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Comparing WP_028585044.1 NCBI__GCF_000429965.1:WP_028585044.1 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)
64% identity, 100% coverage: 3:405/405 of query aligns to 12:418/418 of Q02NB5
- S115 (= S104) modified: Phosphoserine
- T193 (vs. gap) modified: Phosphothreonine
4ajaA 3d structure of e. Coli isocitrate dehydrogenase in complex with isocitrate, calcium(ii) and thionadp (see paper)
66% identity, 100% coverage: 3:405/405 of query aligns to 10:415/415 of 4ajaA
- active site: Y159 (= Y151), K229 (= K218), D282 (= D272), D306 (= D296), D310 (= D300)
- binding calcium ion: D306 (= D296), D310 (= D300)
- binding 7-thionicotinamide-adenine-dinucleotide phosphate: T103 (= T95), T104 (= T96), H338 (= H328), G339 (= G329), T340 (= T330), A341 (= A331), Y344 (= Y334), N351 (= N341), Y390 (= Y380), D391 (= D381), R394 (= R384)
1bl5A Isocitrate dehydrogenase from e. Coli single turnover laue structure of rate-limited product complex, 10 msec time resolution (see paper)
66% identity, 100% coverage: 3:405/405 of query aligns to 9:414/414 of 1bl5A
- active site: Y158 (= Y151), K228 (= K218), D281 (= D272), D305 (= D296), D309 (= D300)
- binding 2-oxoglutaric acid: S111 (= S104), N113 (= N106), R117 (= R110), R127 (= R120)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: H337 (= H328), G338 (= G329), A340 (= A331), Y343 (= Y334), N350 (= N341), Y389 (= Y380)
1ai3A Orbital steering in the catalytic power of enzymes: small structural changes with large catalytic consequences (see paper)
66% identity, 100% coverage: 3:405/405 of query aligns to 9:414/414 of 1ai3A
- active site: Y158 (= Y151), K228 (= K218), D281 (= D272), D305 (= D296), D309 (= D300)
- binding nicotinamide-(6-deamino-6-hydroxy-adenine)-dinucleotide phosphate: I35 (= I30), G99 (= G92), P100 (= P93), L101 (= L94), T102 (= T95), A335 (= A326), T336 (= T327), H337 (= H328), G338 (= G329), T339 (= T330), P341 (= P332), V349 (= V340), N350 (= N341), Y389 (= Y380), D390 (= D381), R393 (= R384)
1ai2A Isocitrate dehydrogenase complexed with isocitrate, NADP+, and calcium (flash-cooled) (see paper)
66% identity, 100% coverage: 3:405/405 of query aligns to 9:414/414 of 1ai2A
- active site: Y158 (= Y151), K228 (= K218), D281 (= D272), D305 (= D296), D309 (= D300)
- binding isocitrate calcium complex: S111 (= S104), N113 (= N106), R117 (= R110), R127 (= R120), Y158 (= Y151), D305 (= D296), D309 (= D300)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I35 (= I30), L101 (= L94), T102 (= T95), T336 (= T327), H337 (= H328), G338 (= G329), T339 (= T330), A340 (= A331), P341 (= P332), Y343 (= Y334), V349 (= V340), N350 (= N341), Y389 (= Y380), D390 (= D381), R393 (= R384)
4aj3A 3d structure of e. Coli isocitrate dehydrogenase in complex with isocitrate, calcium(ii) and NADP - the pseudo-michaelis complex (see paper)
66% identity, 100% coverage: 3:405/405 of query aligns to 11:416/416 of 4aj3A
- active site: Y160 (= Y151), K230 (= K218), D283 (= D272), D307 (= D296), D311 (= D300)
- binding calcium ion: D307 (= D296), D311 (= D300)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P102 (= P93), L103 (= L94), T105 (= T96), N115 (= N106), I320 (≠ L309), E336 (= E325), H339 (= H328), G340 (= G329), T341 (= T330), A342 (= A331), Y345 (= Y334), V351 (= V340), N352 (= N341), Y391 (= Y380), D392 (= D381)
P08200 Isocitrate dehydrogenase [NADP]; IDH; IDP; NADP(+)-specific ICDH; Oxalosuccinate decarboxylase; EC 1.1.1.42 from Escherichia coli (strain K12) (see 9 papers)
66% identity, 100% coverage: 3:405/405 of query aligns to 11:416/416 of P08200
- K100 (= K91) modified: N6-succinyllysine; mutation K->R,E: Abolishes enzymatic activity.
