SitesBLAST
Comparing Ac3H11_2326 FitnessBrowser__acidovorax_3H11:Ac3H11_2326 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)
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)
42% identity, 81% coverage: 22:256/289 of query aligns to 22:257/295 of Q56062
- SGG 45:47 (≠ TGA 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
4iqdA Crystal structure of carboxyvinyl-carboxyphosphonate phosphorylmutase from bacillus anthracis
38% identity, 86% coverage: 8:255/289 of query aligns to 11:255/290 of 4iqdA
- active site: Y46 (= Y43), S48 (≠ T45), G49 (= G46), A50 (= A47), D60 (= D58), D87 (= D85), D89 (= D87), Q114 (= Q112), E116 (= E114), K122 (= K120), C124 (= C122), G125 (= G123), H126 (= H124), R157 (= R157), E187 (= E187), N209 (= N209)
- binding pyruvic acid: E71 (≠ D69), R72 (≠ H70), D75 (≠ R73), G165 (= G165), L166 (≠ F166), Y218 (≠ I218), Y219 (≠ T219)
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)
40% identity, 81% coverage: 22:256/289 of query aligns to 22:257/296 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)
40% identity, 81% coverage: 22:256/289 of query aligns to 20:255/289 of 1mumA
- active site: Y41 (= Y43), S43 (≠ T45), G44 (= G46), G45 (≠ A47), D56 (= D58), D83 (= D85), D85 (= D87), H111 (≠ Q112), E113 (= E114), K119 (= K120), C121 (= C122), G122 (= G123), H123 (= H124), R156 (= R157), E186 (= E187), N208 (= N209), T215 (= T216), L217 (≠ I218)
- binding magnesium ion: D56 (= D58), D85 (= D87)
1zlpB Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
36% identity, 98% coverage: 7:288/289 of query aligns to 1:283/285 of 1zlpB
- active site: F37 (≠ Y43), S39 (≠ T45), G40 (= G46), Y41 (≠ A47), D52 (= D58), D80 (= D85), D82 (= D87), F107 (≠ Q112), E109 (= E114), K115 (= K120), C117 (= C122), G118 (= G123), H119 (= H124), R152 (= R157), E182 (= E187), N204 (= N209), T211 (= T216), L213 (≠ I218)
- binding 5-hydroxypentanal: Y41 (≠ A47), C117 (= C122), R152 (= R157), I206 (≠ V211)
1zlpA Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
36% identity, 98% coverage: 7:288/289 of query aligns to 1:283/284 of 1zlpA
- active site: F37 (≠ Y43), S39 (≠ T45), G40 (= G46), Y41 (≠ A47), D52 (= D58), D80 (= D85), D82 (= D87), F107 (≠ Q112), E109 (= E114), K115 (= K120), C117 (= C122), G118 (= G123), H119 (= H124), R152 (= R157), E182 (= E187), N204 (= N209), T211 (= T216), L213 (≠ I218)
- binding 5-hydroxypentanal: C117 (= C122), G118 (= G123), R152 (= R157), I206 (≠ V211)
- binding magnesium ion: D80 (= D85), K115 (= K120)
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, 98% coverage: 7:288/289 of query aligns to 28:310/318 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
3fa3B Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
38% identity, 84% coverage: 11:254/289 of query aligns to 11:258/302 of 3fa3B
- active site: Y43 (= Y43), T45 (= T45), G46 (= G46), A47 (= A47), D58 (= D58), D86 (= D85), D88 (= D87), H113 (≠ Q112), E115 (= E114), K121 (= K120), C123 (= C122), G124 (= G123), H125 (= H124), R160 (= R157), E190 (= E187), N213 (= N209), T220 (= T216), S222 (≠ I218)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y43 (= Y43), T45 (= T45), G46 (= G46), A47 (= A47), D86 (= D85), G124 (= G123), R160 (= R157), E190 (= E187), N213 (= N209), P239 (≠ A235)
1o5qA Crystal structure of pyruvate and mg2+ bound 2-methylisocitrate lyase (prpb) from salmonella typhimurium (see paper)
39% identity, 81% coverage: 22:256/289 of query aligns to 18:242/271 of 1o5qA
- active site: Y39 (= Y43), S41 (≠ T45), G42 (= G46), G43 (≠ A47), D54 (= D58), D81 (= D85), D83 (= D87), H109 (≠ Q112), E111 (= E114), R143 (= R157), E173 (= E187), N195 (= N209), T202 (= T216), L204 (≠ I218)
- binding pyruvic acid: Y39 (= Y43), S41 (≠ T45), G43 (≠ A47), D81 (= D85), R143 (= R157)
6t4vC Crystal structure of 2-methylisocitrate lyase (prpb) from pseudomonas aeruginosa in apo form.
