SitesBLAST
Comparing WP_012041426.1 NCBI__GCF_000015165.1:WP_012041426.1 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)
4iqdA Crystal structure of carboxyvinyl-carboxyphosphonate phosphorylmutase from bacillus anthracis
38% identity, 96% coverage: 6:280/287 of query aligns to 13:285/290 of 4iqdA
- active site: Y46 (= Y39), S48 (≠ T41), G49 (= G42), A50 (≠ Y43), D60 (= D54), D87 (= D81), D89 (= D83), Q114 (= Q108), E116 (= E110), K122 (= K116), C124 (= C118), G125 (= G119), H126 (= H120), R157 (= R153), E187 (= E183), N209 (= N205)
- binding pyruvic acid: E71 (≠ D65), R72 (= R66), D75 (≠ R69), G165 (= G161), L166 (= L162), Y218 (≠ M214), Y219 (≠ L215)
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)
37% identity, 98% coverage: 2:282/287 of query aligns to 6:285/295 of Q56062
- SGG 45:47 (≠ TGY 41:43) binding substrate
- D58 (= D54) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- D85 (= D81) binding Mg(2+)
- K121 (= K116) mutation to A: 1000-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R122 (≠ K117) mutation to K: 2-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- C123 (= C118) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- H125 (= H120) mutation to A: 750-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R158 (= R153) binding substrate
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)
35% identity, 98% coverage: 2:282/287 of query aligns to 6:285/296 of P77541
- SGG 45:47 (≠ TGY 41:43) binding substrate
- D85 (= D81) binding Mg(2+)
- D87 (= D83) binding Mg(2+)
- C123 (= C118) mutation to S: Inactive.
- CG 123:124 (= CG 118:119) binding substrate
- R158 (= R153) binding substrate
- E188 (= E183) binding substrate
- NIT 210:212 (≠ NMV 205:207) binding substrate
- R241 (≠ L236) binding substrate
- R270 (≠ F267) binding substrate
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1mumA Structure of the 2-methylisocitrate lyase (prpb) from escherichia coli (see paper)
35% identity, 98% coverage: 2:282/287 of query aligns to 4:283/289 of 1mumA
- active site: Y41 (= Y39), S43 (≠ T41), G44 (= G42), G45 (≠ Y43), D56 (= D54), D83 (= D81), D85 (= D83), H111 (≠ Q108), E113 (= E110), K119 (= K116), C121 (= C118), G122 (= G119), H123 (= H120), R156 (= R153), E186 (= E183), N208 (= N205), T215 (= T212), L217 (≠ M214)
- binding magnesium ion: D56 (= D54), D85 (= D83)
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, 92% coverage: 19:283/287 of query aligns to 44:310/318 of Q05957
- D79 (= D54) mutation to A: Reduces catalytic efficiency 1000-fold.
- D107 (≠ A82) binding Mg(2+)
- D109 (≠ T84) binding Mg(2+)
- K142 (= K116) binding Mg(2+)
- C144 (= C118) 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, 92% coverage: 19:283/287 of query aligns to 17:283/284 of 1zlpA
- active site: F37 (≠ Y39), S39 (≠ T41), G40 (= G42), Y41 (= Y43), D52 (= D54), D80 (≠ A82), D82 (≠ T84), F107 (≠ Q108), E109 (= E110), K115 (= K116), C117 (= C118), G118 (= G119), H119 (= H120), R152 (= R153), E182 (= E183), N204 (= N205), T211 (= T212), L213 (≠ M214)
- binding 5-hydroxypentanal: C117 (= C118), G118 (= G119), R152 (= R153), I206 (≠ V207)
- binding magnesium ion: D80 (≠ A82), K115 (= K116)
1zlpB Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
38% identity, 92% coverage: 19:283/287 of query aligns to 17:283/285 of 1zlpB
- active site: F37 (≠ Y39), S39 (≠ T41), G40 (= G42), Y41 (= Y43), D52 (= D54), D80 (≠ A82), D82 (≠ T84), F107 (≠ Q108), E109 (= E110), K115 (= K116), C117 (= C118), G118 (= G119), H119 (= H120), R152 (= R153), E182 (= E183), N204 (= N205), T211 (= T212), L213 (≠ M214)
- binding 5-hydroxypentanal: Y41 (= Y43), C117 (= C118), R152 (= R153), I206 (≠ V207)
3fa3B Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