- T104 (= T95) binding
- S113 (= S104) 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 (= N106) binding
- R119 (= R110) binding
- R129 (= R120) binding
- K142 (= K133) modified: N6-acetyllysine
- R153 (= R144) binding
- Y160 (= Y151) Critical for catalysis; mutation to F: Nearly abolishes enzyme activity. No significant effect on substrate affinity.
- K230 (= K218) Critical for catalysis; mutation to M: Nearly abolishes enzyme activity and strongly reduces substrate affinity.
- K242 (≠ R230) modified: N6-succinyllysine; mutation to E: Strongly impairs enzymatic activity.; mutation to R: Impairs enzymatic activity.
- D307 (= D296) binding
- 339:345 (vs. 328:334, 100% identical) binding
- N352 (= N341) binding
- Y391 (= Y380) binding
- R395 (= R384) binding
1hj6A Isocitrate dehydrogenase s113e mutant complexed with isopropylmalate, NADP+ and magnesium (flash-cooled) (see paper)
65% identity, 100% coverage: 3:405/405 of query aligns to 9:414/414 of 1hj6A
- active site: Y158 (= Y151), K228 (= K218), D281 (= D272), D305 (= D296), D309 (= D300)
- binding 3-isopropylmalic acid: E111 (≠ S104), R117 (= R110), R127 (= R120), R151 (= R144), Y158 (= Y151), D305 (= D296)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P100 (= P93), L101 (= L94), T102 (= T95), N113 (= N106), I318 (≠ L309), G319 (= G310), H337 (= H328), G338 (= G329), T339 (= T330), A340 (= A331), Y343 (= Y334), V349 (= V340), N350 (= N341), Y389 (= Y380), D390 (= D381)
1idcA Isocitrate dehydrogenase from e.Coli (mutant k230m), steady-state intermediate complex determined by laue crystallography (see paper)
65% identity, 100% coverage: 3:405/405 of query aligns to 9:414/414 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)
65% identity, 100% coverage: 3:405/405 of query aligns to 10:415/415 of 4ajcA
- active site: Y159 (= Y151), K229 (= K218), D282 (= D272), D306 (= D296), D310 (= D300)
- binding adenosine-2'-5'-diphosphate: H338 (= H328), G339 (= G329), A341 (= A331), Y344 (= Y334), V350 (= V340), N351 (= N341), Y390 (= Y380), D391 (= D381)
- binding 2-oxoglutaric acid: S112 (= S104), R118 (= R110), R152 (= R144), Y159 (= Y151)
- binding calcium ion: D306 (= D296), D310 (= D300)
1cw4A Crystal structure of k230m isocitrate dehydrogenase in complex with alpha-ketoglutarate (see paper)
65% identity, 100% coverage: 3:405/405 of query aligns to 10:415/415 of 1cw4A
- active site: Y159 (= Y151), M229 (≠ K218), D282 (= D272), D306 (= D296), D310 (= D300)
- binding 2-oxoglutaric acid: S112 (= S104), N114 (= N106), R118 (= R110), R152 (= R144), Y159 (= Y151), D306 (= D296)
- binding manganese (ii) ion: D306 (= D296), D310 (= D300)
- binding sulfate ion: V106 (= V98), G107 (= G99), G109 (= G101)
1cw1A Crystal structure of isocitrate dehydrogenase mutant k230m bound to isocitrate and mn2+ (see paper)
65% identity, 100% coverage: 3:405/405 of query aligns to 10:415/415 of 1cw1A
1groA Regulatory and catalytic mechanisms in escherichia coli isocitrate dehydrogenase: multiple roles for n115 (see paper)
65% identity, 100% coverage: 3:405/405 of query aligns to 9:414/414 of 1groA
1isoA Isocitrate dehydrogenase: structure of an engineered NADP+--> NAD+ specificity-reversal mutant (see paper)
64% identity, 100% coverage: 3:405/405 of query aligns to 9:414/414 of 1isoA
- active site: Y158 (= Y151), K228 (= K218), D281 (= D272), D305 (= D296), D309 (= D300)
- binding nicotinamide-adenine-dinucleotide: I35 (= I30), H337 (= H328), G338 (= G329), A340 (= A331), D342 (≠ K333), A349 (≠ V340), N350 (= N341)
6c0eA Crystal structure of isocitrate dehydrogenase from legionella pneumophila with bound NADPH with an alpha-ketoglutarate adduct
