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Comparing WP_012674929.1 NCBI__GCF_000021545.1:WP_012674929.1 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)
1isoA Isocitrate dehydrogenase: structure of an engineered NADP+--> NAD+ specificity-reversal mutant (see paper)
48% identity, 97% coverage: 10:416/421 of query aligns to 2:412/414 of 1isoA
- active site: Y158 (= Y164), K228 (= K234), D281 (= D281), D305 (= D305), D309 (= D309)
- binding nicotinamide-adenine-dinucleotide: I35 (= I44), H337 (= H337), G338 (= G338), A340 (= A340), D342 (= D342), A349 (= A349), N350 (= N350)
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)
47% identity, 96% coverage: 10:415/421 of query aligns to 5:415/418 of Q02NB5
- S115 (= S118) modified: Phosphoserine
- T193 (≠ P195) modified: Phosphothreonine
6c0eA Crystal structure of isocitrate dehydrogenase from legionella pneumophila with bound NADPH with an alpha-ketoglutarate adduct
47% identity, 97% coverage: 10:416/421 of query aligns to 6:417/419 of 6c0eA
- active site: Y163 (= Y164), K233 (= K234), D286 (= D281), D310 (= D305)
- 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 (= R157), N235 (= N236), I284 (= I279), Q291 (= Q286), R295 (≠ K290), D310 (= D305), I323 (≠ P318), E339 (= E334), H342 (= H337), G343 (= G338), T344 (= T339), A345 (= A340), K347 (≠ D342), Y348 (≠ I343), V354 (≠ A349), N355 (= N350), Y394 (≠ P389), D395 (= D390)
- binding glycine: S23 (≠ T27), L24 (≠ I28), H25 (≠ T29)
4aj3A 3d structure of e. Coli isocitrate dehydrogenase in complex with isocitrate, calcium(ii) and NADP - the pseudo-michaelis complex (see paper)
47% identity, 97% coverage: 8:416/421 of query aligns to 2:414/416 of 4aj3A
- active site: Y160 (= Y164), K230 (= K234), D283 (= D281), D307 (= D305), D311 (= D309)
- binding calcium ion: D307 (= D305), D311 (= D309)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P102 (= P107), L103 (= L108), T105 (= T110), N115 (= N120), I320 (≠ P318), E336 (= E334), H339 (= H337), G340 (= G338), T341 (= T339), A342 (= A340), Y345 (≠ I343), V351 (≠ A349), N352 (= N350), Y391 (≠ P389), D392 (= D390)
1bl5A Isocitrate dehydrogenase from e. Coli single turnover laue structure of rate-limited product complex, 10 msec time resolution (see paper)
47% identity, 97% coverage: 10:416/421 of query aligns to 2:412/414 of 1bl5A
- active site: Y158 (= Y164), K228 (= K234), D281 (= D281), D305 (= D305), D309 (= D309)
- binding 2-oxoglutaric acid: S111 (= S118), N113 (= N120), R117 (= R124), R127 (= R134)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: H337 (= H337), G338 (= G338), A340 (= A340), Y343 (≠ I343), N350 (= N350), Y389 (≠ P389)
1ai3A Orbital steering in the catalytic power of enzymes: small structural changes with large catalytic consequences (see paper)
47% identity, 97% coverage: 10:416/421 of query aligns to 2:412/414 of 1ai3A
- active site: Y158 (= Y164), K228 (= K234), D281 (= D281), D305 (= D305), D309 (= D309)
- binding nicotinamide-(6-deamino-6-hydroxy-adenine)-dinucleotide phosphate: I35 (= I44), G99 (= G106), P100 (= P107), L101 (= L108), T102 (≠ G109), A335 (≠ S335), T336 (= T336), H337 (= H337), G338 (= G338), T339 (= T339), P341 (≠ N341), V349 (≠ A349), N350 (= N350), Y389 (≠ P389), D390 (= D390), R393 (≠ K397)
1ai2A Isocitrate dehydrogenase complexed with isocitrate, NADP+, and calcium (flash-cooled) (see paper)
47% identity, 97% coverage: 10:416/421 of query aligns to 2:412/414 of 1ai2A
- active site: Y158 (= Y164), K228 (= K234), D281 (= D281), D305 (= D305), D309 (= D309)
- binding isocitrate calcium complex: S111 (= S118), N113 (= N120), R117 (= R124), R127 (= R134), Y158 (= Y164), D305 (= D305), D309 (= D309)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I35 (= I44), L101 (= L108), T102 (≠ G109), T336 (= T336), H337 (= H337), G338 (= G338), T339 (= T339), A340 (= A340), P341 (≠ N341), Y343 (≠ I343), V349 (≠ A349), N350 (= N350), Y389 (≠ P389), D390 (= D390), R393 (≠ K397)
P08200 Isocitrate dehydrogenase [NADP]; IDH; IDP; NADP(+)-specific ICDH; Oxalosuccinate decarboxylase; EC 1.1.1.42 from Escherichia coli (strain K12) (see 9 papers)
47% identity, 97% coverage: 8:416/421 of query aligns to 2:414/416 of P08200
- K100 (= K105) modified: N6-succinyllysine; mutation K->R,E: Abolishes enzymatic activity.
