SitesBLAST
Comparing WP_013091796.1 NCBI__GCF_000092885.1:WP_013091796.1 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)
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)
40% identity, 96% coverage: 11:293/294 of query aligns to 9:293/295 of Q56062
- SGG 45:47 (≠ TGA 47:49) binding substrate
- D58 (= D60) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- D85 (= D87) binding Mg(2+)
- K121 (= K122) mutation to A: 1000-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R122 (≠ K123) mutation to K: 2-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- C123 (= C124) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- H125 (= H126) mutation to A: 750-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R158 (= R159) 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)
42% identity, 85% coverage: 11:259/294 of query aligns to 9:258/296 of P77541
- SGG 45:47 (≠ TGA 47:49) binding substrate
- D85 (= D87) binding Mg(2+)
- D87 (= D89) binding Mg(2+)
- C123 (= C124) mutation to S: Inactive.
- CG 123:124 (= CG 124:125) binding substrate
- R158 (= R159) binding substrate
- E188 (= E189) binding substrate
- NIT 210:212 (≠ NIV 211:213) binding substrate
- R241 (≠ Q242) binding substrate
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 270 binding substrate
1mumA Structure of the 2-methylisocitrate lyase (prpb) from escherichia coli (see paper)
42% identity, 85% coverage: 11:259/294 of query aligns to 7:256/289 of 1mumA
- active site: Y41 (= Y45), S43 (≠ T47), G44 (= G48), G45 (≠ A49), D56 (= D60), D83 (= D87), D85 (= D89), H111 (≠ Q114), E113 (= E116), K119 (= K122), C121 (= C124), G122 (= G125), H123 (= H126), R156 (= R159), E186 (= E189), N208 (= N211), T215 (= T218), L217 (≠ V220)
- binding magnesium ion: D56 (= D60), D85 (= D89)
4iqdA Crystal structure of carboxyvinyl-carboxyphosphonate phosphorylmutase from bacillus anthracis
37% identity, 94% coverage: 12:287/294 of query aligns to 13:285/290 of 4iqdA
- active site: Y46 (= Y45), S48 (≠ T47), G49 (= G48), A50 (= A49), D60 (= D60), D87 (= D87), D89 (= D89), Q114 (= Q114), E116 (= E116), K122 (= K122), C124 (= C124), G125 (= G125), H126 (= H126), R157 (= R159), E187 (= E189), N209 (= N211)
- binding pyruvic acid: E71 (= E71), R72 (≠ H72), D75 (≠ R75), G165 (= G167), L166 (≠ I168), Y218 (≠ V220), Y219 (≠ Q221)
1o5qA Crystal structure of pyruvate and mg2+ bound 2-methylisocitrate lyase (prpb) from salmonella typhimurium (see paper)
41% identity, 85% coverage: 11:259/294 of query aligns to 5:243/271 of 1o5qA
- active site: Y39 (= Y45), S41 (≠ T47), G42 (= G48), G43 (≠ A49), D54 (= D60), D81 (= D87), D83 (= D89), H109 (≠ Q114), E111 (= E116), R143 (= R159), E173 (= E189), N195 (= N211), T202 (= T218), L204 (≠ V220)
- binding pyruvic acid: Y39 (= Y45), S41 (≠ T47), G43 (≠ A49), D81 (= D87), R143 (= R159)
6t4vC Crystal structure of 2-methylisocitrate lyase (prpb) from pseudomonas aeruginosa in apo form.
40% identity, 94% coverage: 12:287/294 of query aligns to 8:265/277 of 6t4vC
- active site: Y41 (= Y45), S43 (≠ T47), G44 (= G48), G45 (≠ A49), D56 (= D60), D83 (= D87), D85 (= D89), H111 (≠ Q114), E113 (= E116), R145 (= R159), E175 (= E189), N197 (= N211), T204 (= T218), L206 (≠ V220)
- binding pyruvic acid: F88 (= F92), N94 (= N97)
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)
34% identity, 98% coverage: 2:290/294 of query aligns to 21:310/318 of Q05957
- D79 (= D60) mutation to A: Reduces catalytic efficiency 1000-fold.