36% identity, 92% coverage: 22:287/289 of query aligns to 20:272/277 of 6t4vC
- active site: Y41 (= Y43), S43 (≠ T45), G44 (= G46), G45 (≠ A47), D56 (= D58), D83 (= D85), D85 (= D87), H111 (≠ Q112), E113 (= E114), R145 (= R157), E175 (= E187), N197 (= N209), T204 (= T216), L206 (≠ I218)
- binding pyruvic acid: F88 (= F90), N94 (= N95)
3m0jA Structure of oxaloacetate acetylhydrolase in complex with the inhibitor 3,3-difluorooxalacetate (see paper)
35% identity, 88% coverage: 3:256/289 of query aligns to 4:262/297 of 3m0jA
- binding calcium ion: E218 (≠ I212), N219 (≠ G213)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y44 (= Y43), T46 (= T45), G47 (= G46), A48 (= A47), D88 (= D85), G126 (= G123), R162 (= R157), E192 (= E187), N215 (= N209), S241 (≠ A235)
3fa4A Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, triclinic crystal form (see paper)
35% identity, 84% coverage: 11:254/289 of query aligns to 11:251/284 of 3fa4A
- active site: Y43 (= Y43), T45 (= T45), G46 (= G46), A47 (= A47), D58 (= D58), D86 (= D85), D88 (= D87), H113 (≠ Q112), E115 (= E114), R153 (= R157), E183 (= E187), N206 (= N209), T213 (= T216), S215 (≠ I218)
- binding magnesium ion: D86 (= D85), D88 (= D87)
3fa3J Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
35% identity, 84% coverage: 11:254/289 of query aligns to 10:249/292 of 3fa3J
- active site: Y42 (= Y43), T44 (= T45), G45 (= G46), A46 (= A47), D57 (= D58), D85 (= D85), D87 (= D87), H112 (≠ Q112), E114 (= E114), R151 (= R157), E181 (= E187), N204 (= N209), T211 (= T216), S213 (≠ I218)
- binding manganese (ii) ion: D85 (= D85), D87 (= D87)
3m0kA Structure of oxaloacetate acetylhydrolase in complex with the product oxalate (see paper)
34% identity, 88% coverage: 3:256/289 of query aligns to 4:257/289 of 3m0kA
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)
33% identity, 87% coverage: 7:257/289 of query aligns to 10:253/287 of Q9HUU1
- D88 (= D85) binding
- Y212 (≠ G213) mutation to F: 25-fold increase in substrate affinity and 23-fold decrease in activity.
- H235 (≠ N236) 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)
33% identity, 87% coverage: 7:257/289 of query aligns to 8:251/284 of 3b8iA
- active site: I44 (≠ Y43), G46 (≠ T45), G47 (= G46), S48 (≠ A47), D59 (= D58), D86 (= D85), D88 (= D87), T113 (≠ Q112), E115 (= E114), A121 (≠ K120), F123 (≠ C122), G124 (= G123), R157 (= R157), V186 (≠ E187), M206 (≠ N209)
- binding oxalate ion: S48 (≠ A47), D86 (= D85), H233 (≠ N236)
2hjpA Crystal structure of phosphonopyruvate hydrolase complex with phosphonopyruvate and mg++ (see paper)
31% identity, 99% coverage: 4:288/289 of query aligns to 1:281/283 of 2hjpA
- active site: W40 (≠ Y43), S42 (≠ T45), G43 (= G46), F44 (≠ A47), D54 (= D58), D81 (= D85), D83 (= D87), V108 (≠ Q112), E110 (= E114), K116 (= K120), T118 (≠ G127), R148 (= R157), H179 (≠ E187), V204 (= V211)
- binding phosphonopyruvate: W40 (≠ Y43), S42 (≠ T45), F44 (≠ A47), D81 (= D85), R148 (= R157), H179 (≠ E187), R181 (vs. gap)
- binding alpha-D-xylopyranose: E32 (≠ A35), S75 (≠ E79)
2duaA Crystal structure of phosphonopyruvate hydrolase complex with oxalate and mg++ (see paper)
31% identity, 99% coverage: 4:288/289 of query aligns to 1:281/283 of 2duaA
- active site: W40 (≠ Y43), S42 (≠ T45), G43 (= G46), F44 (≠ A47), D54 (= D58), D81 (= D85), D83 (= D87), V108 (≠ Q112), E110 (= E114), K116 (= K120), T118 (≠ G127), R148 (= R157), H179 (≠ E187), V204 (= V211)
- binding oxalate ion: W40 (≠ Y43), S42 (≠ T45), F44 (≠ A47), D81 (= D85), R148 (= R157)
- binding alpha-D-xylopyranose: E32 (≠ A35), S75 (≠ E79)
Q84G06 Phosphonopyruvate hydrolase; PPH; EC 3.11.1.3 from Variovorax sp. (strain Pal2) (see paper)
31% identity, 99% coverage: 4:288/289 of query aligns to 1:288/290 of Q84G06
- D81 (= D85) binding
- R188 (vs. gap) mutation to A: Reduced affinity for substrate.
5uncA The crystal structure of phosphoenolpyruvate phosphomutase from streptomyces platensis subsp. Rosaceus
32% identity, 86% coverage: 9:257/289 of query aligns to 5:255/289 of 5uncA
- active site: W39 (≠ Y43), S41 (≠ T45), G42 (= G46), L43 (≠ A47), D53 (= D58), D80 (= D85), D82 (= D87), T107 (≠ Q112), E109 (= E114), K115 (= K120), N117 (≠ C122), S118 (≠ G123), R153 (= R157), H184 (≠ E187), V209 (≠ I212)
- binding alpha-D-xylopyranose: H22 (≠ F26), N23 (= N27), G26 (≠ S30), L29 (≠ V33), G239 (≠ A242), V243 (≠ M246)
Query Sequence
>Ac3H11_2326 FitnessBrowser__acidovorax_3H11:Ac3H11_2326
LRFMNTKQQLKALAQARRGVIVPGAFNALSARVVADLGFEAIYVTGAGVTNMWFGLPDQA
FMGLTDIADHTARIRDAVELPLIVDADTGFGNALNTYHAVRTLERAGADCIQLEDQVSPK
RCGHFNGKEVIGTDEMLGKIKAAVDARRDAGTLILARTDACATQGFEAAVERAQRFQEAG
ADILFVEAVTTLDEIRALPQRLAAPQLMNMVIGGKTPITSAEELATLGYGLVLYANAALQ
GAVAGMQKALTVLREQRRIDEDPALVAPFAERQRLVRKTEWDALEARYT
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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