SitesBLAST
Comparing WP_050461878.1 NCBI__GCF_001189915.1:WP_050461878.1 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)
4iqdA Crystal structure of carboxyvinyl-carboxyphosphonate phosphorylmutase from bacillus anthracis
39% identity, 86% coverage: 16:254/278 of query aligns to 22:258/290 of 4iqdA
- active site: Y46 (= Y40), S48 (≠ T42), G49 (= G43), A50 (≠ N44), D60 (= D55), D87 (= D82), D89 (= D84), Q114 (≠ H109), E116 (= E111), K122 (= K117), C124 (= C119), G125 (= G120), H126 (≠ A121), R157 (= R154), E187 (= E184), N209 (= N206)
- binding pyruvic acid: E71 (= E66), R72 (= R67), D75 (≠ A70), G165 (= G162), L166 (= L163), Y218 (≠ P214), Y219 (≠ L215)
3fa3B Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
37% identity, 91% coverage: 1:253/278 of query aligns to 3:261/302 of 3fa3B
- active site: Y43 (= Y40), T45 (= T42), G46 (= G43), A47 (≠ N44), D58 (= D55), D86 (= D82), D88 (= D84), H113 (= H109), E115 (= E111), K121 (= K117), C123 (= C119), G124 (= G120), H125 (≠ A121), R160 (= R154), E190 (= E184), N213 (= N206), T220 (= T212), S222 (≠ P214)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y43 (= Y40), T45 (= T42), G46 (= G43), A47 (≠ N44), D86 (= D82), G124 (= G120), R160 (= R154), E190 (= E184), N213 (= N206), P239 (= P231)
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)
35% identity, 96% coverage: 11:277/278 of query aligns to 35:303/318 of Q05957
- D79 (= D55) mutation to A: Reduces catalytic efficiency 1000-fold.
- D107 (= D82) binding Mg(2+)
- D109 (= D84) binding Mg(2+)
- K142 (= K117) binding Mg(2+)
- C144 (= C119) 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)
35% identity, 96% coverage: 11:277/278 of query aligns to 8:276/285 of 1zlpB
- active site: F37 (≠ Y40), S39 (≠ T42), G40 (= G43), Y41 (≠ N44), D52 (= D55), D80 (= D82), D82 (= D84), F107 (≠ H109), E109 (= E111), K115 (= K117), C117 (= C119), G118 (= G120), H119 (≠ A121), R152 (= R154), E182 (= E184), N204 (= N206), T211 (= T212), L213 (≠ P214)
- binding 5-hydroxypentanal: Y41 (≠ N44), C117 (= C119), R152 (= R154), I206 (≠ V208)
1zlpA Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
35% identity, 96% coverage: 11:277/278 of query aligns to 8:276/284 of 1zlpA
- active site: F37 (≠ Y40), S39 (≠ T42), G40 (= G43), Y41 (≠ N44), D52 (= D55), D80 (= D82), D82 (= D84), F107 (≠ H109), E109 (= E111), K115 (= K117), C117 (= C119), G118 (= G120), H119 (≠ A121), R152 (= R154), E182 (= E184), N204 (= N206), T211 (= T212), L213 (≠ P214)
- binding 5-hydroxypentanal: C117 (= C119), G118 (= G120), R152 (= R154), I206 (≠ V208)
- binding magnesium ion: D80 (= D82), K115 (= K117)
3m0jA Structure of oxaloacetate acetylhydrolase in complex with the inhibitor 3,3-difluorooxalacetate (see paper)
37% identity, 91% coverage: 16:269/278 of query aligns to 20:278/297 of 3m0jA
- binding calcium ion: E218 (vs. gap), N219 (≠ D209)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y44 (= Y40), T46 (= T42), G47 (= G43), A48 (≠ N44), D88 (= D82), G126 (= G120), R162 (= R154), E192 (= E184), N215 (= N206), S241 (≠ P231)
3fa4A Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, triclinic crystal form (see paper)
36% identity, 91% coverage: 1:253/278 of query aligns to 3:254/284 of 3fa4A
- active site: Y43 (= Y40), T45 (= T42), G46 (= G43), A47 (≠ N44), D58 (= D55), D86 (= D82), D88 (= D84), H113 (= H109), E115 (= E111), R153 (= R154), E183 (= E184), N206 (= N206), T213 (= T212), S215 (≠ P214)
- binding magnesium ion: D86 (= D82), D88 (= D84)
3fa3J Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
36% identity, 91% coverage: 1:253/278 of query aligns to 2:252/292 of 3fa3J
- active site: Y42 (= Y40), T44 (= T42), G45 (= G43), A46 (≠ N44), D57 (= D55), D85 (= D82), D87 (= D84), H112 (= H109), E114 (= E111), R151 (= R154), E181 (= E184), N204 (= N206), T211 (= T212), S213 (≠ P214)
