SitesBLAST
Comparing AZOBR_RS27820 FitnessBrowser__azobra:AZOBR_RS27820 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)
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)
40% identity, 95% coverage: 12:287/290 of query aligns to 35:311/318 of Q05957
- D79 (= D56) mutation to A: Reduces catalytic efficiency 1000-fold.
- D107 (= D84) binding
- D109 (= D86) binding
- K142 (= K119) binding
- C144 (= C121) 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)
40% identity, 95% coverage: 12:287/290 of query aligns to 8:284/284 of 1zlpA
- active site: F37 (≠ L41), S39 (= S43), G40 (= G44), Y41 (≠ F45), D52 (= D56), D80 (= D84), D82 (= D86), F107 (≠ L111), E109 (= E113), K115 (= K119), C117 (= C121), G118 (= G122), H119 (= H123), R152 (= R158), E182 (= E188), N204 (= N210), T211 (= T217), L213 (≠ M219)
- binding 5-hydroxypentanal: C117 (= C121), G118 (= G122), R152 (= R158), I206 (≠ V212)
- binding magnesium ion: D80 (= D84), K115 (= K119)
1zlpB Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
40% identity, 95% coverage: 12:287/290 of query aligns to 8:284/285 of 1zlpB
- active site: F37 (≠ L41), S39 (= S43), G40 (= G44), Y41 (≠ F45), D52 (= D56), D80 (= D84), D82 (= D86), F107 (≠ L111), E109 (= E113), K115 (= K119), C117 (= C121), G118 (= G122), H119 (= H123), R152 (= R158), E182 (= E188), N204 (= N210), T211 (= T217), L213 (≠ M219)
- binding 5-hydroxypentanal: Y41 (≠ F45), C117 (= C121), R152 (= R158), I206 (≠ V212)
4iqdA Crystal structure of carboxyvinyl-carboxyphosphonate phosphorylmutase from bacillus anthracis
35% identity, 97% coverage: 5:284/290 of query aligns to 10:283/290 of 4iqdA
- active site: Y46 (≠ L41), S48 (= S43), G49 (= G44), A50 (≠ F45), D60 (= D56), D87 (= D84), D89 (= D86), Q114 (≠ L111), E116 (= E113), K122 (= K119), C124 (= C121), G125 (= G122), H126 (= H123), R157 (= R158), E187 (= E188), N209 (= N210)
- binding pyruvic acid: E71 (≠ D67), R72 (≠ Q68), D75 (≠ N71), G165 (= G166), L166 (≠ F167), Y218 (≠ M219), Y219 (≠ L220)
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)
39% identity, 83% coverage: 3:242/290 of query aligns to 5:242/295 of Q56062
- SGG 45:47 (≠ SGF 43:45) binding
- D58 (= D56) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- D85 (= D84) binding
- K121 (= K119) mutation to A: 1000-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R122 (= R120) mutation to K: 2-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- C123 (= C121) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- H125 (= H123) mutation to A: 750-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R158 (= R158) binding
1mumA Structure of the 2-methylisocitrate lyase (prpb) from escherichia coli (see paper)
38% identity, 81% coverage: 3:238/290 of query aligns to 3:236/289 of 1mumA
- active site: Y41 (≠ L41), S43 (= S43), G44 (= G44), G45 (≠ F45), D56 (= D56), D83 (= D84), D85 (= D86), H111 (≠ L111), E113 (= E113), K119 (= K119), C121 (= C121), G122 (= G122), H123 (= H123), R156 (= R158), E186 (= E188), N208 (= N210), T215 (= T217), L217 (≠ M219)
- binding magnesium ion: D56 (= D56), D85 (= D86)
3fa3B Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
37% identity, 87% coverage: 1:251/290 of query aligns to 2:254/302 of 3fa3B
