SitesBLAST
Comparing PP_2334 FitnessBrowser__Putida:PP_2334 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)
6t4vC Crystal structure of 2-methylisocitrate lyase (prpb) from pseudomonas aeruginosa in apo form.
87% identity, 97% coverage: 6:291/296 of query aligns to 3:277/277 of 6t4vC
- active site: Y41 (= Y44), S43 (= S46), G44 (= G47), G45 (= G48), D56 (= D59), D83 (= D86), D85 (= D88), H111 (= H114), E113 (= E116), R145 (= R159), E175 (= E189), N197 (= N211), T204 (= T218), L206 (= L220)
- binding pyruvic acid: F88 (= F91), N94 (= N97)
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)
78% identity, 98% coverage: 6:295/296 of query aligns to 5:294/295 of Q56062
- SGG 45:47 (= SGG 46:48) binding
- D58 (= D59) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- D85 (= D86) binding
- K121 (= K122) mutation to A: 1000-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R122 (= R123) mutation to K: 2-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- C123 (= C124) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- H125 (= H126) 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)
75% identity, 98% coverage: 6:295/296 of query aligns to 5:294/296 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)
76% identity, 97% coverage: 6:292/296 of query aligns to 3:289/289 of 1mumA
- active site: Y41 (= Y44), S43 (= S46), G44 (= G47), G45 (= G48), D56 (= D59), D83 (= D86), D85 (= D88), H111 (= H114), E113 (= E116), K119 (= K122), C121 (= C124), G122 (= G125), H123 (= H126), R156 (= R159), E186 (= E189), N208 (= N211), T215 (= T218), L217 (= L220)
- binding magnesium ion: D56 (= D59), D85 (= D88)
1o5qA Crystal structure of pyruvate and mg2+ bound 2-methylisocitrate lyase (prpb) from salmonella typhimurium (see paper)
74% identity, 95% coverage: 6:287/296 of query aligns to 1:271/271 of 1o5qA
- active site: Y39 (= Y44), S41 (= S46), G42 (= G47), G43 (= G48), D54 (= D59), D81 (= D86), D83 (= D88), H109 (= H114), E111 (= E116), R143 (= R159), E173 (= E189), N195 (= N211), T202 (= T218), L204 (= L220)
- binding pyruvic acid: Y39 (= Y44), S41 (= S46), G43 (= G48), D81 (= D86), R143 (= R159)
4iqdA Crystal structure of carboxyvinyl-carboxyphosphonate phosphorylmutase from bacillus anthracis
48% identity, 93% coverage: 10:285/296 of query aligns to 12:283/290 of 4iqdA
- active site: Y46 (= Y44), S48 (= S46), G49 (= G47), A50 (≠ G48), D60 (= D59), D87 (= D86), D89 (= D88), Q114 (≠ H114), E116 (= E116), K122 (= K122), C124 (= C124), G125 (= G125), H126 (= H126), R157 (= R159), E187 (= E189), N209 (= N211)
- binding pyruvic acid: E71 (≠ T70), R72 (≠ D71), D75 (≠ R74), G165 (= G167), L166 (= L168), Y218 (≠ L220), Y219 (= Y221)
3fa3B Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
38% identity, 79% coverage: 25:259/296 of query aligns to 24:261/302 of 3fa3B
- active site: Y43 (= Y44), T45 (≠ S46), G46 (= G47), A47 (≠ G48), D58 (= D59), D86 (= D86), D88 (= D88), H113 (= H114), E115 (= E116), K121 (= K122), C123 (= C124), G124 (= G125), H125 (= H126), R160 (= R159), E190 (= E189), N213 (= N211), T220 (= T218), S222 (≠ L220)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y43 (= Y44), T45 (≠ S46), G46 (= G47), A47 (≠ G48), D86 (= D86), G124 (= G125), R160 (= R159), E190 (= E189), N213 (= N211), P239 (= P237)