- D107 (= D87) binding Mg(2+)
- D109 (= D89) binding Mg(2+)
- K142 (= K122) binding Mg(2+)
- C144 (= C124) 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)
34% identity, 94% coverage: 16:290/294 of query aligns to 8:283/284 of 1zlpA
- active site: F37 (≠ Y45), S39 (≠ T47), G40 (= G48), Y41 (≠ A49), D52 (= D60), D80 (= D87), D82 (= D89), F107 (≠ Q114), E109 (= E116), K115 (= K122), C117 (= C124), G118 (= G125), H119 (= H126), R152 (= R159), E182 (= E189), N204 (= N211), T211 (= T218), L213 (≠ V220)
- binding 5-hydroxypentanal: C117 (= C124), G118 (= G125), R152 (= R159), I206 (≠ V213)
- binding magnesium ion: D80 (= D87), K115 (= K122)
1zlpB Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
34% identity, 94% coverage: 16:290/294 of query aligns to 8:283/285 of 1zlpB
- active site: F37 (≠ Y45), S39 (≠ T47), G40 (= G48), Y41 (≠ A49), D52 (= D60), D80 (= D87), D82 (= D89), F107 (≠ Q114), E109 (= E116), K115 (= K122), C117 (= C124), G118 (= G125), H119 (= H126), R152 (= R159), E182 (= E189), N204 (= N211), T211 (= T218), L213 (≠ V220)
- binding 5-hydroxypentanal: Y41 (≠ A49), C117 (= C124), R152 (= R159), I206 (≠ V213)
3fa3B Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
36% identity, 90% coverage: 1:266/294 of query aligns to 2:270/302 of 3fa3B
- active site: Y43 (= Y45), T45 (= T47), G46 (= G48), A47 (= A49), D58 (= D60), D86 (= D87), D88 (= D89), H113 (≠ Q114), E115 (= E116), K121 (= K122), C123 (= C124), G124 (= G125), H125 (= H126), R160 (= R159), E190 (= E189), N213 (= N211), T220 (= T218), S222 (≠ V220)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y43 (= Y45), T45 (= T47), G46 (= G48), A47 (= A49), D86 (= D87), G124 (= G125), R160 (= R159), E190 (= E189), N213 (= N211), P239 (≠ A237)
3b8iA Crystal structure of oxaloacetate decarboxylase from pseudomonas aeruginosa (pa4872) in complex with oxalate and mg2+. (see paper)
36% identity, 81% coverage: 9:245/294 of query aligns to 8:240/284 of 3b8iA
- active site: I44 (≠ Y45), G46 (≠ T47), G47 (= G48), S48 (≠ A49), D59 (= D60), D86 (= D87), D88 (= D89), T113 (≠ Q114), E115 (= E116), A121 (≠ K122), F123 (≠ C124), G124 (= G125), R157 (= R159), V186 (≠ E189), M206 (≠ N211)
- binding oxalate ion: S48 (≠ A49), D86 (= D87), H233 (≠ N238)
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)
36% identity, 81% coverage: 9:245/294 of query aligns to 10:242/287 of Q9HUU1
- D88 (= D87) binding Mg(2+)
- Y212 (≠ G215) mutation to F: 25-fold increase in substrate affinity and 23-fold decrease in activity.
- H235 (≠ N238) 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.
3m0jA Structure of oxaloacetate acetylhydrolase in complex with the inhibitor 3,3-difluorooxalacetate (see paper)
34% identity, 83% coverage: 17:259/294 of query aligns to 16:263/297 of 3m0jA
- binding calcium ion: E218 (≠ I214), N219 (≠ G215)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y44 (= Y45), T46 (= T47), G47 (= G48), A48 (= A49), D88 (= D87), G126 (= G125), R162 (= R159), E192 (= E189), N215 (= N211), S241 (≠ A237)
3fa4A Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, triclinic crystal form (see paper)
34% identity, 90% coverage: 1:266/294 of query aligns to 2:263/284 of 3fa4A
- active site: Y43 (= Y45), T45 (= T47), G46 (= G48), A47 (= A49), D58 (= D60), D86 (= D87), D88 (= D89), H113 (≠ Q114), E115 (= E116), R153 (= R159), E183 (= E189), N206 (= N211), T213 (= T218), S215 (≠ V220)
- binding magnesium ion: D86 (= D87), D88 (= D89)
3fa3J Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
35% identity, 90% coverage: 1:266/294 of query aligns to 1:261/292 of 3fa3J
- active site: Y42 (= Y45), T44 (= T47), G45 (= G48), A46 (= A49), D57 (= D60), D85 (= D87), D87 (= D89), H112 (≠ Q114), E114 (= E116), R151 (= R159), E181 (= E189), N204 (= N211), T211 (= T218), S213 (≠ V220)
- binding manganese (ii) ion: D85 (= D87), D87 (= D89)
3m0kA Structure of oxaloacetate acetylhydrolase in complex with the product oxalate (see paper)
32% identity, 83% coverage: 17:259/294 of query aligns to 16:258/289 of 3m0kA
P56839 Phosphoenolpyruvate phosphomutase; PEP mutase; PEP phosphomutase; Phosphoenolpyruvate mutase; EC 5.4.2.9 from Mytilus edulis (Blue mussel) (see 2 papers)
28% identity, 90% coverage: 3:268/294 of query aligns to 2:263/295 of P56839
- D58 (= D60) mutation D->A,S: Abolishes enzyme activity.; mutation to N: Strongly reduces enzyme activity.
