SitesBLAST
Comparing WP_010437977.1 NCBI__GCF_000192475.1:WP_010437977.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
37% identity, 98% coverage: 1:258/262 of query aligns to 1:261/261 of 2xuaH
6eb3C Structural and enzymatic characterization of an esterase from a metagenomic library
30% identity, 98% coverage: 1:256/262 of query aligns to 1:257/262 of 6eb3C
6eb3A Structural and enzymatic characterization of an esterase from a metagenomic library
31% identity, 98% coverage: 1:256/262 of query aligns to 1:260/265 of 6eb3A
6eb3B Structural and enzymatic characterization of an esterase from a metagenomic library
30% identity, 98% coverage: 1:256/262 of query aligns to 1:263/268 of 6eb3B
4uhfA Structural studies of a thermophilic esterase from thermogutta terrifontis (l37a mutant with butyrate bound) (see paper)
28% identity, 91% coverage: 21:259/262 of query aligns to 25:270/278 of 4uhfA
- active site: F34 (≠ L30), L99 (= L94), S100 (= S95), M101 (≠ I96), D124 (≠ N119), E164 (≠ K156), D221 (= D210), H249 (= H238), L250 (= L239)
- binding butanoic acid: G33 (≠ S29), F34 (≠ L30), S100 (= S95), H249 (= H238)
4uheA Structural studies of a thermophilic esterase from thermogutta terrifontis (malate bound) (see paper)
28% identity, 91% coverage: 21:259/262 of query aligns to 25:270/272 of 4uheA
- active site: F34 (≠ L30), L99 (= L94), S100 (= S95), M101 (≠ I96), D124 (≠ N119), E164 (≠ K156), D221 (= D210), H249 (= H238), L250 (= L239)
- binding d-malate: F34 (≠ L30), S100 (= S95), M101 (≠ I96), Y104 (≠ M99), R138 (= R133), H249 (= H238)
4uhdA Structural studies of a thermophilic esterase from thermogutta terrifontis (acetate bound) (see paper)
28% identity, 91% coverage: 21:259/262 of query aligns to 25:270/274 of 4uhdA
- active site: F34 (≠ L30), L99 (= L94), S100 (= S95), M101 (≠ I96), D124 (≠ N119), E164 (≠ K156), D221 (= D210), H249 (= H238), L250 (= L239)
- binding acetate ion: G33 (≠ S29), F34 (≠ L30), S100 (= S95), Y104 (≠ M99), R138 (= R133), H249 (= H238)
- binding magnesium ion: A233 (≠ V222), I236 (= I225), S239 (= S228)
3heaA The l29p/l124i mutation of pseudomonas fluorescens esterase (see paper)
27% identity, 90% coverage: 21:256/262 of query aligns to 19:269/271 of 3heaA
- active site: W28 (≠ L30), S94 (= S95), M95 (≠ I96), L118 (≠ S118), G119 (≠ N119), D222 (= D210), H251 (= H238)
- binding ethyl acetate: G27 (≠ S29), W28 (≠ L30), S94 (= S95), M95 (≠ I96), H251 (= H238)
3hi4A Switching catalysis from hydrolysis to perhydrolysis in p. Fluorescens esterase (see paper)
26% identity, 90% coverage: 21:256/262 of query aligns to 19:269/271 of 3hi4A
3ia2A Pseudomonas fluorescens esterase complexed to the r-enantiomer of a sulfonate transition state analog (see paper)
26% identity, 90% coverage: 21:256/262 of query aligns to 19:269/271 of 3ia2A
- active site: W28 (≠ L30), S94 (= S95), M95 (≠ I96), G119 (≠ N119), D222 (= D210), H251 (= H238)
- binding (2R)-butane-2-sulfonate: W28 (≠ L30), S94 (= S95), M95 (≠ I96), F198 (≠ I186), I224 (≠ S212), H251 (= H238)
P22862 Arylesterase; Aryl-ester hydrolase; Carboxylic acid perhydrolase; PFE; Putative bromoperoxidase; EC 3.1.1.2; EC 1.-.-.- from Pseudomonas fluorescens (see 5 papers)
26% identity, 90% coverage: 21:256/262 of query aligns to 20:270/272 of P22862
- W29 (≠ L30) binding acetate
- 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 (≠ M70) mutation to M: Does not affect esterase and perhydrolase activities.
