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Comparing Ac3H11_2377 FitnessBrowser__acidovorax_3H11:Ac3H11_2377 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)
75% identity, 99% coverage: 4:419/419 of query aligns to 3:418/418 of Q02NB5
- S115 (= S116) modified: Phosphoserine
- T193 (≠ P194) modified: Phosphothreonine
6c0eA Crystal structure of isocitrate dehydrogenase from legionella pneumophila with bound NADPH with an alpha-ketoglutarate adduct
73% identity, 100% coverage: 3:419/419 of query aligns to 3:419/419 of 6c0eA
- active site: Y163 (= Y163), K233 (= K233), D286 (= D286), D310 (= D310)
- 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 (= P105), L106 (= L106), T108 (= T108), S116 (= S116), N118 (= N118), R122 (= R122), R132 (= R132), R156 (= R156), N235 (= N235), I284 (= I284), Q291 (= Q291), R295 (= R295), D310 (= D310), I323 (= I323), E339 (= E339), H342 (= H342), G343 (= G343), T344 (= T344), A345 (= A345), K347 (= K347), Y348 (= Y348), V354 (= V354), N355 (= N355), Y394 (= Y394), D395 (= D395)
- binding glycine: S23 (= S23), L24 (= L24), H25 (≠ N25)
1bl5A Isocitrate dehydrogenase from e. Coli single turnover laue structure of rate-limited product complex, 10 msec time resolution (see paper)
73% identity, 99% coverage: 7:419/419 of query aligns to 3:414/414 of 1bl5A
- active site: Y158 (= Y163), K228 (= K233), D281 (= D286), D305 (= D310), D309 (= D314)
- binding 2-oxoglutaric acid: S111 (= S116), N113 (= N118), R117 (= R122), R127 (= R132)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: H337 (= H342), G338 (= G343), A340 (= A345), Y343 (= Y348), N350 (= N355), Y389 (= Y394)
1ai3A Orbital steering in the catalytic power of enzymes: small structural changes with large catalytic consequences (see paper)
73% identity, 99% coverage: 7:419/419 of query aligns to 3:414/414 of 1ai3A
- active site: Y158 (= Y163), K228 (= K233), D281 (= D286), D305 (= D310), D309 (= D314)
- binding nicotinamide-(6-deamino-6-hydroxy-adenine)-dinucleotide phosphate: I35 (≠ T40), G99 (= G104), P100 (= P105), L101 (= L106), T102 (= T107), A335 (= A340), T336 (= T341), H337 (= H342), G338 (= G343), T339 (= T344), P341 (= P346), V349 (= V354), N350 (= N355), Y389 (= Y394), D390 (= D395), R393 (= R398)
1ai2A Isocitrate dehydrogenase complexed with isocitrate, NADP+, and calcium (flash-cooled) (see paper)
73% identity, 99% coverage: 7:419/419 of query aligns to 3:414/414 of 1ai2A
- active site: Y158 (= Y163), K228 (= K233), D281 (= D286), D305 (= D310), D309 (= D314)
- binding isocitrate calcium complex: S111 (= S116), N113 (= N118), R117 (= R122), R127 (= R132), Y158 (= Y163), D305 (= D310), D309 (= D314)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I35 (≠ T40), L101 (= L106), T102 (= T107), T336 (= T341), H337 (= H342), G338 (= G343), T339 (= T344), A340 (= A345), P341 (= P346), Y343 (= Y348), V349 (= V354), N350 (= N355), Y389 (= Y394), D390 (= D395), R393 (= R398)
4aj3A 3d structure of e. Coli isocitrate dehydrogenase in complex with isocitrate, calcium(ii) and NADP - the pseudo-michaelis complex (see paper)
73% identity, 99% coverage: 7:419/419 of query aligns to 5:416/416 of 4aj3A
- active site: Y160 (= Y163), K230 (= K233), D283 (= D286), D307 (= D310), D311 (= D314)
- binding calcium ion: D307 (= D310), D311 (= D314)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P102 (= P105), L103 (= L106), T105 (= T108), N115 (= N118), I320 (= I323), E336 (= E339), H339 (= H342), G340 (= G343), T341 (= T344), A342 (= A345), Y345 (= Y348), V351 (= V354), N352 (= N355), Y391 (= Y394), D392 (= D395)
P08200 Isocitrate dehydrogenase [NADP]; IDH; IDP; NADP(+)-specific ICDH; Oxalosuccinate decarboxylase; EC 1.1.1.42 from Escherichia coli (strain K12) (see 9 papers)
73% identity, 99% coverage: 7:419/419 of query aligns to 5:416/416 of P08200
- K100 (= K103) modified: N6-succinyllysine; mutation K->R,E: Abolishes enzymatic activity.
