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Comparing RR42_RS11260 FitnessBrowser__Cup4G11:RR42_RS11260 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.
81% identity, 95% coverage: 11:296/302 of query aligns to 3:277/277 of 6t4vC
- active site: Y41 (= Y49), S43 (= S51), G44 (= G52), G45 (= G53), D56 (= D64), D83 (= D91), D85 (= D93), H111 (= H119), E113 (= E121), R145 (= R164), E175 (= E194), N197 (= N216), T204 (= T223), L206 (= L225)
- binding pyruvic acid: F88 (= F96), N94 (= N102)
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)
75% identity, 97% coverage: 10:302/302 of query aligns to 4:296/296 of P77541
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1mumA Structure of the 2-methylisocitrate lyase (prpb) from escherichia coli (see paper)
76% identity, 95% coverage: 10:297/302 of query aligns to 2:289/289 of 1mumA
- active site: Y41 (= Y49), S43 (= S51), G44 (= G52), G45 (= G53), D56 (= D64), D83 (= D91), D85 (= D93), H111 (= H119), E113 (= E121), K119 (= K127), C121 (= C129), G122 (= G130), H123 (= H131), R156 (= R164), E186 (= E194), N208 (= N216), T215 (= T223), L217 (= L225)
- binding magnesium ion: D56 (= D64), D85 (= D93)
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)
74% identity, 96% coverage: 11:301/302 of query aligns to 5:295/295 of Q56062
- SGG 45:47 (= SGG 51:53) binding
- D58 (= D64) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- D85 (= D91) binding
- K121 (= K127) mutation to A: 1000-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R122 (= R128) 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 (= R164) binding
1o5qA Crystal structure of pyruvate and mg2+ bound 2-methylisocitrate lyase (prpb) from salmonella typhimurium (see paper)
71% identity, 93% coverage: 11:292/302 of query aligns to 1:271/271 of 1o5qA
- active site: Y39 (= Y49), S41 (= S51), G42 (= G52), G43 (= G53), D54 (= D64), D81 (= D91), D83 (= D93), H109 (= H119), E111 (= E121), R143 (= R164), E173 (= E194), N195 (= N216), T202 (= T223), L204 (= L225)
- binding pyruvic acid: Y39 (= Y49), S41 (= S51), G43 (= G53), D81 (= D91), R143 (= R164)
4iqdA Crystal structure of carboxyvinyl-carboxyphosphonate phosphorylmutase from bacillus anthracis
46% identity, 91% coverage: 15:290/302 of query aligns to 12:283/290 of 4iqdA
- active site: Y46 (= Y49), S48 (= S51), G49 (= G52), A50 (≠ G53), D60 (= D64), D87 (= D91), D89 (= D93), Q114 (≠ H119), E116 (= E121), K122 (= K127), C124 (= C129), G125 (= G130), H126 (= H131), R157 (= R164), E187 (= E194), N209 (= N216)
- binding pyruvic acid: E71 (≠ T75), R72 (≠ D76), D75 (≠ R79), G165 (= G172), L166 (= L173), Y218 (≠ L225), Y219 (≠ F226)
1zlpA Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
36% identity, 89% coverage: 20:288/302 of query aligns to 7:276/284 of 1zlpA
- active site: F37 (≠ Y49), S39 (= S51), G40 (= G52), Y41 (≠ G53), D52 (= D64), D80 (≠ V92), D82 (≠ T94), F107 (≠ H119), E109 (= E121), K115 (= K127), C117 (= C129), G118 (= G130), H119 (= H131), R152 (= R164), E182 (= E194), N204 (= N216), T211 (= T223), L213 (= L225)
- binding 5-hydroxypentanal: C117 (= C129), G118 (= G130), R152 (= R164), I206 (≠ T218)
- binding magnesium ion: D80 (≠ V92), K115 (= K127)
1zlpB Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
36% identity, 89% coverage: 20:288/302 of query aligns to 7:276/285 of 1zlpB
- active site: F37 (≠ Y49), S39 (= S51), G40 (= G52), Y41 (≠ G53), D52 (= D64), D80 (≠ V92), D82 (≠ T94), F107 (≠ H119), E109 (= E121), K115 (= K127), C117 (= C129), G118 (= G130), H119 (= H131), R152 (= R164), E182 (= E194), N204 (= N216), T211 (= T223), L213 (= L225)
- binding 5-hydroxypentanal: Y41 (≠ G53), C117 (= C129), R152 (= R164), I206 (≠ T218)
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)
36% identity, 89% coverage: 20:288/302 of query aligns to 34:303/318 of Q05957
- D79 (= D64) mutation to A: Reduces catalytic efficiency 1000-fold.