- binding manganese (ii) ion: D85 (= D82), D87 (= D84)
3m0kA Structure of oxaloacetate acetylhydrolase in complex with the product oxalate (see paper)
36% identity, 91% coverage: 16:269/278 of query aligns to 20:273/289 of 3m0kA
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)
37% identity, 82% coverage: 21:249/278 of query aligns to 24:250/296 of P77541
- SGG 45:47 (≠ TGN 42:44) binding substrate
- D85 (= D82) binding Mg(2+)
- D87 (= D84) binding Mg(2+)
- C123 (= C119) mutation to S: Inactive.
- CG 123:124 (= CG 119:120) binding substrate
- R158 (= R154) binding substrate
- E188 (= E184) binding substrate
- NIT 210:212 (≠ NAV 206:208) binding substrate
- R241 (≠ L236) 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)
37% identity, 82% coverage: 21:249/278 of query aligns to 22:248/289 of 1mumA
- active site: Y41 (= Y40), S43 (≠ T42), G44 (= G43), G45 (≠ N44), D56 (= D55), D83 (= D82), D85 (= D84), H111 (= H109), E113 (= E111), K119 (= K117), C121 (= C119), G122 (= G120), H123 (≠ A121), R156 (= R154), E186 (= E184), N208 (= N206), T215 (= T212), L217 (≠ P214)
- binding magnesium ion: D56 (= D55), D85 (= D84)
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)
34% identity, 89% coverage: 21:267/278 of query aligns to 24:268/295 of Q56062
- SGG 45:47 (≠ TGN 42:44) binding substrate
- D58 (= D55) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- D85 (= D82) binding Mg(2+)
- K121 (= K117) mutation to A: 1000-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R122 (≠ K118) mutation to K: 2-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- C123 (= C119) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- H125 (≠ A121) mutation to A: 750-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R158 (= R154) binding substrate
1o5qA Crystal structure of pyruvate and mg2+ bound 2-methylisocitrate lyase (prpb) from salmonella typhimurium (see paper)
33% identity, 89% coverage: 21:267/278 of query aligns to 20:253/271 of 1o5qA
- active site: Y39 (= Y40), S41 (≠ T42), G42 (= G43), G43 (≠ N44), D54 (= D55), D81 (= D82), D83 (= D84), H109 (= H109), E111 (= E111), R143 (= R154), E173 (= E184), N195 (= N206), T202 (= T212), L204 (≠ P214)
- binding pyruvic acid: Y39 (= Y40), S41 (≠ T42), G43 (≠ N44), D81 (= D82), R143 (= R154)
2hjpA Crystal structure of phosphonopyruvate hydrolase complex with phosphonopyruvate and mg++ (see paper)
43% identity, 68% coverage: 1:188/278 of query aligns to 1:183/283 of 2hjpA
- active site: W40 (≠ Y40), S42 (≠ T42), G43 (= G43), F44 (≠ N44), D54 (= D55), D81 (= D82), D83 (= D84), V108 (≠ H109), E110 (= E111), K116 (= K117), T118 (≠ C119), R148 (= R154), H179 (≠ E184)
- binding phosphonopyruvate: W40 (≠ Y40), S42 (≠ T42), F44 (≠ N44), D81 (= D82), R148 (= R154), H179 (≠ E184), R181 (≠ L186)
- binding alpha-D-xylopyranose: E32 (= E32), S75 (≠ K76)
Sites not aligning to the query:
2duaA Crystal structure of phosphonopyruvate hydrolase complex with oxalate and mg++ (see paper)
43% identity, 68% coverage: 1:188/278 of query aligns to 1:183/283 of 2duaA
- active site: W40 (≠ Y40), S42 (≠ T42), G43 (= G43), F44 (≠ N44), D54 (= D55), D81 (= D82), D83 (= D84), V108 (≠ H109), E110 (= E111), K116 (= K117), T118 (≠ C119), R148 (= R154), H179 (≠ E184)
- binding oxalate ion: W40 (≠ Y40), S42 (≠ T42), F44 (≠ N44), D81 (= D82), R148 (= R154)
- binding alpha-D-xylopyranose: E32 (= E32), S75 (≠ K76)
Sites not aligning to the query:
Q84G06 Phosphonopyruvate hydrolase; PPH; EC 3.11.1.3 from Variovorax sp. (strain Pal2) (see paper)
43% identity, 68% coverage: 1:188/278 of query aligns to 1:190/290 of Q84G06
- D81 (= D82) binding Mg(2+)
- R188 (≠ L186) mutation to A: Reduced affinity for substrate.
