SitesBLAST
Comparing 209413 MicrobesOnline__882:209413 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)
Q02NB5 Isocitrate dehydrogenase [NADP]; IDH; IDP; NADP(+)-specific ICDH; Oxalosuccinate decarboxylase; EC 1.1.1.42 from Pseudomonas aeruginosa (strain UCBPP-PA14) (see 2 papers)
56% identity, 98% coverage: 7:380/380 of query aligns to 33:418/418 of Q02NB5
- S115 (= S87) modified: Phosphoserine
- T193 (≠ D162) modified: Phosphothreonine
2d4vA Crystal structure of NAD dependent isocitrate dehydrogenase from acidithiobacillus thiooxidans (see paper)
54% identity, 98% coverage: 2:372/380 of query aligns to 24:419/427 of 2d4vA
- active site: Y158 (= Y134), K228 (= K201), D294 (= D247), D318 (= D271), D322 (= D275)
- binding citrate anion: T103 (= T79), S111 (= S87), N113 (= N89), R117 (= R93), R127 (= R103), R151 (= R127), Y158 (= Y134), K228 (= K201), I231 (= I204), D318 (= D271)
- binding nicotinamide-adenine-dinucleotide: I35 (= I13), P100 (= P76), L101 (= L77), E102 (≠ G78), T103 (= T79), N113 (= N89), N230 (= N203), I292 (= I245), N295 (≠ A248), I331 (≠ L284), E347 (= E300), T349 (= T302), H350 (= H303), G351 (= G304), T352 (= T305), A353 (= A306), D355 (≠ T308), A362 (= A315), N363 (= N316), D403 (= D356)
1isoA Isocitrate dehydrogenase: structure of an engineered NADP+--> NAD+ specificity-reversal mutant (see paper)
54% identity, 98% coverage: 7:380/380 of query aligns to 29:414/414 of 1isoA
- active site: Y158 (= Y134), K228 (= K201), D281 (= D247), D305 (= D271), D309 (= D275)
- binding nicotinamide-adenine-dinucleotide: I35 (= I13), H337 (= H303), G338 (= G304), A340 (= A306), D342 (≠ T308), A349 (= A315), N350 (= N316)
6c0eA Crystal structure of isocitrate dehydrogenase from legionella pneumophila with bound NADPH with an alpha-ketoglutarate adduct
54% identity, 97% coverage: 7:374/380 of query aligns to 34:413/419 of 6c0eA
- active site: Y163 (= Y134), K233 (= K201), D286 (= D247), D310 (= D271)
- binding (3~{S})-3-[(4~{S})-3-aminocarbonyl-1-[(2~{R},3~{R},4~{S},5~{R})-5-[[[[(2~{R},3~{R},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3-oxidanyl-4-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxymethyl]-3,4-bis(oxidanyl)oxolan-2-yl]-4~{H}-pyridin-4-yl]-2-oxidanylidene-pentanedioic acid: P105 (= P76), L106 (= L77), T108 (= T79), S116 (= S87), N118 (= N89), R122 (= R93), R132 (= R103), R156 (= R127), N235 (= N203), I284 (= I245), Q291 (≠ E252), R295 (= R256), D310 (= D271), I323 (≠ L284), E339 (= E300), H342 (= H303), G343 (= G304), T344 (= T305), A345 (= A306), K347 (≠ T308), Y348 (≠ I309), V354 (≠ A315), N355 (= N316), Y394 (≠ V355), D395 (= D356)
Sites not aligning to the query:
1bl5A Isocitrate dehydrogenase from e. Coli single turnover laue structure of rate-limited product complex, 10 msec time resolution (see paper)
53% identity, 98% coverage: 7:380/380 of query aligns to 29:414/414 of 1bl5A
- active site: Y158 (= Y134), K228 (= K201), D281 (= D247), D305 (= D271), D309 (= D275)
- binding 2-oxoglutaric acid: S111 (= S87), N113 (= N89), R117 (= R93), R127 (= R103)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: H337 (= H303), G338 (= G304), A340 (= A306), Y343 (≠ I309), N350 (= N316), Y389 (≠ V355)
1ai3A Orbital steering in the catalytic power of enzymes: small structural changes with large catalytic consequences (see paper)
53% identity, 98% coverage: 7:380/380 of query aligns to 29:414/414 of 1ai3A
- active site: Y158 (= Y134), K228 (= K201), D281 (= D247), D305 (= D271), D309 (= D275)
- binding nicotinamide-(6-deamino-6-hydroxy-adenine)-dinucleotide phosphate: I35 (= I13), G99 (= G75), P100 (= P76), L101 (= L77), T102 (≠ G78), A335 (= A301), T336 (= T302), H337 (= H303), G338 (= G304), T339 (= T305), P341 (= P307), V349 (≠ A315), N350 (= N316), Y389 (≠ V355), D390 (= D356), R393 (≠ T359)
1ai2A Isocitrate dehydrogenase complexed with isocitrate, NADP+, and calcium (flash-cooled) (see paper)
