SitesBLAST
Comparing PP_1389 FitnessBrowser__Putida:PP_1389 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)
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)
78% identity, 99% coverage: 3:291/291 of query aligns to 1:287/287 of Q9HUU1
- D88 (= D90) binding
- Y212 (= Y214) mutation to F: 25-fold increase in substrate affinity and 23-fold decrease in activity.
- H235 (= H237) 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)
78% identity, 98% coverage: 5:290/291 of query aligns to 1:284/284 of 3b8iA
- active site: I44 (= I48), G46 (= G50), G47 (= G51), S48 (= S52), D59 (= D63), D86 (= D90), D88 (= D92), T113 (= T117), E115 (= E119), A121 (= A125), F123 (= F127), G124 (= G128), R157 (= R161), V186 (= V190), M206 (= M210)
- binding oxalate ion: S48 (= S52), D86 (= D90), H233 (= H237)
4iqdA Crystal structure of carboxyvinyl-carboxyphosphonate phosphorylmutase from bacillus anthracis
32% identity, 90% coverage: 5:265/291 of query aligns to 3:264/290 of 4iqdA
- active site: Y46 (≠ I48), S48 (≠ G50), G49 (= G51), A50 (≠ S52), D60 (= D63), D87 (= D90), D89 (= D92), Q114 (≠ T117), E116 (= E119), K122 (≠ A125), C124 (≠ F127), G125 (= G128), H126 (≠ R129), R157 (= R161), E187 (≠ V190), N209 (vs. gap)
- binding pyruvic acid: E71 (= E74), R72 (≠ Q75), D75 (≠ R78), G165 (≠ S168), L166 (≠ T169), Y218 (≠ L219), Y219 (≠ R220)
2hjpA Crystal structure of phosphonopyruvate hydrolase complex with phosphonopyruvate and mg++ (see paper)
33% identity, 83% coverage: 14:255/291 of query aligns to 6:248/283 of 2hjpA
- active site: W40 (≠ L49), S42 (≠ G51), G43 (≠ S52), F44 (≠ V53), D54 (= D63), D81 (= D90), D83 (= D92), V108 (≠ T117), E110 (= E119), K116 (≠ R129), T118 (≠ S131), R148 (= R161), H179 (≠ V190), V204 (= V212)
- binding phosphonopyruvate: W40 (≠ L49), S42 (≠ G51), F44 (≠ V53), D81 (= D90), R148 (= R161), H179 (≠ V190), R181 (vs. gap)
- binding alpha-D-xylopyranose: E32 (≠ A40), S75 (≠ Q84)
2duaA Crystal structure of phosphonopyruvate hydrolase complex with oxalate and mg++ (see paper)
33% identity, 83% coverage: 14:255/291 of query aligns to 6:248/283 of 2duaA
- active site: W40 (≠ L49), S42 (≠ G51), G43 (≠ S52), F44 (≠ V53), D54 (= D63), D81 (= D90), D83 (= D92), V108 (≠ T117), E110 (= E119), K116 (≠ R129), T118 (≠ S131), R148 (= R161), H179 (≠ V190), V204 (= V212)
- binding oxalate ion: W40 (≠ L49), S42 (≠ G51), F44 (≠ V53), D81 (= D90), R148 (= R161)
- binding alpha-D-xylopyranose: E32 (≠ A40), S75 (≠ Q84)
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)
35% identity, 68% coverage: 14:210/291 of query aligns to 9:208/295 of Q56062
- SGG 45:47 (≠ GGS 50:52) binding
- D58 (= D63) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- D85 (= D90) binding
- K121 (≠ A125) mutation to A: 1000-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R122 (≠ Q126) mutation to K: 2-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- C123 (≠ F127) 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 (= R161) binding
Q84G06 Phosphonopyruvate hydrolase; PPH; EC 3.11.1.3 from Variovorax sp. (strain Pal2) (see paper)
33% identity, 83% coverage: 14:255/291 of query aligns to 6:255/290 of Q84G06
- D81 (= D90) binding
- R188 (vs. gap) mutation to A: Reduced affinity for substrate.
