SitesBLAST
Comparing 3607274 FitnessBrowser__Dino:3607274 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)
4iqdA Crystal structure of carboxyvinyl-carboxyphosphonate phosphorylmutase from bacillus anthracis
41% identity, 88% coverage: 16:272/292 of query aligns to 22:285/290 of 4iqdA
- active site: Y46 (= Y40), S48 (= S42), G49 (= G43), A50 (= A44), D60 (= D55), D87 (= D82), D89 (= D84), Q114 (= Q109), E116 (= E111), K122 (= K117), C124 (= C119), G125 (= G120), H126 (= H121), R157 (= R154), E187 (= E184), N209 (= N208)
- binding pyruvic acid: E71 (= E66), R72 (≠ T67), D75 (≠ L70), G165 (= G162), L166 (≠ F163), Y218 (≠ M217), Y219 (≠ K218)
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)
42% identity, 84% coverage: 21:265/292 of query aligns to 24:267/295 of Q56062
- SGG 45:47 (≠ SGA 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 (= R154) binding
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)
40% identity, 87% coverage: 11:265/292 of query aligns to 14:267/296 of P77541
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 270 binding
1mumA Structure of the 2-methylisocitrate lyase (prpb) from escherichia coli (see paper)
40% identity, 87% coverage: 11:265/292 of query aligns to 12:265/289 of 1mumA
- active site: Y41 (= Y40), S43 (= S42), G44 (= G43), G45 (≠ A44), D56 (= D55), D83 (= D82), D85 (= D84), H111 (≠ Q109), E113 (= E111), K119 (= K117), C121 (= C119), G122 (= G120), H123 (= H121), R156 (= R154), E186 (= E184), N208 (= N208), T215 (= T215), L217 (≠ M217)
- 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)
41% identity, 75% coverage: 17:234/292 of query aligns to 20:239/302 of 3fa3B
- active site: Y43 (= Y40), T45 (≠ S42), G46 (= G43), A47 (= A44), D58 (= D55), D86 (= D82), D88 (= D84), H113 (≠ Q109), E115 (= E111), K121 (= K117), C123 (= C119), G124 (= G120), H125 (= H121), R160 (= R154), E190 (= E184), N213 (= N208), T220 (= T215), S222 (≠ M217)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y43 (= Y40), T45 (≠ S42), G46 (= G43), A47 (= A44), D86 (= D82), G124 (= G120), R160 (= R154), E190 (= E184), N213 (= N208), P239 (= P234)
1o5qA Crystal structure of pyruvate and mg2+ bound 2-methylisocitrate lyase (prpb) from salmonella typhimurium (see paper)
39% identity, 84% coverage: 21:265/292 of query aligns to 20:252/271 of 1o5qA
- active site: Y39 (= Y40), S41 (= S42), G42 (= G43), G43 (≠ A44), D54 (= D55), D81 (= D82), D83 (= D84), H109 (≠ Q109), E111 (= E111), R143 (= R154), E173 (≠ Q187), N195 (= N208), T202 (= T215), L204 (≠ M217)
- binding pyruvic acid: Y39 (= Y40), S41 (= S42), G43 (≠ A44), D81 (= D82), R143 (= R154)
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)
38% identity, 88% coverage: 15:272/292 of query aligns to 39:295/318 of Q05957
- D79 (= D55) mutation to A: Reduces catalytic efficiency 1000-fold.