40% identity, 96% coverage: 5:280/287 of query aligns to 8:287/302 of 3fa3B
- active site: Y43 (= Y39), T45 (= T41), G46 (= G42), A47 (≠ Y43), D58 (= D54), D86 (= D81), D88 (= D83), H113 (≠ Q108), E115 (= E110), K121 (= K116), C123 (= C118), G124 (= G119), H125 (= H120), R160 (= R153), E190 (= E183), N213 (= N205), T220 (= T212), S222 (≠ M214)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y43 (= Y39), T45 (= T41), G46 (= G42), A47 (≠ Y43), D86 (= D81), G124 (= G119), R160 (= R153), E190 (= E183), N213 (= N205), P239 (= P231)
1o5qA Crystal structure of pyruvate and mg2+ bound 2-methylisocitrate lyase (prpb) from salmonella typhimurium (see paper)
35% identity, 98% coverage: 2:282/287 of query aligns to 2:270/271 of 1o5qA
- active site: Y39 (= Y39), S41 (≠ T41), G42 (= G42), G43 (≠ Y43), D54 (= D54), D81 (= D81), D83 (= D83), H109 (≠ Q108), E111 (= E110), R143 (= R153), E173 (= E186), N195 (= N205), T202 (= T212), L204 (≠ M214)
- binding pyruvic acid: Y39 (= Y39), S41 (≠ T41), G43 (≠ Y43), D81 (= D81), R143 (= R153)
3m0jA Structure of oxaloacetate acetylhydrolase in complex with the inhibitor 3,3-difluorooxalacetate (see paper)
40% identity, 87% coverage: 6:255/287 of query aligns to 10:265/297 of 3m0jA
- binding calcium ion: E218 (≠ N208), N219 (≠ G209)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y44 (= Y39), T46 (= T41), G47 (= G42), A48 (≠ Y43), D88 (= D81), G126 (= G119), R162 (= R153), E192 (= E183), N215 (= N205), S241 (≠ P231)
3fa4A Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, triclinic crystal form (see paper)
39% identity, 96% coverage: 5:280/287 of query aligns to 8:280/284 of 3fa4A
- active site: Y43 (= Y39), T45 (= T41), G46 (= G42), A47 (≠ Y43), D58 (= D54), D86 (= D81), D88 (= D83), H113 (≠ Q108), E115 (= E110), R153 (= R153), E183 (= E183), N206 (= N205), T213 (= T212), S215 (≠ M214)
- binding magnesium ion: D86 (= D81), D88 (= D83)
3fa3J Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
39% identity, 96% coverage: 5:280/287 of query aligns to 7:278/292 of 3fa3J
- active site: Y42 (= Y39), T44 (= T41), G45 (= G42), A46 (≠ Y43), D57 (= D54), D85 (= D81), D87 (= D83), H112 (≠ Q108), E114 (= E110), R151 (= R153), E181 (= E183), N204 (= N205), T211 (= T212), S213 (≠ M214)
- binding manganese (ii) ion: D85 (= D81), D87 (= D83)
6t4vC Crystal structure of 2-methylisocitrate lyase (prpb) from pseudomonas aeruginosa in apo form.
35% identity, 90% coverage: 2:259/287 of query aligns to 4:251/277 of 6t4vC
- active site: Y41 (= Y39), S43 (≠ T41), G44 (= G42), G45 (≠ Y43), D56 (= D54), D83 (= D81), D85 (= D83), H111 (≠ Q108), E113 (= E110), R145 (= R153), E175 (= E183), N197 (= N205), T204 (= T212), L206 (≠ M214)
- binding pyruvic acid: F88 (≠ Y86), N94 (= N91)
3m0kA Structure of oxaloacetate acetylhydrolase in complex with the product oxalate (see paper)
39% identity, 87% coverage: 6:255/287 of query aligns to 10:260/289 of 3m0kA
5uncA The crystal structure of phosphoenolpyruvate phosphomutase from streptomyces platensis subsp. Rosaceus
32% identity, 92% coverage: 20:283/287 of query aligns to 20:285/289 of 5uncA
- active site: W39 (≠ Y39), S41 (≠ T41), G42 (= G42), L43 (≠ Y43), D53 (= D54), D80 (= D81), D82 (= D83), T107 (≠ Q108), E109 (= E110), K115 (= K116), N117 (≠ C118), S118 (≠ G119), R153 (= R153), H184 (≠ E183), V209 (≠ N208)
- binding alpha-D-xylopyranose: H22 (≠ Y22), N23 (≠ D23), G26 (≠ S26), L29 (≠ I29), G239 (≠ T238), V243 (≠ L242)
P56839 Phosphoenolpyruvate phosphomutase; PEP mutase; PEP phosphomutase; Phosphoenolpyruvate mutase; EC 5.4.2.9 from Mytilus edulis (Blue mussel) (see 2 papers)
31% identity, 85% coverage: 6:248/287 of query aligns to 11:259/295 of P56839
- D58 (= D54) mutation D->A,S: Abolishes enzyme activity.; mutation to N: Strongly reduces enzyme activity.
