SitesBLAST
Comparing WP_101586816.1 NCBI__GCF_900169175.1:WP_101586816.1 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)
4iqdA Crystal structure of carboxyvinyl-carboxyphosphonate phosphorylmutase from bacillus anthracis
46% identity, 92% coverage: 15:292/301 of query aligns to 13:288/290 of 4iqdA
- active site: Y46 (= Y48), S48 (= S50), G49 (= G51), A50 (≠ G52), D60 (= D62), D87 (= D89), D89 (= D91), Q114 (≠ H116), E116 (= E118), K122 (= K124), C124 (= C126), G125 (= G127), H126 (= H128), R157 (= R161), E187 (= E191), N209 (= N213)
- binding pyruvic acid: E71 (≠ D73), R72 (≠ H74), D75 (≠ S77), G165 (= G169), L166 (= L170), Y218 (≠ L222), Y219 (≠ F223)
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)
47% identity, 94% coverage: 15:297/301 of query aligns to 10:294/296 of P77541
- SGG 45:47 (= SGG 50:52) binding substrate
- D85 (= D89) binding Mg(2+)
- D87 (= D91) binding Mg(2+)
- C123 (= C126) mutation to S: Inactive.
- CG 123:124 (= CG 126:127) binding substrate
- R158 (= R161) binding substrate
- E188 (= E191) binding substrate
- NIT 210:212 (≠ NMT 213:215) binding substrate
- R241 (= R244) binding substrate
- R270 (= R273) 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)
48% identity, 90% coverage: 15:285/301 of query aligns to 8:280/289 of 1mumA
- active site: Y41 (= Y48), S43 (= S50), G44 (= G51), G45 (= G52), D56 (= D62), D83 (= D89), D85 (= D91), H111 (= H116), E113 (= E118), K119 (= K124), C121 (= C126), G122 (= G127), H123 (= H128), R156 (= R161), E186 (= E191), N208 (= N213), T215 (≠ S220), L217 (= L222)
- binding magnesium ion: D56 (= D62), D85 (= D91)
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)
47% identity, 93% coverage: 15:293/301 of query aligns to 10:290/295 of Q56062
- SGG 45:47 (= SGG 50:52) binding substrate
- D58 (= D62) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- D85 (= D89) binding Mg(2+)
- K121 (= K124) mutation to A: 1000-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R122 (= R125) mutation to K: 2-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- C123 (= C126) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- H125 (= H128) mutation to A: 750-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R158 (= R161) binding substrate
6t4vC Crystal structure of 2-methylisocitrate lyase (prpb) from pseudomonas aeruginosa in apo form.
46% identity, 93% coverage: 15:293/301 of query aligns to 8:277/277 of 6t4vC
- active site: Y41 (= Y48), S43 (= S50), G44 (= G51), G45 (= G52), D56 (= D62), D83 (= D89), D85 (= D91), H111 (= H116), E113 (= E118), R145 (= R161), E175 (= E191), N197 (= N213), T204 (≠ S220), L206 (= L222)
- binding pyruvic acid: F88 (≠ W94), N94 (= N99)
1o5qA Crystal structure of pyruvate and mg2+ bound 2-methylisocitrate lyase (prpb) from salmonella typhimurium (see paper)
46% identity, 89% coverage: 15:282/301 of query aligns to 6:264/271 of 1o5qA
- active site: Y39 (= Y48), S41 (= S50), G42 (= G51), G43 (= G52), D54 (= D62), D81 (= D89), D83 (= D91), H109 (= H116), E111 (= E118), R143 (= R161), E173 (= E191), N195 (= N213), T202 (≠ S220), L204 (= L222)
- binding pyruvic acid: Y39 (= Y48), S41 (= S50), G43 (= G52), D81 (= D89), R143 (= R161)
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: 5:298/301 of query aligns to 21:316/318 of Q05957
- D79 (= D62) mutation to A: Reduces catalytic efficiency 1000-fold.
- D107 (= D89) binding Mg(2+)
- D109 (= D91) binding Mg(2+)
- K142 (= K124) binding Mg(2+)
- C144 (= C126) mutation to A: Loss of catalytic activity.
