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Comparing HSERO_RS15660 FitnessBrowser__HerbieS:HSERO_RS15660 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)
6t4vC Crystal structure of 2-methylisocitrate lyase (prpb) from pseudomonas aeruginosa in apo form.
84% identity, 97% coverage: 5:290/296 of query aligns to 3:277/277 of 6t4vC
- active site: Y41 (= Y43), S43 (= S45), G44 (= G46), G45 (= G47), D56 (= D58), D83 (= D85), D85 (= D87), H111 (= H113), E113 (= E115), R145 (= R158), E175 (= E188), N197 (= N210), T204 (= T217), L206 (= L219)
- binding pyruvic acid: F88 (= F90), N94 (= N96)
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)
77% identity, 100% coverage: 1:296/296 of query aligns to 1:296/296 of P77541
- M1 (= M1) modified: Initiator methionine, Removed
- SGG 45:47 (= SGG 45:47) binding
- D85 (= D85) binding
- D87 (= D87) binding
- C123 (= C123) mutation to S: Inactive.
- CG 123:124 (= CG 123:124) binding
- R158 (= R158) binding
- E188 (= E188) binding
- NIT 210:212 (= NIT 210:212) binding
- R241 (= R241) binding
- R270 (= R270) binding
1mumA Structure of the 2-methylisocitrate lyase (prpb) from escherichia coli (see paper)
79% identity, 98% coverage: 3:291/296 of query aligns to 1:289/289 of 1mumA
- active site: Y41 (= Y43), S43 (= S45), G44 (= G46), G45 (= G47), D56 (= D58), D83 (= D85), D85 (= D87), H111 (= H113), E113 (= E115), K119 (= K121), C121 (= C123), G122 (= G124), H123 (= H125), R156 (= R158), E186 (= E188), N208 (= N210), T215 (= T217), L217 (= L219)
- binding magnesium ion: D56 (= D58), D85 (= D87)
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)
75% identity, 100% coverage: 1:295/296 of query aligns to 1:295/295 of Q56062
- SGG 45:47 (= SGG 45:47) binding
- D58 (= D58) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- D85 (= D85) binding
- 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
1o5qA Crystal structure of pyruvate and mg2+ bound 2-methylisocitrate lyase (prpb) from salmonella typhimurium (see paper)
72% identity, 95% coverage: 5:286/296 of query aligns to 1:271/271 of 1o5qA
- active site: Y39 (= Y43), S41 (= S45), G42 (= G46), G43 (= G47), D54 (= D58), D81 (= D85), D83 (= D87), H109 (= H113), E111 (= E115), R143 (= R158), E173 (= E188), N195 (= N210), T202 (= T217), L204 (= L219)
- binding pyruvic acid: Y39 (= Y43), S41 (= S45), G43 (= G47), D81 (= D85), R143 (= R158)
4iqdA Crystal structure of carboxyvinyl-carboxyphosphonate phosphorylmutase from bacillus anthracis
46% identity, 93% coverage: 10:284/296 of query aligns to 13:283/290 of 4iqdA
- active site: Y46 (= Y43), S48 (= S45), G49 (= G46), A50 (≠ G47), D60 (= D58), D87 (= D85), D89 (= D87), Q114 (≠ H113), E116 (= E115), K122 (= K121), C124 (= C123), G125 (= G124), H126 (= H125), R157 (= R158), E187 (= E188), N209 (= N210)
- binding pyruvic acid: E71 (≠ T69), R72 (≠ D70), D75 (≠ R73), G165 (= G166), L166 (= L167), Y218 (≠ L219), Y219 (≠ F220)
3fa3B Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
36% identity, 86% coverage: 5:258/296 of query aligns to 4:261/302 of 3fa3B
- active site: Y43 (= Y43), T45 (≠ S45), G46 (= G46), A47 (≠ G47), D58 (= D58), D86 (= D85), D88 (= D87), H113 (= H113), E115 (= E115), K121 (= K121), C123 (= C123), G124 (= G124), H125 (= H125), R160 (= R158), E190 (= E188), N213 (= N210), T220 (= T217), S222 (≠ L219)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y43 (= Y43), T45 (≠ S45), G46 (= G46), A47 (≠ G47), D86 (= D85), G124 (= G124), R160 (= R158), E190 (= E188), N213 (= N210), P239 (= P236)
