SitesBLAST
Comparing CCNA_01980 FitnessBrowser__Caulo:CCNA_01980 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)
4lsbB Crystal structure of a putative lyase/mutase from burkholderia cenocepacia j2315
49% identity, 84% coverage: 11:225/255 of query aligns to 10:228/278 of 4lsbB
2ze3A Crystal structure of dfa0005 complexed with alpha-ketoglutarate: a novel member of the icl/pepm superfamily from alkali-tolerant deinococcus ficus (see paper)
43% identity, 87% coverage: 11:233/255 of query aligns to 9:238/275 of 2ze3A
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)
32% identity, 81% coverage: 11:216/255 of query aligns to 9:225/296 of P77541
- SGG 45:47 (≠ TSA 46:48) binding substrate
- D85 (= D84) binding Mg(2+)
- D87 (≠ E86) binding Mg(2+)
- C123 (vs. gap) mutation to S: Inactive.
- CG 123:124 (vs. gap) binding substrate
- R158 (= R150) binding substrate
- E188 (≠ P182) binding substrate
- NIT 210:212 (≠ NVL 203:205) binding substrate
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 241 binding substrate
- 270 binding substrate
1mumA Structure of the 2-methylisocitrate lyase (prpb) from escherichia coli (see paper)
32% identity, 81% coverage: 11:216/255 of query aligns to 7:223/289 of 1mumA
- active site: Y41 (≠ A44), S43 (≠ T46), G44 (≠ S47), G45 (≠ A48), D56 (= D58), D83 (= D84), D85 (≠ E86), H111 (≠ S112), E113 (= E114), K119 (≠ E120), C121 (vs. gap), G122 (vs. gap), H123 (vs. gap), R156 (= R150), E186 (≠ P182), N208 (= N203), T215 (vs. gap), L217 (≠ E210)
- binding magnesium ion: D56 (= D58), D85 (≠ E86)
4iqdA Crystal structure of carboxyvinyl-carboxyphosphonate phosphorylmutase from bacillus anthracis
33% identity, 84% coverage: 12:224/255 of query aligns to 13:232/290 of 4iqdA
- active site: Y46 (≠ A44), S48 (≠ T46), G49 (≠ S47), A50 (= A48), D60 (= D58), D87 (= D84), D89 (≠ E86), Q114 (≠ S112), E116 (= E114), K122 (vs. gap), C124 (vs. gap), G125 (vs. gap), H126 (vs. gap), R157 (= R150), E187 (≠ P182), N209 (= N203)
- binding pyruvic acid: E71 (≠ A68), R72 (≠ H69), D75 (≠ T72), G165 (≠ D160), L166 (= L161), Y218 (≠ E210), Y219 (≠ M211)
6t4vC Crystal structure of 2-methylisocitrate lyase (prpb) from pseudomonas aeruginosa in apo form.
