SitesBLAST
Comparing WP_090272481.1 NCBI__GCF_900105005.1:WP_090272481.1 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)
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)
70% identity, 98% coverage: 4:290/294 of query aligns to 5:291/296 of P77541
- SGG 45:47 (= SGG 44:46) binding substrate
- D85 (= D84) binding Mg(2+)
- D87 (= D86) binding Mg(2+)
- C123 (= C122) mutation to S: Inactive.
- CG 123:124 (= CG 122:123) binding substrate
- R158 (= R157) binding substrate
- E188 (= E187) binding substrate
- NIT 210:212 (= NIT 209:211) binding substrate
- R241 (= R240) binding substrate
- R270 (= R269) binding substrate
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
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)
71% identity, 97% coverage: 4:289/294 of query aligns to 5:290/295 of Q56062
- SGG 45:47 (= SGG 44:46) binding substrate
- D58 (= D57) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- D85 (= D84) binding Mg(2+)
- K121 (= K120) mutation to A: 1000-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R122 (= R121) mutation to K: 2-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- C123 (= C122) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- H125 (= H124) mutation to A: 750-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R158 (= R157) binding substrate
1mumA Structure of the 2-methylisocitrate lyase (prpb) from escherichia coli (see paper)
70% identity, 98% coverage: 4:290/294 of query aligns to 3:289/289 of 1mumA
- active site: Y41 (= Y42), S43 (= S44), G44 (= G45), G45 (= G46), D56 (= D57), D83 (= D84), D85 (= D86), H111 (= H112), E113 (= E114), K119 (= K120), C121 (= C122), G122 (= G123), H123 (= H124), R156 (= R157), E186 (= E187), N208 (= N209), T215 (= T216), L217 (= L218)
- binding magnesium ion: D56 (= D57), D85 (= D86)
6t4vC Crystal structure of 2-methylisocitrate lyase (prpb) from pseudomonas aeruginosa in apo form.
70% identity, 97% coverage: 4:289/294 of query aligns to 3:277/277 of 6t4vC
- active site: Y41 (= Y42), S43 (= S44), G44 (= G45), G45 (= G46), D56 (= D57), D83 (= D84), D85 (= D86), H111 (= H112), E113 (= E114), R145 (= R157), E175 (= E187), N197 (= N209), T204 (= T216), L206 (= L218)
- binding pyruvic acid: F88 (= F89), N94 (= N95)
1o5qA Crystal structure of pyruvate and mg2+ bound 2-methylisocitrate lyase (prpb) from salmonella typhimurium (see paper)
67% identity, 96% coverage: 4:285/294 of query aligns to 1:271/271 of 1o5qA
- active site: Y39 (= Y42), S41 (= S44), G42 (= G45), G43 (= G46), D54 (= D57), D81 (= D84), D83 (= D86), H109 (= H112), E111 (= E114), R143 (= R157), E173 (= E187), N195 (= N209), T202 (= T216), L204 (= L218)
- binding pyruvic acid: Y39 (= Y42), S41 (= S44), G43 (= G46), D81 (= D84), R143 (= R157)
4iqdA Crystal structure of carboxyvinyl-carboxyphosphonate phosphorylmutase from bacillus anthracis
45% identity, 94% coverage: 8:282/294 of query aligns to 12:282/290 of 4iqdA
- active site: Y46 (= Y42), S48 (= S44), G49 (= G45), A50 (≠ G46), D60 (= D57), D87 (= D84), D89 (= D86), Q114 (≠ H112), E116 (= E114), K122 (= K120), C124 (= C122), G125 (= G123), H126 (= H124), R157 (= R157), E187 (= E187), N209 (= N209)
- binding pyruvic acid: E71 (≠ I68), R72 (≠ D69), D75 (≠ R72), G165 (= G165), L166 (≠ V166), Y218 (≠ L218), Y219 (≠ F219)
1zlpA Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
36% identity, 88% coverage: 23:281/294 of query aligns to 18:276/284 of 1zlpA
- active site: F37 (≠ Y42), S39 (= S44), G40 (= G45), Y41 (≠ G46), D52 (= D57), D80 (≠ I85), D82 (≠ T87), F107 (≠ H112), E109 (= E114), K115 (= K120), C117 (= C122), G118 (= G123), H119 (= H124), R152 (= R157), E182 (= E187), N204 (= N209), T211 (= T216), L213 (= L218)
- binding 5-hydroxypentanal: C117 (= C122), G118 (= G123), R152 (= R157), I206 (≠ T211)
- binding magnesium ion: D80 (≠ I85), K115 (= K120)
1zlpB Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
36% identity, 88% coverage: 23:281/294 of query aligns to 18:276/285 of 1zlpB
- active site: F37 (≠ Y42), S39 (= S44), G40 (= G45), Y41 (≠ G46), D52 (= D57), D80 (≠ I85), D82 (≠ T87), F107 (≠ H112), E109 (= E114), K115 (= K120), C117 (= C122), G118 (= G123), H119 (= H124), R152 (= R157), E182 (= E187), N204 (= N209), T211 (= T216), L213 (= L218)
- binding 5-hydroxypentanal: Y41 (≠ G46), C117 (= C122), R152 (= R157), I206 (≠ T211)
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)
36% identity, 88% coverage: 23:281/294 of query aligns to 45:303/318 of Q05957
- D79 (= D57) mutation to A: Reduces catalytic efficiency 1000-fold.
