SitesBLAST
Comparing 3607683 FitnessBrowser__Dino:3607683 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)
1zlpA Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
36% identity, 96% coverage: 6:285/293 of query aligns to 3:283/284 of 1zlpA
- active site: F37 (= F40), S39 (= S42), G40 (= G43), Y41 (≠ F44), D52 (= D55), D80 (= D82), D82 (= D84), F107 (≠ M109), E109 (= E111), K115 (= K117), C117 (= C119), G118 (= G120), H119 (= H121), R152 (= R159), E182 (= E189), N204 (= N211), T211 (= T218), L213 (≠ D220)
- binding 5-hydroxypentanal: C117 (= C119), G118 (= G120), R152 (= R159), I206 (≠ V213)
- binding magnesium ion: D80 (= D82), K115 (= K117)
1zlpB Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
36% identity, 96% coverage: 6:287/293 of query aligns to 3:285/285 of 1zlpB
- active site: F37 (= F40), S39 (= S42), G40 (= G43), Y41 (≠ F44), D52 (= D55), D80 (= D82), D82 (= D84), F107 (≠ M109), E109 (= E111), K115 (= K117), C117 (= C119), G118 (= G120), H119 (= H121), R152 (= R159), E182 (= E189), N204 (= N211), T211 (= T218), L213 (≠ D220)
- binding 5-hydroxypentanal: Y41 (≠ F44), C117 (= C119), R152 (= R159), I206 (≠ V213)
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)
36% identity, 96% coverage: 6:287/293 of query aligns to 30:312/318 of Q05957
- D79 (= D55) mutation to A: Reduces catalytic efficiency 1000-fold.
- D107 (= D82) binding
- D109 (= D84) binding
- K142 (= K117) binding
- C144 (= C119) mutation to A: Loss of catalytic activity.
Sites not aligning to the query:
- 1:3 modified: propeptide, Removed in mature form
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, 97% coverage: 2:284/293 of query aligns to 5:285/295 of Q56062
- SGG 45:47 (≠ SGF 42:44) binding
- D58 (= D55) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- D85 (= D82) binding
- K121 (= K117) mutation to A: 1000-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R122 (= R118) mutation to K: 2-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- C123 (= C119) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- H125 (= H121) mutation to A: 750-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R158 (= R159) binding
4iqdA Crystal structure of carboxyvinyl-carboxyphosphonate phosphorylmutase from bacillus anthracis
35% identity, 93% coverage: 4:275/293 of query aligns to 10:278/290 of 4iqdA
- active site: Y46 (≠ F40), S48 (= S42), G49 (= G43), A50 (≠ F44), D60 (= D55), D87 (= D82), D89 (= D84), Q114 (≠ M109), E116 (= E111), K122 (= K117), C124 (= C119), G125 (= G120), H126 (= H121), R157 (= R159), E187 (= E189), N209 (= N211)
- binding pyruvic acid: E71 (≠ D66), R72 (≠ Q67), D75 (≠ N70), G165 (= G167), L166 (= L168), Y218 (≠ D220), Y219 (≠ L221)
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)
36% identity, 97% coverage: 2:284/293 of query aligns to 5:285/296 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)
36% identity, 97% coverage: 2:284/293 of query aligns to 3:283/289 of 1mumA
- active site: Y41 (≠ F40), S43 (= S42), G44 (= G43), G45 (≠ F44), D56 (= D55), D83 (= D82), D85 (= D84), H111 (≠ M109), E113 (= E111), K119 (= K117), C121 (= C119), G122 (= G120), H123 (= H121), R156 (= R159), E186 (= E189), N208 (= N211), T215 (= T218), L217 (≠ D220)
- binding magnesium ion: D56 (= D55), D85 (= D84)
3fa3B Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
36% identity, 90% coverage: 1:263/293 of query aligns to 3:265/302 of 3fa3B