- D107 (≠ T85) binding
- D109 (≠ F87) 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
1zlpA Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
38% identity, 88% coverage: 15:272/292 of query aligns to 12:268/284 of 1zlpA
- active site: F37 (≠ Y40), S39 (= S42), G40 (= G43), Y41 (≠ A44), D52 (= D55), D80 (≠ T85), D82 (≠ F87), F107 (≠ Q109), E109 (= E111), K115 (= K117), C117 (= C119), G118 (= G120), H119 (= H121), R152 (= R154), E182 (= E184), N204 (= N208), T211 (= T215), L213 (≠ M217)
- binding 5-hydroxypentanal: C117 (= C119), G118 (= G120), R152 (= R154), I206 (≠ V210)
- binding magnesium ion: D80 (≠ T85), K115 (= K117)
1zlpB Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
38% identity, 88% coverage: 15:272/292 of query aligns to 12:268/285 of 1zlpB
- active site: F37 (≠ Y40), S39 (= S42), G40 (= G43), Y41 (≠ A44), D52 (= D55), D80 (≠ T85), D82 (≠ F87), F107 (≠ Q109), E109 (= E111), K115 (= K117), C117 (= C119), G118 (= G120), H119 (= H121), R152 (= R154), E182 (= E184), N204 (= N208), T211 (= T215), L213 (≠ M217)
- binding 5-hydroxypentanal: Y41 (≠ A44), C117 (= C119), R152 (= R154), I206 (≠ V210)
6t4vC Crystal structure of 2-methylisocitrate lyase (prpb) from pseudomonas aeruginosa in apo form.
38% identity, 84% coverage: 21:265/292 of query aligns to 22:254/277 of 6t4vC
- active site: Y41 (= Y40), S43 (= S42), G44 (= G43), G45 (≠ A44), D56 (= D55), D83 (= D82), D85 (= D84), H111 (≠ Q109), E113 (= E111), R145 (= R154), E175 (= E184), N197 (= N208), T204 (= T215), L206 (≠ M217)
- binding pyruvic acid: F88 (= F87), N94 (= N92)
3fa3J Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
38% identity, 75% coverage: 17:234/292 of query aligns to 19:230/292 of 3fa3J
- active site: Y42 (= Y40), T44 (≠ S42), G45 (= G43), A46 (= A44), D57 (= D55), D85 (= D82), D87 (= D84), H112 (≠ Q109), E114 (= E111), R151 (= R154), E181 (= E184), N204 (= N208), T211 (= T215), S213 (≠ M217)
- binding manganese (ii) ion: D85 (= D82), D87 (= D84)
3fa4A Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, triclinic crystal form (see paper)
38% identity, 75% coverage: 17:234/292 of query aligns to 20:232/284 of 3fa4A
- active site: Y43 (= Y40), T45 (≠ S42), G46 (= G43), A47 (= A44), D58 (= D55), D86 (= D82), D88 (= D84), H113 (≠ Q109), E115 (= E111), R153 (= R154), E183 (= E184), N206 (= N208), T213 (= T215), S215 (≠ M217)
- binding magnesium ion: D86 (= D82), D88 (= D84)
3m0jA Structure of oxaloacetate acetylhydrolase in complex with the inhibitor 3,3-difluorooxalacetate (see paper)
35% identity, 75% coverage: 16:233/292 of query aligns to 20:240/297 of 3m0jA
- binding calcium ion: E218 (= E211), N219 (≠ G212)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y44 (= Y40), T46 (≠ S42), G47 (= G43), A48 (= A44), D88 (= D82), G126 (= G120), R162 (= R154), E192 (= E184), N215 (= N208)
Sites not aligning to the query:
3m0kA Structure of oxaloacetate acetylhydrolase in complex with the product oxalate (see paper)
34% identity, 75% coverage: 16:233/292 of query aligns to 20:235/289 of 3m0kA
Sites not aligning to the query:
3b8iA Crystal structure of oxaloacetate decarboxylase from pseudomonas aeruginosa (pa4872) in complex with oxalate and mg2+. (see paper)
36% identity, 72% coverage: 22:232/292 of query aligns to 26:230/284 of 3b8iA
- active site: I44 (≠ Y40), G46 (≠ S42), G47 (= G43), S48 (≠ A44), D59 (= D55), D86 (= D82), D88 (= D84), T113 (≠ Q109), E115 (= E111), A121 (≠ K117), F123 (≠ C119), G124 (= G120), R157 (= R154), V186 (≠ E184), M206 (≠ L206)
- binding oxalate ion: S48 (≠ A44), D86 (= D82)
Sites not aligning to the query:
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)
36% identity, 72% coverage: 22:232/292 of query aligns to 28:232/287 of Q9HUU1
- D88 (= D82) binding
- Y212 (≠ G212) mutation to F: 25-fold increase in substrate affinity and 23-fold decrease in activity.
