SitesBLAST
Comparing RR42_RS22765 FitnessBrowser__Cup4G11:RR42_RS22765 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)
3fa3B Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
45% identity, 97% coverage: 1:273/281 of query aligns to 3:282/302 of 3fa3B
- active site: Y43 (= Y40), T45 (= T42), G46 (= G43), A47 (= A44), D58 (= D54), D86 (= D81), D88 (= D83), H113 (= H108), E115 (= E110), K121 (= K116), C123 (= C118), G124 (= G119), H125 (= H120), R160 (= R153), E190 (= E183), N213 (= N205), T220 (= T212), S222 (≠ I214)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y43 (= Y40), T45 (= T42), G46 (= G43), A47 (= A44), D86 (= D81), G124 (= G119), R160 (= R153), E190 (= E183), N213 (= N205), P239 (= P231)
4iqdA Crystal structure of carboxyvinyl-carboxyphosphonate phosphorylmutase from bacillus anthracis
42% identity, 89% coverage: 3:252/281 of query aligns to 9:256/290 of 4iqdA
- active site: Y46 (= Y40), S48 (≠ T42), G49 (= G43), A50 (= A44), D60 (= D54), D87 (= D81), D89 (= D83), Q114 (≠ H108), E116 (= E110), K122 (= K116), C124 (= C118), G125 (= G119), H126 (= H120), R157 (= R153), E187 (= E183), N209 (= N205)
- binding pyruvic acid: E71 (= E65), R72 (≠ N66), D75 (≠ V69), G165 (= G161), L166 (= L162), Y218 (≠ I214), Y219 (≠ F215)
3m0jA Structure of oxaloacetate acetylhydrolase in complex with the inhibitor 3,3-difluorooxalacetate (see paper)
45% identity, 84% coverage: 16:250/281 of query aligns to 20:260/297 of 3m0jA
- binding calcium ion: E218 (≠ P208), N219 (≠ G209)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y44 (= Y40), T46 (= T42), G47 (= G43), A48 (= A44), D88 (= D81), G126 (= G119), R162 (= R153), E192 (= E183), N215 (= N205), S241 (≠ P231)
3fa4A Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, triclinic crystal form (see paper)
43% identity, 97% coverage: 1:273/281 of query aligns to 3:275/284 of 3fa4A
- active site: Y43 (= Y40), T45 (= T42), G46 (= G43), A47 (= A44), D58 (= D54), D86 (= D81), D88 (= D83), H113 (= H108), E115 (= E110), R153 (= R153), E183 (= E183), N206 (= N205), T213 (= T212), S215 (≠ I214)
- binding magnesium ion: D86 (= D81), D88 (= D83)
3fa3J Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
43% identity, 97% coverage: 1:273/281 of query aligns to 2:273/292 of 3fa3J
- active site: Y42 (= Y40), T44 (= T42), G45 (= G43), A46 (= A44), D57 (= D54), D85 (= D81), D87 (= D83), H112 (= H108), E114 (= E110), R151 (= R153), E181 (= E183), N204 (= N205), T211 (= T212), S213 (≠ I214)
- binding manganese (ii) ion: D85 (= D81), D87 (= D83)
3m0kA Structure of oxaloacetate acetylhydrolase in complex with the product oxalate (see paper)
43% identity, 84% coverage: 16:250/281 of query aligns to 20:255/289 of 3m0kA
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)
40% identity, 85% coverage: 21:258/281 of query aligns to 24:263/295 of Q56062
- SGG 45:47 (≠ TGA 42:44) binding
- D58 (= D54) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- D85 (= D81) binding
- K121 (= K116) mutation to A: 1000-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R122 (= R117) mutation to K: 2-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- C123 (= C118) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- H125 (= H120) mutation to A: 750-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R158 (= R153) binding
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)
40% identity, 85% coverage: 21:258/281 of query aligns to 24:263/296 of P77541
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 270 binding
1mumA Structure of the 2-methylisocitrate lyase (prpb) from escherichia coli (see paper)
40% identity, 85% coverage: 21:258/281 of query aligns to 22:261/289 of 1mumA
- active site: Y41 (= Y40), S43 (≠ T42), G44 (= G43), G45 (≠ A44), D56 (= D54), D83 (= D81), D85 (= D83), H111 (= H108), E113 (= E110), K119 (= K116), C121 (= C118), G122 (= G119), H123 (= H120), R156 (= R153), E186 (= E183), N208 (= N205), T215 (= T212), L217 (≠ I214)
- binding magnesium ion: D56 (= D54), D85 (= D83)
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)
43% identity, 79% coverage: 7:227/281 of query aligns to 31:253/318 of Q05957
- D79 (= D54) mutation to A: Reduces catalytic efficiency 1000-fold.