- D107 (≠ V92) binding
- D109 (≠ T94) binding
- K142 (= K127) binding
- C144 (= C129) mutation to A: Loss of catalytic activity.
Sites not aligning to the query:
- 1:3 modified: propeptide, Removed in mature form
3fa3B Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
36% identity, 84% coverage: 11:264/302 of query aligns to 4:261/302 of 3fa3B
- active site: Y43 (= Y49), T45 (≠ S51), G46 (= G52), A47 (≠ G53), D58 (= D64), D86 (= D91), D88 (= D93), H113 (= H119), E115 (= E121), K121 (= K127), C123 (= C129), G124 (= G130), H125 (= H131), R160 (= R164), E190 (= E194), N213 (= N216), T220 (= T223), S222 (≠ L225)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y43 (= Y49), T45 (≠ S51), G46 (= G52), A47 (≠ G53), D86 (= D91), G124 (= G130), R160 (= R164), E190 (= E194), N213 (= N216), P239 (= P242)
3fa4A Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, triclinic crystal form (see paper)
34% identity, 84% coverage: 11:264/302 of query aligns to 4:254/284 of 3fa4A
- active site: Y43 (= Y49), T45 (≠ S51), G46 (= G52), A47 (≠ G53), D58 (= D64), D86 (= D91), D88 (= D93), H113 (= H119), E115 (= E121), R153 (= R164), E183 (= E194), N206 (= N216), T213 (= T223), S215 (≠ L225)
- binding magnesium ion: D86 (= D91), D88 (= D93)
3m0jA Structure of oxaloacetate acetylhydrolase in complex with the inhibitor 3,3-difluorooxalacetate (see paper)
35% identity, 83% coverage: 11:261/302 of query aligns to 5:253/297 of 3m0jA
- binding calcium ion: E218 (= E219), N219 (≠ F220)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y44 (= Y49), T46 (≠ S51), G47 (= G52), A48 (≠ G53), D88 (= D91), G126 (= G130), R162 (= R164), E192 (= E194), N215 (= N216), S241 (≠ A245)
3fa3J Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
34% identity, 84% coverage: 11:264/302 of query aligns to 3:252/292 of 3fa3J
- active site: Y42 (= Y49), T44 (≠ S51), G45 (= G52), A46 (≠ G53), D57 (= D64), D85 (= D91), D87 (= D93), H112 (= H119), E114 (= E121), R151 (= R164), E181 (= E194), N204 (= N216), T211 (= T223), S213 (≠ L225)
- binding manganese (ii) ion: D85 (= D91), D87 (= D93)
3m0kA Structure of oxaloacetate acetylhydrolase in complex with the product oxalate (see paper)
34% identity, 83% coverage: 11:261/302 of query aligns to 5:248/289 of 3m0kA
1pymA Phosphoenolpyruvate mutase from mollusk in with bound mg2-oxalate (see paper)
32% identity, 82% coverage: 33:280/302 of query aligns to 24:272/291 of 1pymA
- active site: W40 (≠ Y49), S42 (= S51), G43 (= G52), L44 (≠ G53), D54 (= D64), D81 (= D91), D83 (= D93), C108 (≠ H119), E110 (= E121), K116 (= K127), N118 (≠ C129), S119 (≠ G130), R155 (= R164), H186 (≠ E194), V211 (≠ N216)
- binding oxalate ion: W40 (≠ Y49), S42 (= S51), G43 (= G52), L44 (≠ G53), D81 (= D91), R155 (= R164)
1m1bA Crystal structure of phosphoenolpyruvate mutase complexed with sulfopyruvate (see paper)
32% identity, 82% coverage: 33:280/302 of query aligns to 24:272/291 of 1m1bA
- active site: W40 (≠ Y49), S42 (= S51), G43 (= G52), L44 (≠ G53), D54 (= D64), D81 (= D91), D83 (= D93), C108 (≠ H119), E110 (= E121), K116 (= K127), N118 (≠ C129), S119 (≠ G130), R155 (= R164), H186 (≠ E194), V211 (≠ N216)
- binding magnesium ion: D81 (= D91), R155 (= R164)
- binding sulfopyruvate: S42 (= S51), G43 (= G52), L44 (≠ G53), D81 (= D91), N118 (≠ C129), S119 (≠ G130), L120 (≠ H131), R155 (= R164)
P56839 Phosphoenolpyruvate phosphomutase; PEP mutase; PEP phosphomutase; Phosphoenolpyruvate mutase; EC 5.4.2.9 from Mytilus edulis (Blue mussel) (see 2 papers)
32% identity, 82% coverage: 33:280/302 of query aligns to 28:276/295 of P56839
- D58 (= D64) mutation D->A,S: Abolishes enzyme activity.; mutation to N: Strongly reduces enzyme activity.
