SitesBLAST
Comparing 199540 FitnessBrowser__MR1:199540 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)
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)
61% identity, 99% coverage: 3:292/292 of query aligns to 4:294/295 of Q56062
- SGG 45:47 (≠ SGA 44:46) binding
- D58 (= D57) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- D85 (= D84) binding
- K121 (= K119) mutation to A: 1000-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R122 (= R120) mutation to K: 2-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- C123 (= C121) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- H125 (= H123) mutation to A: 750-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R158 (= R156) 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)
60% identity, 99% coverage: 3:292/292 of query aligns to 4:294/296 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)
60% identity, 98% coverage: 3:289/292 of query aligns to 2:289/289 of 1mumA
- active site: Y41 (= Y42), S43 (= S44), G44 (= G45), G45 (≠ A46), D56 (= D57), D83 (= D84), D85 (= D86), H111 (= H111), E113 (= E113), K119 (= K119), C121 (= C121), G122 (= G122), H123 (= H123), R156 (= R156), E186 (= E186), N208 (= N208), T215 (= T215), L217 (= L217)
- binding magnesium ion: D56 (= D57), D85 (= D86)
6t4vC Crystal structure of 2-methylisocitrate lyase (prpb) from pseudomonas aeruginosa in apo form.
59% identity, 98% coverage: 4:288/292 of query aligns to 3:277/277 of 6t4vC
- active site: Y41 (= Y42), S43 (= S44), G44 (= G45), G45 (≠ A46), D56 (= D57), D83 (= D84), D85 (= D86), H111 (= H111), E113 (= E113), R145 (= R156), E175 (= E186), N197 (= N208), T204 (= T215), L206 (= L217)
- binding pyruvic acid: F88 (≠ W89), N94 (= N94)
1o5qA Crystal structure of pyruvate and mg2+ bound 2-methylisocitrate lyase (prpb) from salmonella typhimurium (see paper)
59% identity, 96% coverage: 4:284/292 of query aligns to 1:271/271 of 1o5qA
- active site: Y39 (= Y42), S41 (= S44), G42 (= G45), G43 (≠ A46), D54 (= D57), D81 (= D84), D83 (= D86), H109 (= H111), E111 (= E113), R143 (= R156), E173 (= E186), N195 (= N208), T202 (= T215), L204 (= L217)
- binding pyruvic acid: Y39 (= Y42), S41 (= S44), G43 (≠ A46), D81 (= D84), R143 (= R156)
4iqdA Crystal structure of carboxyvinyl-carboxyphosphonate phosphorylmutase from bacillus anthracis
49% identity, 94% coverage: 8:282/292 of query aligns to 12:283/290 of 4iqdA
- active site: Y46 (= Y42), S48 (= S44), G49 (= G45), A50 (= A46), D60 (= D57), D87 (= D84), D89 (= D86), Q114 (≠ H111), E116 (= E113), K122 (= K119), C124 (= C121), G125 (= G122), H126 (= H123), R157 (= R156), E187 (= E186), N209 (= N208)
- binding pyruvic acid: E71 (≠ I68), R72 (≠ D69), D75 (≠ R72), G165 (= G164), L166 (= L165), Y218 (≠ L217), Y219 (≠ F218)
3fa3B Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
35% identity, 93% coverage: 4:276/292 of query aligns to 4:279/302 of 3fa3B
- active site: Y43 (= Y42), T45 (≠ S44), G46 (= G45), A47 (= A46), D58 (= D57), D86 (= D84), D88 (= D86), H113 (= H111), E115 (= E113), K121 (= K119), C123 (= C121), G124 (= G122), H125 (= H123), R160 (= R156), E190 (= E186), N213 (= N208), T220 (= T215), S222 (≠ L217)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y43 (= Y42), T45 (≠ S44), G46 (= G45), A47 (= A46), D86 (= D84), G124 (= G122), R160 (= R156), E190 (= E186), N213 (= N208), P239 (= P234)
1zlpA Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
39% identity, 88% coverage: 23:280/292 of query aligns to 18:276/284 of 1zlpA
- active site: F37 (≠ Y42), S39 (= S44), G40 (= G45), Y41 (≠ A46), D52 (= D57), D80 (= D84), D82 (= D86), F107 (≠ H111), E109 (= E113), K115 (= K119), C117 (= C121), G118 (= G122), H119 (= H123), R152 (= R156), E182 (= E186), N204 (= N208), T211 (= T215), L213 (= L217)
