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Comparing WP_011734398.1 NCBI__GCF_000015045.1:WP_011734398.1 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, 100% coverage: 1:470/470 of query aligns to 1:418/418 of Q02NB5
- S115 (= S118) modified: Phosphoserine
- T193 (≠ P196) modified: Phosphothreonine
4ajaA 3d structure of e. Coli isocitrate dehydrogenase in complex with isocitrate, calcium(ii) and thionadp (see paper)
57% identity, 99% coverage: 6:470/470 of query aligns to 4:415/415 of 4ajaA
- active site: Y159 (= Y165), K229 (= K235), D282 (= D335), D306 (= D359), D310 (= D363)
- binding calcium ion: D306 (= D359), D310 (= D363)
- binding 7-thionicotinamide-adenine-dinucleotide phosphate: T103 (= T109), T104 (= T110), H338 (= H393), G339 (= G394), T340 (= T395), A341 (= A396), Y344 (= Y399), N351 (= N406), Y390 (= Y445), D391 (= D446), R394 (= R449)
1bl5A Isocitrate dehydrogenase from e. Coli single turnover laue structure of rate-limited product complex, 10 msec time resolution (see paper)
57% identity, 99% coverage: 6:470/470 of query aligns to 3:414/414 of 1bl5A
- active site: Y158 (= Y165), K228 (= K235), D281 (= D335), D305 (= D359), D309 (= D363)
- binding 2-oxoglutaric acid: S111 (= S118), N113 (= N120), R117 (= R124), R127 (= R134)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: H337 (= H393), G338 (= G394), A340 (= A396), Y343 (= Y399), N350 (= N406), Y389 (= Y445)
1ai3A Orbital steering in the catalytic power of enzymes: small structural changes with large catalytic consequences (see paper)
57% identity, 99% coverage: 6:470/470 of query aligns to 3:414/414 of 1ai3A
- active site: Y158 (= Y165), K228 (= K235), D281 (= D335), D305 (= D359), D309 (= D363)
- binding nicotinamide-(6-deamino-6-hydroxy-adenine)-dinucleotide phosphate: I35 (≠ T38), G99 (= G106), P100 (= P107), L101 (= L108), T102 (= T109), A335 (= A391), T336 (= T392), H337 (= H393), G338 (= G394), T339 (= T395), P341 (= P397), V349 (= V405), N350 (= N406), Y389 (= Y445), D390 (= D446), R393 (= R449)
1ai2A Isocitrate dehydrogenase complexed with isocitrate, NADP+, and calcium (flash-cooled) (see paper)
57% identity, 99% coverage: 6:470/470 of query aligns to 3:414/414 of 1ai2A
- active site: Y158 (= Y165), K228 (= K235), D281 (= D335), D305 (= D359), D309 (= D363)
- binding isocitrate calcium complex: S111 (= S118), N113 (= N120), R117 (= R124), R127 (= R134), Y158 (= Y165), D305 (= D359), D309 (= D363)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I35 (≠ T38), L101 (= L108), T102 (= T109), T336 (= T392), H337 (= H393), G338 (= G394), T339 (= T395), A340 (= A396), P341 (= P397), Y343 (= Y399), V349 (= V405), N350 (= N406), Y389 (= Y445), D390 (= D446), R393 (= R449)
4aj3A 3d structure of e. Coli isocitrate dehydrogenase in complex with isocitrate, calcium(ii) and NADP - the pseudo-michaelis complex (see paper)
57% identity, 99% coverage: 6:470/470 of query aligns to 5:416/416 of 4aj3A
- active site: Y160 (= Y165), K230 (= K235), D283 (= D335), D307 (= D359), D311 (= D363)
- binding calcium ion: D307 (= D359), D311 (= D363)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P102 (= P107), L103 (= L108), T105 (= T110), N115 (= N120), I320 (= I372), E336 (= E390), H339 (= H393), G340 (= G394), T341 (= T395), A342 (= A396), Y345 (= Y399), V351 (= V405), N352 (= N406), Y391 (= Y445), D392 (= D446)
P08200 Isocitrate dehydrogenase [NADP]; IDH; IDP; NADP(+)-specific ICDH; Oxalosuccinate decarboxylase; EC 1.1.1.42 from Escherichia coli (strain K12) (see 9 papers)
57% identity, 99% coverage: 6:470/470 of query aligns to 5:416/416 of P08200
- K100 (= K105) modified: N6-succinyllysine; mutation K->R,E: Abolishes enzymatic activity.
- T104 (= T109) binding NADP(+)
- S113 (= S118) 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 (= N120) binding substrate
- R119 (= R124) binding substrate
- R129 (= R134) binding substrate
- K142 (= K147) modified: N6-acetyllysine
- R153 (= R158) binding substrate
- Y160 (= Y165) Critical for catalysis; mutation to F: Nearly abolishes enzyme activity. No significant effect on substrate affinity.