32% identity, 77% coverage: 28:224/255 of query aligns to 25:220/277 of 6t4vC
- active site: Y41 (≠ A44), S43 (≠ T46), G44 (≠ S47), G45 (≠ A48), D56 (= D58), D83 (= D84), D85 (≠ E86), H111 (≠ S112), E113 (= E114), R145 (= R150), E175 (≠ P182), N197 (= N203), T204 (vs. gap), L206 (≠ E210)
- binding pyruvic acid: F88 (= F89), N94 (≠ E95)
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)
31% identity, 81% coverage: 11:216/255 of query aligns to 9:225/295 of Q56062
- SGG 45:47 (≠ TSA 46:48) binding substrate
- D58 (= D58) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- D85 (= D84) binding Mg(2+)
- K121 (≠ E120) mutation to A: 1000-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R122 (vs. gap) mutation to K: 2-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- C123 (vs. gap) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
- H125 (vs. gap) mutation to A: 750-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
- R158 (= R150) binding substrate
1o5qA Crystal structure of pyruvate and mg2+ bound 2-methylisocitrate lyase (prpb) from salmonella typhimurium (see paper)
32% identity, 81% coverage: 11:216/255 of query aligns to 5:210/271 of 1o5qA
- active site: Y39 (≠ A44), S41 (≠ T46), G42 (≠ S47), G43 (≠ A48), D54 (= D58), D81 (= D84), D83 (≠ E86), H109 (≠ S112), E111 (= E114), R143 (= R150), E173 (≠ P182), N195 (= N203), T202 (vs. gap), L204 (≠ E210)
- binding pyruvic acid: Y39 (≠ A44), S41 (≠ T46), G43 (≠ A48), D81 (= D84), R143 (= R150)
3b8iA Crystal structure of oxaloacetate decarboxylase from pseudomonas aeruginosa (pa4872) in complex with oxalate and mg2+. (see paper)
29% identity, 96% coverage: 9:254/255 of query aligns to 8:257/284 of 3b8iA
- active site: I44 (vs. gap), G46 (≠ A44), G47 (≠ S45), S48 (≠ T46), D59 (= D57), D86 (= D84), D88 (≠ E86), T113 (≠ S112), E115 (= E114), A121 (vs. gap), F123 (vs. gap), G124 (vs. gap), R157 (= R150), V186 (≠ P182), M206 (≠ V202)
- binding oxalate ion: S48 (≠ T46), D86 (= D84), H233 (vs. gap)
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)
29% identity, 96% coverage: 9:254/255 of query aligns to 10:259/287 of Q9HUU1
- D88 (= D84) binding Mg(2+)
- Y212 (≠ L206) 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.
3fa4A Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, triclinic crystal form (see paper)
28% identity, 93% coverage: 13:249/255 of query aligns to 11:254/284 of 3fa4A
- active site: Y43 (≠ A44), T45 (= T46), G46 (≠ S47), A47 (= A48), D58 (= D58), D86 (= D84), D88 (≠ E86), H113 (≠ S112), E115 (= E114), R153 (= R150), E183 (≠ P182), N206 (= N203), T213 (vs. gap), S215 (≠ E210)
- binding magnesium ion: D86 (= D84), D88 (≠ E86)
3fa3J Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
27% identity, 93% coverage: 13:249/255 of query aligns to 10:252/292 of 3fa3J
- active site: Y42 (≠ A44), T44 (= T46), G45 (≠ S47), A46 (= A48), D57 (= D58), D85 (= D84), D87 (≠ E86), H112 (≠ S112), E114 (= E114), R151 (= R150), E181 (≠ P182), N204 (= N203), T211 (vs. gap), S213 (≠ E210)
- binding manganese (ii) ion: D85 (= D84), D87 (≠ E86)
3fa3B Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
27% identity, 93% coverage: 13:249/255 of query aligns to 11:261/302 of 3fa3B
- active site: Y43 (≠ A44), T45 (= T46), G46 (≠ S47), A47 (= A48), D58 (= D58), D86 (= D84), D88 (≠ E86), H113 (≠ S112), E115 (= E114), K121 (vs. gap), C123 (vs. gap), G124 (vs. gap), H125 (vs. gap), R160 (= R150), E190 (≠ P182), N213 (= N203), T220 (vs. gap), S222 (≠ E210)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y43 (≠ A44), T45 (= T46), G46 (≠ S47), A47 (= A48), D86 (= D84), G124 (vs. gap), R160 (= R150), E190 (≠ P182), N213 (= N203), P239 (≠ G227)