- active site: Y43 (≠ L41), T45 (≠ S43), G46 (= G44), A47 (≠ F45), D58 (= D56), D86 (= D84), D88 (= D86), H113 (≠ L111), E115 (= E113), K121 (= K119), C123 (= C121), G124 (= G122), H125 (= H123), R160 (= R158), E190 (= E188), N213 (= N210), T220 (= T217), S222 (≠ M219)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y43 (≠ L41), T45 (≠ S43), G46 (= G44), A47 (≠ F45), D86 (= D84), G124 (= G122), R160 (= R158), E190 (= E188), N213 (= N210), P239 (= P236)
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)
38% identity, 81% coverage: 3:238/290 of query aligns to 5:238/296 of P77541
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 241 binding
- 270 binding
3m0jA Structure of oxaloacetate acetylhydrolase in complex with the inhibitor 3,3-difluorooxalacetate (see paper)
36% identity, 87% coverage: 5:256/290 of query aligns to 7:261/297 of 3m0jA
- binding calcium ion: E218 (≠ R213), N219 (≠ G214)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y44 (≠ L41), T46 (≠ S43), G47 (= G44), A48 (≠ F45), D88 (= D84), G126 (= G122), R162 (= R158), E192 (= E188), N215 (= N210), S241 (≠ P236)
3m0kA Structure of oxaloacetate acetylhydrolase in complex with the product oxalate (see paper)
35% identity, 87% coverage: 5:256/290 of query aligns to 7:256/289 of 3m0kA
1o5qA Crystal structure of pyruvate and mg2+ bound 2-methylisocitrate lyase (prpb) from salmonella typhimurium (see paper)
37% identity, 81% coverage: 3:238/290 of query aligns to 1:223/271 of 1o5qA
- active site: Y39 (≠ L41), S41 (= S43), G42 (= G44), G43 (≠ F45), D54 (= D56), D81 (= D84), D83 (= D86), H109 (≠ L111), E111 (= E113), R143 (= R158), E173 (= E188), N195 (= N210), T202 (= T217), L204 (≠ M219)
- binding pyruvic acid: Y39 (≠ L41), S41 (= S43), G43 (≠ F45), D81 (= D84), R143 (= R158)
3fa4A Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, triclinic crystal form (see paper)
35% identity, 87% coverage: 1:251/290 of query aligns to 2:247/284 of 3fa4A
- active site: Y43 (≠ L41), T45 (≠ S43), G46 (= G44), A47 (≠ F45), D58 (= D56), D86 (= D84), D88 (= D86), H113 (≠ L111), E115 (= E113), R153 (= R158), E183 (= E188), N206 (= N210), T213 (= T217), S215 (≠ M219)
- binding magnesium ion: D86 (= D84), D88 (= D86)
3fa3J Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
34% identity, 87% coverage: 1:251/290 of query aligns to 1:245/292 of 3fa3J
- active site: Y42 (≠ L41), T44 (≠ S43), G45 (= G44), A46 (≠ F45), D57 (= D56), D85 (= D84), D87 (= D86), H112 (≠ L111), E114 (= E113), R151 (= R158), E181 (= E188), N204 (= N210), T211 (= T217), S213 (≠ M219)
- binding manganese (ii) ion: D85 (= D84), D87 (= D86)
6t4vC Crystal structure of 2-methylisocitrate lyase (prpb) from pseudomonas aeruginosa in apo form.
35% identity, 97% coverage: 3:284/290 of query aligns to 3:271/277 of 6t4vC
- active site: Y41 (≠ L41), S43 (= S43), G44 (= G44), G45 (≠ F45), D56 (= D56), D83 (= D84), D85 (= D86), H111 (≠ L111), E113 (= E113), R145 (= R158), E175 (= E188), N197 (= N210), T204 (= T217), L206 (≠ M219)
- binding pyruvic acid: F88 (≠ Y89), N94 (= N94)
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, 89% coverage: 24:281/290 of query aligns to 29:276/287 of Q9HUU1
- D88 (= D84) binding
- Y212 (≠ G214) mutation to F: 25-fold increase in substrate affinity and 23-fold decrease in activity.
- H235 (vs. gap) 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.