1mumA Structure of the 2-methylisocitrate lyase (prpb) from escherichia coli (see paper)
31% identity, 85% coverage: 14:259/291 of query aligns to 7:259/289 of 1mumA
- active site: Y41 (≠ I48), S43 (≠ G50), G44 (= G51), G45 (≠ S52), D56 (= D63), D83 (= D90), D85 (= D92), H111 (≠ T117), E113 (= E119), K119 (≠ A125), C121 (≠ F127), G122 (= G128), H123 (vs. gap), R156 (= R161), E186 (≠ V190), N208 (vs. gap), T215 (≠ P217), L217 (= L219)
- binding magnesium ion: D56 (= D63), D85 (= D92)
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)
31% identity, 85% coverage: 14:259/291 of query aligns to 9:261/296 of P77541
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 270 binding
1o5qA Crystal structure of pyruvate and mg2+ bound 2-methylisocitrate lyase (prpb) from salmonella typhimurium (see paper)
31% identity, 85% coverage: 14:260/291 of query aligns to 5:247/271 of 1o5qA
- active site: Y39 (≠ I48), S41 (≠ G50), G42 (= G51), G43 (≠ S52), D54 (= D63), D81 (= D90), D83 (= D92), H109 (≠ T117), E111 (= E119), R143 (= R161), E173 (≠ V190), N195 (vs. gap), T202 (≠ P217), L204 (= L219)
- binding pyruvic acid: Y39 (≠ I48), S41 (≠ G50), G43 (≠ S52), D81 (= D90), R143 (= R161)
3fa3B Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
32% identity, 83% coverage: 14:255/291 of query aligns to 8:259/302 of 3fa3B
- active site: Y43 (≠ I48), T45 (≠ G50), G46 (= G51), A47 (≠ S52), D58 (= D63), D86 (= D90), D88 (= D92), H113 (≠ T117), E115 (= E119), K121 (≠ A125), C123 (≠ F127), G124 (= G128), H125 (≠ R129), R160 (= R161), E190 (≠ V190), N213 (vs. gap), T220 (≠ N216), S222 (≠ N218)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y43 (≠ I48), T45 (≠ G50), G46 (= G51), A47 (≠ S52), D86 (= D90), G124 (= G128), R160 (= R161), E190 (≠ V190), N213 (vs. gap), P239 (≠ G236)
3fa4A Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, triclinic crystal form (see paper)
33% identity, 83% coverage: 14:255/291 of query aligns to 8:252/284 of 3fa4A
- active site: Y43 (≠ I48), T45 (≠ G50), G46 (= G51), A47 (≠ S52), D58 (= D63), D86 (= D90), D88 (= D92), H113 (≠ T117), E115 (= E119), R153 (= R161), E183 (≠ V190), N206 (vs. gap), T213 (≠ N216), S215 (≠ N218)
- binding magnesium ion: D86 (= D90), D88 (= D92)
3fa3J Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
32% identity, 83% coverage: 14:255/291 of query aligns to 7:250/292 of 3fa3J
- active site: Y42 (≠ I48), T44 (≠ G50), G45 (= G51), A46 (≠ S52), D57 (= D63), D85 (= D90), D87 (= D92), H112 (≠ T117), E114 (= E119), R151 (= R161), E181 (≠ V190), N204 (vs. gap), T211 (≠ N216), S213 (≠ N218)
- binding manganese (ii) ion: D85 (= D90), D87 (= D92)
6t4vC Crystal structure of 2-methylisocitrate lyase (prpb) from pseudomonas aeruginosa in apo form.