- D107 (= D81) binding
- D109 (= D83) binding
- K142 (= K116) binding
- C144 (= C118) 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)
43% identity, 79% coverage: 7:227/281 of query aligns to 4:226/284 of 1zlpA
- active site: F37 (≠ Y40), S39 (≠ T42), G40 (= G43), Y41 (≠ A44), D52 (= D54), D80 (= D81), D82 (= D83), F107 (≠ H108), E109 (= E110), K115 (= K116), C117 (= C118), G118 (= G119), H119 (= H120), R152 (= R153), E182 (= E183), N204 (= N205), T211 (= T212), L213 (≠ I214)
- binding 5-hydroxypentanal: C117 (= C118), G118 (= G119), R152 (= R153), I206 (≠ V207)
- binding magnesium ion: D80 (= D81), K115 (= K116)
1zlpB Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
43% identity, 79% coverage: 7:227/281 of query aligns to 4:226/285 of 1zlpB
- active site: F37 (≠ Y40), S39 (≠ T42), G40 (= G43), Y41 (≠ A44), D52 (= D54), D80 (= D81), D82 (= D83), F107 (≠ H108), E109 (= E110), K115 (= K116), C117 (= C118), G118 (= G119), H119 (= H120), R152 (= R153), E182 (= E183), N204 (= N205), T211 (= T212), L213 (≠ I214)
- binding 5-hydroxypentanal: Y41 (≠ A44), C117 (= C118), R152 (= R153), I206 (≠ V207)
1o5qA Crystal structure of pyruvate and mg2+ bound 2-methylisocitrate lyase (prpb) from salmonella typhimurium (see paper)
38% identity, 85% coverage: 21:258/281 of query aligns to 20:248/271 of 1o5qA
- active site: Y39 (= Y40), S41 (≠ T42), G42 (= G43), G43 (≠ A44), D54 (= D54), D81 (= D81), D83 (= D83), H109 (= H108), E111 (= E110), R143 (= R153), E173 (= E183), N195 (= N205), T202 (= T212), L204 (≠ I214)
- binding pyruvic acid: Y39 (= Y40), S41 (≠ T42), G43 (≠ A44), D81 (= D81), R143 (= R153)
6t4vC Crystal structure of 2-methylisocitrate lyase (prpb) from pseudomonas aeruginosa in apo form.
34% identity, 93% coverage: 21:281/281 of query aligns to 22:273/277 of 6t4vC
- active site: Y41 (= Y40), S43 (≠ T42), G44 (= G43), G45 (≠ A44), D56 (= D54), D83 (= D81), D85 (= D83), H111 (= H108), E113 (= E110), R145 (= R153), E175 (= E183), N197 (= N205), T204 (= T212), L206 (≠ I214)
- binding pyruvic acid: F88 (≠ Y86), N94 (= N91)
5uncA The crystal structure of phosphoenolpyruvate phosphomutase from streptomyces platensis subsp. Rosaceus
37% identity, 99% coverage: 4:281/281 of query aligns to 3:285/289 of 5uncA
- active site: W39 (≠ Y40), S41 (≠ T42), G42 (= G43), L43 (≠ A44), D53 (= D54), D80 (= D81), D82 (= D83), T107 (≠ H108), E109 (= E110), K115 (= K116), N117 (≠ C118), S118 (≠ G119), R153 (= R153), H184 (≠ E183), V209 (= V207)
- binding alpha-D-xylopyranose: H22 (≠ Y23), N23 (≠ D24), G26 (= G27), L29 (= L30), G239 (≠ A238), V243 (≠ G242)
2hjpA Crystal structure of phosphonopyruvate hydrolase complex with phosphonopyruvate and mg++ (see paper)
38% identity, 89% coverage: 1:250/281 of query aligns to 1:247/283 of 2hjpA
