SitesBLAST
Comparing WP_077279739.1 NCBI__GCF_002000365.1:WP_077279739.1 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)
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)
71% identity, 96% coverage: 8:295/301 of query aligns to 5:293/295 of Q56062
- SGG 45:47 (= SGG 48:50) binding substrate
- D58 (= D61) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- D85 (= D88) 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 (= R160) 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)
70% identity, 95% coverage: 8:292/301 of query aligns to 5:290/296 of P77541
- SGG 45:47 (= SGG 48:50) binding substrate
- D85 (= D88) binding Mg(2+)
- D87 (= D90) binding Mg(2+)
- C123 (= C126) mutation to S: Inactive.
- CG 123:124 (= CG 126:127) binding substrate
- R158 (= R160) binding substrate
- E188 (= E190) binding substrate
- NIT 210:212 (= NIT 212:214) binding substrate
- R241 (= R243) binding substrate
- R270 (= R272) 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)
70% identity, 95% coverage: 8:292/301 of query aligns to 3:288/289 of 1mumA
- active site: Y41 (= Y46), S43 (= S48), G44 (= G49), G45 (= G50), D56 (= D61), D83 (= D88), D85 (= D90), H111 (= H116), E113 (= E118), K119 (= K124), C121 (= C126), G122 (= G127), H123 (= H128), R156 (= R160), E186 (= E190), N208 (= N212), T215 (= T219), L217 (= L221)
- binding magnesium ion: D56 (= D61), D85 (= D90)
6t4vC Crystal structure of 2-methylisocitrate lyase (prpb) from pseudomonas aeruginosa in apo form.
69% identity, 95% coverage: 6:292/301 of query aligns to 1:277/277 of 6t4vC
- active site: Y41 (= Y46), S43 (= S48), G44 (= G49), G45 (= G50), D56 (= D61), D83 (= D88), D85 (= D90), H111 (= H116), E113 (= E118), R145 (= R160), E175 (= E190), N197 (= N212), T204 (= T219), L206 (= L221)
- binding pyruvic acid: F88 (= F93), N94 (= N99)
1o5qA Crystal structure of pyruvate and mg2+ bound 2-methylisocitrate lyase (prpb) from salmonella typhimurium (see paper)
69% identity, 93% coverage: 8:288/301 of query aligns to 1:271/271 of 1o5qA
- active site: Y39 (= Y46), S41 (= S48), G42 (= G49), G43 (= G50), D54 (= D61), D81 (= D88), D83 (= D90), H109 (= H116), E111 (= E118), R143 (= R160), E173 (= E190), N195 (= N212), T202 (= T219), L204 (= L221)
- binding pyruvic acid: Y39 (= Y46), S41 (= S48), G43 (= G50), D81 (= D88), R143 (= R160)
4iqdA Crystal structure of carboxyvinyl-carboxyphosphonate phosphorylmutase from bacillus anthracis
44% identity, 91% coverage: 12:286/301 of query aligns to 12:283/290 of 4iqdA
- active site: Y46 (= Y46), S48 (= S48), G49 (= G49), A50 (≠ G50), D60 (= D61), D87 (= D88), D89 (= D90), Q114 (≠ H116), E116 (= E118), K122 (= K124), C124 (= C126), G125 (= G127), H126 (= H128), R157 (= R160), E187 (= E190), N209 (= N212)
- binding pyruvic acid: E71 (= E72), R72 (≠ D73), D75 (≠ R76), G165 (= G168), L166 (= L169), Y218 (≠ L221), Y219 (≠ F222)
3fa3B Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
38% identity, 84% coverage: 7:260/301 of query aligns to 3:261/302 of 3fa3B
- active site: Y43 (= Y46), T45 (≠ S48), G46 (= G49), A47 (≠ G50), D58 (= D61), D86 (= D88), D88 (= D90), H113 (= H116), E115 (= E118), K121 (= K124), C123 (= C126), G124 (= G127), H125 (= H128), R160 (= R160), E190 (= E190), N213 (= N212), T220 (= T219), S222 (≠ L221)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y43 (= Y46), T45 (≠ S48), G46 (= G49), A47 (≠ G50), D86 (= D88), G124 (= G127), R160 (= R160), E190 (= E190), N213 (= N212), P239 (= P238)
1zlpB Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
36% identity, 90% coverage: 13:284/301 of query aligns to 4:276/285 of 1zlpB
- active site: F37 (≠ Y46), S39 (= S48), G40 (= G49), Y41 (≠ G50), D52 (= D61), D80 (≠ A89), D82 (≠ T91), F107 (≠ H116), E109 (= E118), K115 (= K124), C117 (= C126), G118 (= G127), H119 (= H128), R152 (= R160), E182 (= E190), N204 (= N212), T211 (= T219), L213 (= L221)
- binding 5-hydroxypentanal: Y41 (≠ G50), C117 (= C126), R152 (= R160), I206 (≠ T214)
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, 90% coverage: 13:284/301 of query aligns to 31:303/318 of Q05957
- D79 (= D61) mutation to A: Reduces catalytic efficiency 1000-fold.