- active site: Y43 (≠ F40), T45 (≠ S42), G46 (= G43), A47 (≠ F44), D58 (= D55), D86 (= D82), D88 (= D84), H113 (≠ M109), E115 (= E111), K121 (= K117), C123 (= C119), G124 (= G120), H125 (= H121), R160 (= R159), E190 (= E189), N213 (= N211), T220 (= T218), S222 (≠ D220)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y43 (≠ F40), T45 (≠ S42), G46 (= G43), A47 (≠ F44), D86 (= D82), G124 (= G120), R160 (= R159), E190 (= E189), N213 (= N211), P239 (= P237)
3m0jA Structure of oxaloacetate acetylhydrolase in complex with the inhibitor 3,3-difluorooxalacetate (see paper)
37% identity, 88% coverage: 1:257/293 of query aligns to 4:261/297 of 3m0jA
- binding calcium ion: E218 (= E214), N219 (≠ G215)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y44 (≠ F40), T46 (≠ S42), G47 (= G43), A48 (≠ F44), D88 (= D82), G126 (= G120), R162 (= R159), E192 (= E189), N215 (= N211), S241 (≠ P237)
3fa4A Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, triclinic crystal form (see paper)
35% identity, 90% coverage: 1:263/293 of query aligns to 3:258/284 of 3fa4A
- active site: Y43 (≠ F40), T45 (≠ S42), G46 (= G43), A47 (≠ F44), D58 (= D55), D86 (= D82), D88 (= D84), H113 (≠ M109), E115 (= E111), R153 (= R159), E183 (= E189), N206 (= N211), T213 (= T218), S215 (≠ D220)
- binding magnesium ion: D86 (= D82), D88 (= D84)
1o5qA Crystal structure of pyruvate and mg2+ bound 2-methylisocitrate lyase (prpb) from salmonella typhimurium (see paper)
35% identity, 97% coverage: 2:284/293 of query aligns to 1:270/271 of 1o5qA
- active site: Y39 (≠ F40), S41 (= S42), G42 (= G43), G43 (≠ F44), D54 (= D55), D81 (= D82), D83 (= D84), H109 (≠ M109), E111 (= E111), R143 (= R159), E173 (= E189), N195 (= N211), T202 (= T218), L204 (≠ D220)
- binding pyruvic acid: Y39 (≠ F40), S41 (= S42), G43 (≠ F44), D81 (= D82), R143 (= R159)
3fa3J Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
34% identity, 90% coverage: 1:263/293 of query aligns to 2:256/292 of 3fa3J
- active site: Y42 (≠ F40), T44 (≠ S42), G45 (= G43), A46 (≠ F44), D57 (= D55), D85 (= D82), D87 (= D84), H112 (≠ M109), E114 (= E111), R151 (= R159), E181 (= E189), N204 (= N211), T211 (= T218), S213 (≠ D220)
- binding manganese (ii) ion: D85 (= D82), D87 (= D84)
3m0kA Structure of oxaloacetate acetylhydrolase in complex with the product oxalate (see paper)
36% identity, 88% coverage: 1:257/293 of query aligns to 4:256/289 of 3m0kA
6t4vC Crystal structure of 2-methylisocitrate lyase (prpb) from pseudomonas aeruginosa in apo form.
35% identity, 87% coverage: 23:278/293 of query aligns to 24:269/277 of 6t4vC
- active site: Y41 (≠ F40), S43 (= S42), G44 (= G43), G45 (≠ F44), D56 (= D55), D83 (= D82), D85 (= D84), H111 (≠ M109), E113 (= E111), R145 (= R159), E175 (= E189), N197 (= N211), T204 (= T218), L206 (≠ D220)
- binding pyruvic acid: F88 (≠ Y87), N94 (= N92)
3b8iA Crystal structure of oxaloacetate decarboxylase from pseudomonas aeruginosa (pa4872) in complex with oxalate and mg2+. (see paper)
31% identity, 95% coverage: 7:284/293 of query aligns to 11:278/284 of 3b8iA
- active site: I44 (≠ F40), G46 (≠ S42), G47 (= G43), S48 (≠ F44), D59 (= D55), D86 (= D82), D88 (= D84), T113 (≠ M109), E115 (= E111), A121 (≠ K117), F123 (≠ C119), G124 (= G120), R157 (= R159), V186 (≠ E189), M206 (= M209)
- binding oxalate ion: S48 (≠ F44), D86 (= D82), H233 (≠ L238)
Q9HUU1 Oxaloacetate decarboxylase; EC 4.1.1.112 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see paper)
31% identity, 95% coverage: 7:284/293 of query aligns to 13:280/287 of Q9HUU1
- D88 (= D82) binding
- Y212 (≠ G215) mutation to F: 25-fold increase in substrate affinity and 23-fold decrease in activity.
