SitesBLAST
Comparing WP_013136520.1 NCBI__GCF_000092245.1:WP_013136520.1 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)
65% identity, 100% coverage: 2:294/294 of query aligns to 5:296/296 of P77541
- SGG 45:47 (= SGG 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 (= R156) binding substrate
- E188 (= E186) binding substrate
- NIT 210:212 (= NIT 208:210) binding substrate
- R241 (= R239) binding substrate
- R270 (= R268) 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)
66% identity, 98% coverage: 2:289/294 of query aligns to 3:289/289 of 1mumA
- active site: Y41 (= Y40), S43 (= S42), G44 (= G43), G45 (= G44), D56 (= D55), D83 (= D82), D85 (= D84), H111 (= H109), E113 (= E111), K119 (= K117), C121 (= C119), G122 (= G120), H123 (= H121), R156 (= R156), E186 (= E186), N208 (= N208), T215 (= T215), L217 (≠ M217)
- 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)
62% identity, 99% coverage: 2:293/294 of query aligns to 5:295/295 of Q56062
- SGG 45:47 (= SGG 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 (= R118) 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 (= H121) mutation to A: 750-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R158 (= R156) binding substrate
6t4vC Crystal structure of 2-methylisocitrate lyase (prpb) from pseudomonas aeruginosa in apo form.
61% identity, 98% coverage: 1:288/294 of query aligns to 2:277/277 of 6t4vC
- active site: Y41 (= Y40), S43 (= S42), G44 (= G43), G45 (= G44), D56 (= D55), D83 (= D82), D85 (= D84), H111 (= H109), E113 (= E111), R145 (= R156), E175 (= E186), N197 (= N208), T204 (= T215), L206 (≠ M217)
- binding pyruvic acid: F88 (≠ W87), N94 (= N92)
1o5qA Crystal structure of pyruvate and mg2+ bound 2-methylisocitrate lyase (prpb) from salmonella typhimurium (see paper)
60% identity, 96% coverage: 2:284/294 of query aligns to 1:271/271 of 1o5qA
- active site: Y39 (= Y40), S41 (= S42), G42 (= G43), G43 (= G44), D54 (= D55), D81 (= D82), D83 (= D84), H109 (= H109), E111 (= E111), R143 (= R156), E173 (= E186), N195 (= N208), T202 (= T215), L204 (≠ M217)
- binding pyruvic acid: Y39 (= Y40), S41 (= S42), G43 (= G44), D81 (= D82), R143 (= R156)
4iqdA Crystal structure of carboxyvinyl-carboxyphosphonate phosphorylmutase from bacillus anthracis
44% identity, 98% coverage: 4:290/294 of query aligns to 10:290/290 of 4iqdA
- active site: Y46 (= Y40), S48 (= S42), G49 (= G43), A50 (≠ G44), D60 (= D55), D87 (= D82), D89 (= D84), Q114 (≠ H109), E116 (= E111), K122 (= K117), C124 (= C119), G125 (= G120), H126 (= H121), R157 (= R156), E187 (= E186), N209 (= N208)
- binding pyruvic acid: E71 (≠ I66), R72 (≠ D67), D75 (≠ R70), G165 (= G164), L166 (≠ Q165), Y218 (≠ M217), Y219 (≠ F218)
3fa3B Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
35% identity, 97% coverage: 1:286/294 of query aligns to 3:288/302 of 3fa3B
- active site: Y43 (= Y40), T45 (≠ S42), G46 (= G43), A47 (≠ G44), D58 (= D55), D86 (= D82), D88 (= D84), H113 (= H109), E115 (= E111), K121 (= K117), C123 (= C119), G124 (= G120), H125 (= H121), R160 (= R156), E190 (= E186), N213 (= N208), T220 (= T215), S222 (≠ M217)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y43 (= Y40), T45 (≠ S42), G46 (= G43), A47 (≠ G44), D86 (= D82), G124 (= G120), R160 (= R156), E190 (= E186), N213 (= N208), P239 (= P234)
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)
34% identity, 95% coverage: 11:290/294 of query aligns to 35:316/318 of Q05957
- D79 (= D55) mutation to A: Reduces catalytic efficiency 1000-fold.