- active site: W40 (≠ Y40), S42 (≠ T42), G43 (= G43), F44 (≠ A44), D54 (= D54), D81 (= D81), D83 (= D83), V108 (≠ H108), E110 (= E110), K116 (= K116), T118 (≠ G123), R148 (= R153), H179 (≠ E183), V204 (= V207)
- binding phosphonopyruvate: W40 (≠ Y40), S42 (≠ T42), F44 (≠ A44), D81 (= D81), R148 (= R153), H179 (≠ E183), R181 (≠ T185)
- binding alpha-D-xylopyranose: E32 (= E32), S75 (= S75)
2duaA Crystal structure of phosphonopyruvate hydrolase complex with oxalate and mg++ (see paper)
38% identity, 89% coverage: 1:250/281 of query aligns to 1:247/283 of 2duaA
- active site: W40 (≠ Y40), S42 (≠ T42), G43 (= G43), F44 (≠ A44), D54 (= D54), D81 (= D81), D83 (= D83), V108 (≠ H108), E110 (= E110), K116 (= K116), T118 (≠ G123), R148 (= R153), H179 (≠ E183), V204 (= V207)
- binding oxalate ion: W40 (≠ Y40), S42 (≠ T42), F44 (≠ A44), D81 (= D81), R148 (= R153)
- binding alpha-D-xylopyranose: E32 (= E32), S75 (= S75)
Q84G06 Phosphonopyruvate hydrolase; PPH; EC 3.11.1.3 from Variovorax sp. (strain Pal2) (see paper)
38% identity, 89% coverage: 1:250/281 of query aligns to 1:254/290 of Q84G06
- D81 (= D81) binding
- R188 (≠ T185) mutation to A: Reduced affinity for substrate.
P56839 Phosphoenolpyruvate phosphomutase; PEP mutase; PEP phosphomutase; Phosphoenolpyruvate mutase; EC 5.4.2.9 from Mytilus edulis (Blue mussel) (see 2 papers)
31% identity, 95% coverage: 7:273/281 of query aligns to 11:283/295 of P56839
- D58 (= D54) mutation D->A,S: Abolishes enzyme activity.; mutation to N: Strongly reduces enzyme activity.
- D85 (= D81) mutation to A: Strongly reduces enzyme activity and increases KM.
- D87 (= D83) mutation to A: Strongly reduces enzyme activity.
- E114 (= E110) mutation to A: Strongly reduces enzyme activity.
- N122 (≠ C118) mutation N->A,D: Strongly reduces enzyme activity.
- R159 (= R153) mutation to A: Strongly reduces enzyme activity.
- H190 (≠ E183) mutation to A: Strongly reduces enzyme activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1pymA Phosphoenolpyruvate mutase from mollusk in with bound mg2-oxalate (see paper)
31% identity, 95% coverage: 7:273/281 of query aligns to 7:279/291 of 1pymA
- active site: W40 (≠ Y40), S42 (≠ T42), G43 (= G43), L44 (≠ A44), D54 (= D54), D81 (= D81), D83 (= D83), C108 (≠ H108), E110 (= E110), K116 (= K116), N118 (≠ C118), S119 (≠ G119), R155 (= R153), H186 (≠ E183), V211 (≠ N205)
- binding oxalate ion: W40 (≠ Y40), S42 (≠ T42), G43 (= G43), L44 (≠ A44), D81 (= D81), R155 (= R153)
Query Sequence
>RR42_RS22765 FitnessBrowser__Cup4G11:RR42_RS22765
MTLAAILRQRLQAPGMIIAPGAYDAIGARLIEQAGFSACYMTGAGTSAARGFPDFGLLTM
SEMVENAAVMARSVSIPLIADADTGYGNQLNVTRTVREYEARGVAAIHIEDQVAPKRCGH
LDGKEVVSREEFVSKIRAAVQARRTPDFVIIARTDARAMLGLEEAIWRANAALEAGADLA
FVEATQTIEEVAAVPRLVRGPCLLNVVPGGRTPIFDLREAEVMGYKLAILPGLMLKAAIQ
AGDEALAELKATFTAPGVSASVGQTFRRFGADEWDSLRQRF
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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