SitesBLAST
Comparing GFF4115 FitnessBrowser__WCS417:GFF4115 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
6t4vC Crystal structure of 2-methylisocitrate lyase (prpb) from pseudomonas aeruginosa in apo form.
86% identity, 96% coverage: 8:293/297 of query aligns to 3:277/277 of 6t4vC
- active site: Y41 (= Y46), S43 (= S48), G44 (= G49), G45 (= G50), D56 (= D61), D83 (= D88), D85 (= D90), H111 (= H116), E113 (= E118), R145 (= R161), E175 (= E191), N197 (= N213), T204 (= T220), L206 (= L222)
- binding pyruvic acid: F88 (= F93), N94 (= N99)
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)
76% identity, 98% coverage: 8:297/297 of query aligns to 5:294/295 of Q56062
- SGG 45:47 (= SGG 48:50) binding
- D58 (= D61) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- D85 (= D88) binding
- K121 (= K124) mutation to A: 1000-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R122 (= R125) mutation to K: 2-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- C123 (= C126) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- H125 (= H128) mutation to A: 750-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R158 (= R161) 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)
75% identity, 97% coverage: 8:294/297 of query aligns to 5:291/296 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)
75% identity, 97% coverage: 8:294/297 of query aligns to 3:289/289 of 1mumA
- active site: Y41 (= Y46), S43 (= S48), G44 (= G49), G45 (= G50), D56 (= D61), D83 (= D88), D85 (= D90), H111 (= H116), E113 (= E118), K119 (= K124), C121 (= C126), G122 (= G127), H123 (= H128), R156 (= R161), E186 (= E191), N208 (= N213), T215 (= T220), L217 (= L222)
- binding magnesium ion: D56 (= D61), D85 (= D90)
1o5qA Crystal structure of pyruvate and mg2+ bound 2-methylisocitrate lyase (prpb) from salmonella typhimurium (see paper)
73% identity, 95% coverage: 8:289/297 of query aligns to 1:271/271 of 1o5qA
- active site: Y39 (= Y46), S41 (= S48), G42 (= G49), G43 (= G50), D54 (= D61), D81 (= D88), D83 (= D90), H109 (= H116), E111 (= E118), R143 (= R161), E173 (= E191), N195 (= N213), T202 (= T220), L204 (= L222)
- binding pyruvic acid: Y39 (= Y46), S41 (= S48), G43 (= G50), D81 (= D88), R143 (= R161)
4iqdA Crystal structure of carboxyvinyl-carboxyphosphonate phosphorylmutase from bacillus anthracis
47% identity, 93% coverage: 12:287/297 of query aligns to 12:283/290 of 4iqdA
- active site: Y46 (= Y46), S48 (= S48), G49 (= G49), A50 (≠ G50), D60 (= D61), D87 (= D88), D89 (= D90), Q114 (≠ H116), E116 (= E118), K122 (= K124), C124 (= C126), G125 (= G127), H126 (= H128), R157 (= R161), E187 (= E191), N209 (= N213)
- binding pyruvic acid: E71 (≠ T72), R72 (≠ D73), D75 (≠ R76), G165 (= G169), L166 (= L170), Y218 (≠ L222), Y219 (= Y223)
3fa3B Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
38% identity, 79% coverage: 27:261/297 of query aligns to 24:261/302 of 3fa3B
- active site: Y43 (= Y46), T45 (≠ S48), G46 (= G49), A47 (≠ G50), D58 (= D61), D86 (= D88), D88 (= D90), H113 (= H116), E115 (= E118), K121 (= K124), C123 (= C126), G124 (= G127), H125 (= H128), R160 (= R161), E190 (= E191), N213 (= N213), T220 (= T220), S222 (≠ L222)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y43 (= Y46), T45 (≠ S48), G46 (= G49), A47 (≠ G50), D86 (= D88), G124 (= G127), R160 (= R161), E190 (= E191), N213 (= N213), P239 (= P239)
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)
34% identity, 87% coverage: 27:285/297 of query aligns to 45:303/318 of Q05957
- D79 (= D61) mutation to A: Reduces catalytic efficiency 1000-fold.
- D107 (≠ V89) binding
- D109 (≠ T91) binding
- K142 (= K124) binding
- C144 (= C126) mutation to A: Loss of catalytic activity.
