SitesBLAST
Comparing WP_011813871.1 NCBI__GCF_000015585.1:WP_011813871.1 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)
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)
64% identity, 95% coverage: 6:292/301 of query aligns to 5:292/296 of P77541
- SGG 45:47 (≠ SGA 46:48) binding substrate
- D85 (= D86) binding Mg(2+)
- D87 (= D88) binding Mg(2+)
- C123 (= C123) mutation to S: Inactive.
- CG 123:124 (= CG 123:124) binding substrate
- R158 (= R158) binding substrate
- E188 (= E188) binding substrate
- NIT 210:212 (= NIT 210:212) binding substrate
- R241 (= R241) binding substrate
- R270 (= R270) 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)
64% identity, 95% coverage: 6:290/301 of query aligns to 3:288/289 of 1mumA
- active site: Y41 (= Y44), S43 (= S46), G44 (= G47), G45 (≠ A48), D56 (= D59), D83 (= D86), D85 (= D88), H111 (= H113), E113 (= E115), K119 (= K121), C121 (= C123), G122 (= G124), H123 (= H125), R156 (= R158), E186 (= E188), N208 (= N210), T215 (= T217), L217 (≠ Y219)
- binding magnesium ion: D56 (= D59), D85 (= D88)
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)
64% identity, 95% coverage: 6:290/301 of query aligns to 5:290/295 of Q56062
- SGG 45:47 (≠ SGA 46:48) binding substrate
- D58 (= D59) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- D85 (= D86) binding Mg(2+)
- K121 (= K121) mutation to A: 1000-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R122 (= R122) mutation to K: 2-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- C123 (= C123) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- H125 (= H125) mutation to A: 750-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R158 (= R158) binding substrate
6t4vC Crystal structure of 2-methylisocitrate lyase (prpb) from pseudomonas aeruginosa in apo form.
63% identity, 95% coverage: 6:290/301 of query aligns to 3:277/277 of 6t4vC
- active site: Y41 (= Y44), S43 (= S46), G44 (= G47), G45 (≠ A48), D56 (= D59), D83 (= D86), D85 (= D88), H111 (= H113), E113 (= E115), R145 (= R158), E175 (= E188), N197 (= N210), T204 (= T217), L206 (≠ Y219)
- binding pyruvic acid: F88 (= F91), N94 (≠ S96)
1o5qA Crystal structure of pyruvate and mg2+ bound 2-methylisocitrate lyase (prpb) from salmonella typhimurium (see paper)
61% identity, 93% coverage: 6:286/301 of query aligns to 1:271/271 of 1o5qA
- active site: Y39 (= Y44), S41 (= S46), G42 (= G47), G43 (≠ A48), D54 (= D59), D81 (= D86), D83 (= D88), H109 (= H113), E111 (= E115), R143 (= R158), E173 (= E188), N195 (= N210), T202 (= T217), L204 (≠ Y219)
- binding pyruvic acid: Y39 (= Y44), S41 (= S46), G43 (≠ A48), D81 (= D86), R143 (= R158)
4iqdA Crystal structure of carboxyvinyl-carboxyphosphonate phosphorylmutase from bacillus anthracis
50% identity, 93% coverage: 4:283/301 of query aligns to 6:282/290 of 4iqdA
- active site: Y46 (= Y44), S48 (= S46), G49 (= G47), A50 (= A48), D60 (= D59), D87 (= D86), D89 (= D88), Q114 (≠ H113), E116 (= E115), K122 (= K121), C124 (= C123), G125 (= G124), H126 (= H125), R157 (= R158), E187 (= E188), N209 (= N210)
- binding pyruvic acid: E71 (= E70), R72 (≠ D71), D75 (≠ R74), G165 (= G166), L166 (= L167), Y218 (= Y219), Y219 (≠ F220)
3fa3B Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
40% identity, 91% coverage: 25:298/301 of query aligns to 24:292/302 of 3fa3B
- active site: Y43 (= Y44), T45 (≠ S46), G46 (= G47), A47 (= A48), D58 (= D59), D86 (= D86), D88 (= D88), H113 (= H113), E115 (= E115), K121 (= K121), C123 (= C123), G124 (= G124), H125 (= H125), R160 (= R158), E190 (= E188), N213 (= N210), T220 (= T217), S222 (≠ Y219)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y43 (= Y44), T45 (≠ S46), G46 (= G47), A47 (= A48), D86 (= D86), G124 (= G124), R160 (= R158), E190 (= E188), N213 (= N210), P239 (= P236)
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: 25:289/301 of query aligns to 45:313/318 of Q05957
- D79 (= D59) mutation to A: Reduces catalytic efficiency 1000-fold.
