SitesBLAST
Comparing GFF2686 FitnessBrowser__WCS417:GFF2686 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)
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)
76% identity, 100% coverage: 1:289/289 of query aligns to 1:287/287 of Q9HUU1
- D88 (= D88) binding
- Y212 (= Y212) mutation to F: 25-fold increase in substrate affinity and 23-fold decrease in activity.
- H235 (= H235) 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.
3b8iA Crystal structure of oxaloacetate decarboxylase from pseudomonas aeruginosa (pa4872) in complex with oxalate and mg2+. (see paper)
76% identity, 99% coverage: 3:288/289 of query aligns to 1:284/284 of 3b8iA
- active site: I44 (= I46), G46 (= G48), G47 (= G49), S48 (= S50), D59 (= D61), D86 (= D88), D88 (= D90), T113 (= T115), E115 (= E117), A121 (= A123), F123 (= F125), G124 (= G126), R157 (= R159), V186 (= V188), M206 (= M208)
- binding oxalate ion: S48 (= S50), D86 (= D88), H233 (= H235)
4iqdA Crystal structure of carboxyvinyl-carboxyphosphonate phosphorylmutase from bacillus anthracis
33% identity, 79% coverage: 5:232/289 of query aligns to 5:233/290 of 4iqdA
- active site: Y46 (≠ I46), S48 (≠ G48), G49 (= G49), A50 (≠ S50), D60 (= D61), D87 (= D88), D89 (= D90), Q114 (≠ T115), E116 (= E117), K122 (≠ A123), C124 (≠ F125), G125 (= G126), H126 (≠ R127), R157 (= R159), E187 (≠ V188), N209 (vs. gap)
- binding pyruvic acid: E71 (= E72), R72 (≠ Q73), D75 (≠ R76), G165 (≠ P166), L166 (≠ T167), Y218 (≠ L217), Y219 (≠ N218)
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)
34% identity, 68% coverage: 13:208/289 of query aligns to 10:208/295 of Q56062
- SGG 45:47 (≠ GGS 48:50) binding
- D58 (= D61) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- D85 (= D88) binding
- K121 (≠ A123) mutation to A: 1000-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R122 (≠ Q124) mutation to K: 2-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- C123 (≠ F125) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- H125 (vs. gap) mutation to A: 750-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R158 (= R159) 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)
30% identity, 84% coverage: 11:252/289 of query aligns to 8:257/296 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)
30% identity, 84% coverage: 11:252/289 of query aligns to 6:255/289 of 1mumA
- active site: Y41 (≠ I46), S43 (≠ G48), G44 (= G49), G45 (≠ S50), D56 (= D61), D83 (= D88), D85 (= D90), H111 (≠ T115), E113 (= E117), K119 (≠ A123), C121 (≠ F125), G122 (= G126), H123 (vs. gap), R156 (= R159), E186 (≠ V188), N208 (vs. gap), T215 (≠ P215), L217 (= L217)
- binding magnesium ion: D56 (= D61), D85 (= D90)
1o5qA Crystal structure of pyruvate and mg2+ bound 2-methylisocitrate lyase (prpb) from salmonella typhimurium (see paper)
33% identity, 69% coverage: 11:208/289 of query aligns to 4:193/271 of 1o5qA
- active site: Y39 (≠ I46), S41 (≠ G48), G42 (= G49), G43 (≠ S50), D54 (= D61), D81 (= D88), D83 (= D90), H109 (≠ T115), E111 (= E117), R143 (= R159), E173 (≠ V188)
- binding pyruvic acid: Y39 (≠ I46), S41 (≠ G48), G43 (≠ S50), D81 (= D88), R143 (= R159)
Sites not aligning to the query:
6t4vC Crystal structure of 2-methylisocitrate lyase (prpb) from pseudomonas aeruginosa in apo form.