- T104 (= T107) binding
- S113 (= S116) binding ; 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 (= N118) binding
- R119 (= R122) binding
- R129 (= R132) binding
- K142 (= K145) modified: N6-acetyllysine
- R153 (= R156) binding
- Y160 (= Y163) Critical for catalysis; mutation to F: Nearly abolishes enzyme activity. No significant effect on substrate affinity.
- K230 (= K233) Critical for catalysis; mutation to M: Nearly abolishes enzyme activity and strongly reduces substrate affinity.
- K242 (≠ R245) modified: N6-succinyllysine; mutation to E: Strongly impairs enzymatic activity.; mutation to R: Impairs enzymatic activity.
- D307 (= D310) binding
- 339:345 (vs. 342:348, 100% identical) binding
- N352 (= N355) binding
- Y391 (= Y394) binding
- R395 (= R398) binding
4ajaA 3d structure of e. Coli isocitrate dehydrogenase in complex with isocitrate, calcium(ii) and thionadp (see paper)
73% identity, 99% coverage: 7:419/419 of query aligns to 4:415/415 of 4ajaA
- active site: Y159 (= Y163), K229 (= K233), D282 (= D286), D306 (= D310), D310 (= D314)
- binding calcium ion: D306 (= D310), D310 (= D314)
- binding 7-thionicotinamide-adenine-dinucleotide phosphate: T103 (= T107), T104 (= T108), H338 (= H342), G339 (= G343), T340 (= T344), A341 (= A345), Y344 (= Y348), N351 (= N355), Y390 (= Y394), D391 (= D395), R394 (= R398)
1hj6A Isocitrate dehydrogenase s113e mutant complexed with isopropylmalate, NADP+ and magnesium (flash-cooled) (see paper)
72% identity, 99% coverage: 7:419/419 of query aligns to 3:414/414 of 1hj6A
- active site: Y158 (= Y163), K228 (= K233), D281 (= D286), D305 (= D310), D309 (= D314)
- binding 3-isopropylmalic acid: E111 (≠ S116), R117 (= R122), R127 (= R132), R151 (= R156), Y158 (= Y163), D305 (= D310)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P100 (= P105), L101 (= L106), T102 (= T107), N113 (= N118), I318 (= I323), G319 (= G324), H337 (= H342), G338 (= G343), T339 (= T344), A340 (= A345), Y343 (= Y348), V349 (= V354), N350 (= N355), Y389 (= Y394), D390 (= D395)
1idcA Isocitrate dehydrogenase from e.Coli (mutant k230m), steady-state intermediate complex determined by laue crystallography (see paper)
72% identity, 99% coverage: 7:419/419 of query aligns to 3:414/414 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)
72% identity, 99% coverage: 7:419/419 of query aligns to 4:415/415 of 4ajcA
- active site: Y159 (= Y163), K229 (= K233), D282 (= D286), D306 (= D310), D310 (= D314)
- binding adenosine-2'-5'-diphosphate: H338 (= H342), G339 (= G343), A341 (= A345), Y344 (= Y348), V350 (= V354), N351 (= N355), Y390 (= Y394), D391 (= D395)
- binding 2-oxoglutaric acid: S112 (= S116), R118 (= R122), R152 (= R156), Y159 (= Y163)
- binding calcium ion: D306 (= D310), D310 (= D314)
1cw4A Crystal structure of k230m isocitrate dehydrogenase in complex with alpha-ketoglutarate (see paper)
72% identity, 99% coverage: 7:419/419 of query aligns to 4:415/415 of 1cw4A
- active site: Y159 (= Y163), M229 (≠ K233), D282 (= D286), D306 (= D310), D310 (= D314)
- binding 2-oxoglutaric acid: S112 (= S116), N114 (= N118), R118 (= R122), R152 (= R156), Y159 (= Y163), D306 (= D310)
- binding manganese (ii) ion: D306 (= D310), D310 (= D314)
- binding sulfate ion: V106 (= V110), G107 (= G111), G109 (= G113)
1cw1A Crystal structure of isocitrate dehydrogenase mutant k230m bound to isocitrate and mn2+ (see paper)
72% identity, 99% coverage: 7:419/419 of query aligns to 4:415/415 of 1cw1A
