SitesBLAST
Comparing H281DRAFT_06209 FitnessBrowser__Burk376:H281DRAFT_06209 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)
1zlpB Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
37% identity, 97% coverage: 9:289/290 of query aligns to 4:285/285 of 1zlpB
- active site: F37 (= F42), S39 (≠ T44), G40 (= G45), Y41 (≠ A46), D52 (= D57), D80 (= D84), D82 (= D86), F107 (≠ M111), E109 (= E113), K115 (= K119), C117 (= C121), G118 (= G122), H119 (= H123), R152 (= R156), E182 (= E186), N204 (= N208), T211 (= T215), L213 (= L217)
- binding 5-hydroxypentanal: Y41 (≠ A46), C117 (= C121), R152 (= R156), I206 (≠ V210)
Q05957 Petal death protein; (R)-2-methylmalate lyase; D-citramalate lyase; Oxalacetic hydrolase; PSR132; EC 3.7.1.1; EC 4.1.3.- from Dianthus caryophyllus (Carnation) (Clove pink) (see 2 papers)
37% identity, 97% coverage: 9:289/290 of query aligns to 31:312/318 of Q05957
- D79 (= D57) mutation to A: Reduces catalytic efficiency 1000-fold.
- D107 (= D84) binding
- D109 (= D86) binding
- K142 (= K119) binding
- C144 (= C121) mutation to A: Loss of catalytic activity.
Sites not aligning to the query:
- 1:3 modified: propeptide, Removed in mature form
1zlpA Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
38% identity, 94% coverage: 9:280/290 of query aligns to 4:276/284 of 1zlpA
- active site: F37 (= F42), S39 (≠ T44), G40 (= G45), Y41 (≠ A46), D52 (= D57), D80 (= D84), D82 (= D86), F107 (≠ M111), E109 (= E113), K115 (= K119), C117 (= C121), G118 (= G122), H119 (= H123), R152 (= R156), E182 (= E186), N204 (= N208), T211 (= T215), L213 (= L217)
- binding 5-hydroxypentanal: C117 (= C121), G118 (= G122), R152 (= R156), I206 (≠ V210)
- binding magnesium ion: D80 (= D84), K115 (= K119)
P77541 2-methylisocitrate lyase; 2-MIC; MICL; (2R,3S)-2-methylisocitrate lyase; EC 4.1.3.30 from Escherichia coli (strain K12) (see 3 papers)
39% identity, 96% coverage: 3:281/290 of query aligns to 4:283/296 of P77541
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1mumA Structure of the 2-methylisocitrate lyase (prpb) from escherichia coli (see paper)
39% identity, 96% coverage: 3:281/290 of query aligns to 2:281/289 of 1mumA
- active site: Y41 (≠ F42), S43 (≠ T44), G44 (= G45), G45 (≠ A46), D56 (= D57), D83 (= D84), D85 (= D86), H111 (≠ M111), E113 (= E113), K119 (= K119), C121 (= C121), G122 (= G122), H123 (= H123), R156 (= R156), E186 (≠ S189), N208 (= N208), T215 (= T215), L217 (= L217)
- binding magnesium ion: D56 (= D57), D85 (= D86)
Q56062 2-methylisocitrate lyase; 2-MIC; MICL; (2R,3S)-2-methylisocitrate lyase; EC 4.1.3.30 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
38% identity, 96% coverage: 3:281/290 of query aligns to 4:283/295 of Q56062
- SGG 45:47 (≠ TGA 44:46) binding
- D58 (= D57) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- D85 (= D84) binding
- K121 (= K119) mutation to A: 1000-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R122 (= R120) mutation to K: 2-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- C123 (= C121) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- H125 (= H123) mutation to A: 750-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R158 (= R156) binding
3fa3B Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
40% identity, 86% coverage: 9:256/290 of query aligns to 9:261/302 of 3fa3B
- active site: Y43 (≠ F42), T45 (= T44), G46 (= G45), A47 (= A46), D58 (= D57), D86 (= D84), D88 (= D86), H113 (≠ M111), E115 (= E113), K121 (= K119), C123 (= C121), G124 (= G122), H125 (= H123), R160 (= R156), E190 (= E186), N213 (= N208), T220 (= T215), S222 (≠ L217)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y43 (≠ F42), T45 (= T44), G46 (= G45), A47 (= A46), D86 (= D84), G124 (= G122), R160 (= R156), E190 (= E186), N213 (= N208), P239 (≠ A234)
4iqdA Crystal structure of carboxyvinyl-carboxyphosphonate phosphorylmutase from bacillus anthracis
33% identity, 95% coverage: 9:283/290 of query aligns to 13:284/290 of 4iqdA