1zlpB Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
34% identity, 92% coverage: 11:282/296 of query aligns to 5:276/285 of 1zlpB
- active site: F37 (≠ Y43), S39 (= S45), G40 (= G46), Y41 (≠ G47), D52 (= D58), D80 (≠ V86), D82 (≠ T88), F107 (≠ H113), E109 (= E115), K115 (= K121), C117 (= C123), G118 (= G124), H119 (= H125), R152 (= R158), E182 (= E188), N204 (= N210), T211 (= T217), L213 (= L219)
- binding 5-hydroxypentanal: Y41 (≠ G47), C117 (= C123), R152 (= R158), I206 (≠ T212)
1zlpA Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
34% identity, 92% coverage: 11:282/296 of query aligns to 5:276/284 of 1zlpA
- active site: F37 (≠ Y43), S39 (= S45), G40 (= G46), Y41 (≠ G47), D52 (= D58), D80 (≠ V86), D82 (≠ T88), F107 (≠ H113), E109 (= E115), K115 (= K121), C117 (= C123), G118 (= G124), H119 (= H125), R152 (= R158), E182 (= E188), N204 (= N210), T211 (= T217), L213 (= L219)
- binding 5-hydroxypentanal: C117 (= C123), G118 (= G124), R152 (= R158), I206 (≠ T212)
- binding magnesium ion: D80 (≠ V86), K115 (= K121)
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, 92% coverage: 11:282/296 of query aligns to 32:303/318 of Q05957
- D79 (= D58) mutation to A: Reduces catalytic efficiency 1000-fold.
- D107 (≠ V86) binding
- D109 (≠ T88) binding
- K142 (= K121) binding
- C144 (= C123) mutation to A: Loss of catalytic activity.
Sites not aligning to the query:
- 1:3 modified: propeptide, Removed in mature form
3m0jA Structure of oxaloacetate acetylhydrolase in complex with the inhibitor 3,3-difluorooxalacetate (see paper)
37% identity, 73% coverage: 24:240/296 of query aligns to 25:245/297 of 3m0jA
- binding calcium ion: E218 (= E213), N219 (≠ F214)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y44 (= Y43), T46 (≠ S45), G47 (= G46), A48 (≠ G47), D88 (= D85), G126 (= G124), R162 (= R158), E192 (= E188), N215 (= N210), S241 (≠ P236)
3fa4A Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, triclinic crystal form (see paper)
34% identity, 86% coverage: 5:258/296 of query aligns to 4:254/284 of 3fa4A
- active site: Y43 (= Y43), T45 (≠ S45), G46 (= G46), A47 (≠ G47), D58 (= D58), D86 (= D85), D88 (= D87), H113 (= H113), E115 (= E115), R153 (= R158), E183 (= E188), N206 (= N210), T213 (= T217), S215 (≠ L219)
- binding magnesium ion: D86 (= D85), D88 (= D87)
3fa3J Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
34% identity, 86% coverage: 5:258/296 of query aligns to 3:252/292 of 3fa3J
- active site: Y42 (= Y43), T44 (≠ S45), G45 (= G46), A46 (≠ G47), D57 (= D58), D85 (= D85), D87 (= D87), H112 (= H113), E114 (= E115), R151 (= R158), E181 (= E188), N204 (= N210), T211 (= T217), S213 (≠ L219)
- binding manganese (ii) ion: D85 (= D85), D87 (= D87)
3m0kA Structure of oxaloacetate acetylhydrolase in complex with the product oxalate (see paper)
36% identity, 73% coverage: 24:240/296 of query aligns to 25:240/289 of 3m0kA
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)
31% identity, 73% coverage: 4:219/296 of query aligns to 7:217/287 of Q9HUU1
- D88 (= D85) binding
- Y212 (≠ F214) 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.