- D85 (= D87) mutation to A: Strongly reduces enzyme activity and increases KM.
- D87 (= D89) mutation to A: Strongly reduces enzyme activity.
- E114 (= E116) mutation to A: Strongly reduces enzyme activity.
- N122 (≠ C124) mutation N->A,D: Strongly reduces enzyme activity.
- R159 (= R159) mutation to A: Strongly reduces enzyme activity.
- H190 (≠ E189) mutation to A: Strongly reduces enzyme activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5uncA The crystal structure of phosphoenolpyruvate phosphomutase from streptomyces platensis subsp. Rosaceus
30% identity, 89% coverage: 10:272/294 of query aligns to 4:267/289 of 5uncA
- active site: W39 (≠ Y45), S41 (≠ T47), G42 (= G48), L43 (≠ A49), D53 (= D60), D80 (= D87), D82 (= D89), T107 (≠ Q114), E109 (= E116), K115 (= K122), N117 (≠ C124), S118 (≠ G125), R153 (= R159), H184 (≠ E189), V209 (≠ I214)
- binding alpha-D-xylopyranose: H22 (≠ F28), N23 (= N29), G26 (≠ S32), L29 (≠ V35), G239 (≠ A244), V243 (≠ M248)
1pymA Phosphoenolpyruvate mutase from mollusk in with bound mg2-oxalate (see paper)
29% identity, 87% coverage: 12:268/294 of query aligns to 7:259/291 of 1pymA
- active site: W40 (≠ Y45), S42 (≠ T47), G43 (= G48), L44 (≠ A49), D54 (= D60), D81 (= D87), D83 (= D89), C108 (≠ Q114), E110 (= E116), K116 (= K122), N118 (≠ C124), S119 (≠ G125), R155 (= R159), H186 (≠ E189), V211 (≠ N211)
- binding oxalate ion: W40 (≠ Y45), S42 (≠ T47), G43 (= G48), L44 (≠ A49), D81 (= D87), R155 (= R159)
1m1bA Crystal structure of phosphoenolpyruvate mutase complexed with sulfopyruvate (see paper)
29% identity, 87% coverage: 12:268/294 of query aligns to 7:259/291 of 1m1bA
- active site: W40 (≠ Y45), S42 (≠ T47), G43 (= G48), L44 (≠ A49), D54 (= D60), D81 (= D87), D83 (= D89), C108 (≠ Q114), E110 (= E116), K116 (= K122), N118 (≠ C124), S119 (≠ G125), R155 (= R159), H186 (≠ E189), V211 (≠ N211)
- binding magnesium ion: D81 (= D87), R155 (= R159)
- binding sulfopyruvate: S42 (≠ T47), G43 (= G48), L44 (≠ A49), D81 (= D87), N118 (≠ C124), S119 (≠ G125), L120 (≠ H126), R155 (= R159)
Query Sequence
>WP_013091796.1 NCBI__GCF_000092885.1:WP_013091796.1
MTTTSATRRAAFRAKVNQRQGLLVPGAFNAMSARVIEDAGFEAVYITGAGVTNMSLGLPD
LGFIGLAEVAEHTARIRDAVALPLIVDADTGFGNALNVRQTVRVLERSGADVIQFEDQVM
PKKCGHFSGKEVIATSEMVGKIRAAVDAREDANLQIMARTDAAAVHGIEDAIERGHRFIE
AGADILFIEATESLADIERLPGLFDVPQLINIVIGGKTPVQSRDALAKLGYGIVLYANAA
LQGAVLGMQRALGTLQSNGRLDEDATIVAPFSERQRLVNKPLYDRLDKEYAAKD
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