- D85 (= D91) mutation to A: Strongly reduces enzyme activity and increases KM.
- D87 (= D93) mutation to A: Strongly reduces enzyme activity.
- E114 (= E121) mutation to A: Strongly reduces enzyme activity.
- N122 (≠ C129) mutation N->A,D: Strongly reduces enzyme activity.
- R159 (= R164) mutation to A: Strongly reduces enzyme activity.
- H190 (≠ E194) 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
31% identity, 88% coverage: 26:291/302 of query aligns to 16:281/289 of 5uncA
- active site: W39 (≠ Y49), S41 (= S51), G42 (= G52), L43 (≠ G53), D53 (= D64), D80 (= D91), D82 (= D93), T107 (≠ H119), E109 (= E121), K115 (= K127), N117 (≠ C129), S118 (≠ G130), R153 (= R164), H184 (vs. gap), V209 (≠ N216)
- binding alpha-D-xylopyranose: H22 (≠ I32), N23 (= N33), G26 (≠ H36), L29 (= L39), G239 (≠ M249), V243 (≠ A253)
3b8iA Crystal structure of oxaloacetate decarboxylase from pseudomonas aeruginosa (pa4872) in complex with oxalate and mg2+. (see paper)
29% identity, 79% coverage: 14:252/302 of query aligns to 9:242/284 of 3b8iA
- active site: I44 (≠ Y49), G46 (≠ S51), G47 (= G52), S48 (≠ G53), D59 (= D64), D86 (= D91), D88 (= D93), T113 (≠ H119), E115 (= E121), A121 (≠ K127), F123 (≠ C129), G124 (= G130), R157 (= R164), V186 (≠ E194), M206 (≠ L214)
- binding oxalate ion: S48 (≠ G53), D86 (= D91), H233 (≠ L243)
Q84G06 Phosphonopyruvate hydrolase; PPH; EC 3.11.1.3 from Variovorax sp. (strain Pal2) (see paper)
33% identity, 89% coverage: 15:284/302 of query aligns to 15:277/290 of Q84G06
- D81 (= D91) binding
- R188 (≠ M196) mutation to A: Reduced affinity for substrate.
Query Sequence
>RR42_RS11260 FitnessBrowser__Cup4G11:RR42_RS11260
MTFSTSDLARSAGARFRQALADEHPLQVVGTINANHALLAKRAGYRAIYLSGGGVAAGSL
GLPDLGISNLDDVLTDVRRITDVCDVPLLVDVDTGFGASAFNVARTTRSLIKFGAGAMHI
EDQVGAKRCGHRPGKEIVSQGEMADRIKAAVDARTDENFVIMARTDALAVEGLDKAIERA
VACVEAGADAIFPEAMTDLAMYRKFVDAVKVPVLANITEFGATPLFTTEELGGAGVSMVL
YPLSAFRAMNKAAENVYAAIRRDGTQQNVVDTMQTRAELYESIGYHAYEQKLDALFAQGK
AK
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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