- H235 (≠ L238) mutation to A: 2-fold increase in substrate affinity and 15-fold decrease in activity.; mutation to Q: No change in substrate affinity and 3-fold decrease in activity.
Q84G06 Phosphonopyruvate hydrolase; PPH; EC 3.11.1.3 from Variovorax sp. (strain Pal2) (see paper)
32% identity, 80% coverage: 1:233/293 of query aligns to 1:233/290 of Q84G06
- D81 (= D82) binding
- R188 (vs. gap) mutation to A: Reduced affinity for substrate.
1pymA Phosphoenolpyruvate mutase from mollusk in with bound mg2-oxalate (see paper)
26% identity, 86% coverage: 7:259/293 of query aligns to 7:256/291 of 1pymA
- active site: W40 (≠ F40), S42 (= S42), G43 (= G43), L44 (≠ F44), D54 (= D55), D81 (= D82), D83 (= D84), C108 (≠ M109), E110 (= E111), K116 (= K117), N118 (≠ C119), S119 (≠ G120), R155 (= R159), H186 (≠ E189), V211 (≠ E214)
- binding oxalate ion: W40 (≠ F40), S42 (= S42), G43 (= G43), L44 (≠ F44), D81 (= D82), R155 (= R159)
1m1bA Crystal structure of phosphoenolpyruvate mutase complexed with sulfopyruvate (see paper)
26% identity, 86% coverage: 7:259/293 of query aligns to 7:256/291 of 1m1bA
- active site: W40 (≠ F40), S42 (= S42), G43 (= G43), L44 (≠ F44), D54 (= D55), D81 (= D82), D83 (= D84), C108 (≠ M109), E110 (= E111), K116 (= K117), N118 (≠ C119), S119 (≠ G120), R155 (= R159), H186 (≠ E189), V211 (≠ E214)
- binding magnesium ion: D81 (= D82), R155 (= R159)
- binding sulfopyruvate: S42 (= S42), G43 (= G43), L44 (≠ F44), D81 (= D82), N118 (≠ C119), S119 (≠ G120), L120 (≠ H121), R155 (= R159)
P56839 Phosphoenolpyruvate phosphomutase; PEP mutase; PEP phosphomutase; Phosphoenolpyruvate mutase; EC 5.4.2.9 from Mytilus edulis (Blue mussel) (see 2 papers)
26% identity, 86% coverage: 7:259/293 of query aligns to 11:260/295 of P56839
- D58 (= D55) mutation D->A,S: Abolishes enzyme activity.; mutation to N: Strongly reduces enzyme activity.
- D85 (= D82) mutation to A: Strongly reduces enzyme activity and increases KM.
- D87 (= D84) mutation to A: Strongly reduces enzyme activity.
- E114 (= E111) mutation to A: Strongly reduces enzyme activity.
- N122 (≠ C119) mutation N->A,D: Strongly reduces enzyme activity.
- R159 (= R159) mutation to A: Strongly reduces enzyme activity.
- H190 (≠ E189) mutation to A: Strongly reduces enzyme activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
Query Sequence
>3607683 FitnessBrowser__Dino:3607683
MSAARTLRSLLAQDRCHVMPCCFDALSAKLIAQEGYDLTFMSGFAASASRIGAPDLGLMS
YGEVVDQARNITEAVDIPLIGDGDTGYGNAMNVRRTVTGFAKAGCASVMIEDQLAPKRCG
HTPGKAVVGRDEAFDRIRAAVDAREEIRAAGGDILILARTDARHEHGLAEAIDRAARFAE
LGADILFVEAPRTEAEMRTVCAELPGPKMANIVEGGATPDLPNAAMHDIGYAIAAYPLSL
MAAAMQAMVRTLRGMRDDRRPDLMDFAELRTRIGFDAYYAASERYASSRRTPD
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