- D107 (≠ I85) binding Mg(2+)
- D109 (≠ T87) binding Mg(2+)
- K142 (= K120) binding Mg(2+)
- C144 (= C122) mutation to A: Loss of catalytic activity.
Sites not aligning to the query:
- 1:3 modified: propeptide, Removed in mature form
3fa3B Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
36% identity, 86% coverage: 4:257/294 of query aligns to 4:261/302 of 3fa3B
- active site: Y43 (= Y42), T45 (≠ S44), G46 (= G45), A47 (≠ G46), D58 (= D57), D86 (= D84), D88 (= D86), H113 (= H112), E115 (= E114), K121 (= K120), C123 (= C122), G124 (= G123), H125 (= H124), R160 (= R157), E190 (= E187), N213 (= N209), T220 (= T216), S222 (≠ L218)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y43 (= Y42), T45 (≠ S44), G46 (= G45), A47 (≠ G46), D86 (= D84), G124 (= G123), R160 (= R157), E190 (= E187), N213 (= N209), P239 (= P235)
3m0jA Structure of oxaloacetate acetylhydrolase in complex with the inhibitor 3,3-difluorooxalacetate (see paper)
36% identity, 85% coverage: 7:257/294 of query aligns to 8:263/297 of 3m0jA
- binding calcium ion: E218 (= E212), N219 (≠ F213)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y44 (= Y42), T46 (≠ S44), G47 (= G45), A48 (≠ G46), D88 (= D84), G126 (= G123), R162 (= R157), E192 (= E187), N215 (= N209), S241 (≠ P235)
3fa4A Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, triclinic crystal form (see paper)
34% identity, 86% coverage: 4:257/294 of query aligns to 4:254/284 of 3fa4A
- active site: Y43 (= Y42), T45 (≠ S44), G46 (= G45), A47 (≠ G46), D58 (= D57), D86 (= D84), D88 (= D86), H113 (= H112), E115 (= E114), R153 (= R157), E183 (= E187), N206 (= N209), T213 (= T216), S215 (≠ L218)
- binding magnesium ion: D86 (= D84), D88 (= D86)
3m0kA Structure of oxaloacetate acetylhydrolase in complex with the product oxalate (see paper)
35% identity, 85% coverage: 7:257/294 of query aligns to 8:258/289 of 3m0kA
3fa3J Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
33% identity, 86% coverage: 4:257/294 of query aligns to 3:252/292 of 3fa3J
- active site: Y42 (= Y42), T44 (≠ S44), G45 (= G45), A46 (≠ G46), D57 (= D57), D85 (= D84), D87 (= D86), H112 (= H112), E114 (= E114), R151 (= R157), E181 (= E187), N204 (= N209), T211 (= T216), S213 (≠ L218)
- binding manganese (ii) ion: D85 (= D84), D87 (= D86)
P56839 Phosphoenolpyruvate phosphomutase; PEP mutase; PEP phosphomutase; Phosphoenolpyruvate mutase; EC 5.4.2.9 from Mytilus edulis (Blue mussel) (see 2 papers)
29% identity, 90% coverage: 8:273/294 of query aligns to 10:276/295 of P56839
- D58 (= D57) mutation D->A,S: Abolishes enzyme activity.; mutation to N: Strongly reduces enzyme activity.
