SitesBLAST
Comparing Pf1N1B4_4192 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_4192 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)
6eb3C Structural and enzymatic characterization of an esterase from a metagenomic library
32% identity, 85% coverage: 42:286/288 of query aligns to 21:257/262 of 6eb3C
6eb3B Structural and enzymatic characterization of an esterase from a metagenomic library
32% identity, 85% coverage: 42:286/288 of query aligns to 21:263/268 of 6eb3B
6eb3A Structural and enzymatic characterization of an esterase from a metagenomic library
32% identity, 85% coverage: 42:286/288 of query aligns to 21:260/265 of 6eb3A
Sites not aligning to the query:
4lyeA Crystal structure of the s105a mutant of a c-c hydrolase, dxnb2 from sphingomonas wittichii rw1, in complex with substrate hopda (see paper)
27% identity, 85% coverage: 42:286/288 of query aligns to 27:273/276 of 4lyeA
- active site: G34 (≠ W49), G37 (≠ A52), N104 (≠ F113), A105 (≠ S114), M106 (≠ L115), M128 (≠ T137), R180 (= R198), D227 (= D240), H255 (= H268), W256 (≠ G269)
- binding (3e)-2,6-dioxo-6-phenylhex-3-enoate: G33 (≠ H48), G34 (≠ W49), G35 (= G50), N104 (≠ F113), A105 (≠ S114), L146 (≠ P168), L166 (≠ A184), R180 (= R198), M229 (= M242), H255 (= H268), W256 (≠ G269)
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)
27% identity, 85% coverage: 42:286/288 of query aligns to 27:273/276 of 4lxiA
- active site: G34 (≠ W49), G37 (≠ A52), N104 (≠ F113), A105 (≠ S114), M106 (≠ L115), M128 (≠ T137), R180 (= R198), D227 (= D240), H255 (= H268), W256 (≠ G269)
- binding (3E,5R)-5-fluoro-6-(2-fluorophenyl)-2,6-dioxohex-3-enoic acid: G33 (≠ H48), G34 (≠ W49), G35 (= G50), A38 (≠ L53), N43 (= N55), N104 (≠ F113), A105 (≠ S114), M106 (≠ L115), V149 (≠ Y171), M150 (≠ L172), L166 (≠ A184), R180 (= R198), M229 (= M242), W256 (≠ G269)
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)
27% identity, 85% coverage: 42:286/288 of query aligns to 27:273/276 of 4lxhA
- active site: G34 (≠ W49), G37 (≠ A52), N104 (≠ F113), A105 (≠ S114), M106 (≠ L115), M128 (≠ T137), R180 (= R198), D227 (= D240), H255 (= H268), W256 (≠ G269)
- binding (2Z,4E)-3-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid: G33 (≠ H48), G34 (≠ W49), G35 (= G50), N104 (≠ F113), A105 (≠ S114), M106 (≠ L115), L166 (≠ A184), W256 (≠ G269)
P77044 2-hydroxy-6-oxononadienedioate/2-hydroxy-6-oxononatrienedioate hydrolase; 2-hydroxy-6-ketonona-2,4-diene-1,9-dioic acid 5,6-hydrolase; 2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioic acid 5,6-hydrolase; 2-hydroxy-6-oxonona-2,4-diene-1,9-dioic acid 5,6-hydrolase; EC 3.7.1.14 from Escherichia coli (strain K12) (see 3 papers)
29% identity, 83% coverage: 49:286/288 of query aligns to 51:285/288 of P77044
- N113 (≠ F113) mutation to A: 200-fold decrease in catalytic activity and almost 2-fold increase in affinity.; mutation to H: 350-fold decrease in catalytic activity and almost 2-fold increase in affinity.
- S114 (= S114) Transition state stabilizer; mutation to A: Weakly active. 3-fold decrease in affinity. Fast ketonisation and slow C-C cleavage.; mutation to G: Weakly active. 3-fold decrease in affinity. Fast ketonisation and slow C-C cleavage.
- H118 (≠ F118) mutation to A: More than 2-fold decrease in catalytic efficiency and 3-fold increase affinity.
- F177 (= F173) mutation to D: 100-fold decrease in catalytic activity.; mutation to G: 4-fold and 8-fold decrease in catalytic activity and affinity, respectively.
- R192 (= R190) Catalytic role in ketonization of the dienol substrate (substrate destabilization); mutation to K: 40-fold and 5-fold decrease in catalytic activity and affinity, respectively.; mutation to Q: 280-fold and 10-fold decrease in catalytic activity and affinity, respectively.