1zlpB Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
35% identity, 88% coverage: 25:283/296 of query aligns to 18:276/285 of 1zlpB
- active site: F37 (≠ Y44), S39 (= S46), G40 (= G47), Y41 (≠ G48), D52 (= D59), D80 (≠ V87), D82 (≠ T89), F107 (≠ H114), E109 (= E116), K115 (= K122), C117 (= C124), G118 (= G125), H119 (= H126), R152 (= R159), E182 (= E189), N204 (= N211), T211 (= T218), L213 (= L220)
- binding 5-hydroxypentanal: Y41 (≠ G48), C117 (= C124), R152 (= R159), I206 (≠ T213)
1zlpA Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
35% identity, 88% coverage: 25:283/296 of query aligns to 18:276/284 of 1zlpA
- active site: F37 (≠ Y44), S39 (= S46), G40 (= G47), Y41 (≠ G48), D52 (= D59), D80 (≠ V87), D82 (≠ T89), F107 (≠ H114), E109 (= E116), K115 (= K122), C117 (= C124), G118 (= G125), H119 (= H126), R152 (= R159), E182 (= E189), N204 (= N211), T211 (= T218), L213 (= L220)
- binding 5-hydroxypentanal: C117 (= C124), G118 (= G125), R152 (= R159), I206 (≠ T213)
- binding magnesium ion: D80 (≠ V87), K115 (= K122)
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)
35% identity, 88% coverage: 25:283/296 of query aligns to 45:303/318 of Q05957
- D79 (= D59) mutation to A: Reduces catalytic efficiency 1000-fold.
- D107 (≠ V87) binding
- D109 (≠ T89) binding
- K142 (= K122) binding
- C144 (= C124) mutation to A: Loss of catalytic activity.
Sites not aligning to the query:
- 1:3 modified: propeptide, Removed in mature form
3fa4A Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, triclinic crystal form (see paper)
36% identity, 79% coverage: 25:259/296 of query aligns to 24:254/284 of 3fa4A
- active site: Y43 (= Y44), T45 (≠ S46), G46 (= G47), A47 (≠ G48), D58 (= D59), D86 (= D86), D88 (= D88), H113 (= H114), E115 (= E116), R153 (= R159), E183 (= E189), N206 (= N211), T213 (= T218), S215 (≠ L220)
- binding magnesium ion: D86 (= D86), D88 (= D88)
3fa3J Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
36% identity, 79% coverage: 25:259/296 of query aligns to 23:252/292 of 3fa3J
- active site: Y42 (= Y44), T44 (≠ S46), G45 (= G47), A46 (≠ G48), D57 (= D59), D85 (= D86), D87 (= D88), H112 (= H114), E114 (= E116), R151 (= R159), E181 (= E189), N204 (= N211), T211 (= T218), S213 (≠ L220)
- binding manganese (ii) ion: D85 (= D86), D87 (= D88)
3m0jA Structure of oxaloacetate acetylhydrolase in complex with the inhibitor 3,3-difluorooxalacetate (see paper)
35% identity, 79% coverage: 25:259/296 of query aligns to 25:263/297 of 3m0jA
- binding calcium ion: E218 (= E214), N219 (≠ F215)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y44 (= Y44), T46 (≠ S46), G47 (= G47), A48 (≠ G48), D88 (= D86), G126 (= G125), R162 (= R159), E192 (= E189), N215 (= N211), S241 (≠ P237)
3m0kA Structure of oxaloacetate acetylhydrolase in complex with the product oxalate (see paper)
34% identity, 79% coverage: 25:259/296 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)
33% identity, 93% coverage: 6:279/296 of query aligns to 2:277/290 of Q84G06
- D81 (= D86) binding
- R188 (vs. gap) mutation to A: Reduced affinity for substrate.