- D107 (≠ T89) binding Mg(2+)
- D109 (≠ F91) binding Mg(2+)
- K142 (= K121) binding Mg(2+)
- C144 (= C123) 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)
39% identity, 87% coverage: 25:286/301 of query aligns to 18:283/285 of 1zlpB
- active site: F37 (≠ Y44), S39 (= S46), G40 (= G47), Y41 (≠ A48), D52 (= D59), D80 (≠ T89), D82 (≠ F91), F107 (≠ H113), E109 (= E115), K115 (= K121), C117 (= C123), G118 (= G124), H119 (= H125), R152 (= R158), E182 (= E188), N204 (= N210), T211 (= T217), L213 (≠ Y219)
- binding 5-hydroxypentanal: Y41 (≠ A48), C117 (= C123), R152 (= R158), I206 (≠ T212)
1zlpA Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
39% identity, 87% coverage: 25:286/301 of query aligns to 18:283/284 of 1zlpA
- active site: F37 (≠ Y44), S39 (= S46), G40 (= G47), Y41 (≠ A48), D52 (= D59), D80 (≠ T89), D82 (≠ F91), F107 (≠ H113), E109 (= E115), K115 (= K121), C117 (= C123), G118 (= G124), H119 (= H125), R152 (= R158), E182 (= E188), N204 (= N210), T211 (= T217), L213 (≠ Y219)
- binding 5-hydroxypentanal: C117 (= C123), G118 (= G124), R152 (= R158), I206 (≠ T212)
- binding magnesium ion: D80 (≠ T89), K115 (= K121)
3fa4A Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, triclinic crystal form (see paper)
38% identity, 91% coverage: 25:297/301 of query aligns to 24:284/284 of 3fa4A
- active site: Y43 (= Y44), T45 (≠ S46), G46 (= G47), A47 (= A48), D58 (= D59), D86 (= D86), D88 (= D88), H113 (= H113), E115 (= E115), R153 (= R158), E183 (= E188), N206 (= N210), T213 (= T217), S215 (≠ Y219)
- binding magnesium ion: D86 (= D86), D88 (= D88)
3fa3J Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
37% identity, 91% coverage: 25:298/301 of query aligns to 23:283/292 of 3fa3J
- active site: Y42 (= Y44), T44 (≠ S46), G45 (= G47), A46 (= A48), D57 (= D59), D85 (= D86), D87 (= D88), H112 (= H113), E114 (= E115), R151 (= R158), E181 (= E188), N204 (= N210), T211 (= T217), S213 (≠ Y219)
- binding manganese (ii) ion: D85 (= D86), D87 (= D88)
3m0jA Structure of oxaloacetate acetylhydrolase in complex with the inhibitor 3,3-difluorooxalacetate (see paper)
36% identity, 93% coverage: 3:281/301 of query aligns to 2:284/297 of 3m0jA
- binding calcium ion: E218 (= E213), N219 (≠ F214)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y44 (= Y44), T46 (≠ S46), G47 (= G47), A48 (= A48), D88 (= D86), G126 (= G124), R162 (= R158), E192 (= E188), N215 (= N210), S241 (≠ A239)
3m0kA Structure of oxaloacetate acetylhydrolase in complex with the product oxalate (see paper)
34% identity, 93% coverage: 3:281/301 of query aligns to 2:279/289 of 3m0kA
1pymA Phosphoenolpyruvate mutase from mollusk in with bound mg2-oxalate (see paper)
32% identity, 84% coverage: 23:274/301 of query aligns to 19:272/291 of 1pymA
- active site: W40 (≠ Y44), S42 (= S46), G43 (= G47), L44 (≠ A48), D54 (= D59), D81 (= D86), D83 (= D88), C108 (≠ H113), E110 (= E115), K116 (= K121), N118 (≠ C123), S119 (≠ G124), R155 (= R158), H186 (= H191), V211 (≠ L208)