- D107 (≠ A89) binding Mg(2+)
- D109 (≠ T91) 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
1zlpA Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
36% identity, 90% coverage: 13:284/301 of query aligns to 4:276/284 of 1zlpA
- active site: F37 (≠ Y46), S39 (= S48), G40 (= G49), Y41 (≠ G50), D52 (= D61), D80 (≠ A89), D82 (≠ T91), F107 (≠ H116), E109 (= E118), K115 (= K124), C117 (= C126), G118 (= G127), H119 (= H128), R152 (= R160), E182 (= E190), N204 (= N212), T211 (= T219), L213 (= L221)
- binding 5-hydroxypentanal: C117 (= C126), G118 (= G127), R152 (= R160), I206 (≠ T214)
- binding magnesium ion: D80 (≠ A89), K115 (= K124)
3fa4A Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, triclinic crystal form (see paper)
36% identity, 84% coverage: 7:260/301 of query aligns to 3:254/284 of 3fa4A
- active site: Y43 (= Y46), T45 (≠ S48), G46 (= G49), A47 (≠ G50), D58 (= D61), D86 (= D88), D88 (= D90), H113 (= H116), E115 (= E118), R153 (= R160), E183 (= E190), N206 (= N212), T213 (= T219), S215 (≠ L221)
- binding magnesium ion: D86 (= D88), D88 (= D90)
3m0jA Structure of oxaloacetate acetylhydrolase in complex with the inhibitor 3,3-difluorooxalacetate (see paper)
37% identity, 77% coverage: 12:242/301 of query aligns to 9:245/297 of 3m0jA
- binding calcium ion: E218 (= E215), N219 (≠ F216)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y44 (= Y46), T46 (≠ S48), G47 (= G49), A48 (≠ G50), D88 (= D88), G126 (= G127), R162 (= R160), E192 (= E190), N215 (= N212), S241 (≠ P238)
3fa3J Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
35% identity, 84% coverage: 7:260/301 of query aligns to 2:252/292 of 3fa3J
- active site: Y42 (= Y46), T44 (≠ S48), G45 (= G49), A46 (≠ G50), D57 (= D61), D85 (= D88), D87 (= D90), H112 (= H116), E114 (= E118), R151 (= R160), E181 (= E190), N204 (= N212), T211 (= T219), S213 (≠ L221)
- binding manganese (ii) ion: D85 (= D88), D87 (= D90)
3m0kA Structure of oxaloacetate acetylhydrolase in complex with the product oxalate (see paper)
36% identity, 77% coverage: 12:242/301 of query aligns to 9:240/289 of 3m0kA
1pymA Phosphoenolpyruvate mutase from mollusk in with bound mg2-oxalate (see paper)
31% identity, 88% coverage: 12:276/301 of query aligns to 6:272/291 of 1pymA
- active site: W40 (≠ Y46), S42 (= S48), G43 (= G49), L44 (≠ G50), D54 (= D61), D81 (= D88), D83 (= D90), C108 (≠ H116), E110 (= E118), K116 (= K124), N118 (≠ C126), S119 (≠ G127), R155 (= R160), H186 (≠ E190), V211 (≠ N212)
- binding oxalate ion: W40 (≠ Y46), S42 (= S48), G43 (= G49), L44 (≠ G50), D81 (= D88), R155 (= R160)
1m1bA Crystal structure of phosphoenolpyruvate mutase complexed with sulfopyruvate (see paper)