- T104 (≠ G109) 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 (≠ P146) modified: N6-acetyllysine
- R153 (= R157) binding substrate
- Y160 (= Y164) Critical for catalysis; mutation to F: Nearly abolishes enzyme activity. No significant effect on substrate affinity.
- K230 (= K234) Critical for catalysis; mutation to M: Nearly abolishes enzyme activity and strongly reduces substrate affinity.
- K242 (≠ I246) modified: N6-succinyllysine; mutation to E: Strongly impairs enzymatic activity.; mutation to R: Impairs enzymatic activity.
- D307 (= D305) binding Mg(2+)
- 339:345 (vs. 337:343, 57% identical) binding NADP(+)
- N352 (= N350) binding NADP(+)
- Y391 (≠ P389) binding NADP(+)
- R395 (≠ K397) binding NADP(+)
4ajaA 3d structure of e. Coli isocitrate dehydrogenase in complex with isocitrate, calcium(ii) and thionadp (see paper)
47% identity, 97% coverage: 8:416/421 of query aligns to 1:413/415 of 4ajaA
- active site: Y159 (= Y164), K229 (= K234), D282 (= D281), D306 (= D305), D310 (= D309)
- binding calcium ion: D306 (= D305), D310 (= D309)
- binding 7-thionicotinamide-adenine-dinucleotide phosphate: T103 (≠ G109), T104 (= T110), H338 (= H337), G339 (= G338), T340 (= T339), A341 (= A340), Y344 (≠ I343), N351 (= N350), Y390 (≠ P389), D391 (= D390), R394 (≠ K397)
1hj6A Isocitrate dehydrogenase s113e mutant complexed with isopropylmalate, NADP+ and magnesium (flash-cooled) (see paper)
47% identity, 97% coverage: 10:416/421 of query aligns to 2:412/414 of 1hj6A
- active site: Y158 (= Y164), K228 (= K234), D281 (= D281), D305 (= D305), D309 (= D309)
- binding 3-isopropylmalic acid: E111 (≠ S118), R117 (= R124), R127 (= R134), R151 (= R157), Y158 (= Y164), D305 (= D305)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P100 (= P107), L101 (= L108), T102 (≠ G109), N113 (= N120), I318 (≠ P318), G319 (= G319), H337 (= H337), G338 (= G338), T339 (= T339), A340 (= A340), Y343 (≠ I343), V349 (≠ A349), N350 (= N350), Y389 (≠ P389), D390 (= D390)
4ajcA 3d structure of e. Coli isocitrate dehydrogenase k100m mutant in complex with alpha-ketoglutarate, calcium(ii) and adenine nucleotide phosphate (see paper)
47% identity, 97% coverage: 8:416/421 of query aligns to 1:413/415 of 4ajcA
- active site: Y159 (= Y164), K229 (= K234), D282 (= D281), D306 (= D305), D310 (= D309)
- binding adenosine-2'-5'-diphosphate: H338 (= H337), G339 (= G338), A341 (= A340), Y344 (≠ I343), V350 (≠ A349), N351 (= N350), Y390 (≠ P389), D391 (= D390)
- binding 2-oxoglutaric acid: S112 (= S118), R118 (= R124), R152 (= R157), Y159 (= Y164)
- binding calcium ion: D306 (= D305), D310 (= D309)
1cw4A Crystal structure of k230m isocitrate dehydrogenase in complex with alpha-ketoglutarate (see paper)
47% identity, 97% coverage: 8:416/421 of query aligns to 1:413/415 of 1cw4A
- active site: Y159 (= Y164), M229 (≠ K234), D282 (= D281), D306 (= D305), D310 (= D309)
- binding 2-oxoglutaric acid: S112 (= S118), N114 (= N120), R118 (= R124), R152 (= R157), Y159 (= Y164), D306 (= D305)
- binding manganese (ii) ion: D306 (= D305), D310 (= D309)
- binding sulfate ion: V106 (= V112), G107 (= G113), G109 (= G115)
1cw1A Crystal structure of isocitrate dehydrogenase mutant k230m bound to isocitrate and mn2+ (see paper)
47% identity, 97% coverage: 8:416/421 of query aligns to 1:413/415 of 1cw1A
