (≠ A140), V224 (≠ G218), H250 (= H244)
1uk9A Crystal structure of a meta-cleavage product hydrolase (cumd) complexed with isovalerate (see paper)
26% identity, 91% coverage: 13:265/277 of query aligns to 15:271/271 of 1uk9A
- active site: S32 (≠ V30), G33 (= G31), G35 (≠ N33), N100 (≠ F94), A101 (≠ S95), F102 (≠ M96), G125 (≠ N119), V140 (≠ A139), R172 (= R172), F185 (≠ L175), D222 (= D216), H250 (= H244), W251 (≠ M245)
- binding isovaleric acid: S32 (≠ V30), A101 (≠ S95), F102 (≠ M96), W141 (≠ A140), H250 (= H244)
Query Sequence
>AO356_25770 FitnessBrowser__pseudo5_N2C3_1:AO356_25770
MIRLTAELTPAGTSYLATGQGQPVVLIHGVGLNKEMWGGQVVGLATQYRVIAYDMLGHGA
SPRPQSGTALLGYADQLLELLDHLQLPQATVIGFSMGGLVARAFALHYPQRLQGLVVLNS
VFNRSAEQRAGVIARTAQAAEHGPDANAEAALSRWFSREYQAANPAQIAALRQTLAQNDP
QGYLTTYELFATQDMYRADDLGNIQVPTLIATGELDPGSTPEMARQLAERIPGASVAVLA
EQRHMMPVESPRLVNQLLLEFLDTANARQNQIKGIVA
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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