Sites not aligning to the query:
- 1:3 modified: propeptide, Removed in mature form
1zlpB Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
37% identity, 92% coverage: 18:294/301 of query aligns to 7:285/285 of 1zlpB
- active site: F37 (≠ Y48), S39 (= S50), G40 (= G51), Y41 (≠ G52), D52 (= D62), D80 (= D89), D82 (= D91), F107 (≠ H116), E109 (= E118), K115 (= K124), C117 (= C126), G118 (= G127), H119 (= H128), R152 (= R161), E182 (= E191), N204 (= N213), T211 (≠ S220), L213 (= L222)
- binding 5-hydroxypentanal: Y41 (≠ G52), C117 (= C126), R152 (= R161), I206 (≠ T215)
1zlpA Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
37% identity, 91% coverage: 18:290/301 of query aligns to 7:281/284 of 1zlpA
- active site: F37 (≠ Y48), S39 (= S50), G40 (= G51), Y41 (≠ G52), D52 (= D62), D80 (= D89), D82 (= D91), F107 (≠ H116), E109 (= E118), K115 (= K124), C117 (= C126), G118 (= G127), H119 (= H128), R152 (= R161), E182 (= E191), N204 (= N213), T211 (≠ S220), L213 (= L222)
- binding 5-hydroxypentanal: C117 (= C126), G118 (= G127), R152 (= R161), I206 (≠ T215)
- binding magnesium ion: D80 (= D89), K115 (= K124)
3fa3B Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
32% identity, 82% coverage: 16:261/301 of query aligns to 11:261/302 of 3fa3B
- active site: Y43 (= Y48), T45 (≠ S50), G46 (= G51), A47 (vs. gap), D58 (= D62), D86 (= D89), D88 (= D91), H113 (= H116), E115 (= E118), K121 (= K124), C123 (= C126), G124 (= G127), H125 (= H128), R160 (= R161), E190 (= E191), N213 (= N213), T220 (≠ S220), S222 (≠ L222)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y43 (= Y48), T45 (≠ S50), G46 (= G51), A47 (vs. gap), D86 (= D89), G124 (= G127), R160 (= R161), E190 (= E191), N213 (= N213), P239 (= P239)
3m0jA Structure of oxaloacetate acetylhydrolase in complex with the inhibitor 3,3-difluorooxalacetate (see paper)
36% identity, 82% coverage: 15:262/301 of query aligns to 10:264/297 of 3m0jA
- binding calcium ion: E218 (= E216), N219 (≠ F217)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y44 (= Y48), T46 (≠ S50), G47 (= G51), A48 (≠ G52), D88 (= D89), G126 (= G127), R162 (= R161), E192 (= E191), N215 (= N213), S241 (≠ P239)
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)
37% identity, 75% coverage: 12:237/301 of query aligns to 10:232/287 of Q9HUU1
- D88 (= D89) binding Mg(2+)
- Y212 (≠ F217) mutation to F: 25-fold increase in substrate affinity and 23-fold decrease in activity.
Sites not aligning to the query:
- 235 H→A: 2-fold increase in substrate affinity and 15-fold decrease in activity.; H→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)
37% identity, 75% coverage: 12:237/301 of query aligns to 8:230/284 of 3b8iA
- active site: I44 (= I49), G46 (= G51), G47 (= G52), S48 (≠ A53), D59 (= D62), D86 (= D89), D88 (= D91), T113 (≠ H116), E115 (= E118), A121 (≠ K124), F123 (≠ C126), G124 (= G127), R157 (= R161), V186 (≠ E191), M206 (≠ L211)
- binding oxalate ion: S48 (≠ A53), D86 (= D89)
Sites not aligning to the query:
5uncA The crystal structure of phosphoenolpyruvate phosphomutase from streptomyces platensis subsp. Rosaceus
32% identity, 95% coverage: 13:299/301 of query aligns to 4:289/289 of 5uncA
- active site: W39 (≠ Y48), S41 (= S50), G42 (= G51), L43 (≠ G52), D53 (= D62), D80 (= D89), D82 (= D91), T107 (≠ H116), E109 (= E118), K115 (= K124), N117 (≠ C126), S118 (≠ G127), R153 (= R161), H184 (vs. gap), V209 (≠ N213)
- binding alpha-D-xylopyranose: H22 (≠ I31), N23 (= N32), G26 (≠ N35), L29 (= L38), G239 (≠ A246), V243 (≠ I250)
3m0kA Structure of oxaloacetate acetylhydrolase in complex with the product oxalate (see paper)
34% identity, 82% coverage: 15:262/301 of query aligns to 10:259/289 of 3m0kA
P56839 Phosphoenolpyruvate phosphomutase; PEP mutase; PEP phosphomutase; Phosphoenolpyruvate mutase; EC 5.4.2.9 from Mytilus edulis (Blue mussel) (see 2 papers)
30% identity, 90% coverage: 7:277/301 of query aligns to 3:276/295 of P56839