30% identity, 84% coverage: 11:254/289 of query aligns to 6:243/277 of 6t4vC
- active site: Y41 (≠ I46), S43 (≠ G48), G44 (= G49), G45 (≠ S50), D56 (= D61), D83 (= D88), D85 (= D90), H111 (≠ T115), E113 (= E117), R145 (= R159), E175 (≠ V188), N197 (vs. gap), T204 (≠ P215), L206 (= L217)
- binding pyruvic acid: F88 (≠ Y93), N94 (= N98)
5uncA The crystal structure of phosphoenolpyruvate phosphomutase from streptomyces platensis subsp. Rosaceus
36% identity, 52% coverage: 12:162/289 of query aligns to 5:156/289 of 5uncA
- active site: W39 (≠ L47), S41 (≠ G49), G42 (≠ S50), L43 (≠ V51), D53 (= D61), D80 (= D88), D82 (= D90), T107 (= T115), E109 (= E117), K115 (≠ A123), N117 (vs. gap), S118 (≠ Q124), R153 (= R159)
- binding alpha-D-xylopyranose: H22 (≠ F29), N23 (≠ D30), G26 (≠ S33), L29 (≠ I36)
Sites not aligning to the query:
2hjpA Crystal structure of phosphonopyruvate hydrolase complex with phosphonopyruvate and mg++ (see paper)
33% identity, 75% coverage: 30:245/289 of query aligns to 24:239/283 of 2hjpA
- active site: W40 (≠ L47), S42 (≠ G49), G43 (≠ S50), F44 (≠ V51), D54 (= D61), D81 (= D88), D83 (= D90), V108 (≠ T115), E110 (= E117), K116 (≠ R127), T118 (≠ S129), R148 (= R159), H179 (≠ E194), V204 (= V210)
- binding phosphonopyruvate: W40 (≠ L47), S42 (≠ G49), F44 (≠ V51), D81 (= D88), R148 (= R159), H179 (≠ E194), R181 (≠ L196)
- binding alpha-D-xylopyranose: E32 (≠ A38), S75 (≠ Q82)
2duaA Crystal structure of phosphonopyruvate hydrolase complex with oxalate and mg++ (see paper)
33% identity, 75% coverage: 30:245/289 of query aligns to 24:239/283 of 2duaA
- active site: W40 (≠ L47), S42 (≠ G49), G43 (≠ S50), F44 (≠ V51), D54 (= D61), D81 (= D88), D83 (= D90), V108 (≠ T115), E110 (= E117), K116 (≠ R127), T118 (≠ S129), R148 (= R159), H179 (≠ E194), V204 (= V210)
- binding oxalate ion: W40 (≠ L47), S42 (≠ G49), F44 (≠ V51), D81 (= D88), R148 (= R159)
- binding alpha-D-xylopyranose: E32 (≠ A38), S75 (≠ Q82)
Q84G06 Phosphonopyruvate hydrolase; PPH; EC 3.11.1.3 from Variovorax sp. (strain Pal2) (see paper)
32% identity, 75% coverage: 30:247/289 of query aligns to 24:248/290 of Q84G06
- D81 (= D88) binding
- R188 (≠ L196) mutation to A: Reduced affinity for substrate.
3m0jA Structure of oxaloacetate acetylhydrolase in complex with the inhibitor 3,3-difluorooxalacetate (see paper)
32% identity, 83% coverage: 11:250/289 of query aligns to 8:260/297 of 3m0jA
- binding calcium ion: E218 (≠ T211), N219 (≠ Y212)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y44 (≠ I46), T46 (≠ G48), G47 (= G49), A48 (≠ S50), D88 (= D88), G126 (= G126), R162 (= R159), E192 (≠ V188), N215 (vs. gap), S241 (vs. gap)
3fa3B Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
30% identity, 82% coverage: 13:250/289 of query aligns to 9:258/302 of 3fa3B
- active site: Y43 (≠ I46), T45 (≠ G48), G46 (= G49), A47 (≠ S50), D58 (= D61), D86 (= D88), D88 (= D90), H113 (≠ T115), E115 (= E117), K121 (≠ A123), C123 (≠ F125), G124 (= G126), H125 (≠ R127), R160 (= R159), E190 (≠ V188), N213 (vs. gap), T220 (≠ P215), S222 (≠ L217)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y43 (≠ I46), T45 (≠ G48), G46 (= G49), A47 (≠ S50), D86 (= D88), G124 (= G126), R160 (= R159), E190 (≠ V188), N213 (vs. gap), P239 (vs. gap)
3m0kA Structure of oxaloacetate acetylhydrolase in complex with the product oxalate (see paper)
32% identity, 83% coverage: 11:250/289 of query aligns to 8:255/289 of 3m0kA
3fa4A Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, triclinic crystal form (see paper)
30% identity, 83% coverage: 12:250/289 of query aligns to 8:251/284 of 3fa4A
- active site: Y43 (≠ I46), T45 (≠ G48), G46 (= G49), A47 (≠ S50), D58 (= D61), D86 (= D88), D88 (= D90), H113 (≠ T115), E115 (= E117), R153 (= R159), E183 (≠ V188), N206 (vs. gap), T213 (≠ P215), S215 (≠ L217)
- binding magnesium ion: D86 (= D88), D88 (= D90)
P56839 Phosphoenolpyruvate phosphomutase; PEP mutase; PEP phosphomutase; Phosphoenolpyruvate mutase; EC 5.4.2.9 from Mytilus edulis (Blue mussel) (see 2 papers)
31% identity, 80% coverage: 32:262/289 of query aligns to 30:269/295 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 (= E117) mutation to A: Strongly reduces enzyme activity.