- C265 (≠ A266) mutation to A: 2-fold decrease in catalytic activity and almost 2-fold increase in affinity.
- H267 (= H268) active site, Proton acceptor; mutation to A: Weakly active, 1000-fold decrease in catalytic efficiency. Very slow ketonisation and C-C cleavage.
- W268 (≠ G269) mutation to G: 10-fold and 20-fold decrease in catalytic activity and affinity, respectively.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 44 S→A: 2-fold decrease in catalytic efficiency and more than 5-fold increase in affinity for the natural substrate.
Q8NFV4 sn-1-specific diacylglycerol lipase ABHD11; Alpha/beta hydrolase domain-containing protein 11; Abhydrolase domain-containing protein 11; Williams-Beuren syndrome chromosomal region 21 protein; EC 3.1.1.116 from Homo sapiens (Human) (see paper)
27% identity, 90% coverage: 28:286/288 of query aligns to 44:305/306 of Q8NFV4
- S132 (= S114) mutation to A: Loss of p-nitrophenyl ester hydrolysis. Does not affect mitochondrion location. Loss of DLST lipoylation.
- H287 (= H268) mutation to A: Loss of DLST lipoylation.
Q86WA6 Valacyclovir hydrolase; VACVase; Valacyclovirase; Biphenyl hydrolase-like protein; Biphenyl hydrolase-related protein; Bph-rp; Breast epithelial mucin-associated antigen; MCNAA; EC 3.1.-.- from Homo sapiens (Human) (see 2 papers)
25% identity, 96% coverage: 10:286/288 of query aligns to 31:290/291 of Q86WA6
- S139 (= S114) active site, Nucleophile; mutation to A: <0.1% of wild type activity.
- D244 (= D240) active site, Charge relay system; mutation to N: <0.1% of wild type activity.
- H272 (= H268) active site, Charge relay system; mutation to A: Complete loss of activity.
Sites not aligning to the query:
2ociA Crystal structure of valacyclovir hydrolase complexed with a product analogue (see paper)
26% identity, 94% coverage: 17:286/288 of query aligns to 1:253/254 of 2ociA
- active site: S102 (= S114)
- binding manganese (ii) ion: H15 (≠ A31), E37 (≠ L53), D58 (= D74), H64 (≠ G80)
- binding l-tyrosinamide: G31 (≠ N47), M32 (≠ H48), S102 (= S114), D103 (≠ L115), I138 (≠ M158), Y139 (≠ I159), I142 (≠ L165), W172 (≠ Q195)
2ocgA Crystal structure of human valacyclovir hydrolase (see paper)
26% identity, 94% coverage: 17:286/288 of query aligns to 1:253/254 of 2ocgA
1iunB Meta-cleavage product hydrolase from pseudomonas fluorescens ip01 (cumd) s103a mutant hexagonal (see paper)
24% identity, 93% coverage: 21:287/288 of query aligns to 7:270/276 of 1iunB
- active site: S33 (≠ W49), G34 (= G50), G36 (≠ A52), N101 (≠ F113), A102 (≠ S114), F103 (≠ L115), G126 (= G138), V141 (≠ T154), R173 (≠ E186), F186 (≠ D199), D223 (= D240), H251 (= H268), W252 (≠ G269)
- binding acetate ion: H244 (≠ I261), R260 (≠ D277)
1ukaA Crystal structure of a meta-cleavage product hydrolase (cumd) complexed with (s)-2-methylbutyrate (see paper)
24% identity, 93% coverage: 21:287/288 of query aligns to 6:269/271 of 1ukaA
- active site: S32 (≠ W49), G33 (= G50), G35 (≠ A52), N100 (≠ F113), A101 (≠ S114), F102 (≠ L115), G125 (= G138), V140 (≠ T154), R172 (≠ E186), F185 (≠ D199), D222 (= D240), H250 (= H268), W251 (≠ G269)
- binding 2-methylbutanoic acid: S32 (≠ W49), A101 (≠ S114), F102 (≠ L115), W141 (= W155), V224 (≠ M242), H250 (= H268)
1uk9A Crystal structure of a meta-cleavage product hydrolase (cumd) complexed with isovalerate (see paper)
24% identity, 93% coverage: 21:287/288 of query aligns to 6:269/271 of 1uk9A
