SitesBLAST
Comparing WP_086511658.1 NCBI__GCF_002151265.1:WP_086511658.1 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)
61% identity, 98% coverage: 1:294/301 of query aligns to 1:295/296 of P77541
- M1 (= M1) modified: Initiator methionine, Removed
- SGG 45:47 (= SGG 45:47) binding
- D85 (= D85) binding
- D87 (= D87) binding
- C123 (= C122) mutation to S: Inactive.
- CG 123:124 (= CG 122:123) binding
- R158 (= R157) binding
- E188 (= E187) binding
- NIT 210:212 (= NIT 209:211) binding
- R241 (= R240) binding
- R270 (= R269) binding
1mumA Structure of the 2-methylisocitrate lyase (prpb) from escherichia coli (see paper)
62% identity, 95% coverage: 5:290/301 of query aligns to 3:289/289 of 1mumA
- active site: Y41 (= Y43), S43 (= S45), G44 (= G46), G45 (= G47), D56 (= D58), D83 (= D85), D85 (= D87), 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 (= D58), D85 (= D87)
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)
60% identity, 96% coverage: 1:289/301 of query aligns to 1:290/295 of Q56062
- SGG 45:47 (= SGG 45:47) binding
- D58 (= D58) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- D85 (= D85) binding
- 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
6t4vC Crystal structure of 2-methylisocitrate lyase (prpb) from pseudomonas aeruginosa in apo form.
60% identity, 95% coverage: 5:289/301 of query aligns to 3:277/277 of 6t4vC
- active site: Y41 (= Y43), S43 (= S45), G44 (= G46), G45 (= G47), D56 (= D58), D83 (= D85), D85 (= D87), H111 (= H112), E113 (= E114), R145 (= R157), E175 (= E187), N197 (= N209), T204 (= T216), L206 (= L218)
- binding pyruvic acid: F88 (≠ W90), N94 (= N95)
1o5qA Crystal structure of pyruvate and mg2+ bound 2-methylisocitrate lyase (prpb) from salmonella typhimurium (see paper)
57% identity, 93% coverage: 5:285/301 of query aligns to 1:271/271 of 1o5qA
- active site: Y39 (= Y43), S41 (= S45), G42 (= G46), G43 (= G47), D54 (= D58), D81 (= D85), D83 (= D87), H109 (= H112), E111 (= E114), R143 (= R157), E173 (= E187), N195 (= N209), T202 (= T216), L204 (= L218)
- binding pyruvic acid: Y39 (= Y43), S41 (= S45), G43 (= G47), D81 (= D85), R143 (= R157)
4iqdA Crystal structure of carboxyvinyl-carboxyphosphonate phosphorylmutase from bacillus anthracis
48% identity, 94% coverage: 2:283/301 of query aligns to 5:283/290 of 4iqdA
- active site: Y46 (= Y43), S48 (= S45), G49 (= G46), A50 (≠ G47), D60 (= D58), D87 (= D85), D89 (= D87), Q114 (≠ H112), E116 (= E114), K122 (= K120), C124 (= C122), G125 (= G123), H126 (= H124), R157 (= R157), E187 (= E187), N209 (= N209)
- binding pyruvic acid: E71 (≠ Q69), R72 (≠ D70), D75 (≠ R73), G165 (= G165), L166 (= L166), Y218 (≠ L218), Y219 (≠ F219)
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)
38% identity, 86% coverage: 24:281/301 of query aligns to 45:303/318 of Q05957
- D79 (= D58) mutation to A: Reduces catalytic efficiency 1000-fold.
- D107 (= D85) binding
- D109 (= D87) binding
- K142 (= K120) binding
- C144 (= C122) mutation to A: Loss of catalytic activity.
Sites not aligning to the query:
- 1:3 modified: propeptide, Removed in mature form
1zlpA Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
38% identity, 86% coverage: 24:281/301 of query aligns to 18:276/284 of 1zlpA
- active site: F37 (≠ Y43), S39 (= S45), G40 (= G46), Y41 (≠ G47), D52 (= D58), D80 (= D85), D82 (= D87), 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 (= D85), K115 (= K120)
1zlpB Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
38% identity, 86% coverage: 24:281/301 of query aligns to 18:276/285 of 1zlpB
- active site: F37 (≠ Y43), S39 (= S45), G40 (= G46), Y41 (≠ G47), D52 (= D58), D80 (= D85), D82 (= D87), 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 (≠ G47), C117 (= C122), R152 (= R157), I206 (≠ T211)
3fa3B Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
35% identity, 84% coverage: 5:257/301 of query aligns to 4:261/302 of 3fa3B
- active site: Y43 (= Y43), T45 (≠ S45), G46 (= G46), A47 (≠ G47), D58 (= D58), D86 (= D85), D88 (= D87), 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 (= Y43), T45 (≠ S45), G46 (= G46), A47 (≠ G47), D86 (= D85), 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)
34% identity, 85% coverage: 3:257/301 of query aligns to 2:263/297 of 3m0jA