3b8iA Crystal structure of oxaloacetate decarboxylase from pseudomonas aeruginosa (pa4872) in complex with oxalate and mg2+. (see paper)
33% identity, 89% coverage: 24:281/290 of query aligns to 27:274/284 of 3b8iA
- active site: I44 (≠ L41), G46 (≠ S43), G47 (= G44), S48 (≠ F45), D59 (= D56), D86 (= D84), D88 (= D86), T113 (≠ L111), E115 (= E113), A121 (≠ K119), F123 (≠ C121), G124 (= G122), R157 (= R158), V186 (≠ E188), M206 (= M208)
- binding oxalate ion: S48 (≠ F45), D86 (= D84), H233 (vs. gap)
1pymA Phosphoenolpyruvate mutase from mollusk in with bound mg2-oxalate (see paper)
29% identity, 87% coverage: 7:258/290 of query aligns to 6:256/291 of 1pymA
- active site: W40 (≠ L41), S42 (= S43), G43 (= G44), L44 (≠ F45), D54 (= D56), D81 (= D84), D83 (= D86), C108 (≠ L111), E110 (= E113), K116 (= K119), N118 (≠ C121), S119 (≠ G122), R155 (= R158), H186 (≠ E188), V211 (≠ N210)
- binding oxalate ion: W40 (≠ L41), S42 (= S43), G43 (= G44), L44 (≠ F45), D81 (= D84), R155 (= R158)
1m1bA Crystal structure of phosphoenolpyruvate mutase complexed with sulfopyruvate (see paper)
29% identity, 87% coverage: 7:258/290 of query aligns to 6:256/291 of 1m1bA
- active site: W40 (≠ L41), S42 (= S43), G43 (= G44), L44 (≠ F45), D54 (= D56), D81 (= D84), D83 (= D86), C108 (≠ L111), E110 (= E113), K116 (= K119), N118 (≠ C121), S119 (≠ G122), R155 (= R158), H186 (≠ E188), V211 (≠ N210)
- binding magnesium ion: D81 (= D84), R155 (= R158)
- binding sulfopyruvate: S42 (= S43), G43 (= G44), L44 (≠ F45), D81 (= D84), N118 (≠ C121), S119 (≠ G122), L120 (≠ H123), R155 (= R158)
P56839 Phosphoenolpyruvate phosphomutase; PEP mutase; PEP phosphomutase; Phosphoenolpyruvate mutase; EC 5.4.2.9 from Mytilus edulis (Blue mussel) (see 2 papers)
29% identity, 87% coverage: 7:258/290 of query aligns to 10:260/295 of P56839
- D58 (= D56) mutation D->A,S: Abolishes enzyme activity.; mutation to N: Strongly reduces enzyme activity.
- D85 (= D84) mutation to A: Strongly reduces enzyme activity and increases KM.
- D87 (= D86) mutation to A: Strongly reduces enzyme activity.
- E114 (= E113) mutation to A: Strongly reduces enzyme activity.
- N122 (≠ C121) mutation N->A,D: Strongly reduces enzyme activity.
- R159 (= R158) mutation to A: Strongly reduces enzyme activity.
- H190 (≠ E188) 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
38% identity, 59% coverage: 5:175/290 of query aligns to 3:171/289 of 5uncA
- active site: W39 (≠ L41), S41 (= S43), G42 (= G44), L43 (≠ F45), D53 (= D56), D80 (= D84), D82 (= D86), T107 (≠ L111), E109 (= E113), K115 (= K119), N117 (≠ C121), S118 (≠ G122), R153 (= R158)
- binding alpha-D-xylopyranose: H22 (≠ F24), N23 (≠ D25), G26 (≠ S28), L29 (= L31)
Sites not aligning to the query:
Query Sequence
>AZOBR_RS27820 FitnessBrowser__azobra:AZOBR_RS27820
VTTPAQRLKTALEAPGLHLMPCCFDALSARLIEQAGFRVSLMSGFAVSATRLGMPDTGLI
SFAEMLDQLRNVCQAAPGLLVIGDGDTGYGNAMNVQRTVRDYARAGAAAVLIEDQVSPKR
CGHTKGKQVVGRAEARMKIRAAVDAARSGANDILILARTDARAVHGFDAALERCQDFVEE
GADIIFMEAPHDETEMAAFCAGIDRPAMANMVRGGQTPMLPPRELEALGFKLAAYPLTLM
SAAIDAMRAALAAVADGQESRVAQADFEALKSLVGFPDYYEREQAYRAAE
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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