31% identity, 88% coverage: 12:276/301 of query aligns to 6:272/291 of 1m1bA
- active site: W40 (≠ Y46), S42 (= S48), G43 (= G49), L44 (≠ G50), D54 (= D61), D81 (= D88), D83 (= D90), C108 (≠ H116), E110 (= E118), K116 (= K124), N118 (≠ C126), S119 (≠ G127), R155 (= R160), H186 (≠ E190), V211 (≠ N212)
- binding magnesium ion: D81 (= D88), R155 (= R160)
- binding sulfopyruvate: S42 (= S48), G43 (= G49), L44 (≠ G50), D81 (= D88), N118 (≠ C126), S119 (≠ G127), L120 (≠ H128), R155 (= R160)
P56839 Phosphoenolpyruvate phosphomutase; PEP mutase; PEP phosphomutase; Phosphoenolpyruvate mutase; EC 5.4.2.9 from Mytilus edulis (Blue mussel) (see 2 papers)
31% identity, 88% coverage: 12:276/301 of query aligns to 10:276/295 of P56839
- D58 (= D61) mutation D->A,S: Abolishes enzyme activity.; mutation to N: Strongly reduces enzyme activity.
- D85 (= D88) mutation to A: Strongly reduces enzyme activity and increases KM.
- D87 (= D90) mutation to A: Strongly reduces enzyme activity.
- E114 (= E118) mutation to A: Strongly reduces enzyme activity.
- N122 (≠ C126) mutation N->A,D: Strongly reduces enzyme activity.
- R159 (= R160) mutation to A: Strongly reduces enzyme activity.
- H190 (≠ E190) 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
31% identity, 94% coverage: 11:293/301 of query aligns to 4:287/289 of 5uncA
- active site: W39 (≠ Y46), S41 (= S48), G42 (= G49), L43 (≠ G50), D53 (= D61), D80 (= D88), D82 (= D90), T107 (≠ H116), E109 (= E118), K115 (= K124), N117 (≠ C126), S118 (≠ G127), R153 (= R160), H184 (vs. gap), V209 (≠ N212)
- binding alpha-D-xylopyranose: H22 (≠ I29), N23 (= N30), G26 (≠ H33), L29 (= L36), G239 (≠ M245), V243 (≠ A249)
Q84G06 Phosphonopyruvate hydrolase; PPH; EC 3.11.1.3 from Variovorax sp. (strain Pal2) (see paper)
32% identity, 91% coverage: 7:280/301 of query aligns to 1:277/290 of Q84G06
- D81 (= D88) binding Mg(2+)
- R188 (≠ V192) mutation to A: Reduced affinity for substrate.
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)
29% identity, 83% coverage: 11:259/301 of query aligns to 11:252/287 of Q9HUU1
- D88 (= D88) binding Mg(2+)
- Y212 (≠ F216) mutation to F: 25-fold increase in substrate affinity and 23-fold decrease in activity.
- H235 (≠ L239) 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.
Query Sequence
>WP_077279739.1 NCBI__GCF_002000365.1:WP_077279739.1
MSDLNALTPGARLRQAVSEEKPLQVVGAINAYHATLAEHAGYRALYLSGGGVAAGSLALP
DLGISTLHDVLEDVRRITYITQLPLLVDADTGFGPSAFNIARTVRELIRAGAAGCHIEDQ
VQSKRCGHRPGKAIVSKGEMVDRIKAAADARTDDFVIMARTDALAGEGLEAALERAVACV
DAGADMIFPEAVTELDQYRRFVEATGVPVLANITEFGQTPLFTTGELRDAGVGLALYPLS
AFRAMNQAAMKVYEAIRRDGTQKAVLDIMQTRDELYEHLGYHAYEQQLDRLYRQEGDNAD
D
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