- binding oxalate ion: W40 (≠ Y44), S42 (= S46), G43 (= G47), L44 (≠ A48), D81 (= D86), R155 (= R158)
1m1bA Crystal structure of phosphoenolpyruvate mutase complexed with sulfopyruvate (see paper)
32% identity, 84% coverage: 23:274/301 of query aligns to 19:272/291 of 1m1bA
- active site: W40 (≠ Y44), S42 (= S46), G43 (= G47), L44 (≠ A48), D54 (= D59), D81 (= D86), D83 (= D88), C108 (≠ H113), E110 (= E115), K116 (= K121), N118 (≠ C123), S119 (≠ G124), R155 (= R158), H186 (= H191), V211 (≠ L208)
- binding magnesium ion: D81 (= D86), R155 (= R158)
- binding sulfopyruvate: S42 (= S46), G43 (= G47), L44 (≠ A48), D81 (= D86), N118 (≠ C123), S119 (≠ G124), L120 (≠ H125), R155 (= R158)
P56839 Phosphoenolpyruvate phosphomutase; PEP mutase; PEP phosphomutase; Phosphoenolpyruvate mutase; EC 5.4.2.9 from Mytilus edulis (Blue mussel) (see 2 papers)
32% identity, 84% coverage: 23:274/301 of query aligns to 23:276/295 of P56839
- D58 (= D59) mutation D->A,S: Abolishes enzyme activity.; mutation to N: Strongly reduces enzyme activity.
- D85 (= D86) mutation to A: Strongly reduces enzyme activity and increases KM.
- D87 (= D88) mutation to A: Strongly reduces enzyme activity.
- E114 (= E115) mutation to A: Strongly reduces enzyme activity.
- N122 (≠ C123) mutation N->A,D: Strongly reduces enzyme activity.
- R159 (= R158) mutation to A: Strongly reduces enzyme activity.
- H190 (= H191) 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
35% identity, 88% coverage: 21:285/301 of query aligns to 16:281/289 of 5uncA
- active site: W39 (≠ Y44), S41 (= S46), G42 (= G47), L43 (≠ A48), D53 (= D59), D80 (= D86), D82 (= D88), T107 (≠ H113), E109 (= E115), K115 (= K121), N117 (≠ C123), S118 (≠ G124), R153 (= R158), H184 (≠ E188), V209 (≠ N210)
- binding alpha-D-xylopyranose: H22 (≠ I27), N23 (= N28), G26 (≠ S31), L29 (= L34), G239 (≠ M243), V243 (≠ A247)
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)
33% identity, 66% coverage: 11:208/301 of query aligns to 13:208/287 of Q9HUU1
- D88 (= D86) binding Mg(2+)
Sites not aligning to the query:
- 212 Y→F: 25-fold increase in substrate affinity and 23-fold decrease in activity.
- 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)
33% identity, 66% coverage: 11:208/301 of query aligns to 11:206/284 of 3b8iA
- active site: I44 (≠ Y44), G46 (≠ S46), G47 (= G47), S48 (≠ A48), D59 (= D59), D86 (= D86), D88 (= D88), T113 (≠ H113), E115 (= E115), A121 (≠ K121), F123 (≠ C123), G124 (= G124), R157 (= R158), V186 (≠ E188), M206 (≠ L208)
- binding oxalate ion: S48 (≠ A48), D86 (= D86)
Sites not aligning to the query:
Query Sequence
>WP_011813871.1 NCBI__GCF_000015585.1:WP_011813871.1
MTEQSSAGRRFRDAVADERPLQVVGAINAYSALLAERAGFRALYVSGAGVANASYGLPDL
GITQLADVVEDVRRITDATRTPVLVDIDTGFGGAFSVARTVRELTRAGAAAVHIEDQVQA
KRCGHRPGKELVSTAEMVDRVKAAVDARTDPELVVMARTDARASEGLEAAVERAEAYVEA
GADMVFAEAMHSLDDIRAFTDRVPVPVLANITEFGKTPYFTVEELREAGAGLVLYPLSAF
RAMSRAAEAVYGAIRADGTQERVLDRMQTREELYEVLGYHDYERKLDELFGRDGRTGGGQ
R
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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