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Comparing WP_012411727.1 NCBI__GCF_000020025.1:WP_012411727.1 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)
4aj3A 3d structure of e. Coli isocitrate dehydrogenase in complex with isocitrate, calcium(ii) and NADP - the pseudo-michaelis complex (see paper)
52% identity, 100% coverage: 1:472/473 of query aligns to 1:416/416 of 4aj3A
- active site: Y160 (= Y160), K230 (= K237), D283 (= D338), D307 (= D362), D311 (= D366)
- binding calcium ion: D307 (= D362), D311 (= D366)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P102 (= P102), L103 (= L103), T105 (= T105), N115 (= N115), I320 (≠ L375), E336 (= E391), H339 (= H394), G340 (= G395), T341 (= T396), A342 (= A397), Y345 (≠ H400), V351 (≠ I406), N352 (= N407), Y391 (= Y446), D392 (= D447)
P08200 Isocitrate dehydrogenase [NADP]; IDH; IDP; NADP(+)-specific ICDH; Oxalosuccinate decarboxylase; EC 1.1.1.42 from Escherichia coli (strain K12) (see 9 papers)
52% identity, 100% coverage: 1:472/473 of query aligns to 1:416/416 of P08200
- K100 (= K100) modified: N6-succinyllysine; mutation K->R,E: Abolishes enzymatic activity.
- T104 (= T104) binding NADP(+)
- S113 (= S113) 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 (= N115) binding substrate
- R119 (= R119) binding substrate
- R129 (= R129) binding substrate
- K142 (= K142) modified: N6-acetyllysine
- R153 (= R153) binding substrate
- Y160 (= Y160) Critical for catalysis; mutation to F: Nearly abolishes enzyme activity. No significant effect on substrate affinity.
- K230 (= K237) Critical for catalysis; mutation to M: Nearly abolishes enzyme activity and strongly reduces substrate affinity.
- K242 (≠ R249) modified: N6-succinyllysine; mutation to E: Strongly impairs enzymatic activity.; mutation to R: Impairs enzymatic activity.
- D307 (= D362) binding Mg(2+)
- 339:345 (vs. 394:400, 86% identical) binding NADP(+)
- N352 (= N407) binding NADP(+)
- Y391 (= Y446) binding NADP(+)
- R395 (= R450) binding NADP(+)
4ajaA 3d structure of e. Coli isocitrate dehydrogenase in complex with isocitrate, calcium(ii) and thionadp (see paper)
52% identity, 99% coverage: 4:472/473 of query aligns to 3:415/415 of 4ajaA
- active site: Y159 (= Y160), K229 (= K237), D282 (= D338), D306 (= D362), D310 (= D366)
- binding calcium ion: D306 (= D362), D310 (= D366)
- binding 7-thionicotinamide-adenine-dinucleotide phosphate: T103 (= T104), T104 (= T105), H338 (= H394), G339 (= G395), T340 (= T396), A341 (= A397), Y344 (≠ H400), N351 (= N407), Y390 (= Y446), D391 (= D447), R394 (= R450)
1bl5A Isocitrate dehydrogenase from e. Coli single turnover laue structure of rate-limited product complex, 10 msec time resolution (see paper)
52% identity, 99% coverage: 4:472/473 of query aligns to 2:414/414 of 1bl5A
- active site: Y158 (= Y160), K228 (= K237), D281 (= D338), D305 (= D362), D309 (= D366)
- binding 2-oxoglutaric acid: S111 (= S113), N113 (= N115), R117 (= R119), R127 (= R129)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: H337 (= H394), G338 (= G395), A340 (= A397), Y343 (≠ H400), N350 (= N407), Y389 (= Y446)
1ai3A Orbital steering in the catalytic power of enzymes: small structural changes with large catalytic consequences (see paper)
52% identity, 99% coverage: 4:472/473 of query aligns to 2:414/414 of 1ai3A
- active site: Y158 (= Y160), K228 (= K237), D281 (= D338), D305 (= D362), D309 (= D366)
- binding nicotinamide-(6-deamino-6-hydroxy-adenine)-dinucleotide phosphate: I35 (≠ T37), G99 (= G101), P100 (= P102), L101 (= L103), T102 (= T104), A335 (= A392), T336 (= T393), H337 (= H394), G338 (= G395), T339 (= T396), P341 (= P398), V349 (≠ I406), N350 (= N407), Y389 (= Y446), D390 (= D447), R393 (= R450)