5uncA The crystal structure of phosphoenolpyruvate phosphomutase from streptomyces platensis subsp. Rosaceus
40% identity, 65% coverage: 8:187/278 of query aligns to 3:198/289 of 5uncA
- active site: W39 (≠ Y40), S41 (≠ T42), G42 (= G43), L43 (≠ N44), D53 (= D55), D80 (= D82), D82 (= D84), T107 (≠ H109), E109 (= E111), K115 (= K117), N117 (≠ C119), S118 (≠ G120), R153 (= R154), H184 (≠ Y173)
- binding alpha-D-xylopyranose: H22 (= H23), N23 (≠ D24), G26 (= G27), L29 (≠ I30)
Sites not aligning to the query:
6t4vC Crystal structure of 2-methylisocitrate lyase (prpb) from pseudomonas aeruginosa in apo form.
33% identity, 77% coverage: 21:234/278 of query aligns to 22:226/277 of 6t4vC
- active site: Y41 (= Y40), S43 (≠ T42), G44 (= G43), G45 (≠ N44), D56 (= D55), D83 (= D82), D85 (= D84), H111 (= H109), E113 (= E111), R145 (= R154), E175 (= E184), N197 (= N206), T204 (= T212), L206 (≠ P214)
- binding pyruvic acid: F88 (≠ Y87), N94 (= N92)
3b8iA Crystal structure of oxaloacetate decarboxylase from pseudomonas aeruginosa (pa4872) in complex with oxalate and mg2+. (see paper)
37% identity, 74% coverage: 24:228/278 of query aligns to 28:229/284 of 3b8iA
- active site: I44 (≠ Y40), G46 (≠ T42), G47 (= G43), S48 (≠ N44), D59 (= D55), D86 (= D82), D88 (= D84), T113 (≠ H109), E115 (= E111), A121 (≠ K117), F123 (≠ C119), G124 (= G120), R157 (= R154), V186 (≠ E184), M206 (= M204)
- binding oxalate ion: S48 (≠ N44), D86 (= D82)
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)
37% identity, 74% coverage: 24:228/278 of query aligns to 30:231/287 of Q9HUU1
- D88 (= D82) binding Mg(2+)
- Y212 (≠ G210) 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_050461878.1 NCBI__GCF_001189915.1:WP_050461878.1
MTQTLSLAARLRQPGIVVAPGCHDALGARIFEQAGFEAVYMTGNGLSASLLGAPDIGLLG
MSEMTERGRAFAATVKVPVIADADTGYGNLNNVERTVRDYEAAGVQAIHLEDQVTPKKCG
AMKGLALISKEEHADKIRVAVQTRKHADFLIIGRSDARIPLGLDEAIARGQAYAEAGADL
VLLEMLQSEEEMQRAIASIDAPLMFNAVDGKTPPLTAMQLETLGFRLLSFPISSTLAYAH
MMLRFAEHIKHTGNAFGSPGGAVSIAEYEALLGIANYR
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