- active site: Y46 (≠ F42), S48 (≠ T44), G49 (= G45), A50 (= A46), D60 (= D57), D87 (= D84), D89 (= D86), Q114 (≠ M111), E116 (= E113), K122 (= K119), C124 (= C121), G125 (= G122), H126 (= H123), R157 (= R156), E187 (= E186), N209 (= N208)
- binding pyruvic acid: E71 (≠ A68), R72 (≠ H69), D75 (≠ A72), G165 (= G164), L166 (≠ F165), Y218 (≠ L217), Y219 (≠ L218)
1o5qA Crystal structure of pyruvate and mg2+ bound 2-methylisocitrate lyase (prpb) from salmonella typhimurium (see paper)
36% identity, 95% coverage: 6:281/290 of query aligns to 3:268/271 of 1o5qA
- active site: Y39 (≠ F42), S41 (≠ T44), G42 (= G45), G43 (≠ A46), D54 (= D57), D81 (= D84), D83 (= D86), H109 (≠ M111), E111 (= E113), R143 (= R156), E173 (= E186), N195 (= N208), T202 (= T215), L204 (= L217)
- binding pyruvic acid: Y39 (≠ F42), S41 (≠ T44), G43 (≠ A46), D81 (= D84), R143 (= R156)
3fa4A Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, triclinic crystal form (see paper)
38% identity, 86% coverage: 9:256/290 of query aligns to 9:254/284 of 3fa4A
- active site: Y43 (≠ F42), T45 (= T44), G46 (= G45), A47 (= A46), D58 (= D57), D86 (= D84), D88 (= D86), H113 (≠ M111), E115 (= E113), R153 (= R156), E183 (= E186), N206 (= N208), T213 (= T215), S215 (≠ L217)
- binding magnesium ion: D86 (= D84), D88 (= D86)
3fa3J Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
38% identity, 86% coverage: 9:256/290 of query aligns to 8:252/292 of 3fa3J
- active site: Y42 (≠ F42), T44 (= T44), G45 (= G45), A46 (= A46), D57 (= D57), D85 (= D84), D87 (= D86), H112 (≠ M111), E114 (= E113), R151 (= R156), E181 (= E186), N204 (= N208), T211 (= T215), S213 (≠ L217)
- binding manganese (ii) ion: D85 (= D84), D87 (= D86)
3m0jA Structure of oxaloacetate acetylhydrolase in complex with the inhibitor 3,3-difluorooxalacetate (see paper)
38% identity, 89% coverage: 9:265/290 of query aligns to 10:271/297 of 3m0jA
- binding calcium ion: E218 (≠ I211), N219 (≠ G212)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y44 (≠ F42), T46 (= T44), G47 (= G45), A48 (= A46), D88 (= D84), G126 (= G122), R162 (= R156), E192 (= E186), N215 (= N208), S241 (≠ A234)
6t4vC Crystal structure of 2-methylisocitrate lyase (prpb) from pseudomonas aeruginosa in apo form.
32% identity, 95% coverage: 6:281/290 of query aligns to 5:270/277 of 6t4vC
- active site: Y41 (≠ F42), S43 (≠ T44), G44 (= G45), G45 (≠ A46), D56 (= D57), D83 (= D84), D85 (= D86), H111 (≠ M111), E113 (= E113), R145 (= R156), E175 (≠ S189), N197 (= N208), T204 (= T215), L206 (= L217)
- binding pyruvic acid: F88 (= F89), N94 (= N94)
3m0kA Structure of oxaloacetate acetylhydrolase in complex with the product oxalate (see paper)
36% identity, 86% coverage: 9:258/290 of query aligns to 10:260/289 of 3m0kA
1pymA Phosphoenolpyruvate mutase from mollusk in with bound mg2-oxalate (see paper)
31% identity, 90% coverage: 9:270/290 of query aligns to 7:270/291 of 1pymA
- active site: W40 (≠ F42), S42 (≠ T44), G43 (= G45), L44 (≠ A46), D54 (= D57), D81 (= D84), D83 (= D86), C108 (≠ M111), E110 (= E113), K116 (= K119), N118 (≠ C121), S119 (≠ G122), R155 (= R156), H186 (≠ E186), V211 (≠ I211)
- binding oxalate ion: W40 (≠ F42), S42 (≠ T44), G43 (= G45), L44 (≠ A46), D81 (= D84), R155 (= R156)
1m1bA Crystal structure of phosphoenolpyruvate mutase complexed with sulfopyruvate (see paper)
31% identity, 90% coverage: 9:270/290 of query aligns to 7:270/291 of 1m1bA
- active site: W40 (≠ F42), S42 (≠ T44), G43 (= G45), L44 (≠ A46), D54 (= D57), D81 (= D84), D83 (= D86), C108 (≠ M111), E110 (= E113), K116 (= K119), N118 (≠ C121), S119 (≠ G122), R155 (= R156), H186 (≠ E186), V211 (≠ I211)
- binding magnesium ion: D81 (= D84), R155 (= R156)
- binding sulfopyruvate: S42 (≠ T44), G43 (= G45), L44 (≠ A46), D81 (= D84), N118 (≠ C121), S119 (≠ G122), L120 (≠ H123), R155 (= R156)
P56839 Phosphoenolpyruvate phosphomutase; PEP mutase; PEP phosphomutase; Phosphoenolpyruvate mutase; EC 5.4.2.9 from Mytilus edulis (Blue mussel) (see 2 papers)
31% identity, 90% coverage: 9:270/290 of query aligns to 11:274/295 of P56839
- D58 (= D57) mutation D->A,S: Abolishes enzyme activity.; mutation to N: Strongly reduces enzyme activity.