3b8iA Crystal structure of oxaloacetate decarboxylase from pseudomonas aeruginosa (pa4872) in complex with oxalate and mg2+. (see paper)
31% identity, 73% coverage: 4:219/296 of query aligns to 5:215/284 of 3b8iA
- active site: I44 (≠ Y43), G46 (≠ S45), G47 (= G46), S48 (≠ G47), D59 (= D58), D86 (= D85), D88 (= D87), T113 (≠ H113), E115 (= E115), A121 (≠ K121), F123 (≠ C123), G124 (= G124), R157 (= R158), V186 (≠ E188), M206 (≠ L208)
- binding oxalate ion: S48 (≠ G47), D86 (= D85)
Sites not aligning to the query:
Q84G06 Phosphonopyruvate hydrolase; PPH; EC 3.11.1.3 from Variovorax sp. (strain Pal2) (see paper)
35% identity, 86% coverage: 9:263/296 of query aligns to 6:262/290 of Q84G06
- D81 (= D85) binding
- R188 (vs. gap) mutation to A: Reduced affinity for substrate.
2hjpA Crystal structure of phosphonopyruvate hydrolase complex with phosphonopyruvate and mg++ (see paper)
35% identity, 86% coverage: 9:263/296 of query aligns to 6:255/283 of 2hjpA
- active site: W40 (≠ Y43), S42 (= S45), G43 (= G46), F44 (≠ G47), D54 (= D58), D81 (= D85), D83 (= D87), V108 (≠ H113), E110 (= E115), K116 (= K121), T118 (≠ C123), R148 (= R158), H179 (vs. gap), V204 (≠ N210)
- binding phosphonopyruvate: W40 (≠ Y43), S42 (= S45), F44 (≠ G47), D81 (= D85), R148 (= R158), H179 (vs. gap), R181 (vs. gap)
- binding alpha-D-xylopyranose: E32 (≠ K35), S75 (≠ D79)
2duaA Crystal structure of phosphonopyruvate hydrolase complex with oxalate and mg++ (see paper)
35% identity, 86% coverage: 9:263/296 of query aligns to 6:255/283 of 2duaA
- active site: W40 (≠ Y43), S42 (= S45), G43 (= G46), F44 (≠ G47), D54 (= D58), D81 (= D85), D83 (= D87), V108 (≠ H113), E110 (= E115), K116 (= K121), T118 (≠ C123), R148 (= R158), H179 (vs. gap), V204 (≠ N210)
- binding oxalate ion: W40 (≠ Y43), S42 (= S45), F44 (≠ G47), D81 (= D85), R148 (= R158)
- binding alpha-D-xylopyranose: E32 (≠ K35), S75 (≠ D79)
1pymA Phosphoenolpyruvate mutase from mollusk in with bound mg2-oxalate (see paper)
30% identity, 85% coverage: 22:274/296 of query aligns to 19:272/291 of 1pymA
- active site: W40 (≠ Y43), S42 (= S45), G43 (= G46), L44 (≠ G47), D54 (= D58), D81 (= D85), D83 (= D87), C108 (≠ H113), E110 (= E115), K116 (= K121), N118 (≠ C123), S119 (≠ G124), R155 (= R158), H186 (vs. gap), V211 (≠ N210)
- binding oxalate ion: W40 (≠ Y43), S42 (= S45), G43 (= G46), L44 (≠ G47), D81 (= D85), R155 (= R158)
Query Sequence
>HSERO_RS15660 FitnessBrowser__HerbieS:HSERO_RS15660
MALHSAGAAFRKAVQEESPLQVIGAINANHALLAKRAGFRAIYLSGGGVAAGSLGLPDLG
ISNLDDVLTDVRRITDVCDLPLLVDVDTGFGASAFNVARTVKSMIKFGAAAMHIEDQVGA
KRCGHRPNKEIVSKQEMVDRIKAAVDARTDENFVIMARTDALAVEGLDAAIERAVACVEA
GADMIFPEAITDLAMYKQFANAVKVPILANITEFGSTPLFTVDELKGADVGLVLYPLSAF
RAMNKAAENVYQAIRRDGTQKNVVDTMQTRMELYDRIDYHSYEQRLDALFAQQKNK
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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