- N122 (vs. gap) mutation N->A,D: Strongly reduces enzyme activity.
- R159 (= R159) mutation to A: Strongly reduces enzyme activity.
- H190 (vs. gap) 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, 80% coverage: 32:262/289 of query aligns to 26:265/291 of 1pymA
- active site: W40 (≠ L47), S42 (≠ G49), G43 (≠ S50), L44 (≠ V51), D54 (= D61), D81 (= D88), D83 (= D90), C108 (≠ T115), E110 (= E117), K116 (≠ A123), N118 (vs. gap), S119 (vs. gap), R155 (= R159), H186 (vs. gap), V211 (= V210)
- binding oxalate ion: W40 (≠ L47), S42 (≠ G49), G43 (≠ S50), L44 (≠ V51), D81 (= D88), R155 (= R159)
1m1bA Crystal structure of phosphoenolpyruvate mutase complexed with sulfopyruvate (see paper)
31% identity, 80% coverage: 32:262/289 of query aligns to 26:265/291 of 1m1bA
- active site: W40 (≠ L47), S42 (≠ G49), G43 (≠ S50), L44 (≠ V51), D54 (= D61), D81 (= D88), D83 (= D90), C108 (≠ T115), E110 (= E117), K116 (≠ A123), N118 (vs. gap), S119 (vs. gap), R155 (= R159), H186 (vs. gap), V211 (= V210)
- binding magnesium ion: D81 (= D88), R155 (= R159)
- binding sulfopyruvate: S42 (≠ G49), G43 (≠ S50), L44 (≠ V51), D81 (= D88), N118 (vs. gap), S119 (vs. gap), L120 (vs. gap), R155 (= R159)
3fa3J Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
29% identity, 83% coverage: 12:250/289 of query aligns to 7:249/292 of 3fa3J
- active site: Y42 (≠ I46), T44 (≠ G48), G45 (= G49), A46 (≠ S50), D57 (= D61), D85 (= D88), D87 (= D90), H112 (≠ T115), E114 (= E117), R151 (= R159), E181 (≠ V188), N204 (vs. gap), T211 (≠ P215), S213 (≠ L217)
- binding manganese (ii) ion: D85 (= D88), D87 (= D90)
Query Sequence
>GFF2686 FitnessBrowser__WCS417:GFF2686
MPKISHSALRRKFRELLATPTCVETASVFDPMSARIAADLGFEVGILGGSVASLQVLAAP
DFALITLSEFVEQATRIGRVAQLPFIADADHGYGNALNVMRTVEELERAGVAALTIEDTL
LPAQFGRKSTDLISIEEGIGKVRAALEARVDPQLSIIARTNAGVLPTEAVIERTLAYQQA
GADGICMVGVADFEHLEKIAENLTVPLMLVTYGNPKLNDAKRLASLGVRVVVAGHGAYFA
AIKATYDSLRAQRQLTHSTDNLSATELTHTYTLPESYVAWAEEFMDVKE
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