29% identity, 84% coverage: 15:259/291 of query aligns to 8:249/277 of 6t4vC
- active site: Y41 (≠ I48), S43 (≠ G50), G44 (= G51), G45 (≠ S52), D56 (= D63), D83 (= D90), D85 (= D92), H111 (≠ T117), E113 (= E119), R145 (= R161), E175 (≠ V190), N197 (vs. gap), T204 (≠ P217), L206 (= L219)
- binding pyruvic acid: F88 (≠ Y95), N94 (= N100)
1zlpB Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
30% identity, 81% coverage: 30:264/291 of query aligns to 19:258/285 of 1zlpB
- active site: F37 (≠ I48), S39 (≠ G50), G40 (= G51), Y41 (≠ S52), D52 (= D63), D80 (= D90), D82 (= D92), F107 (≠ T117), E109 (= E119), K115 (≠ A125), C117 (≠ F127), G118 (= G128), H119 (≠ R129), R152 (= R161), E182 (≠ V190), N204 (≠ L209), T211 (≠ P217), L213 (= L219)
- binding 5-hydroxypentanal: Y41 (≠ S52), C117 (≠ F127), R152 (= R161), I206 (≠ V212)
1zlpA Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
30% identity, 81% coverage: 30:264/291 of query aligns to 19:258/284 of 1zlpA
- active site: F37 (≠ I48), S39 (≠ G50), G40 (= G51), Y41 (≠ S52), D52 (= D63), D80 (= D90), D82 (= D92), F107 (≠ T117), E109 (= E119), K115 (≠ A125), C117 (≠ F127), G118 (= G128), H119 (≠ R129), R152 (= R161), E182 (≠ V190), N204 (≠ L209), T211 (≠ P217), L213 (= L219)
- binding 5-hydroxypentanal: C117 (≠ F127), G118 (= G128), R152 (= R161), I206 (≠ V212)
- binding magnesium ion: D80 (= D90), K115 (≠ A125)
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)
30% identity, 81% coverage: 30:264/291 of query aligns to 46:285/318 of Q05957
- D79 (= D63) mutation to A: Reduces catalytic efficiency 1000-fold.
- D107 (= D90) binding
- D109 (= D92) binding
- K142 (≠ A125) binding
- C144 (≠ F127) mutation to A: Loss of catalytic activity.
Sites not aligning to the query:
- 1:3 modified: propeptide, Removed in mature form
3m0jA Structure of oxaloacetate acetylhydrolase in complex with the inhibitor 3,3-difluorooxalacetate (see paper)
33% identity, 77% coverage: 29:252/291 of query aligns to 25:260/297 of 3m0jA
- binding calcium ion: E218 (≠ T213), N219 (≠ Y214)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y44 (≠ I48), T46 (≠ G50), G47 (= G51), A48 (≠ S52), D88 (= D90), G126 (= G128), R162 (= R161), E192 (≠ V190), N215 (vs. gap), S241 (≠ G236)
1pymA Phosphoenolpyruvate mutase from mollusk in with bound mg2-oxalate (see paper)
32% identity, 60% coverage: 15:189/291 of query aligns to 7:185/291 of 1pymA
- active site: W40 (≠ L49), S42 (≠ G51), G43 (≠ S52), L44 (≠ V53), D54 (= D63), D81 (= D90), D83 (= D92), C108 (≠ T117), E110 (= E119), K116 (≠ A125), N118 (vs. gap), S119 (vs. gap), R155 (= R161)
- binding oxalate ion: W40 (≠ L49), S42 (≠ G51), G43 (≠ S52), L44 (≠ V53), D81 (= D90), R155 (= R161)
Sites not aligning to the query:
1m1bA Crystal structure of phosphoenolpyruvate mutase complexed with sulfopyruvate (see paper)
32% identity, 60% coverage: 15:189/291 of query aligns to 7:185/291 of 1m1bA
- active site: W40 (≠ L49), S42 (≠ G51), G43 (≠ S52), L44 (≠ V53), D54 (= D63), D81 (= D90), D83 (= D92), C108 (≠ T117), E110 (= E119), K116 (≠ A125), N118 (vs. gap), S119 (vs. gap), R155 (= R161)
- binding magnesium ion: D81 (= D90), R155 (= R161)
- binding sulfopyruvate: S42 (≠ G51), G43 (≠ S52), L44 (≠ V53), D81 (= D90), N118 (vs. gap), S119 (vs. gap), L120 (vs. gap), R155 (= R161)
Sites not aligning to the query:
Query Sequence
>PP_1389 FitnessBrowser__Putida:PP_1389
MIMPKASHQDLRFAFRELLASGSCFHTASVFDPMSARIAADLGFEVGILGGSVASLQVLA
APDFALITLSEFVEQATRIGRVAQLPVLADADHGYGNALNVMRTVIELERAGVAALTIED
TLLPAQFGRKSTDLIPVEEGVGKIRAALEARVDSSLSIIARTNAGVLSTEEIIVRTQSYQ
KAGADGICMVGVKDFEQLEQIAEHLTVPLMLVTYGNPNLRDDERLARLGVRIVVDGHAAY
FAAIKATYDCLRLQRGRQNKSENLSATELSHTYTQPEDYIRWAKEYMSVEE
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