SitesBLAST
Comparing BPHYT_RS20310 FitnessBrowser__BFirm:BPHYT_RS20310 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)
8pi1B Bicyclic incypro pseudomonas fluorescens esterase (see paper)
28% identity, 88% coverage: 31:269/272 of query aligns to 3:271/276 of 8pi1B
Sites not aligning to the query:
P22862 Arylesterase; Aryl-ester hydrolase; Carboxylic acid perhydrolase; PFE; Putative bromoperoxidase; EC 3.1.1.2; EC 1.-.-.- from Pseudomonas fluorescens (see 5 papers)
28% identity, 88% coverage: 31:269/272 of query aligns to 4:272/272 of P22862
- W29 (≠ G56) binding
- L30 (= L57) 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 (≠ H85) mutation to H: 50-fold increase in catalytic efficiency with acetic acid as substrate; when associated with P-30.
- Y70 (= Y97) mutation to M: Does not affect esterase and perhydrolase activities.
- M96 (vs. gap) binding ; mutation to T: 4-fold decrease in esterase activity. Loss of perhydrolase activity.
- D100 (≠ C126) mutation to E: Small decrease in esterase and perhydrolase activities.
- T123 (≠ M149) mutation to P: Does not affect esterase and perhydrolase activities.
- F228 (≠ P226) 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)
28% identity, 88% coverage: 31:269/272 of query aligns to 3:271/271 of 3ia2A
- active site: W28 (≠ G56), S94 (= S122), M95 (vs. gap), G119 (= G146), D222 (= D221), H251 (= H249)
- binding (2R)-butane-2-sulfonate: W28 (≠ G56), S94 (= S122), M95 (vs. gap), F198 (vs. gap), I224 (≠ F223), H251 (= H249)
3heaA The l29p/l124i mutation of pseudomonas fluorescens esterase (see paper)
28% identity, 88% coverage: 31:269/272 of query aligns to 3:271/271 of 3heaA
- active site: W28 (≠ G56), S94 (= S122), M95 (vs. gap), L118 (≠ F145), G119 (= G146), D222 (= D221), H251 (= H249)
- binding ethyl acetate: G27 (= G55), W28 (≠ G56), S94 (= S122), M95 (vs. gap), H251 (= H249)
3hi4A Switching catalysis from hydrolysis to perhydrolysis in p. Fluorescens esterase (see paper)
28% identity, 88% coverage: 31:269/272 of query aligns to 3:271/271 of 3hi4A
2xuaH Crystal structure of the enol-lactonase from burkholderia xenovorans lb400 (see paper)
33% identity, 81% coverage: 47:267/272 of query aligns to 22:259/261 of 2xuaH
1ek2A Crystal structure of murine soluble epoxide hydrolase complexed with cdu inhibitor (see paper)
23% identity, 91% coverage: 21:268/272 of query aligns to 167:485/487 of 1ek2A
- active site: F208 (≠ G56), D276 (≠ S122), W277 (≠ D123), N300 (≠ G146), I319 (vs. gap), Y324 (vs. gap), Y408 (≠ M194), D438 (= D221), H466 (= H249)
- binding n-cyclohexyl-n'-decylurea: F208 (≠ G56), D276 (≠ S122), Y324 (vs. gap), Q325 (vs. gap), F349 (≠ Y174), Y408 (≠ M194), H466 (= H249), W467 (≠ F250)
P34914 Bifunctional epoxide hydrolase 2; EC 3.3.2.10; EC 3.1.3.76 from Mus musculus (Mouse) (see 2 papers)
23% identity, 91% coverage: 21:268/272 of query aligns to 224:542/554 of P34914
- D333 (≠ S122) active site, Nucleophile
- Y465 (≠ M194) active site, Proton donor
- H523 (= H249) active site, Proton acceptor