- M96 (≠ I96) binding acetate; 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 (≠ A122) mutation to P: Does not affect esterase and perhydrolase activities.
- F228 (≠ P215) 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
P46544 Proline iminopeptidase; PIP; Prolyl aminopeptidase; PAP; EC 3.4.11.5 from Lactobacillus delbrueckii subsp. bulgaricus (see paper)
26% identity, 82% coverage: 47:260/262 of query aligns to 55:295/295 of P46544
- D62 (= D54) mutation to G: Loss of activity.
- G65 (= G57) mutation to D: Loss of activity.
- S69 (= S61) mutation to F: Loss of activity.
- P72 (vs. gap) mutation to A: 95.4% of wild-type activity.
- E88 (≠ D76) mutation to K: Loss of activity.
- G105 (= G93) mutation to E: 0.2% of wild-type activity.
- Q106 (≠ L94) mutation to L: 21.8% of wild-type activity. KM=0.2 mM for prolyl-pNA.
- S107 (= S95) mutation S->G,N: Loss of activity.
- W108 (≠ I96) mutation to Y: 37.9% of wild-type activity. KM=4.0 mM for prolyl-pNA.
- G109 (= G97) mutation to A: 0.2% of wild-type activity. KM=2.3 mM for prolyl-pNA.; mutation G->S,D: Loss of activity.
- G110 (= G98) mutation to E: Loss of activity.
- S132 (≠ N119) mutation to F: Loss of activity.
- E143 (≠ R133) mutation to K: Loss of activity.
- P237 (= P201) mutation to A: 89.2% of wild-type activity.
- G243 (= G207) mutation to D: Loss of activity.
- D245 (≠ E209) mutation to G: 22.5% of wild-type activity. KM=1.0 mM for prolyl-pNA.
- D246 (= D210) mutation to G: 0.1% of wild-type activity. KM=1.0 mM for prolyl-pNA.
- H273 (= H238) mutation to Q: Loss of activity.
Sites not aligning to the query:
- 34 H→Q: 0.1% of wild-type activity.
- 35 G→D: 0.1% of wild-type activity.
- 36 G→E: Loss of activity.
- 37 P→L: Loss of activity.
- 38 G→D: Loss of activity.
8pi1B Bicyclic incypro pseudomonas fluorescens esterase (see paper)
26% identity, 92% coverage: 21:261/262 of query aligns to 19:274/276 of 8pi1B
Sites not aligning to the query:
O07015 Sigma factor SigB regulation protein RsbQ from Bacillus subtilis (strain 168) (see paper)
23% identity, 94% coverage: 12:256/262 of query aligns to 10:265/269 of O07015
- S96 (= S95) mutation to A: Loss of energy stress signaling.
- H247 (= H238) mutation to A: Loss of energy stress signaling.
5h3hB Esterase (eaest) from exiguobacterium antarcticum (see paper)
24% identity, 82% coverage: 43:256/262 of query aligns to 44:266/269 of 5h3hB
Sites not aligning to the query:
5aljA Ligand complex structure of soluble epoxide hydrolase (see paper)
22% identity, 95% coverage: 9:256/262 of query aligns to 234:518/523 of 5aljA
- active site: F253 (≠ L30), H320 (≠ L94), D321 (≠ S95), W322 (≠ I96), N345 (= N119), Y363 (≠ D132), Y442 (≠ L198), D472 (= D210), H500 (= H238)
- binding 2-(3-fluoro-4-methyl-anilino)-4-methyl-quinolin-5-ol: F253 (≠ L30), D321 (≠ S95), W322 (≠ I96), F361 (≠ W130), Q364 (≠ R133), Y442 (≠ L198), M445 (vs. gap)
5z7xA Crystal structure of striga hermonthica htl4 (shhtl4) (see paper)
23% identity, 85% coverage: 24:246/262 of query aligns to 21:255/270 of 5z7xA
Q9SQR3 Strigolactone esterase D14; Protein DWARF 14; AtD14; EC 3.1.-.- from Arabidopsis thaliana (Mouse-ear cress) (see 4 papers)
21% identity, 93% coverage: 10:252/262 of query aligns to 9:261/267 of Q9SQR3