- D85 (= D84) mutation to A: Strongly reduces enzyme activity and increases KM.
- D87 (= D86) mutation to A: Strongly reduces enzyme activity.
- E114 (= E113) mutation to A: Strongly reduces enzyme activity.
- N122 (≠ C121) mutation N->A,D: Strongly reduces enzyme activity.
- R159 (= R156) mutation to A: Strongly reduces enzyme activity.
- H190 (≠ E186) mutation to A: Strongly reduces enzyme activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2hjpA Crystal structure of phosphonopyruvate hydrolase complex with phosphonopyruvate and mg++ (see paper)
36% identity, 80% coverage: 26:258/290 of query aligns to 24:252/283 of 2hjpA
- active site: W40 (≠ F42), S42 (≠ T44), G43 (= G45), F44 (≠ A46), D54 (= D57), D81 (= D84), D83 (= D86), V108 (≠ M111), E110 (= E113), K116 (= K119), T118 (≠ G126), R148 (= R156), H179 (≠ E186), V204 (≠ I211)
- binding phosphonopyruvate: W40 (≠ F42), S42 (≠ T44), F44 (≠ A46), D81 (= D84), R148 (= R156), H179 (≠ E186), R181 (vs. gap)
- binding alpha-D-xylopyranose: E32 (= E34), S75 (= S78)
2duaA Crystal structure of phosphonopyruvate hydrolase complex with oxalate and mg++ (see paper)
36% identity, 80% coverage: 26:258/290 of query aligns to 24:252/283 of 2duaA
- active site: W40 (≠ F42), S42 (≠ T44), G43 (= G45), F44 (≠ A46), D54 (= D57), D81 (= D84), D83 (= D86), V108 (≠ M111), E110 (= E113), K116 (= K119), T118 (≠ G126), R148 (= R156), H179 (≠ E186), V204 (≠ I211)
- binding oxalate ion: W40 (≠ F42), S42 (≠ T44), F44 (≠ A46), D81 (= D84), R148 (= R156)
- binding alpha-D-xylopyranose: E32 (= E34), S75 (= S78)
Q84G06 Phosphonopyruvate hydrolase; PPH; EC 3.11.1.3 from Variovorax sp. (strain Pal2) (see paper)
36% identity, 80% coverage: 26:258/290 of query aligns to 24:259/290 of Q84G06
- D81 (= D84) binding
- R188 (vs. gap) mutation to A: Reduced affinity for substrate.
Query Sequence
>H281DRAFT_06209 FitnessBrowser__Burk376:H281DRAFT_06209
MSHECGAFLRRTLQPSAALLLPGVSNALAARIAEEAGYAAVFVTGAGIANSYLGAPDIGL
TTVTEVGAHINAIREAVSIPIIADADTGFGNALNVMRTVRLFERAGANCIMLEDQTFPKR
CGHFEGKAVVSIEEMTAKIKAAVDARANADTLIMARTDSRAIEGFERSLERIRTYRDAGA
DVLFVEAPSSLEELARIPREAPGVQVCNMVIGGKTPLLPQAQLSELGYAGVIYANAALQA
AMFAMKNVLEHLRSHGSIEGREDQIMSFAERQKMVNFARYDALAKQCAND
Or try a new SitesBLAST search
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