SitesBLAST
Comparing GFF4008 FitnessBrowser__WCS417:GFF4008 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)
6eb3B Structural and enzymatic characterization of an esterase from a metagenomic library
32% identity, 96% coverage: 1:257/267 of query aligns to 1:263/268 of 6eb3B
6eb3A Structural and enzymatic characterization of an esterase from a metagenomic library
32% identity, 96% coverage: 1:257/267 of query aligns to 1:260/265 of 6eb3A
6eb3C Structural and enzymatic characterization of an esterase from a metagenomic library
31% identity, 96% coverage: 1:257/267 of query aligns to 1:257/262 of 6eb3C
2xuaH Crystal structure of the enol-lactonase from burkholderia xenovorans lb400 (see paper)
29% identity, 96% coverage: 1:257/267 of query aligns to 1:259/261 of 2xuaH
4lyeA Crystal structure of the s105a mutant of a c-c hydrolase, dxnb2 from sphingomonas wittichii rw1, in complex with substrate hopda (see paper)
28% identity, 96% coverage: 3:257/267 of query aligns to 9:273/276 of 4lyeA
- active site: G34 (≠ L28), G37 (≠ S31), N104 (≠ L92), A105 (≠ S93), M106 (= M94), M128 (≠ V116), R180 (= R166), D227 (= D212), H255 (= H239), W256 (≠ A240)
- binding (3e)-2,6-dioxo-6-phenylhex-3-enoate: G33 (= G27), G34 (≠ L28), G35 (= G29), N104 (≠ L92), A105 (≠ S93), L146 (= L139), L166 (= L152), R180 (= R166), M229 (≠ Y213), H255 (= H239), W256 (≠ A240)
4lxiA Crystal structure of the s105a mutant of a carbon-carbon bond hydrolase, dxnb2 from sphingomonas wittichii rw1, in complex with 5, 8-dif hopda (see paper)
28% identity, 96% coverage: 3:257/267 of query aligns to 9:273/276 of 4lxiA
- active site: G34 (≠ L28), G37 (≠ S31), N104 (≠ L92), A105 (≠ S93), M106 (= M94), M128 (≠ V116), R180 (= R166), D227 (= D212), H255 (= H239), W256 (≠ A240)
- binding (3E,5R)-5-fluoro-6-(2-fluorophenyl)-2,6-dioxohex-3-enoic acid: G33 (= G27), G34 (≠ L28), G35 (= G29), A38 (≠ S32), N43 (≠ D34), N104 (≠ L92), A105 (≠ S93), M106 (= M94), V149 (= V142), M150 (≠ L143), L166 (= L152), R180 (= R166), M229 (≠ Y213), W256 (≠ A240)
4lxhA Crystal structure of the s105a mutant of a carbon-carbon bond hydrolase, dxnb2 from sphingomonas wittichii rw1, in complex with 3- cl hopda (see paper)
28% identity, 96% coverage: 3:257/267 of query aligns to 9:273/276 of 4lxhA
- active site: G34 (≠ L28), G37 (≠ S31), N104 (≠ L92), A105 (≠ S93), M106 (= M94), M128 (≠ V116), R180 (= R166), D227 (= D212), H255 (= H239), W256 (≠ A240)
- binding (2Z,4E)-3-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid: G33 (= G27), G34 (≠ L28), G35 (= G29), N104 (≠ L92), A105 (≠ S93), M106 (= M94), L166 (= L152), W256 (≠ A240)
3heaA The l29p/l124i mutation of pseudomonas fluorescens esterase (see paper)
29% identity, 94% coverage: 7:258/267 of query aligns to 7:270/271 of 3heaA
- active site: W28 (≠ L28), S94 (= S93), M95 (= M94), L118 (≠ V116), G119 (≠ N117), D222 (= D212), H251 (= H239)
- binding ethyl acetate: G27 (= G27), W28 (≠ L28), S94 (= S93), M95 (= M94), H251 (= H239)
3hi4A Switching catalysis from hydrolysis to perhydrolysis in p. Fluorescens esterase (see paper)
29% identity, 94% coverage: 7:258/267 of query aligns to 7:270/271 of 3hi4A
7p4kA Soluble epoxide hydrolase in complex with fl217 (see paper)
24% identity, 93% coverage: 11:259/267 of query aligns to 22:310/313 of 7p4kA
- binding ~{N}-[[4-(cyclopropylsulfonylamino)-2-(trifluoromethyl)phenyl]methyl]-1-[(3-fluorophenyl)methyl]indole-5-carboxamide: F39 (≠ L28), D107 (≠ S93), W108 (≠ M94), M111 (= M97), P133 (≠ A119), Y149 (= Y130), M185 (≠ L145), Y232 (≠ F185), V264 (≠ T214), M269 (≠ K219), H290 (= H239)
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, 94% coverage: 7:258/267 of query aligns to 8:271/272 of P22862
- W29 (≠ L28) binding
- L30 (≠ G29) 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 (≠ I68) mutation to M: Does not affect esterase and perhydrolase activities.
- M96 (= M94) 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 (≠ P120) mutation to P: Does not affect esterase and perhydrolase activities.