2hjpA Crystal structure of phosphonopyruvate hydrolase complex with phosphonopyruvate and mg++ (see paper)
33% identity, 93% coverage: 6:279/296 of query aligns to 2:270/283 of 2hjpA
- active site: W40 (≠ Y44), S42 (= S46), G43 (= G47), F44 (≠ G48), D54 (= D59), D81 (= D86), D83 (= D88), V108 (≠ H114), E110 (= E116), K116 (= K122), T118 (≠ C124), R148 (= R159), H179 (vs. gap), V204 (≠ N211)
- binding phosphonopyruvate: W40 (≠ Y44), S42 (= S46), F44 (≠ G48), D81 (= D86), R148 (= R159), H179 (vs. gap), R181 (vs. gap)
- binding alpha-D-xylopyranose: E32 (≠ K36), S75 (≠ D80)
2duaA Crystal structure of phosphonopyruvate hydrolase complex with oxalate and mg++ (see paper)
33% identity, 93% coverage: 6:279/296 of query aligns to 2:270/283 of 2duaA
- active site: W40 (≠ Y44), S42 (= S46), G43 (= G47), F44 (≠ G48), D54 (= D59), D81 (= D86), D83 (= D88), V108 (≠ H114), E110 (= E116), K116 (= K122), T118 (≠ C124), R148 (= R159), H179 (vs. gap), V204 (≠ N211)
- binding oxalate ion: W40 (≠ Y44), S42 (= S46), F44 (≠ G48), D81 (= D86), R148 (= R159)
- binding alpha-D-xylopyranose: E32 (≠ K36), S75 (≠ D80)
5uncA The crystal structure of phosphoenolpyruvate phosphomutase from streptomyces platensis subsp. Rosaceus
31% identity, 90% coverage: 21:286/296 of query aligns to 16:281/289 of 5uncA
- active site: W39 (≠ Y44), S41 (= S46), G42 (= G47), L43 (≠ G48), D53 (= D59), D80 (= D86), D82 (= D88), T107 (≠ H114), E109 (= E116), K115 (= K122), N117 (≠ C124), S118 (≠ G125), R153 (= R159), H184 (≠ E189), V209 (≠ N211)
- binding alpha-D-xylopyranose: H22 (≠ I27), N23 (= N28), G26 (≠ H31), L29 (= L34), G239 (≠ M244), V243 (≠ A248)
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, 77% coverage: 32:258/296 of query aligns to 34:252/287 of Q9HUU1
- D88 (= D86) binding
- Y212 (≠ F215) 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.
3b8iA Crystal structure of oxaloacetate decarboxylase from pseudomonas aeruginosa (pa4872) in complex with oxalate and mg2+. (see paper)
31% identity, 77% coverage: 32:258/296 of query aligns to 32:250/284 of 3b8iA
- active site: I44 (≠ Y44), G46 (≠ S46), G47 (= G47), S48 (≠ G48), D59 (= D59), D86 (= D86), D88 (= D88), T113 (≠ H114), E115 (= E116), A121 (≠ K122), F123 (≠ C124), G124 (= G125), R157 (= R159), V186 (≠ E189), M206 (≠ L209)
- binding oxalate ion: S48 (≠ G48), D86 (= D86), H233 (≠ L238)
Query Sequence
>PP_2334 FitnessBrowser__Putida:PP_2334
MTVKSTPGQRFRDAVAAEHPLQVVGAINANHALLAKRAGFKAIYLSGGGVAAGSLGLPDL
GITGLDDVLTDVRRITDVCDLPLLVDVDTGFGASAFNVARTVRSMSKFGAAAIHIEDQVG
AKRCGHRPNKEIVSQQEMVDRIKAAVDARSDDSFVIMARTDALAVEGLNAALDRAQACVE
AGADMIFPEAITELQMYKTFADRVKAPILANITEFGATPLYTTEELASVDVSLVLYPLSA
FRAMNKAAENVYTALRRDGTQKNVIDTMQTRMELYDAIGYHAFEQSLDALFAQKKG
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