SitesBLAST
Comparing WP_092350749.1 NCBI__GCF_900107645.1:WP_092350749.1 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
50% identity, 93% coverage: 17:295/299 of query aligns to 12:290/290 of 4iqdA
- active site: Y46 (= Y51), S48 (= S53), G49 (= G54), A50 (≠ G55), D60 (= D65), D87 (= D92), D89 (= D94), Q114 (≠ H119), E116 (= E121), K122 (= K127), C124 (= C129), G125 (= G130), H126 (= H131), R157 (= R162), E187 (= E192), N209 (= N214)
- binding pyruvic acid: E71 (≠ G76), R72 (≠ F77), D75 (≠ T80), G165 (= G170), L166 (= L171), Y218 (= Y223), Y219 (≠ L224)
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)
43% identity, 92% coverage: 14:287/299 of query aligns to 6:283/295 of Q56062
- SGG 45:47 (= SGG 53:55) binding substrate
- D58 (= D65) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- D85 (= D92) binding Mg(2+)
- K121 (= K127) mutation to A: 1000-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R122 (≠ K128) mutation to K: 2-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- C123 (= C129) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- H125 (= H131) mutation to A: 750-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R158 (= R162) 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, 96% coverage: 14:299/299 of query aligns to 6:296/296 of P77541
- SGG 45:47 (= SGG 53:55) binding substrate
- D85 (= D92) binding Mg(2+)
- D87 (= D94) binding Mg(2+)
- C123 (= C129) mutation to S: Inactive.
- CG 123:124 (= CG 129:130) binding substrate
- R158 (= R162) binding substrate
- E188 (= E192) binding substrate
- NIT 210:212 (≠ NMT 214:216) binding substrate
- R241 (= R245) binding substrate
- R270 (= R274) 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)
42% identity, 92% coverage: 14:287/299 of query aligns to 4:281/289 of 1mumA
- active site: Y41 (= Y51), S43 (= S53), G44 (= G54), G45 (= G55), D56 (= D65), D83 (= D92), D85 (= D94), H111 (= H119), E113 (= E121), K119 (= K127), C121 (= C129), G122 (= G130), H123 (= H131), R156 (= R162), E186 (= E192), N208 (= N214), T215 (= T221), L217 (≠ Y223)
- binding magnesium ion: D56 (= D65), D85 (= D94)
1o5qA Crystal structure of pyruvate and mg2+ bound 2-methylisocitrate lyase (prpb) from salmonella typhimurium (see paper)
41% identity, 92% coverage: 14:287/299 of query aligns to 2:268/271 of 1o5qA
- active site: Y39 (= Y51), S41 (= S53), G42 (= G54), G43 (= G55), D54 (= D65), D81 (= D92), D83 (= D94), H109 (= H119), E111 (= E121), R143 (= R162), E173 (= E192), N195 (= N214), T202 (= T221), L204 (≠ Y223)
- binding pyruvic acid: Y39 (= Y51), S41 (= S53), G43 (= G55), D81 (= D92), R143 (= R162)
6t4vC Crystal structure of 2-methylisocitrate lyase (prpb) from pseudomonas aeruginosa in apo form.
40% identity, 92% coverage: 14:287/299 of query aligns to 4:270/277 of 6t4vC
- active site: Y41 (= Y51), S43 (= S53), G44 (= G54), G45 (= G55), D56 (= D65), D83 (= D92), D85 (= D94), H111 (= H119), E113 (= E121), R145 (= R162), E175 (= E192), N197 (= N214), T204 (= T221), L206 (≠ Y223)
- binding pyruvic acid: F88 (≠ Y97), N94 (= N102)
3fa3B Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
38% identity, 86% coverage: 25:280/299 of query aligns to 17:277/302 of 3fa3B
- active site: Y43 (= Y51), T45 (≠ S53), G46 (= G54), A47 (≠ G55), D58 (= D65), D86 (= D92), D88 (= D94), H113 (= H119), E115 (= E121), K121 (= K127), C123 (= C129), G124 (= G130), H125 (= H131), R160 (= R162), E190 (= E192), N213 (= N214), T220 (= T221), S222 (≠ Y223)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y43 (= Y51), T45 (≠ S53), G46 (= G54), A47 (≠ G55), D86 (= D92), G124 (= G130), R160 (= R162), E190 (= E192), N213 (= N214), P239 (= P240)
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: 18:291/299 of query aligns to 31:308/318 of Q05957
- D79 (= D65) mutation to A: Reduces catalytic efficiency 1000-fold.