Sites not aligning to the query:
- 1:3 modified: propeptide, Removed in mature form
1zlpB Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
34% identity, 87% coverage: 27:285/297 of query aligns to 18:276/285 of 1zlpB
- active site: F37 (≠ Y46), S39 (= S48), G40 (= G49), Y41 (≠ G50), D52 (= D61), D80 (≠ V89), D82 (≠ T91), F107 (≠ H116), E109 (= E118), K115 (= K124), C117 (= C126), G118 (= G127), H119 (= H128), R152 (= R161), E182 (= E191), N204 (= N213), T211 (= T220), L213 (= L222)
- binding 5-hydroxypentanal: Y41 (≠ G50), C117 (= C126), R152 (= R161), I206 (≠ T215)
1zlpA Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
34% identity, 87% coverage: 27:285/297 of query aligns to 18:276/284 of 1zlpA
- active site: F37 (≠ Y46), S39 (= S48), G40 (= G49), Y41 (≠ G50), D52 (= D61), D80 (≠ V89), D82 (≠ T91), F107 (≠ H116), E109 (= E118), K115 (= K124), C117 (= C126), G118 (= G127), H119 (= H128), R152 (= R161), E182 (= E191), N204 (= N213), T211 (= T220), L213 (= L222)
- binding 5-hydroxypentanal: C117 (= C126), G118 (= G127), R152 (= R161), I206 (≠ T215)
- binding magnesium ion: D80 (≠ V89), K115 (= K124)
3m0jA Structure of oxaloacetate acetylhydrolase in complex with the inhibitor 3,3-difluorooxalacetate (see paper)
35% identity, 79% coverage: 27:261/297 of query aligns to 25:263/297 of 3m0jA
- binding calcium ion: E218 (= E216), N219 (≠ F217)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y44 (= Y46), T46 (≠ S48), G47 (= G49), A48 (≠ G50), D88 (= D88), G126 (= G127), R162 (= R161), E192 (= E191), N215 (= N213), S241 (≠ P239)
3fa4A Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, triclinic crystal form (see paper)
36% identity, 79% coverage: 27:261/297 of query aligns to 24:254/284 of 3fa4A
- active site: Y43 (= Y46), T45 (≠ S48), G46 (= G49), A47 (≠ G50), D58 (= D61), D86 (= D88), D88 (= D90), H113 (= H116), E115 (= E118), R153 (= R161), E183 (= E191), N206 (= N213), T213 (= T220), S215 (≠ L222)
- binding magnesium ion: D86 (= D88), D88 (= D90)
3fa3J Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
36% identity, 79% coverage: 27:261/297 of query aligns to 23:252/292 of 3fa3J
- active site: Y42 (= Y46), T44 (≠ S48), G45 (= G49), A46 (≠ G50), D57 (= D61), D85 (= D88), D87 (= D90), H112 (= H116), E114 (= E118), R151 (= R161), E181 (= E191), N204 (= N213), T211 (= T220), S213 (≠ L222)
- binding manganese (ii) ion: D85 (= D88), D87 (= D90)
3m0kA Structure of oxaloacetate acetylhydrolase in complex with the product oxalate (see paper)
34% identity, 79% coverage: 27:261/297 of query aligns to 25:258/289 of 3m0kA
Q84G06 Phosphonopyruvate hydrolase; PPH; EC 3.11.1.3 from Variovorax sp. (strain Pal2) (see paper)
37% identity, 87% coverage: 8:266/297 of query aligns to 2:262/290 of Q84G06
- D81 (= D88) binding
- R188 (= R205) mutation to A: Reduced affinity for substrate.