- binding 5-hydroxypentanal: C117 (= C121), G118 (= G122), R152 (= R156), I206 (≠ T210)
- binding magnesium ion: D80 (= D84), K115 (= K119)
1zlpB Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
39% identity, 88% coverage: 23:280/292 of query aligns to 18:276/285 of 1zlpB
- active site: F37 (≠ Y42), S39 (= S44), G40 (= G45), Y41 (≠ A46), D52 (= D57), D80 (= D84), D82 (= D86), F107 (≠ H111), E109 (= E113), K115 (= K119), C117 (= C121), G118 (= G122), H119 (= H123), R152 (= R156), E182 (= E186), N204 (= N208), T211 (= T215), L213 (= L217)
- binding 5-hydroxypentanal: Y41 (≠ A46), C117 (= C121), R152 (= R156), I206 (≠ T210)
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)
39% identity, 88% coverage: 23:280/292 of query aligns to 45:303/318 of Q05957
- D79 (= D57) mutation to A: Reduces catalytic efficiency 1000-fold.
- D107 (= D84) binding
- D109 (= D86) binding
- K142 (= K119) binding
- C144 (= C121) 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)
34% identity, 87% coverage: 4:256/292 of query aligns to 5:263/297 of 3m0jA
- binding calcium ion: E218 (= E211), N219 (≠ F212)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y44 (= Y42), T46 (≠ S44), G47 (= G45), A48 (= A46), D88 (= D84), G126 (= G122), R162 (= R156), E192 (= E186), N215 (= N208), S241 (≠ P234)
3fa4A Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, triclinic crystal form (see paper)
33% identity, 93% coverage: 4:276/292 of query aligns to 4:272/284 of 3fa4A
- active site: Y43 (= Y42), T45 (≠ S44), G46 (= G45), A47 (= A46), D58 (= D57), D86 (= D84), D88 (= D86), H113 (= H111), E115 (= E113), R153 (= R156), E183 (= E186), N206 (= N208), T213 (= T215), S215 (≠ L217)
- binding magnesium ion: D86 (= D84), D88 (= D86)
3fa3J Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
33% identity, 93% coverage: 4:276/292 of query aligns to 3:270/292 of 3fa3J
- active site: Y42 (= Y42), T44 (≠ S44), G45 (= G45), A46 (= A46), D57 (= D57), D85 (= D84), D87 (= D86), H112 (= H111), E114 (= E113), R151 (= R156), E181 (= E186), N204 (= N208), T211 (= T215), S213 (≠ L217)
- binding manganese (ii) ion: D85 (= D84), D87 (= D86)
3m0kA Structure of oxaloacetate acetylhydrolase in complex with the product oxalate (see paper)
34% identity, 87% coverage: 4:256/292 of query aligns to 5:258/289 of 3m0kA
5uncA The crystal structure of phosphoenolpyruvate phosphomutase from streptomyces platensis subsp. Rosaceus
31% identity, 91% coverage: 19:283/292 of query aligns to 16:281/289 of 5uncA
- active site: W39 (≠ Y42), S41 (= S44), G42 (= G45), L43 (≠ A46), D53 (= D57), D80 (= D84), D82 (= D86), T107 (≠ H111), E109 (= E113), K115 (= K119), N117 (≠ C121), S118 (≠ G122), R153 (= R156), H184 (≠ E186), V209 (≠ N208)
- binding alpha-D-xylopyranose: H22 (≠ T25), N23 (= N26), G26 (≠ F29), L29 (≠ M32), G239 (≠ A241), V243 (≠ A245)
3b8iA Crystal structure of oxaloacetate decarboxylase from pseudomonas aeruginosa (pa4872) in complex with oxalate and mg2+. (see paper)
29% identity, 83% coverage: 9:250/292 of query aligns to 11:248/284 of 3b8iA
- active site: I44 (≠ Y42), G46 (≠ S44), G47 (= G45), S48 (≠ A46), D59 (= D57), D86 (= D84), D88 (= D86), T113 (≠ H111), E115 (= E113), A121 (≠ K119), F123 (≠ C121), G124 (= G122), R157 (= R156), V186 (≠ E186), M206 (≠ L206)
- binding oxalate ion: S48 (≠ A46), D86 (= D84), H233 (≠ L235)
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)
30% identity, 83% coverage: 9:250/292 of query aligns to 13:250/287 of Q9HUU1
- D88 (= D84) binding
- Y212 (≠ F212) mutation to F: 25-fold increase in substrate affinity and 23-fold decrease in activity.