- D107 (= D92) binding Mg(2+)
- D109 (= D94) binding Mg(2+)
- K142 (= K127) binding Mg(2+)
- C144 (= C129) 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: 18:291/299 of query aligns to 4:281/284 of 1zlpA
- active site: F37 (≠ Y51), S39 (= S53), G40 (= G54), Y41 (≠ G55), D52 (= D65), D80 (= D92), D82 (= D94), F107 (≠ H119), E109 (= E121), K115 (= K127), C117 (= C129), G118 (= G130), H119 (= H131), R152 (= R162), E182 (= E192), N204 (= N214), T211 (= T221), L213 (≠ Y223)
- binding 5-hydroxypentanal: C117 (= C129), G118 (= G130), R152 (= R162), I206 (≠ T216)
- binding magnesium ion: D80 (= D92), K115 (= K127)
1zlpB Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
38% identity, 92% coverage: 18:291/299 of query aligns to 4:281/285 of 1zlpB
- active site: F37 (≠ Y51), S39 (= S53), G40 (= G54), Y41 (≠ G55), D52 (= D65), D80 (= D92), D82 (= D94), F107 (≠ H119), E109 (= E121), K115 (= K127), C117 (= C129), G118 (= G130), H119 (= H131), R152 (= R162), E182 (= E192), N204 (= N214), T211 (= T221), L213 (≠ Y223)
- binding 5-hydroxypentanal: Y41 (≠ G55), C117 (= C129), R152 (= R162), I206 (≠ T216)
3fa4A Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, triclinic crystal form (see paper)
37% identity, 86% coverage: 25:280/299 of query aligns to 17:270/284 of 3fa4A
- active site: Y43 (= Y51), T45 (≠ S53), G46 (= G54), A47 (≠ G55), D58 (= D65), D86 (= D92), D88 (= D94), H113 (= H119), E115 (= E121), R153 (= R162), E183 (= E192), N206 (= N214), T213 (= T221), S215 (≠ Y223)
- binding magnesium ion: D86 (= D92), D88 (= D94)
3fa3J Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
37% identity, 86% coverage: 25:280/299 of query aligns to 16:268/292 of 3fa3J
- active site: Y42 (= Y51), T44 (≠ S53), G45 (= G54), A46 (≠ G55), D57 (= D65), D85 (= D92), D87 (= D94), H112 (= H119), E114 (= E121), R151 (= R162), E181 (= E192), N204 (= N214), T211 (= T221), S213 (≠ Y223)
- binding manganese (ii) ion: D85 (= D92), D87 (= D94)
3m0jA Structure of oxaloacetate acetylhydrolase in complex with the inhibitor 3,3-difluorooxalacetate (see paper)
34% identity, 89% coverage: 16:280/299 of query aligns to 8:279/297 of 3m0jA
- binding calcium ion: E218 (= E217), N219 (≠ F218)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y44 (= Y51), T46 (≠ S53), G47 (= G54), A48 (≠ G55), D88 (= D92), G126 (= G130), R162 (= R162), E192 (= E192), N215 (= N214), S241 (≠ P240)
1pymA Phosphoenolpyruvate mutase from mollusk in with bound mg2-oxalate (see paper)
31% identity, 88% coverage: 17:280/299 of query aligns to 6:274/291 of 1pymA
- active site: W40 (≠ Y51), S42 (= S53), G43 (= G54), L44 (≠ G55), D54 (= D65), D81 (= D92), D83 (= D94), C108 (≠ H119), E110 (= E121), K116 (= K128), N118 (≠ G130), S119 (≠ H131), R155 (= R162), H186 (≠ E192), V211 (≠ N214)
- binding oxalate ion: W40 (≠ Y51), S42 (= S53), G43 (= G54), L44 (≠ G55), D81 (= D92), R155 (= R162)
1m1bA Crystal structure of phosphoenolpyruvate mutase complexed with sulfopyruvate (see paper)
31% identity, 88% coverage: 17:280/299 of query aligns to 6:274/291 of 1m1bA
- active site: W40 (≠ Y51), S42 (= S53), G43 (= G54), L44 (≠ G55), D54 (= D65), D81 (= D92), D83 (= D94), C108 (≠ H119), E110 (= E121), K116 (= K128), N118 (≠ G130), S119 (≠ H131), R155 (= R162), H186 (≠ E192), V211 (≠ N214)
- binding magnesium ion: D81 (= D92), R155 (= R162)
- binding sulfopyruvate: S42 (= S53), G43 (= G54), L44 (≠ G55), D81 (= D92), N118 (≠ G130), S119 (≠ H131), L120 (= L132), R155 (= R162)
P56839 Phosphoenolpyruvate phosphomutase; PEP mutase; PEP phosphomutase; Phosphoenolpyruvate mutase; EC 5.4.2.9 from Mytilus edulis (Blue mussel) (see 2 papers)
30% identity, 91% coverage: 9:280/299 of query aligns to 2:278/295 of P56839
- D58 (= D65) mutation D->A,S: Abolishes enzyme activity.; mutation to N: Strongly reduces enzyme activity.