1idcA Isocitrate dehydrogenase from e.Coli (mutant k230m), steady-state intermediate complex determined by laue crystallography (see paper)
47% identity, 97% coverage: 10:416/421 of query aligns to 2:412/414 of 1idcA
1groA Regulatory and catalytic mechanisms in escherichia coli isocitrate dehydrogenase: multiple roles for n115 (see paper)
46% identity, 97% coverage: 10:416/421 of query aligns to 2:412/414 of 1groA
2iv0A Thermal stability of isocitrate dehydrogenase from archaeoglobus fulgidus studied by crystal structure analysis and engineering of chimers (see paper)
46% identity, 98% coverage: 10:420/421 of query aligns to 5:411/412 of 2iv0A
2d4vA Crystal structure of NAD dependent isocitrate dehydrogenase from acidithiobacillus thiooxidans (see paper)
43% identity, 97% coverage: 10:416/421 of query aligns to 2:425/427 of 2d4vA
- active site: Y158 (= Y164), K228 (= K234), D294 (= D281), D318 (= D305), D322 (= D309)
- binding citrate anion: T103 (= T110), S111 (= S118), N113 (= N120), R117 (= R124), R127 (= R134), R151 (= R157), Y158 (= Y164), K228 (= K234), I231 (= I237), D318 (= D305)
- binding nicotinamide-adenine-dinucleotide: I35 (= I44), P100 (= P107), L101 (= L108), E102 (≠ G109), T103 (= T110), N113 (= N120), N230 (= N236), I292 (= I279), N295 (≠ Q282), I331 (≠ P318), E347 (= E334), T349 (= T336), H350 (= H337), G351 (= G338), T352 (= T339), A353 (= A340), D355 (= D342), A362 (= A349), N363 (= N350), D403 (= D390)
2e5mA Crystal structure of isocitrate dehydrogenase from sulfolobus tokodaii strain 7 (see paper)
45% identity, 96% coverage: 14:416/421 of query aligns to 6:398/403 of 2e5mA
- active site: Y150 (= Y164), K217 (= K234), D268 (= D281), D292 (= D305), D296 (= D309)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L99 (= L108), T101 (= T110), N105 (= N120), E321 (= E334), H324 (= H337), G325 (= G338), K329 (≠ D342), Y330 (≠ I343), N337 (= N350)
1tyoA Isocitrate dehydrogenase from the hyperthermophile aeropyrum pernix in complex with etheno-NADP (see paper)
43% identity, 90% coverage: 14:393/421 of query aligns to 12:395/427 of 1tyoA
1xkdA Ternary complex of isocitrate dehydrogenase from the hyperthermophile aeropyrum pernix (see paper)
43% identity, 90% coverage: 14:393/421 of query aligns to 13:392/427 of 1xkdA
- active site: Y158 (= Y164), K225 (= K234), D279 (= D281), D303 (= D305), D307 (= D309)
- binding calcium ion: D303 (= D305), D307 (= D309)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P105 (= P107), L106 (= L108), T108 (= T110), N114 (= N120), I277 (= I279), N280 (≠ Q282), Q283 (≠ M285), Q284 (= Q286), R288 (≠ K290), G317 (= G319), E332 (= E334), H335 (= H337), G336 (= G338), T337 (= T339), A338 (= A340), Y341 (≠ I343), I347 (≠ A349), N348 (= N350), D389 (= D390), R392 (≠ N393)
Query Sequence
>WP_012674929.1 NCBI__GCF_000021545.1:WP_012674929.1
MENIFWWKGKVEIPSEGSFIKLNPDKTITVPDNPIIPFIMGDGIGFEITPEMIKVVNAAV
EKVYGNSKKIYWLEVLAGDKAEENGLNRMPQETLDLLKQSIVSIKGPLGTPVGKGGKSLN
AILRQSMDFYSAIRPVFYMGQPSPIPNPERVNVTVFRENSDDVYMAIEYMPKTEEVKKVK
EFFINQMGVSEYALPEDVGITVKPMSEYKTKRHVRKAFRYALENGKKHIAVVGKGNIMKA
TEGAFINWAFEVAQEDEFKGKIITEGEPQEGQAKIYKVITDQMLMQLVLKPEYYDVIITQ
NLNGDYISDLASALVGGPGFVPSGNIGDGYALFESTHGTANDIAGKGIANPLSIILSGAM
MLEYLGWKDASNVIYKAVKQVISEGKGTPDIANGFRKLGKQAVELSTQAFGDEIVKAIKN
N
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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