1ek1A Crystal structure of murine soluble epoxide hydrolase complexed with ciu inhibitor (see paper)
23% identity, 91% coverage: 21:268/272 of query aligns to 170:488/490 of 1ek1A
- active site: F211 (≠ G56), D279 (≠ S122), W280 (≠ D123), N303 (≠ G146), I322 (vs. gap), Y327 (vs. gap), Y411 (≠ M194), D441 (= D221), H469 (= H249)
- binding n-cyclohexyl-n'-(4-iodophenyl)urea: F211 (≠ G56), D279 (≠ S122), W280 (≠ D123), Y327 (vs. gap), Q328 (vs. gap), F352 (≠ Y174), Y411 (≠ M194)
1cr6B Crystal structure of murine soluble epoxide hydrolase complexed with cpu inhibitor (see paper)
23% identity, 91% coverage: 21:268/272 of query aligns to 221:539/541 of 1cr6B
- active site: F262 (≠ G56), D330 (≠ S122), W331 (≠ D123), N354 (≠ G146), I373 (vs. gap), Y378 (vs. gap), Y462 (≠ M194), D492 (= D221), H520 (= H249)
- binding n-cyclohexyl-n'-(propyl)phenyl urea: D330 (≠ S122), W331 (≠ D123), Y462 (≠ M194), V494 (≠ F223), H520 (= H249)
5h3hB Esterase (eaest) from exiguobacterium antarcticum (see paper)
38% identity, 35% coverage: 35:129/272 of query aligns to 9:103/269 of 5h3hB
Sites not aligning to the query:
4uhfA Structural studies of a thermophilic esterase from thermogutta terrifontis (l37a mutant with butyrate bound) (see paper)
24% identity, 85% coverage: 41:270/272 of query aligns to 19:270/278 of 4uhfA
- active site: F34 (≠ G56), L99 (≠ W121), S100 (= S122), M101 (≠ D123), D124 (≠ G146), E164 (= E164), D221 (= D221), H249 (= H249), L250 (≠ F250)
- binding butanoic acid: G33 (= G55), F34 (≠ G56), S100 (= S122), H249 (= H249)
4uhdA Structural studies of a thermophilic esterase from thermogutta terrifontis (acetate bound) (see paper)
24% identity, 85% coverage: 41:270/272 of query aligns to 19:270/274 of 4uhdA
- active site: F34 (≠ G56), L99 (≠ W121), S100 (= S122), M101 (≠ D123), D124 (≠ G146), E164 (= E164), D221 (= D221), H249 (= H249), L250 (≠ F250)
- binding acetate ion: G33 (= G55), F34 (≠ G56), S100 (= S122), Y104 (≠ C126), R138 (vs. gap), H249 (= H249)
- binding magnesium ion: A233 (= A233), I236 (= I236), S239 (≠ A239)
4uheA Structural studies of a thermophilic esterase from thermogutta terrifontis (malate bound) (see paper)
24% identity, 85% coverage: 41:270/272 of query aligns to 19:270/272 of 4uheA
- active site: F34 (≠ G56), L99 (≠ W121), S100 (= S122), M101 (≠ D123), D124 (≠ G146), E164 (= E164), D221 (= D221), H249 (= H249), L250 (≠ F250)
- binding d-malate: F34 (≠ G56), S100 (= S122), M101 (≠ D123), Y104 (≠ C126), R138 (vs. gap), H249 (= H249)
5alrA Ligand complex structure of soluble epoxide hydrolase (see paper)
23% identity, 91% coverage: 21:267/272 of query aligns to 225:537/542 of 5alrA
- active site: F266 (≠ G56), H333 (≠ W121), D334 (≠ S122), W335 (≠ D123), N358 (≠ G146), Y378 (vs. gap), Y461 (≠ M194), D491 (= D221), H519 (= H249)
- binding n-[4-(trifluoromethylsulfanyl)phenyl]quinazolin-4-amine: F266 (≠ G56), D334 (≠ S122), W335 (≠ D123), Y378 (vs. gap), Q379 (vs. gap), F382 (vs. gap), L403 (vs. gap), Y461 (≠ M194), H519 (= H249)
5aljA Ligand complex structure of soluble epoxide hydrolase (see paper)