- D85 (= D92) mutation to A: Strongly reduces enzyme activity and increases KM.
- D87 (= D94) mutation to A: Strongly reduces enzyme activity.
- E114 (= E121) mutation to A: Strongly reduces enzyme activity.
- N122 (≠ G130) mutation N->A,D: Strongly reduces enzyme activity.
- R159 (= R162) mutation to A: Strongly reduces enzyme activity.
- H190 (≠ E192) mutation to A: Strongly reduces enzyme activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
3m0kA Structure of oxaloacetate acetylhydrolase in complex with the product oxalate (see paper)
32% identity, 89% coverage: 16:280/299 of query aligns to 8:274/289 of 3m0kA
5uncA The crystal structure of phosphoenolpyruvate phosphomutase from streptomyces platensis subsp. Rosaceus
34% identity, 82% coverage: 17:262/299 of query aligns to 5:254/289 of 5uncA
- active site: W39 (≠ Y51), S41 (= S53), G42 (= G54), L43 (≠ G55), D53 (= D65), D80 (= D92), D82 (= D94), T107 (≠ H119), E109 (= E121), K115 (= K127), N117 (≠ C129), S118 (≠ G130), R153 (= R162), H184 (≠ E192), V209 (≠ G219)
- binding alpha-D-xylopyranose: H22 (= H34), N23 (= N35), G26 (≠ A38), L29 (= L41), G239 (≠ A247), V243 (≠ M251)
3b8iA Crystal structure of oxaloacetate decarboxylase from pseudomonas aeruginosa (pa4872) in complex with oxalate and mg2+. (see paper)
36% identity, 68% coverage: 35:238/299 of query aligns to 28:230/284 of 3b8iA
- active site: I44 (≠ Y51), G46 (= G54), G47 (= G55), S48 (≠ A56), D59 (= D65), D86 (= D92), D88 (= D94), T113 (≠ H119), E115 (= E121), A121 (≠ K127), F123 (≠ C129), G124 (= G130), R157 (= R162), V186 (≠ E192), M206 (≠ L212)
- binding oxalate ion: S48 (≠ A56), D86 (= D92)
Sites not aligning to the query:
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, 68% coverage: 35:238/299 of query aligns to 30:232/287 of Q9HUU1
- D88 (= D92) binding Mg(2+)
- Y212 (≠ F218) 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.
Query Sequence
>WP_092350749.1 NCBI__GCF_900107645.1:WP_092350749.1
MNWLEGNNAIEVLPGERLDQLLQRDGILKIPGAHNALAGLLAREAGFEALYLSGGAISAS
MGLADLGIMTIEELCGFVKTIARATNLPIIVDGDTGYGEALNVMRLVRELETSGAAAVHI
EDQVLPKKCGHLSDKCLIPAEAMAEKIAAAVKARTHLKIIARTDSFASEGLEGLINRSKR
YLDAGADAIFPEALTSIEEFQTVANALDCPLLANMTEFGQTPYLTADEFEQLGYKMLIWP
VSSLRIAAGAMETFYNQLFENGTAKPQLEKMLTRKRLYQVLDYEGYEALDSAILKSSYK
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