- D85 (= D84) mutation to A: Strongly reduces enzyme activity and increases KM.
- D87 (= D86) mutation to A: Strongly reduces enzyme activity.
- E114 (= E114) mutation to A: Strongly reduces enzyme activity.
- N122 (≠ C122) mutation N->A,D: Strongly reduces enzyme activity.
- R159 (= R157) mutation to A: Strongly reduces enzyme activity.
- H190 (≠ E187) 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)
29% identity, 90% coverage: 8:273/294 of query aligns to 6:272/291 of 1pymA
- active site: W40 (≠ Y42), S42 (= S44), G43 (= G45), L44 (≠ G46), D54 (= D57), D81 (= D84), D83 (= D86), C108 (≠ H112), E110 (= E114), K116 (= K120), N118 (≠ C122), S119 (≠ G123), R155 (= R157), H186 (≠ E187), V211 (≠ N209)
- binding oxalate ion: W40 (≠ Y42), S42 (= S44), G43 (= G45), L44 (≠ G46), D81 (= D84), R155 (= R157)
1m1bA Crystal structure of phosphoenolpyruvate mutase complexed with sulfopyruvate (see paper)
29% identity, 90% coverage: 8:273/294 of query aligns to 6:272/291 of 1m1bA
- active site: W40 (≠ Y42), S42 (= S44), G43 (= G45), L44 (≠ G46), D54 (= D57), D81 (= D84), D83 (= D86), C108 (≠ H112), E110 (= E114), K116 (= K120), N118 (≠ C122), S119 (≠ G123), R155 (= R157), H186 (≠ E187), V211 (≠ N209)
- binding magnesium ion: D81 (= D84), R155 (= R157)
- binding sulfopyruvate: S42 (= S44), G43 (= G45), L44 (≠ G46), D81 (= D84), N118 (≠ C122), S119 (≠ G123), L120 (≠ H124), R155 (= R157)
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)
32% identity, 84% coverage: 9:256/294 of query aligns to 13:252/287 of Q9HUU1
- D88 (= D84) binding Mg(2+)
- Y212 (≠ F213) mutation to F: 25-fold increase in substrate affinity and 23-fold decrease in activity.
- H235 (≠ L236) 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)
32% identity, 84% coverage: 9:256/294 of query aligns to 11:250/284 of 3b8iA
- active site: I44 (≠ Y42), G46 (≠ S44), G47 (= G45), S48 (≠ G46), D59 (= D57), D86 (= D84), D88 (= D86), T113 (≠ H112), E115 (= E114), A121 (≠ K120), F123 (≠ C122), G124 (= G123), R157 (= R157), V186 (≠ E187), M206 (≠ L207)
- binding oxalate ion: S48 (≠ G46), D86 (= D84), H233 (≠ L236)
5uncA The crystal structure of phosphoenolpyruvate phosphomutase from streptomyces platensis subsp. Rosaceus
32% identity, 90% coverage: 19:282/294 of query aligns to 16:279/289 of 5uncA
- active site: W39 (≠ Y42), S41 (= S44), G42 (= G45), L43 (≠ G46), D53 (= D57), D80 (= D84), D82 (= D86), T107 (≠ H112), E109 (= E114), K115 (= K120), N117 (≠ C122), S118 (≠ G123), R153 (= R157), H184 (≠ E187), V209 (≠ N209)
- binding alpha-D-xylopyranose: H22 (≠ I25), N23 (= N26), G26 (≠ H29), L29 (= L32), G239 (≠ A242), V243 (≠ A246)
Query Sequence
>WP_090272481.1 NCBI__GCF_900105005.1:WP_090272481.1
MNKTPGQRFRQALAEEQPLQVIGAINANHALLAKRAGFKAIYLSGGGVAAGSLGLPDLGI
NTLEDVLIDVRRITDVCDLPLMVDIDTGFGPSAFNIERTVKSLIKAGAAAAHIEDQVGAK
RCGHRPGKEIVSTEEMVDRVRAAADAKTDPDFFLIARTDAIQAEGVEAALERCKRYVEAG
ADAIFAEAAYDLPTYERFVKELNVPVLANITEFGATPLFTREELASVGVAIQLYPLSAFR
AANKAAENVYNAVRTEGHQQNVIDSMQTREELYDRIGYHVFEGKLDALFAAGKK
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