53% identity, 98% coverage: 7:380/380 of query aligns to 29:414/414 of 1ai2A
- active site: Y158 (= Y134), K228 (= K201), D281 (= D247), D305 (= D271), D309 (= D275)
- binding isocitrate calcium complex: S111 (= S87), N113 (= N89), R117 (= R93), R127 (= R103), Y158 (= Y134), D305 (= D271), D309 (= D275)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I35 (= I13), L101 (= L77), T102 (≠ G78), T336 (= T302), H337 (= H303), G338 (= G304), T339 (= T305), A340 (= A306), P341 (= P307), Y343 (≠ I309), V349 (≠ A315), N350 (= N316), Y389 (≠ V355), D390 (= D356), R393 (≠ T359)
4aj3A 3d structure of e. Coli isocitrate dehydrogenase in complex with isocitrate, calcium(ii) and NADP - the pseudo-michaelis complex (see paper)
53% identity, 98% coverage: 7:380/380 of query aligns to 31:416/416 of 4aj3A
- active site: Y160 (= Y134), K230 (= K201), D283 (= D247), D307 (= D271), D311 (= D275)
- binding calcium ion: D307 (= D271), D311 (= D275)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P102 (= P76), L103 (= L77), T105 (= T79), N115 (= N89), I320 (≠ L284), E336 (= E300), H339 (= H303), G340 (= G304), T341 (= T305), A342 (= A306), Y345 (≠ I309), V351 (≠ A315), N352 (= N316), Y391 (≠ V355), D392 (= D356)
P08200 Isocitrate dehydrogenase [NADP]; IDH; IDP; NADP(+)-specific ICDH; Oxalosuccinate decarboxylase; EC 1.1.1.42 from Escherichia coli (strain K12) (see 9 papers)
53% identity, 98% coverage: 7:380/380 of query aligns to 31:416/416 of P08200
- K100 (= K74) modified: N6-succinyllysine; mutation K->R,E: Abolishes enzymatic activity.
- T104 (≠ G78) binding NADP(+)
- S113 (= S87) binding substrate; modified: Phosphoserine; mutation S->A,T: Decreased enzyme activity. Loss of phosphorylation.; mutation S->D,E: Reduced affinity for isocitrate.; mutation to D: Loss of enzyme activity.
- N115 (= N89) binding substrate
- R119 (= R93) binding substrate
- R129 (= R103) binding substrate
- K142 (= K116) modified: N6-acetyllysine
- R153 (= R127) binding substrate
- Y160 (= Y134) Critical for catalysis; mutation to F: Nearly abolishes enzyme activity. No significant effect on substrate affinity.
- K230 (= K201) Critical for catalysis; mutation to M: Nearly abolishes enzyme activity and strongly reduces substrate affinity.
- K242 (≠ R213) modified: N6-succinyllysine; mutation to E: Strongly impairs enzymatic activity.; mutation to R: Impairs enzymatic activity.
- D307 (= D271) binding Mg(2+)
- 339:345 (vs. 303:309, 71% identical) binding NADP(+)
- N352 (= N316) binding NADP(+)
- Y391 (≠ V355) binding NADP(+)
- R395 (≠ T359) binding NADP(+)
4ajaA 3d structure of e. Coli isocitrate dehydrogenase in complex with isocitrate, calcium(ii) and thionadp (see paper)
53% identity, 98% coverage: 7:380/380 of query aligns to 30:415/415 of 4ajaA
- active site: Y159 (= Y134), K229 (= K201), D282 (= D247), D306 (= D271), D310 (= D275)
- binding calcium ion: D306 (= D271), D310 (= D275)
- binding 7-thionicotinamide-adenine-dinucleotide phosphate: T103 (≠ G78), T104 (= T79), H338 (= H303), G339 (= G304), T340 (= T305), A341 (= A306), Y344 (≠ I309), N351 (= N316), Y390 (≠ V355), D391 (= D356), R394 (≠ T359)
1hj6A Isocitrate dehydrogenase s113e mutant complexed with isopropylmalate, NADP+ and magnesium (flash-cooled) (see paper)
53% identity, 98% coverage: 7:380/380 of query aligns to 29:414/414 of 1hj6A
- active site: Y158 (= Y134), K228 (= K201), D281 (= D247), D305 (= D271), D309 (= D275)
- binding 3-isopropylmalic acid: E111 (≠ S87), R117 (= R93), R127 (= R103), R151 (= R127), Y158 (= Y134), D305 (= D271)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P100 (= P76), L101 (= L77), T102 (≠ G78), N113 (= N89), I318 (≠ L284), G319 (= G285), H337 (= H303), G338 (= G304), T339 (= T305), A340 (= A306), Y343 (≠ I309), V349 (≠ A315), N350 (= N316), Y389 (≠ V355), D390 (= D356)