- K230 (= K235) Critical for catalysis; mutation to M: Nearly abolishes enzyme activity and strongly reduces substrate affinity.
- K242 (= K247) modified: N6-succinyllysine; mutation to E: Strongly impairs enzymatic activity.; mutation to R: Impairs enzymatic activity.
- D307 (= D359) binding Mg(2+)
- 339:345 (vs. 393:399, 100% identical) binding NADP(+)
- N352 (= N406) binding NADP(+)
- Y391 (= Y445) binding NADP(+)
- R395 (= R449) binding NADP(+)
1hj6A Isocitrate dehydrogenase s113e mutant complexed with isopropylmalate, NADP+ and magnesium (flash-cooled) (see paper)
56% identity, 99% coverage: 6:470/470 of query aligns to 3:414/414 of 1hj6A
- active site: Y158 (= Y165), K228 (= K235), D281 (= D335), D305 (= D359), D309 (= D363)
- binding 3-isopropylmalic acid: E111 (≠ S118), R117 (= R124), R127 (= R134), R151 (= R158), Y158 (= Y165), D305 (= D359)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P100 (= P107), L101 (= L108), T102 (= T109), N113 (= N120), I318 (= I372), G319 (= G373), H337 (= H393), G338 (= G394), T339 (= T395), A340 (= A396), Y343 (= Y399), V349 (= V405), N350 (= N406), Y389 (= Y445), D390 (= D446)
4ajcA 3d structure of e. Coli isocitrate dehydrogenase k100m mutant in complex with alpha-ketoglutarate, calcium(ii) and adenine nucleotide phosphate (see paper)
56% identity, 99% coverage: 6:470/470 of query aligns to 4:415/415 of 4ajcA
- active site: Y159 (= Y165), K229 (= K235), D282 (= D335), D306 (= D359), D310 (= D363)
- binding adenosine-2'-5'-diphosphate: H338 (= H393), G339 (= G394), A341 (= A396), Y344 (= Y399), V350 (= V405), N351 (= N406), Y390 (= Y445), D391 (= D446)
- binding 2-oxoglutaric acid: S112 (= S118), R118 (= R124), R152 (= R158), Y159 (= Y165)
- binding calcium ion: D306 (= D359), D310 (= D363)
1cw4A Crystal structure of k230m isocitrate dehydrogenase in complex with alpha-ketoglutarate (see paper)
56% identity, 99% coverage: 6:470/470 of query aligns to 4:415/415 of 1cw4A
- active site: Y159 (= Y165), M229 (≠ K235), D282 (= D335), D306 (= D359), D310 (= D363)
- binding 2-oxoglutaric acid: S112 (= S118), N114 (= N120), R118 (= R124), R152 (= R158), Y159 (= Y165), D306 (= D359)
- binding manganese (ii) ion: D306 (= D359), D310 (= D363)
- binding sulfate ion: V106 (≠ I112), G107 (= G113), G109 (= G115)
1cw1A Crystal structure of isocitrate dehydrogenase mutant k230m bound to isocitrate and mn2+ (see paper)
56% identity, 99% coverage: 6:470/470 of query aligns to 4:415/415 of 1cw1A
1idcA Isocitrate dehydrogenase from e.Coli (mutant k230m), steady-state intermediate complex determined by laue crystallography (see paper)
56% identity, 99% coverage: 6:470/470 of query aligns to 3:414/414 of 1idcA
6c0eA Crystal structure of isocitrate dehydrogenase from legionella pneumophila with bound NADPH with an alpha-ketoglutarate adduct
56% identity, 100% coverage: 1:470/470 of query aligns to 2:419/419 of 6c0eA
- active site: Y163 (= Y165), K233 (= K235), D286 (= D335), D310 (= D359)
- 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 (= P107), L106 (= L108), T108 (= T110), S116 (= S118), N118 (= N120), R122 (= R124), R132 (= R134), R156 (= R158), N235 (= N237), I284 (= I333), Q291 (= Q340), R295 (= R344), D310 (= D359), I323 (= I372), E339 (= E390), H342 (= H393), G343 (= G394), T344 (= T395), A345 (= A396), K347 (= K398), Y348 (= Y399), V354 (= V405), N355 (= N406), Y394 (= Y445), D395 (= D446)
- binding glycine: S23 (≠ K21), L24 (= L22), H25 (≠ R23)
1groA Regulatory and catalytic mechanisms in escherichia coli isocitrate dehydrogenase: multiple roles for n115 (see paper)