1groA Regulatory and catalytic mechanisms in escherichia coli isocitrate dehydrogenase: multiple roles for n115 (see paper)
72% identity, 99% coverage: 7:419/419 of query aligns to 3:414/414 of 1groA
1isoA Isocitrate dehydrogenase: structure of an engineered NADP+--> NAD+ specificity-reversal mutant (see paper)
71% identity, 99% coverage: 7:419/419 of query aligns to 3:414/414 of 1isoA
- active site: Y158 (= Y163), K228 (= K233), D281 (= D286), D305 (= D310), D309 (= D314)
- binding nicotinamide-adenine-dinucleotide: I35 (≠ T40), H337 (= H342), G338 (= G343), A340 (= A345), D342 (≠ K347), A349 (≠ V354), N350 (= N355)
2d4vA Crystal structure of NAD dependent isocitrate dehydrogenase from acidithiobacillus thiooxidans (see paper)
60% identity, 98% coverage: 6:416/419 of query aligns to 2:424/427 of 2d4vA
- active site: Y158 (= Y163), K228 (= K233), D294 (= D286), D318 (= D310), D322 (= D314)
- binding citrate anion: T103 (= T108), S111 (= S116), N113 (= N118), R117 (= R122), R127 (= R132), R151 (= R156), Y158 (= Y163), K228 (= K233), I231 (= I236), D318 (= D310)
- binding nicotinamide-adenine-dinucleotide: I35 (≠ T40), P100 (= P105), L101 (= L106), E102 (≠ T107), T103 (= T108), N113 (= N118), N230 (= N235), I292 (= I284), N295 (≠ A287), I331 (= I323), E347 (= E339), T349 (= T341), H350 (= H342), G351 (= G343), T352 (= T344), A353 (= A345), D355 (≠ K347), A362 (≠ V354), N363 (= N355), D403 (= D395)
2iv0A Thermal stability of isocitrate dehydrogenase from archaeoglobus fulgidus studied by crystal structure analysis and engineering of chimers (see paper)
52% identity, 99% coverage: 4:419/419 of query aligns to 3:409/412 of 2iv0A
2e5mA Crystal structure of isocitrate dehydrogenase from sulfolobus tokodaii strain 7 (see paper)
47% identity, 98% coverage: 10:419/419 of query aligns to 6:400/403 of 2e5mA
- active site: Y150 (= Y163), K217 (= K233), D268 (= D286), D292 (= D310), D296 (= D314)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L99 (= L106), T101 (= T108), N105 (= N118), E321 (= E339), H324 (= H342), G325 (= G343), K329 (= K347), Y330 (= Y348), N337 (= N355)
1tyoA Isocitrate dehydrogenase from the hyperthermophile aeropyrum pernix in complex with etheno-NADP (see paper)
46% identity, 98% coverage: 10:419/419 of query aligns to 11:416/427 of 1tyoA
1xkdA Ternary complex of isocitrate dehydrogenase from the hyperthermophile aeropyrum pernix (see paper)
46% identity, 98% coverage: 10:419/419 of query aligns to 12:413/427 of 1xkdA
- active site: Y158 (= Y163), K225 (= K233), D279 (= D286), D303 (= D310), D307 (= D314)
- binding calcium ion: D303 (= D310), D307 (= D314)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P105 (= P105), L106 (= L106), T108 (= T108), N114 (= N118), I277 (= I284), N280 (≠ A287), Q283 (= Q290), Q284 (= Q291), R288 (= R295), G317 (= G324), E332 (= E339), H335 (= H342), G336 (= G343), T337 (= T344), A338 (= A345), Y341 (= Y348), I347 (≠ V354), N348 (= N355), D389 (= D395), R392 (= R398)
Query Sequence
>Ac3H11_2377 FitnessBrowser__acidovorax_3H11:Ac3H11_2377
MTTYQHIVVPAAGQKITVNADMSLNVPDEPIIPFIEGDGTGLDITPVMIKVVNAAVAKAY
GGKKKIHWMEVYAGEKSTKVYGPDVWLPEETLAVLREYVVSIKGPLTTPVGGGIRSLNVA
LRQELDLYVCLRPVQYFKGVPSPLKEPEKTNMVIFRENSEDIYAGIEFEAESDKAKKLIK
FLQDEMGVKKIRFPNTSGLGVKPVSREGTERLVRKAIQYAIDNDKPSVTIVHKGNIMKFT
EGGFRDWAYALAQKEFGAELIDGGPWCKLKNPKTGKDITVKDSIADAFLQQILLRPAEYS
VVATLNLNGDYISDALAAQVGGIGIAPGANMSDSVACFEATHGTAPKYAGKDYVNPGSEI
LSAEMMLRHMGWTAAANLIISSLEKSIASKKVTYDFARLMDGATQVSCSGFGQVMIDHM
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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