- D107 (≠ L79) binding Mg(2+)
- D109 (≠ V81) 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, 94% coverage: 11:286/294 of query aligns to 8:285/285 of 1zlpB
- active site: F37 (≠ Y40), S39 (= S42), G40 (= G43), Y41 (≠ G44), D52 (= D55), D80 (≠ L79), D82 (≠ V81), F107 (≠ H109), E109 (= E111), K115 (= K117), C117 (= C119), G118 (= G120), H119 (= H121), R152 (= R156), E182 (= E186), N204 (= N208), T211 (= T215), L213 (≠ M217)
- binding 5-hydroxypentanal: Y41 (≠ G44), C117 (= C119), R152 (= R156), I206 (≠ T210)
1zlpA Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
35% identity, 93% coverage: 11:284/294 of query aligns to 8:283/284 of 1zlpA
- active site: F37 (≠ Y40), S39 (= S42), G40 (= G43), Y41 (≠ G44), D52 (= D55), D80 (≠ L79), D82 (≠ V81), F107 (≠ H109), E109 (= E111), K115 (= K117), C117 (= C119), G118 (= G120), H119 (= H121), R152 (= R156), E182 (= E186), N204 (= N208), T211 (= T215), L213 (≠ M217)
- binding 5-hydroxypentanal: C117 (= C119), G118 (= G120), R152 (= R156), I206 (≠ T210)
- binding magnesium ion: D80 (≠ L79), K115 (= K117)
3m0jA Structure of oxaloacetate acetylhydrolase in complex with the inhibitor 3,3-difluorooxalacetate (see paper)
34% identity, 95% coverage: 1:279/294 of query aligns to 4:284/297 of 3m0jA
- binding calcium ion: E218 (= E211), N219 (≠ F212)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y44 (= Y40), T46 (≠ S42), G47 (= G43), A48 (≠ G44), D88 (= D82), G126 (= G120), R162 (= R156), E192 (= E186), N215 (= N208), S241 (≠ P234)
3fa4A Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, triclinic crystal form (see paper)
33% identity, 97% coverage: 1:286/294 of query aligns to 3:281/284 of 3fa4A
- active site: Y43 (= Y40), T45 (≠ S42), G46 (= G43), A47 (≠ G44), D58 (= D55), D86 (= D82), D88 (= D84), H113 (= H109), E115 (= E111), R153 (= R156), E183 (= E186), N206 (= N208), T213 (= T215), S215 (≠ M217)
- 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)
33% identity, 97% coverage: 1:286/294 of query aligns to 2:279/292 of 3fa3J
- active site: Y42 (= Y40), T44 (≠ S42), G45 (= G43), A46 (≠ G44), D57 (= D55), D85 (= D82), D87 (= D84), H112 (= H109), E114 (= E111), R151 (= R156), E181 (= E186), N204 (= N208), T211 (= T215), S213 (≠ M217)
- binding manganese (ii) ion: D85 (= D82), D87 (= D84)
3m0kA Structure of oxaloacetate acetylhydrolase in complex with the product oxalate (see paper)
34% identity, 95% coverage: 1:279/294 of query aligns to 4:279/289 of 3m0kA
3b8iA Crystal structure of oxaloacetate decarboxylase from pseudomonas aeruginosa (pa4872) in complex with oxalate and mg2+. (see paper)
30% identity, 84% coverage: 7:253/294 of query aligns to 11:251/284 of 3b8iA
- active site: I44 (≠ Y40), G46 (≠ S42), G47 (= G43), S48 (≠ G44), D59 (= D55), D86 (= D82), D88 (= D84), T113 (≠ H109), E115 (= E111), A121 (≠ K117), F123 (≠ C119), G124 (= G120), R157 (= R156), V186 (≠ E186), M206 (≠ L206)
- binding oxalate ion: S48 (≠ G44), D86 (= D82), H233 (≠ L235)
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)
30% identity, 84% coverage: 7:253/294 of query aligns to 13:253/287 of Q9HUU1
- D88 (= D82) binding Mg(2+)
- Y212 (≠ F212) mutation to F: 25-fold increase in substrate affinity and 23-fold decrease in activity.
- H235 (≠ L235) 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.
6lrtA Crystal structure of isocitrate lyase (caur_3889) from chloroflexus aurantiacus in complex with isocitrate and manganese ion
27% identity, 86% coverage: 5:256/294 of query aligns to 50:364/423 of 6lrtA
5uncA The crystal structure of phosphoenolpyruvate phosphomutase from streptomyces platensis subsp. Rosaceus
31% identity, 94% coverage: 17:291/294 of query aligns to 16:288/289 of 5uncA
- active site: W39 (≠ Y40), S41 (= S42), G42 (= G43), L43 (≠ G44), D53 (= D55), D80 (= D82), D82 (= D84), T107 (≠ H109), E109 (= E111), K115 (= K117), N117 (≠ C119), S118 (≠ G120), R153 (= R156), H184 (≠ E186), V209 (≠ N208)
- binding alpha-D-xylopyranose: H22 (≠ I23), N23 (= N24), G26 (≠ Q27), L29 (≠ Q30), G239 (≠ M241), V243 (≠ A245)
Q84G06 Phosphonopyruvate hydrolase; PPH; EC 3.11.1.3 from Variovorax sp. (strain Pal2) (see paper)
31% identity, 94% coverage: 1:276/294 of query aligns to 1:277/290 of Q84G06
- D81 (= D82) binding Mg(2+)
- R188 (≠ V188) mutation to A: Reduced affinity for substrate.
2hjpA Crystal structure of phosphonopyruvate hydrolase complex with phosphonopyruvate and mg++ (see paper)
31% identity, 94% coverage: 1:276/294 of query aligns to 1:270/283 of 2hjpA
- active site: W40 (≠ Y40), S42 (= S42), G43 (= G43), F44 (≠ G44), D54 (= D55), D81 (= D82), D83 (= D84), V108 (≠ H109), E110 (= E111), K116 (= K117), T118 (≠ C119), R148 (= R156), H179 (≠ E186), V204 (≠ N208)
- binding phosphonopyruvate: W40 (≠ Y40), S42 (= S42), F44 (≠ G44), D81 (= D82), R148 (= R156), H179 (≠ E186), R181 (≠ V188)
- binding alpha-D-xylopyranose: E32 (≠ T32), S75 (≠ D76)
Query Sequence
>WP_013136520.1 NCBI__GCF_000092245.1:WP_013136520.1
MSAGKRFREALKEERPLQIVGTINAYQALQATKVGFKAIYLSGGGIANASYGLPDLGMTM
IEDVCIDIRRVTSICDTPLIVDADTGWGHAFNVARTVKEFIRSGAAGLHIEDQVAAKRCG
HRPNKELVSTEEMCDRIRAAVDAKMELDPDFYIIARTDAHASEGQEAAVARAKAYVEAGA
DAIFAEAVHTLKEYKEFCDQMSVPVLANITEFGATPMFTTEELGSVGIEMVLYPLSAFRA
MNKAALHVYQELRDKGTQESTLDTMQTRMELYEMLGYHEYEQKMDSLFAKGKAK
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