2hjpA Crystal structure of phosphonopyruvate hydrolase complex with phosphonopyruvate and mg++ (see paper)
37% identity, 87% coverage: 8:266/297 of query aligns to 2:255/283 of 2hjpA
- active site: W40 (≠ Y46), S42 (= S48), G43 (= G49), F44 (≠ G50), D54 (= D61), D81 (= D88), D83 (= D90), V108 (≠ H116), E110 (= E118), K116 (= K124), T118 (≠ C126), R148 (= R161), H179 (≠ A203), V204 (vs. gap)
- binding phosphonopyruvate: W40 (≠ Y46), S42 (= S48), F44 (≠ G50), D81 (= D88), R148 (= R161), H179 (≠ A203), R181 (= R205)
- binding alpha-D-xylopyranose: E32 (≠ K38), S75 (≠ D82)
2duaA Crystal structure of phosphonopyruvate hydrolase complex with oxalate and mg++ (see paper)
37% identity, 87% coverage: 8:266/297 of query aligns to 2:255/283 of 2duaA
- active site: W40 (≠ Y46), S42 (= S48), G43 (= G49), F44 (≠ G50), D54 (= D61), D81 (= D88), D83 (= D90), V108 (≠ H116), E110 (= E118), K116 (= K124), T118 (≠ C126), R148 (= R161), H179 (≠ A203), V204 (vs. gap)
- binding oxalate ion: W40 (≠ Y46), S42 (= S48), F44 (≠ G50), D81 (= D88), R148 (= R161)
- binding alpha-D-xylopyranose: E32 (≠ K38), S75 (≠ D82)
P56839 Phosphoenolpyruvate phosphomutase; PEP mutase; PEP phosphomutase; Phosphoenolpyruvate mutase; EC 5.4.2.9 from Mytilus edulis (Blue mussel) (see 2 papers)
30% identity, 85% coverage: 25:277/297 of query aligns to 23:276/295 of P56839
- D58 (= D61) mutation D->A,S: Abolishes enzyme activity.; mutation to N: Strongly reduces enzyme activity.
- D85 (= D88) mutation to A: Strongly reduces enzyme activity and increases KM.
- D87 (= D90) mutation to A: Strongly reduces enzyme activity.
- E114 (= E118) mutation to A: Strongly reduces enzyme activity.
- N122 (≠ C126) mutation N->A,D: Strongly reduces enzyme activity.
- R159 (= R161) mutation to A: Strongly reduces enzyme activity.
- H190 (≠ E191) 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)
30% identity, 85% coverage: 25:277/297 of query aligns to 19:272/291 of 1pymA
- active site: W40 (≠ Y46), S42 (= S48), G43 (= G49), L44 (≠ G50), D54 (= D61), D81 (= D88), D83 (= D90), C108 (≠ H116), E110 (= E118), K116 (= K124), N118 (≠ C126), S119 (≠ G127), R155 (= R161), H186 (≠ E191), V211 (≠ N213)
- binding oxalate ion: W40 (≠ Y46), S42 (= S48), G43 (= G49), L44 (≠ G50), D81 (= D88), R155 (= R161)
1m1bA Crystal structure of phosphoenolpyruvate mutase complexed with sulfopyruvate (see paper)
30% identity, 85% coverage: 25:277/297 of query aligns to 19:272/291 of 1m1bA
- active site: W40 (≠ Y46), S42 (= S48), G43 (= G49), L44 (≠ G50), D54 (= D61), D81 (= D88), D83 (= D90), C108 (≠ H116), E110 (= E118), K116 (= K124), N118 (≠ C126), S119 (≠ G127), R155 (= R161), H186 (≠ E191), V211 (≠ N213)
- binding magnesium ion: D81 (= D88), R155 (= R161)
- binding sulfopyruvate: S42 (= S48), G43 (= G49), L44 (≠ G50), D81 (= D88), N118 (≠ C126), S119 (≠ G127), L120 (≠ H128), R155 (= R161)
Query Sequence
>GFF4115 FitnessBrowser__WCS417:GFF4115
MSSNNKTTPGQRFRDAVASEHPLQVVGAINANHALLAKRAGFKAIYLSGGGVAAGSLGVP
DLGITGLDDVLTDVRRITDVCDLPLLVDVDTGFGSSAFNVARTVKSMIKFGAAAIHIEDQ
VGAKRCGHRPNKEIVSQQEMVDRIKAAVDARTDDSFVIMARTDALAVEGLESALERAAAC
IEAGADMVFPEAITELEMYKLFASRVKAPILANITEFGATPLYATEQLKSADVSIVLYPL
SAFRAMNKAAENVYTAIRRDGTQQNVIDTMQTRMELYDRIDYHTFEQKLDALFAAKK
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