- H235 (≠ L235) 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.
1pymA Phosphoenolpyruvate mutase from mollusk in with bound mg2-oxalate (see paper)
29% identity, 89% coverage: 13:273/292 of query aligns to 10:273/291 of 1pymA
- active site: W40 (≠ Y42), S42 (= S44), G43 (= G45), L44 (≠ A46), D54 (= D57), D81 (= D84), D83 (= D86), C108 (≠ H111), E110 (= E113), K116 (= K119), N118 (≠ C121), S119 (≠ G122), R155 (= R156), H186 (vs. gap), V211 (≠ N208)
- binding oxalate ion: W40 (≠ Y42), S42 (= S44), G43 (= G45), L44 (≠ A46), D81 (= D84), R155 (= R156)
1m1bA Crystal structure of phosphoenolpyruvate mutase complexed with sulfopyruvate (see paper)
29% identity, 89% coverage: 13:273/292 of query aligns to 10:273/291 of 1m1bA
- active site: W40 (≠ Y42), S42 (= S44), G43 (= G45), L44 (≠ A46), D54 (= D57), D81 (= D84), D83 (= D86), C108 (≠ H111), E110 (= E113), K116 (= K119), N118 (≠ C121), S119 (≠ G122), R155 (= R156), H186 (vs. gap), V211 (≠ N208)
- binding magnesium ion: D81 (= D84), R155 (= R156)
- binding sulfopyruvate: S42 (= S44), G43 (= G45), L44 (≠ A46), D81 (= D84), N118 (≠ C121), S119 (≠ G122), L120 (≠ H123), R155 (= R156)
P56839 Phosphoenolpyruvate phosphomutase; PEP mutase; PEP phosphomutase; Phosphoenolpyruvate mutase; EC 5.4.2.9 from Mytilus edulis (Blue mussel) (see 2 papers)
29% identity, 89% coverage: 13:273/292 of query aligns to 14:277/295 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 (= E113) mutation to A: Strongly reduces enzyme activity.
- N122 (≠ C121) mutation N->A,D: Strongly reduces enzyme activity.
- R159 (= R156) mutation to A: Strongly reduces enzyme activity.
- H190 (vs. gap) mutation to A: Strongly reduces enzyme activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
Query Sequence
>199540 FitnessBrowser__MR1:199540
MTQSAGLRFRQALANSKPLQIVGTTNAYFALMAEQTGFQALYLSGAGVANASYGLPDLGM
TSMNDVLIDAGRITSATQLPLLVDIDTGWGGAFNIARTIKEFEKIGVAAVHMEDQVSQKR
CGHRPNKAVVSTEEMVDRIKAAVDARTDPNFVIMARTDAVAVEGLEAGIERAKAYIAAGA
DMIFAEALTELDQYRHFKAQVKAPILANMTEFGQTQLFNKEELAQAGADMVLYPLGTFRA
ANQAALKVMQALMNDGHQRNVLDTMQTRADLYKYLGYHAFEDKLDQLFSQDK
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