1idcA Isocitrate dehydrogenase from e.Coli (mutant k230m), steady-state intermediate complex determined by laue crystallography (see paper)
53% identity, 98% coverage: 7:380/380 of query aligns to 29:414/414 of 1idcA
4ajcA 3d structure of e. Coli isocitrate dehydrogenase k100m mutant in complex with alpha-ketoglutarate, calcium(ii) and adenine nucleotide phosphate (see paper)
53% identity, 98% coverage: 7:380/380 of query aligns to 30:415/415 of 4ajcA
- active site: Y159 (= Y134), K229 (= K201), D282 (= D247), D306 (= D271), D310 (= D275)
- binding adenosine-2'-5'-diphosphate: H338 (= H303), G339 (= G304), A341 (= A306), Y344 (≠ I309), V350 (≠ A315), N351 (= N316), Y390 (≠ V355), D391 (= D356)
- binding 2-oxoglutaric acid: S112 (= S87), R118 (= R93), R152 (= R127), Y159 (= Y134)
- binding calcium ion: D306 (= D271), D310 (= D275)
1cw4A Crystal structure of k230m isocitrate dehydrogenase in complex with alpha-ketoglutarate (see paper)
53% identity, 98% coverage: 7:380/380 of query aligns to 30:415/415 of 1cw4A
- active site: Y159 (= Y134), M229 (≠ K201), D282 (= D247), D306 (= D271), D310 (= D275)
- binding 2-oxoglutaric acid: S112 (= S87), N114 (= N89), R118 (= R93), R152 (= R127), Y159 (= Y134), D306 (= D271)
- binding manganese (ii) ion: D306 (= D271), D310 (= D275)
- binding sulfate ion: V106 (= V81), G107 (= G82), G109 (= G84)
1cw1A Crystal structure of isocitrate dehydrogenase mutant k230m bound to isocitrate and mn2+ (see paper)
53% identity, 98% coverage: 7:380/380 of query aligns to 30:415/415 of 1cw1A
1groA Regulatory and catalytic mechanisms in escherichia coli isocitrate dehydrogenase: multiple roles for n115 (see paper)
53% identity, 98% coverage: 7:380/380 of query aligns to 29:414/414 of 1groA
2iv0A Thermal stability of isocitrate dehydrogenase from archaeoglobus fulgidus studied by crystal structure analysis and engineering of chimers (see paper)
52% identity, 98% coverage: 7:380/380 of query aligns to 32:409/412 of 2iv0A
2e5mA Crystal structure of isocitrate dehydrogenase from sulfolobus tokodaii strain 7 (see paper)
47% identity, 98% coverage: 2:374/380 of query aligns to 24:394/403 of 2e5mA
- active site: Y150 (= Y134), K217 (= K201), D268 (= D247), D292 (= D271), D296 (= D275)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L99 (= L77), T101 (= T79), N105 (= N89), E321 (= E300), H324 (= H303), G325 (= G304), K329 (≠ T308), Y330 (≠ I309), N337 (= N316)
1tyoA Isocitrate dehydrogenase from the hyperthermophile aeropyrum pernix in complex with etheno-NADP (see paper)
49% identity, 99% coverage: 4:378/380 of query aligns to 32:414/427 of 1tyoA
Sites not aligning to the query:
1xkdA Ternary complex of isocitrate dehydrogenase from the hyperthermophile aeropyrum pernix (see paper)
48% identity, 99% coverage: 4:378/380 of query aligns to 33:411/427 of 1xkdA
- active site: Y158 (= Y134), K225 (= K201), D279 (= D247), D303 (= D271), D307 (= D275)
- binding calcium ion: D303 (= D271), D307 (= D275)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P105 (= P76), L106 (= L77), T108 (= T79), N114 (= N89), I277 (= I245), N280 (≠ A248), Q283 (= Q251), Q284 (≠ E252), R288 (= R256), G317 (= G285), E332 (= E300), H335 (= H303), G336 (= G304), T337 (= T305), A338 (= A306), Y341 (≠ I309), I347 (≠ A315), N348 (= N316), D389 (= D356), R392 (≠ T359)
Query Sequence
>209413 MicrobesOnline__882:209413
MRKTVYWIEGDGIGPEVWKAARPVIDAAVEKSYGDSRSIEWKELLAGEKAHRETGEYLPQ
STLDTLATAELAIKGPLGTPVGKGFRSLNVTMRQTLDLYACIRPIRYFDGIMSPVKRPDL
VDMVVFRENTEDVYAGIEYRAGTPEAKRLIAFLRDELGAKVDIEAAVGIKPMTEKGSKRL
VRRALRFAIDQKRPNLTLVHKGNIMKFTEGGFREWGYEVARDEFADLTTTETEGTAGRLV
VKDRIADAMFQEVLIRPQQYSVIATSNLNGDYISDALAAQVGGLGLAPGVNMSDSLAFFE
ATHGTAPTIAGQDKANPGSLILCGALMLEHMGWNEAAERIYKAVNEAIASRRVTVDLATQ
MENATTVGTVAFGDIVTAGL
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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