- binding calcium ion: E218 (= E212), N219 (≠ F213)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y44 (= Y43), T46 (≠ S45), G47 (= G46), A48 (≠ G47), D88 (= D85), 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)
33% identity, 84% coverage: 5:257/301 of query aligns to 4:254/284 of 3fa4A
- active site: Y43 (= Y43), T45 (≠ S45), G46 (= G46), A47 (≠ G47), D58 (= D58), D86 (= D85), D88 (= D87), H113 (= H112), E115 (= E114), R153 (= R157), E183 (= E187), N206 (= N209), T213 (= T216), S215 (≠ L218)
- binding magnesium ion: D86 (= D85), D88 (= D87)
3m0kA Structure of oxaloacetate acetylhydrolase in complex with the product oxalate (see paper)
34% identity, 85% coverage: 3:257/301 of query aligns to 2:258/289 of 3m0kA
3fa3J Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
33% identity, 84% coverage: 5:257/301 of query aligns to 3:252/292 of 3fa3J
- active site: Y42 (= Y43), T44 (≠ S45), G45 (= G46), A46 (≠ G47), D57 (= D58), D85 (= D85), D87 (= D87), H112 (= H112), E114 (= E114), R151 (= R157), E181 (= E187), N204 (= N209), T211 (= T216), S213 (≠ L218)
- binding manganese (ii) ion: D85 (= D85), D87 (= D87)
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, 83% coverage: 8:257/301 of query aligns to 11:254/287 of Q9HUU1
- D88 (= D85) binding
- 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, 83% coverage: 8:257/301 of query aligns to 9:252/284 of 3b8iA
- active site: I44 (≠ Y43), G46 (≠ S45), G47 (= G46), S48 (≠ G47), D59 (= D58), D86 (= D85), D88 (= D87), T113 (≠ H112), E115 (= E114), A121 (≠ K120), F123 (≠ C122), G124 (= G123), R157 (= R157), V186 (≠ E187), M206 (≠ L207)
- binding oxalate ion: S48 (≠ G47), D86 (= D85), H233 (≠ L236)
5uncA The crystal structure of phosphoenolpyruvate phosphomutase from streptomyces platensis subsp. Rosaceus
31% identity, 92% coverage: 8:284/301 of query aligns to 4:281/289 of 5uncA
- active site: W39 (≠ Y43), S41 (= S45), G42 (= G46), L43 (≠ G47), D53 (= D58), D80 (= D85), D82 (= D87), T107 (≠ H112), E109 (= E114), K115 (= K120), N117 (≠ C122), S118 (≠ G123), R153 (= R157), H184 (≠ E187), V209 (≠ N209)
- binding alpha-D-xylopyranose: H22 (≠ I26), N23 (= N27), G26 (≠ T30), L29 (≠ M33), G239 (≠ M242), V243 (≠ A246)
1pymA Phosphoenolpyruvate mutase from mollusk in with bound mg2-oxalate (see paper)
29% identity, 82% coverage: 27:273/301 of query aligns to 24:272/291 of 1pymA
- active site: W40 (≠ Y43), S42 (= S45), G43 (= G46), L44 (≠ G47), D54 (= D58), D81 (= D85), D83 (= D87), C108 (≠ H112), E110 (= E114), K116 (= K120), N118 (≠ C122), S119 (≠ G123), R155 (= R157), H186 (≠ E187), V211 (≠ N209)
- binding oxalate ion: W40 (≠ Y43), S42 (= S45), G43 (= G46), L44 (≠ G47), D81 (= D85), R155 (= R157)
1m1bA Crystal structure of phosphoenolpyruvate mutase complexed with sulfopyruvate (see paper)
29% identity, 82% coverage: 27:273/301 of query aligns to 24:272/291 of 1m1bA
- active site: W40 (≠ Y43), S42 (= S45), G43 (= G46), L44 (≠ G47), D54 (= D58), D81 (= D85), D83 (= D87), C108 (≠ H112), E110 (= E114), K116 (= K120), N118 (≠ C122), S119 (≠ G123), R155 (= R157), H186 (≠ E187), V211 (≠ N209)
- binding magnesium ion: D81 (= D85), R155 (= R157)
- binding sulfopyruvate: S42 (= S45), G43 (= G46), L44 (≠ G47), D81 (= D85), N118 (≠ C122), S119 (≠ G123), L120 (≠ H124), R155 (= R157)
P56839 Phosphoenolpyruvate phosphomutase; PEP mutase; PEP phosphomutase; Phosphoenolpyruvate mutase; EC 5.4.2.9 from Mytilus edulis (Blue mussel) (see 2 papers)
29% identity, 82% coverage: 27:273/301 of query aligns to 28:276/295 of P56839
- D58 (= D58) mutation D->A,S: Abolishes enzyme activity.; mutation to N: Strongly reduces enzyme activity.
- D85 (= D85) mutation to A: Strongly reduces enzyme activity and increases KM.
- D87 (= D87) 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
Query Sequence
>WP_086511658.1 NCBI__GCF_002151265.1:WP_086511658.1
MTQPTPGARFRAALEANRPLPIVGTINAYTAMMAERVGHQAIYLSGGGVANASFGLPDLG
MTSMNDVVQDAHRICGATDLPLLVDIDTGWGGAFNIARTVKEMQRAGVAAVHLEDQVAQK
RCGHRPNKEIVSKQEMVDRIKAAADARIDPDFYLIARTDAFQKEGLDAAIERANACIEAG
ADAIFAEAVHTLDDYRAFCERVDAPILANITEFGATPLFTQQELGEVGCRMVLYPLSAFR
AMNAAALKVYRSIHEKGHQRDVVELMQTRDELYDFLNYHAFEQKLDALFAENQLSGKGDN
A
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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