- D85 (= D81) mutation to A: Strongly reduces enzyme activity and increases KM.
- D87 (= D83) mutation to A: Strongly reduces enzyme activity.
- E114 (= E110) mutation to A: Strongly reduces enzyme activity.
- N122 (≠ H120) mutation N->A,D: Strongly reduces enzyme activity.
- R159 (= R153) mutation to A: Strongly reduces enzyme activity.
- H190 (≠ E183) 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)
31% identity, 85% coverage: 6:248/287 of query aligns to 7:255/291 of 1pymA
- active site: W40 (≠ Y39), S42 (≠ T41), G43 (= G42), L44 (≠ Y43), D54 (= D54), D81 (= D81), D83 (= D83), C108 (≠ Q108), E110 (= E110), K116 (= K116), N118 (≠ H120), S119 (≠ T121), R155 (= R153), H186 (≠ E183), V211 (≠ N205)
- binding oxalate ion: W40 (≠ Y39), S42 (≠ T41), G43 (= G42), L44 (≠ Y43), D81 (= D81), R155 (= R153)
1m1bA Crystal structure of phosphoenolpyruvate mutase complexed with sulfopyruvate (see paper)
31% identity, 85% coverage: 6:248/287 of query aligns to 7:255/291 of 1m1bA
- active site: W40 (≠ Y39), S42 (≠ T41), G43 (= G42), L44 (≠ Y43), D54 (= D54), D81 (= D81), D83 (= D83), C108 (≠ Q108), E110 (= E110), K116 (= K116), N118 (≠ H120), S119 (≠ T121), R155 (= R153), H186 (≠ E183), V211 (≠ N205)
- binding magnesium ion: D81 (= D81), R155 (= R153)
- binding sulfopyruvate: S42 (≠ T41), G43 (= G42), L44 (≠ Y43), D81 (= D81), N118 (≠ H120), S119 (≠ T121), L120 (≠ P122), R155 (= R153)
2hjpA Crystal structure of phosphonopyruvate hydrolase complex with phosphonopyruvate and mg++ (see paper)
36% identity, 63% coverage: 3:184/287 of query aligns to 4:180/283 of 2hjpA
- active site: W40 (≠ Y39), S42 (≠ T41), G43 (= G42), F44 (≠ Y43), D54 (= D54), D81 (= D81), D83 (= D83), V108 (≠ Q108), E110 (= E110), K116 (= K116), T118 (≠ C118), R148 (= R153), H179 (≠ E183)
- binding phosphonopyruvate: W40 (≠ Y39), S42 (≠ T41), F44 (≠ Y43), D81 (= D81), R148 (= R153), H179 (≠ E183)
- binding alpha-D-xylopyranose: E32 (≠ D31), S75 (≠ K75)
Sites not aligning to the query:
2duaA Crystal structure of phosphonopyruvate hydrolase complex with oxalate and mg++ (see paper)
36% identity, 63% coverage: 3:184/287 of query aligns to 4:180/283 of 2duaA
- active site: W40 (≠ Y39), S42 (≠ T41), G43 (= G42), F44 (≠ Y43), D54 (= D54), D81 (= D81), D83 (= D83), V108 (≠ Q108), E110 (= E110), K116 (= K116), T118 (≠ C118), R148 (= R153), H179 (≠ E183)
- binding oxalate ion: W40 (≠ Y39), S42 (≠ T41), F44 (≠ Y43), D81 (= D81), R148 (= R153)
- binding alpha-D-xylopyranose: E32 (≠ D31), S75 (≠ K75)
Sites not aligning to the query:
Query Sequence
>WP_012041426.1 NCBI__GCF_000015165.1:WP_012041426.1
MPDPALRQALATGDFIAAPGVYDLISALIADRMGFKALYVTGYGTVASSLGLPDAGLATY
SEMLDRIARIVAMTKTPVIADADTGYGGLLNVRHTVRGYEKAGVTAIQLEDQEFPKKCGH
TPHRRVIPTADMIRKIKVASDARSSADFLIIARTDARSGKGLDEAISRGRAYADAGADIV
FVESPESEAEMAEIGRMIDKPLLANMVNGGRTPMLSADRLKQLGFAVAIFPAVGFLATAE
ALTRAYDDLRRHGTTTEAVPMFSFAEFNRLIGFEDVWEFERRYSETE
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