- active site: S32 (≠ W49), G33 (= G50), G35 (≠ A52), N100 (≠ F113), A101 (≠ S114), F102 (≠ L115), G125 (= G138), V140 (≠ T154), R172 (≠ E186), F185 (≠ D199), D222 (= D240), H250 (= H268), W251 (≠ G269)
- binding isovaleric acid: S32 (≠ W49), A101 (≠ S114), F102 (≠ L115), W141 (= W155), H250 (= H268)
1uk8A Crystal structure of a meta-cleavage product hydrolase (cumd) complexed with n-valerate (see paper)
24% identity, 93% coverage: 21:287/288 of query aligns to 6:269/271 of 1uk8A
- active site: S32 (≠ W49), G33 (= G50), G35 (≠ A52), N100 (≠ F113), A101 (≠ S114), F102 (≠ L115), G125 (= G138), V140 (≠ T154), R172 (≠ E186), F185 (≠ D199), D222 (= D240), H250 (= H268), W251 (≠ G269)
- binding pentanoic acid: S32 (≠ W49), A101 (≠ S114), F102 (≠ L115), L137 (vs. gap), W141 (= W155), L231 (= L249), G234 (≠ A252), E235 (≠ K253), H250 (= H268)
1uk7A Crystal structure of a meta-cleavage product hydrolase (cumd) complexed with n-butyrate (see paper)
24% identity, 93% coverage: 21:287/288 of query aligns to 6:269/271 of 1uk7A
- active site: S32 (≠ W49), G33 (= G50), G35 (≠ A52), N100 (≠ F113), A101 (≠ S114), F102 (≠ L115), G125 (= G138), V140 (≠ T154), R172 (≠ E186), F185 (≠ D199), D222 (= D240), H250 (= H268), W251 (≠ G269)
- binding butanoic acid: S32 (≠ W49), A101 (≠ S114), F102 (≠ L115), L137 (vs. gap), H250 (= H268)
1iupA Meta-cleavage product hydrolase from pseudomonas fluorescens ip01 (cumd) s103a mutant complexed with isobutyrates (see paper)
24% identity, 93% coverage: 21:287/288 of query aligns to 6:269/271 of 1iupA
- active site: S32 (≠ W49), G33 (= G50), G35 (≠ A52), N100 (≠ F113), A101 (≠ S114), F102 (≠ L115), G125 (= G138), V140 (≠ T154), R172 (≠ E186), F185 (≠ D199), D222 (= D240), H250 (= H268), W251 (≠ G269)
- binding 2-methyl-propionic acid: S32 (≠ W49), A40 (vs. gap), N41 (≠ D57), Y74 (≠ V89), W79 (≠ M92), A101 (≠ S114), F102 (≠ L115), L137 (vs. gap), W141 (= W155), R172 (≠ E186), M188 (≠ P202), W196 (≠ Q210), V224 (≠ M242), H250 (= H268), W251 (≠ G269)
2d0dA Crystal structure of a meta-cleavage product hydrolase (cumd) a129v mutant (see paper)
25% identity, 93% coverage: 21:287/288 of query aligns to 6:269/271 of 2d0dA
- active site: S32 (≠ W49), G33 (= G50), G35 (≠ A52), N100 (≠ F113), S101 (= S114), F102 (≠ L115), G125 (= G138), V140 (≠ T154), R172 (≠ E186), F185 (≠ D199), D222 (= D240), H250 (= H268), W251 (≠ G269)
- binding chloride ion: S32 (≠ W49), S101 (= S114), F102 (≠ L115)
2xuaH Crystal structure of the enol-lactonase from burkholderia xenovorans lb400 (see paper)
26% identity, 91% coverage: 25:286/288 of query aligns to 6:259/261 of 2xuaH
P25026 Non-heme chloroperoxidase; Chloride peroxidase; Chloroperoxidase P; CPO-P; EC 1.11.1.- from Burkholderia pyrrocinia (Pseudomonas pyrrocinia) (see paper)
24% identity, 89% coverage: 32:288/288 of query aligns to 14:278/278 of P25026
- S97 (= S114) mutation S->A,C: Very low activity.
- D229 (= D240) mutation to A: Loss of activity.
- H258 (= H268) mutation to Q: Loss of activity.
Query Sequence
>Pf1N1B4_4192 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_4192
MTLIATSNHPGSQSFINAANQSVLIGGIPFAYRDLGPRTEVPLVMFNHWGAALDNFDPRI
IDGLAKNRRVITTDYRGIGGSGGAAPLTVGEMADDAVGLIRALGFDKVDLLGFSLGGFVA
QDIAMKAPERVRRLILTGTGPAGGTGIDSVGSVTWPLMIKGLLTLRDPKFYLFFTTTANG
QRAASEYLQRLKERQQDRDKGPTPRAFLRQLKAITAWGKQAPQELGRLRMPTLIANGDND
IMVPTVNSLELAKRIPNAQLIIYQDAGHGSIFQHHTDFVANALAFLDA
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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