23% identity, 91% coverage: 21:267/272 of query aligns to 212:518/523 of 5aljA
- active site: F253 (≠ G56), H320 (≠ W121), D321 (≠ S122), W322 (≠ D123), N345 (≠ G146), Y363 (vs. gap), Y442 (≠ M194), D472 (= D221), H500 (= H249)
- binding 2-(3-fluoro-4-methyl-anilino)-4-methyl-quinolin-5-ol: F253 (≠ G56), D321 (≠ S122), W322 (≠ D123), F361 (vs. gap), Q364 (vs. gap), Y442 (≠ M194), M445 (≠ T197)
5fp0A Ligand complex structure of soluble epoxide hydrolase (see paper)
23% identity, 91% coverage: 21:267/272 of query aligns to 225:538/543 of 5fp0A
- active site: F266 (≠ G56), H333 (≠ W121), D334 (≠ S122), W335 (≠ D123), N358 (≠ G146), N374 (≠ R155), Y379 (vs. gap), Y462 (≠ M194), D492 (= D221), H520 (= H249)
- binding N-cyclopentyl-2-[4-(trifluoromethyl)phenyl]-3H-benzimidazole-4-sulfonamide: F266 (≠ G56), D334 (≠ S122), W335 (≠ D123), M338 (≠ C126), Y379 (vs. gap), Q380 (vs. gap), Y462 (≠ M194), M499 (≠ H228), H520 (= H249)
5alsA Ligand complex structure of soluble epoxide hydrolase (see paper)
23% identity, 91% coverage: 21:267/272 of query aligns to 225:536/541 of 5alsA
- active site: F266 (≠ G56), H333 (≠ W121), D334 (≠ S122), W335 (≠ D123), N358 (≠ G146), Y377 (vs. gap), Y460 (≠ M194), D490 (= D221), H518 (= H249)
- binding n-cyclopentyl-2-[4-(trifluoromethyl)phenyl]-3h-imidazo[4,5-b]pyridine-7-sulfonamide: F266 (≠ G56), D334 (≠ S122), W335 (≠ D123), M338 (≠ C126), Y377 (vs. gap), Q378 (vs. gap), Y460 (≠ M194), V492 (≠ F223), M497 (≠ H228)
5alvA Ligand complex structure of soluble epoxide hydrolase (see paper)
23% identity, 91% coverage: 21:267/272 of query aligns to 220:532/537 of 5alvA
- active site: F261 (≠ G56), H328 (≠ W121), D329 (≠ S122), W330 (≠ D123), N353 (≠ G146), N372 (vs. gap), Y377 (vs. gap), Y456 (≠ M194), D486 (= D221), H514 (= H249)
- binding 3-(3-fluorophenyl)-1H-pyrazole: D329 (≠ S122), W330 (≠ D123), M333 (≠ C126), T354 (≠ C147), Y377 (vs. gap), Q378 (vs. gap), Y456 (≠ M194)
5am2A Ligand complex structure of soluble epoxide hydrolase (see paper)
22% identity, 91% coverage: 21:267/272 of query aligns to 220:532/537 of 5am2A
- active site: F261 (≠ G56), H328 (≠ W121), D329 (≠ S122), W330 (≠ D123), N353 (≠ G146), N372 (vs. gap), Y377 (vs. gap), Y456 (≠ M194), D486 (= D221), H514 (= H249)
- binding 7-methyl-2h-isoquinolin-1-one: F261 (≠ G56), W330 (≠ D123), M333 (≠ C126), Y337 (≠ V130), I357 (vs. gap), S368 (≠ T154), Y377 (vs. gap), F381 (vs. gap), L402 (≠ Y174), L418 (vs. gap), M459 (≠ T197), N462 (= N200), D486 (= D221), F487 (≠ E222), V488 (≠ F223), H514 (= H249), W515 (≠ F250)
Query Sequence
>BPHYT_RS20310 FitnessBrowser__BFirm:BPHYT_RS20310
MEPSTHPHDDDLERFEAHGAAPLPVPSDEGYVEHEGARIWYASYGAGAPVILLHGGLGHS
GNWGYQVPALLDAGRRVVVVDSRGHGRSTRDARPYRYELMASDVLAVMDTLQLERAALVG
WSDGACVAMVLGATAAERVAGVFFFGCNMDPSGTRPFVPTPAIERCFSRHAKDYAQLSAT
PDDFEAFVGAVSTMMKTEPNYSAGDLAQIRVPVAIVQSEHDEFIKPEHADYLARSIPGAE
LILLPGVSHFAPLQRPAQFNRVVLDFLRRIAD
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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