- F228 (≠ A217) 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, 94% coverage: 7:258/267 of query aligns to 7:270/271 of 3ia2A
- active site: W28 (≠ L28), S94 (= S93), M95 (= M94), G119 (≠ N117), D222 (= D212), H251 (= H239)
- binding (2R)-butane-2-sulfonate: W28 (≠ L28), S94 (= S93), M95 (= M94), F198 (vs. gap), I224 (≠ T214), H251 (= H239)
5h3hB Esterase (eaest) from exiguobacterium antarcticum (see paper)
25% identity, 95% coverage: 7:259/267 of query aligns to 9:268/269 of 5h3hB
8pi1B Bicyclic incypro pseudomonas fluorescens esterase (see paper)
29% identity, 94% coverage: 7:258/267 of query aligns to 7:270/276 of 8pi1B
Sites not aligning to the query:
5akkA Ligand complex structure of soluble epoxide hydrolase (see paper)
24% identity, 93% coverage: 11:259/267 of query aligns to 246:538/541 of 5akkA
- active site: F263 (≠ L28), H330 (≠ L92), D331 (≠ S93), W332 (≠ M94), N355 (= N117), N374 (≠ R125), Y379 (= Y130), Y460 (≠ F185), D490 (= D212), H518 (= H239)
- binding 6-bromo-1,3-dihydro-2H-indol-2-one: M306 (≠ I68), M335 (= M97), Y339 (≠ Q101), P367 (vs. gap), M463 (≠ I188), N466 (vs. gap), N466 (vs. gap), A470 (≠ G192)
5aljA Ligand complex structure of soluble epoxide hydrolase (see paper)
24% identity, 93% coverage: 11:259/267 of query aligns to 236:520/523 of 5aljA
- active site: F253 (≠ L28), H320 (≠ L92), D321 (≠ S93), W322 (≠ M94), N345 (= N117), Y363 (= Y130), Y442 (≠ F185), D472 (= D212), H500 (= H239)
- binding 2-(3-fluoro-4-methyl-anilino)-4-methyl-quinolin-5-ol: F253 (≠ L28), D321 (≠ S93), W322 (≠ M94), F361 (≠ D128), Q364 (≠ W131), Y442 (≠ F185), M445 (≠ I188)
1iunB Meta-cleavage product hydrolase from pseudomonas fluorescens ip01 (cumd) s103a mutant hexagonal (see paper)
26% identity, 96% coverage: 8:262/267 of query aligns to 13:274/276 of 1iunB
- active site: S33 (≠ L28), G34 (= G29), G36 (vs. gap), N101 (≠ L92), A102 (≠ S93), F103 (≠ M94), G126 (≠ N117), V141 (vs. gap), R173 (≠ L143), F186 (vs. gap), D223 (= D212), H251 (= H239), W252 (≠ A240)
- binding acetate ion: H244 (≠ V232), R260 (≠ V248)
1ukaA Crystal structure of a meta-cleavage product hydrolase (cumd) complexed with (s)-2-methylbutyrate (see paper)
26% identity, 94% coverage: 8:258/267 of query aligns to 12:269/271 of 1ukaA
- active site: S32 (≠ L28), G33 (= G29), G35 (vs. gap), N100 (≠ L92), A101 (≠ S93), F102 (≠ M94), G125 (≠ N117), V140 (vs. gap), R172 (≠ L143), F185 (vs. gap), D222 (= D212), H250 (= H239), W251 (≠ A240)
- binding 2-methylbutanoic acid: S32 (≠ L28), A101 (≠ S93), F102 (≠ M94), W141 (vs. gap), V224 (≠ Y213), H250 (= H239)
1uk9A Crystal structure of a meta-cleavage product hydrolase (cumd) complexed with isovalerate (see paper)
26% identity, 94% coverage: 8:258/267 of query aligns to 12:269/271 of 1uk9A
- active site: S32 (≠ L28), G33 (= G29), G35 (vs. gap), N100 (≠ L92), A101 (≠ S93), F102 (≠ M94), G125 (≠ N117), V140 (vs. gap), R172 (≠ L143), F185 (vs. gap), D222 (= D212), H250 (= H239), W251 (≠ A240)
- binding isovaleric acid: S32 (≠ L28), A101 (≠ S93), F102 (≠ M94), W141 (vs. gap), H250 (= H239)
1uk8A Crystal structure of a meta-cleavage product hydrolase (cumd) complexed with n-valerate (see paper)
26% identity, 94% coverage: 8:258/267 of query aligns to 12:269/271 of 1uk8A
- active site: S32 (≠ L28), G33 (= G29), G35 (vs. gap), N100 (≠ L92), A101 (≠ S93), F102 (≠ M94), G125 (≠ N117), V140 (vs. gap), R172 (≠ L143), F185 (vs. gap), D222 (= D212), H250 (= H239), W251 (≠ A240)
- binding pentanoic acid: S32 (≠ L28), A101 (≠ S93), F102 (≠ M94), L137 (vs. gap), W141 (vs. gap), L231 (≠ E220), G234 (≠ V223), E235 (≠ K224), H250 (= H239)
Query Sequence
>GFF4008 FitnessBrowser__WCS417:GFF4008
MAWFDHEGCSLHYEEYGHGTPLILIHGLGSSSQDWELQIPVLARHYRLIVVDVRGHGRSD
KPRERYSIQGFTLDLLALIEHLDLPAAHVVGLSMGGMIAFQLAVDEPAQVKSLCIVNSAP
EVKVRSADDYWQWAKRWSLARVLSLATIGKALGDRLFPKPQQADLRRKMAERWAKNDKRA
YLASFDAIVGWGVQERLSRITCPTLVISADHDYTPVAQKENYVKLLPNARLVVIEDSRHA
TPLDQPEVFNATLLDFLKTVETTTQDH
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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