56% identity, 99% coverage: 6:470/470 of query aligns to 3:414/414 of 1groA
1isoA Isocitrate dehydrogenase: structure of an engineered NADP+--> NAD+ specificity-reversal mutant (see paper)
56% identity, 99% coverage: 6:470/470 of query aligns to 3:414/414 of 1isoA
- active site: Y158 (= Y165), K228 (= K235), D281 (= D335), D305 (= D359), D309 (= D363)
- binding nicotinamide-adenine-dinucleotide: I35 (≠ T38), H337 (= H393), G338 (= G394), A340 (= A396), D342 (≠ K398), A349 (≠ V405), N350 (= N406)
2d4vA Crystal structure of NAD dependent isocitrate dehydrogenase from acidithiobacillus thiooxidans (see paper)
54% identity, 96% coverage: 19:467/470 of query aligns to 16:424/427 of 2d4vA
- active site: Y158 (= Y165), K228 (= K235), D294 (= D335), D318 (= D359), D322 (= D363)
- binding citrate anion: T103 (= T110), S111 (= S118), N113 (= N120), R117 (= R124), R127 (= R134), R151 (= R158), Y158 (= Y165), K228 (= K235), I231 (= I238), D318 (= D359)
- binding nicotinamide-adenine-dinucleotide: I35 (≠ T38), P100 (= P107), L101 (= L108), E102 (≠ T109), T103 (= T110), N113 (= N120), N230 (= N237), I292 (= I333), N295 (≠ I336), I331 (= I372), E347 (= E390), T349 (= T392), H350 (= H393), G351 (= G394), T352 (= T395), A353 (= A396), D355 (≠ K398), A362 (≠ V405), N363 (= N406), D403 (= D446)
2iv0A Thermal stability of isocitrate dehydrogenase from archaeoglobus fulgidus studied by crystal structure analysis and engineering of chimers (see paper)
48% identity, 100% coverage: 1:470/470 of query aligns to 1:409/412 of 2iv0A
1tyoA Isocitrate dehydrogenase from the hyperthermophile aeropyrum pernix in complex with etheno-NADP (see paper)
44% identity, 98% coverage: 6:467/470 of query aligns to 9:413/427 of 1tyoA
1xkdA Ternary complex of isocitrate dehydrogenase from the hyperthermophile aeropyrum pernix (see paper)
43% identity, 98% coverage: 6:467/470 of query aligns to 10:410/427 of 1xkdA
- active site: Y158 (= Y165), K225 (= K235), D279 (= D335), D303 (= D359), D307 (= D363)
- binding calcium ion: D303 (= D359), D307 (= D363)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P105 (= P107), L106 (= L108), T108 (= T110), N114 (= N120), I277 (= I333), N280 (≠ I336), Q283 (= Q339), Q284 (= Q340), R288 (= R344), G317 (= G373), E332 (= E390), H335 (= H393), G336 (= G394), T337 (= T395), A338 (= A396), Y341 (= Y399), I347 (≠ V405), N348 (= N406), D389 (= D446), R392 (= R449)
2e5mA Crystal structure of isocitrate dehydrogenase from sulfolobus tokodaii strain 7 (see paper)
42% identity, 99% coverage: 5:470/470 of query aligns to 3:400/403 of 2e5mA
- active site: Y150 (= Y165), K217 (= K235), D268 (= D335), D292 (= D359), D296 (= D363)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L99 (= L108), T101 (= T110), N105 (= N120), E321 (= E390), H324 (= H393), G325 (= G394), K329 (= K398), Y330 (= Y399), N337 (= N406)
Query Sequence
>WP_011734398.1 NCBI__GCF_000015045.1:WP_011734398.1
MNYTYLTVPQGEKISMGSDGKLRVPANPIIPFIEGDGTGPDIWRAAKRVLDAAVARAYGG
ARKISWMEVFAGEKSFNMFRESMGDRAWLPDETVDAYREFLVGIKGPLTTPIGGGIRSLN
VALRQLLDLYVCLRPVRYFQGVPSPVKKPQDVDMVIFRENTEDIYAGIEWMQGTTECEKL
KRFLLEEMKVTNIRFPGSVSLGVKPISKEGSQRLVRAAIDYALEQGRRSVTLVHKGNIMK
YTEGAFKEWGYQVATEQFRDRVVTERESWIIANQDKNPTMAPEENARLIEPGYDLMTPNQ
RQRIVDEVQAALGLMATHGNGQWKKLLLIKDSIADIALQQVLTRAKEFDVIATMNLEGDF
LSDALAAQVGGIGIAPGANINYLTGHAIFEATHGTAPKYANQDKVNPGSVILSGVMMLEY
LGWREAADLVIAAIDRTISQKKVTYDFERLMEGATLVSCSGFADALIGNM
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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