3m0jA Structure of oxaloacetate acetylhydrolase in complex with the inhibitor 3,3-difluorooxalacetate (see paper)
29% identity, 99% coverage: 3:254/255 of query aligns to 2:269/297 of 3m0jA
- binding calcium ion: E218 (≠ L206), N219 (≠ W207)
- binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y44 (≠ A44), T46 (= T46), G47 (≠ S47), A48 (= A48), D88 (= D84), G126 (vs. gap), R162 (= R150), E192 (≠ P182), N215 (= N203), S241 (≠ G227)
3m0kA Structure of oxaloacetate acetylhydrolase in complex with the product oxalate (see paper)
30% identity, 99% coverage: 3:254/255 of query aligns to 2:264/289 of 3m0kA
6lrtA Crystal structure of isocitrate lyase (caur_3889) from chloroflexus aurantiacus in complex with isocitrate and manganese ion
41% identity, 29% coverage: 80:152/255 of query aligns to 144:225/423 of 6lrtA
Sites not aligning to the query:
1pymA Phosphoenolpyruvate mutase from mollusk in with bound mg2-oxalate (see paper)
26% identity, 65% coverage: 31:196/255 of query aligns to 27:201/291 of 1pymA
- active site: W40 (≠ A44), S42 (≠ T46), G43 (≠ S47), L44 (≠ A48), D54 (= D57), D81 (= D84), D83 (≠ E86), C108 (≠ S112), E110 (= E114), K116 (vs. gap), N118 (vs. gap), S119 (vs. gap), R155 (= R150), H186 (≠ A181)
- binding oxalate ion: W40 (≠ A44), S42 (≠ T46), G43 (≠ S47), L44 (≠ A48), D81 (= D84), R155 (= R150)
Sites not aligning to the query:
1m1bA Crystal structure of phosphoenolpyruvate mutase complexed with sulfopyruvate (see paper)
26% identity, 65% coverage: 31:196/255 of query aligns to 27:201/291 of 1m1bA
- active site: W40 (≠ A44), S42 (≠ T46), G43 (≠ S47), L44 (≠ A48), D54 (= D57), D81 (= D84), D83 (≠ E86), C108 (≠ S112), E110 (= E114), K116 (vs. gap), N118 (vs. gap), S119 (vs. gap), R155 (= R150), H186 (≠ A181)
- binding magnesium ion: D81 (= D84), R155 (= R150)
- binding sulfopyruvate: S42 (≠ T46), G43 (≠ S47), L44 (≠ A48), D81 (= D84), N118 (vs. gap), S119 (vs. gap), L120 (vs. gap), R155 (= R150)
Sites not aligning to the query:
P56839 Phosphoenolpyruvate phosphomutase; PEP mutase; PEP phosphomutase; Phosphoenolpyruvate mutase; EC 5.4.2.9 from Mytilus edulis (Blue mussel) (see 2 papers)
26% identity, 65% coverage: 31:196/255 of query aligns to 31:205/295 of P56839
- D58 (= D57) 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 (≠ E86) mutation to A: Strongly reduces enzyme activity.
- E114 (= E114) mutation to A: Strongly reduces enzyme activity.
- N122 (vs. gap) mutation N->A,D: Strongly reduces enzyme activity.
- R159 (= R150) mutation to A: Strongly reduces enzyme activity.
- H190 (≠ A181) mutation to A: Strongly reduces enzyme activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5e9hA Structural insights of isocitrate lyases from fusarium graminearum (see paper)
35% identity, 29% coverage: 80:152/255 of query aligns to 163:244/518 of 5e9hA
Sites not aligning to the query:
Query Sequence
>CCNA_01980 FitnessBrowser__Caulo:CCNA_01980
MPDPYSTRRAAFRALHAEGCFVLPNPWDAGGARRLERRGFKALASTSAGMAWAMGRDDGQ
VTRDEVIAHLRTLCSATELPVNADFENGFGETPAEVAESVTLAIQAGVAGLSIEDWSGSE
LYPLEVAVDRLKAARAAIDASGQDVILVARTEGYLRGCRDLQPTLERLGAYAAAGADCLY
APAVSDPAEIKAIVDAVAPKPVNVLLWGPEMTVESLAKLGVRRVSTGGALAAAAWAGFDA
AAQRLAEQGRISPDA
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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