Sites not aligning to the query:
- 235 H→A: 2-fold increase in substrate affinity and 15-fold decrease in activity.; H→Q: No change in substrate affinity and 3-fold decrease in activity.
P56839 Phosphoenolpyruvate phosphomutase; PEP mutase; PEP phosphomutase; Phosphoenolpyruvate mutase; EC 5.4.2.9 from Mytilus edulis (Blue mussel) (see 2 papers)
31% identity, 75% coverage: 23:240/292 of query aligns to 27:244/295 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 (≠ G120) mutation N->A,D: Strongly reduces enzyme activity.
- R159 (= R154) mutation to A: Strongly reduces enzyme activity.
- H190 (≠ E184) mutation to A: Strongly reduces enzyme activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1pymA Phosphoenolpyruvate mutase from mollusk in with bound mg2-oxalate (see paper)
31% identity, 75% coverage: 23:240/292 of query aligns to 23:240/291 of 1pymA
- active site: W40 (≠ Y40), S42 (= S42), G43 (= G43), L44 (≠ A44), D54 (= D55), D81 (= D82), D83 (= D84), C108 (≠ Q109), E110 (= E111), K116 (= K117), N118 (≠ G120), S119 (≠ H121), R155 (= R154), H186 (≠ E184), V211 (≠ N208)
- binding oxalate ion: W40 (≠ Y40), S42 (= S42), G43 (= G43), L44 (≠ A44), D81 (= D82), R155 (= R154)
1m1bA Crystal structure of phosphoenolpyruvate mutase complexed with sulfopyruvate (see paper)
31% identity, 75% coverage: 23:240/292 of query aligns to 23:240/291 of 1m1bA
- active site: W40 (≠ Y40), S42 (= S42), G43 (= G43), L44 (≠ A44), D54 (= D55), D81 (= D82), D83 (= D84), C108 (≠ Q109), E110 (= E111), K116 (= K117), N118 (≠ G120), S119 (≠ H121), R155 (= R154), H186 (≠ E184), V211 (≠ N208)
- binding magnesium ion: D81 (= D82), R155 (= R154)
- binding sulfopyruvate: S42 (= S42), G43 (= G43), L44 (≠ A44), D81 (= D82), N118 (≠ G120), S119 (≠ H121), L120 (= L122), R155 (= R154)
Q84G06 Phosphonopyruvate hydrolase; PPH; EC 3.11.1.3 from Variovorax sp. (strain Pal2) (see paper)
37% identity, 63% coverage: 23:206/292 of query aligns to 23:209/290 of Q84G06
- D81 (= D82) binding
- R188 (≠ P186) mutation to A: Reduced affinity for substrate.
Query Sequence
>3607274 FitnessBrowser__Dino:3607274
MSGPATPCWDFTRPGIVMAPGVYDALTASLAEAAGFPALYLSGAAVSYTRLGRPDIGLTS
VTEMTETLSLIRDRVSTPIIIDADTGFGNALNAQRTMRLYERAGANALQIEDQAYPKRCG
HLADKTLIPAQEMAGKIRAMADARHAAQTLIIARTDAVAVEGFEAAQERAETYLEAGADI
LFIEAPQSEAQLTAIAQRFRGRVPLLANMVEGGETPMKSARELEALGYALVIFPGGIVRA
LARTAEAYYLSLSETGSNAAFRDRMFDFQDLNARLGTAEMLARGKAYEGPGT
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