61% identity, 100% coverage: 3:405/405 of query aligns to 13:419/419 of 6c0eA
- active site: Y163 (= Y151), K233 (= K218), D286 (= D272), D310 (= D296)
- 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 (= P93), L106 (= L94), T108 (= T96), S116 (= S104), N118 (= N106), R122 (= R110), R132 (= R120), R156 (= R144), N235 (= N220), I284 (= I270), Q291 (= Q277), R295 (= R281), D310 (= D296), I323 (≠ L309), E339 (= E325), H342 (= H328), G343 (= G329), T344 (= T330), A345 (= A331), K347 (= K333), Y348 (= Y334), V354 (= V340), N355 (= N341), Y394 (= Y380), D395 (= D381)
- binding glycine: S23 (= S13), L24 (= L14), H25 (≠ N15)
2iv0A Thermal stability of isocitrate dehydrogenase from archaeoglobus fulgidus studied by crystal structure analysis and engineering of chimers (see paper)
61% identity, 98% coverage: 11:405/405 of query aligns to 19:409/412 of 2iv0A
2d4vA Crystal structure of NAD dependent isocitrate dehydrogenase from acidithiobacillus thiooxidans (see paper)
58% identity, 97% coverage: 11:402/405 of query aligns to 16:424/427 of 2d4vA
- active site: Y158 (= Y151), K228 (= K218), D294 (= D272), D318 (= D296), D322 (= D300)
- binding citrate anion: T103 (= T96), S111 (= S104), N113 (= N106), R117 (= R110), R127 (= R120), R151 (= R144), Y158 (= Y151), K228 (= K218), I231 (= I221), D318 (= D296)
- binding nicotinamide-adenine-dinucleotide: I35 (= I30), P100 (= P93), L101 (= L94), E102 (≠ T95), T103 (= T96), N113 (= N106), N230 (= N220), I292 (= I270), N295 (≠ A273), I331 (≠ L309), E347 (= E325), T349 (= T327), H350 (= H328), G351 (= G329), T352 (= T330), A353 (= A331), D355 (≠ K333), A362 (≠ V340), N363 (= N341), D403 (= D381)
1tyoA Isocitrate dehydrogenase from the hyperthermophile aeropyrum pernix in complex with etheno-NADP (see paper)
51% identity, 98% coverage: 10:405/405 of query aligns to 21:416/427 of 1tyoA
1xkdA Ternary complex of isocitrate dehydrogenase from the hyperthermophile aeropyrum pernix (see paper)
50% identity, 97% coverage: 10:403/405 of query aligns to 22:411/427 of 1xkdA
- active site: Y158 (= Y151), K225 (= K218), D279 (= D272), D303 (= D296), D307 (= D300)
- binding calcium ion: D303 (= D296), D307 (= D300)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P105 (= P93), L106 (= L94), T108 (= T96), N114 (= N106), I277 (= I270), N280 (≠ A273), Q283 (= Q276), Q284 (= Q277), R288 (= R281), G317 (= G310), E332 (= E325), H335 (= H328), G336 (= G329), T337 (= T330), A338 (= A331), Y341 (= Y334), I347 (≠ V340), N348 (= N341), D389 (= D381), R392 (= R384)
2e5mA Crystal structure of isocitrate dehydrogenase from sulfolobus tokodaii strain 7 (see paper)
49% identity, 97% coverage: 12:402/405 of query aligns to 17:397/403 of 2e5mA
- active site: Y150 (= Y151), K217 (= K218), D268 (= D272), D292 (= D296), D296 (= D300)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L99 (= L94), T101 (= T96), N105 (= N106), E321 (= E325), H324 (= H328), G325 (= G329), K329 (= K333), Y330 (= Y334), N337 (= N341)
Query Sequence
>WP_028585044.1 NCBI__GCF_000429965.1:WP_028585044.1
MAGDIITINTDGSLNVTDTPTIPYIEGDGIGPDIWAAARNVVDAAIKKTYTGQKKINWLE
IFAGEKALDTTGEWLPQETLDALKKYVVGIKGPLTTPVGEGMRSLNVTLRQVLDLYACVR
PVRYYQGVVSPVKEPGDVDMVIFRENTEDVYAGIEWQAGTDQANKVIEFLRNEMGADIRD
NSGIGIKPISEFGTKRLVRKAIQYAIDHQRDSVTLVHKGNIMKFTEGAFRNWGYELAAEE
FADITISEDDLWKHHNGELPPGKILIKDRIADAMFQQILLRPREYSVLAMPNLNGDYMSD
ALAAQVGGLGIAPGANIGDGVALFEATHGTAPKYAGLDKVNPGSVLLSAVMMLEYLGWQE
AADAIKTALETTIGDKTVTYDLARLMDGATELSCSAFGEAIIANL
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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