1ai2A Isocitrate dehydrogenase complexed with isocitrate, NADP+, and calcium (flash-cooled) (see paper)
52% identity, 99% coverage: 4:472/473 of query aligns to 2:414/414 of 1ai2A
- active site: Y158 (= Y160), K228 (= K237), D281 (= D338), D305 (= D362), D309 (= D366)
- binding isocitrate calcium complex: S111 (= S113), N113 (= N115), R117 (= R119), R127 (= R129), Y158 (= Y160), D305 (= D362), D309 (= D366)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I35 (≠ T37), L101 (= L103), T102 (= T104), T336 (= T393), H337 (= H394), G338 (= G395), T339 (= T396), A340 (= A397), P341 (= P398), Y343 (≠ H400), V349 (≠ I406), N350 (= N407), Y389 (= Y446), D390 (= D447), R393 (= R450)
1hj6A Isocitrate dehydrogenase s113e mutant complexed with isopropylmalate, NADP+ and magnesium (flash-cooled) (see paper)
52% identity, 99% coverage: 4:472/473 of query aligns to 2:414/414 of 1hj6A
- active site: Y158 (= Y160), K228 (= K237), D281 (= D338), D305 (= D362), D309 (= D366)
- binding 3-isopropylmalic acid: E111 (≠ S113), R117 (= R119), R127 (= R129), R151 (= R153), Y158 (= Y160), D305 (= D362)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P100 (= P102), L101 (= L103), T102 (= T104), N113 (= N115), I318 (≠ L375), G319 (= G376), H337 (= H394), G338 (= G395), T339 (= T396), A340 (= A397), Y343 (≠ H400), V349 (≠ I406), N350 (= N407), Y389 (= Y446), D390 (= D447)
1idcA Isocitrate dehydrogenase from e.Coli (mutant k230m), steady-state intermediate complex determined by laue crystallography (see paper)
52% identity, 99% coverage: 4:472/473 of query aligns to 2:414/414 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)
52% identity, 99% coverage: 4:472/473 of query aligns to 3:415/415 of 4ajcA
- active site: Y159 (= Y160), K229 (= K237), D282 (= D338), D306 (= D362), D310 (= D366)
- binding adenosine-2'-5'-diphosphate: H338 (= H394), G339 (= G395), A341 (= A397), Y344 (≠ H400), V350 (≠ I406), N351 (= N407), Y390 (= Y446), D391 (= D447)
- binding 2-oxoglutaric acid: S112 (= S113), R118 (= R119), R152 (= R153), Y159 (= Y160)
- binding calcium ion: D306 (= D362), D310 (= D366)
1cw4A Crystal structure of k230m isocitrate dehydrogenase in complex with alpha-ketoglutarate (see paper)
52% identity, 99% coverage: 4:472/473 of query aligns to 3:415/415 of 1cw4A
- active site: Y159 (= Y160), M229 (≠ K237), D282 (= D338), D306 (= D362), D310 (= D366)
- binding 2-oxoglutaric acid: S112 (= S113), N114 (= N115), R118 (= R119), R152 (= R153), Y159 (= Y160), D306 (= D362)
- binding manganese (ii) ion: D306 (= D362), D310 (= D366)
- binding sulfate ion: V106 (= V107), G107 (= G108), G109 (= G110)
1cw1A Crystal structure of isocitrate dehydrogenase mutant k230m bound to isocitrate and mn2+ (see paper)
52% identity, 99% coverage: 4:472/473 of query aligns to 3:415/415 of 1cw1A
1groA Regulatory and catalytic mechanisms in escherichia coli isocitrate dehydrogenase: multiple roles for n115 (see paper)
52% identity, 99% coverage: 4:472/473 of query aligns to 2:414/414 of 1groA
1isoA Isocitrate dehydrogenase: structure of an engineered NADP+--> NAD+ specificity-reversal mutant (see paper)
52% identity, 99% coverage: 4:472/473 of query aligns to 2:414/414 of 1isoA
- active site: Y158 (= Y160), K228 (= K237), D281 (= D338), D305 (= D362), D309 (= D366)
- binding nicotinamide-adenine-dinucleotide: I35 (≠ T37), H337 (= H394), G338 (= G395), A340 (= A397), D342 (≠ K399), A349 (≠ I406), N350 (= N407)
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)
51% identity, 99% coverage: 2:469/473 of query aligns to 3:415/418 of Q02NB5
- S115 (= S113) modified: Phosphoserine
- T193 (vs. gap) modified: Phosphothreonine
2d4vA Crystal structure of NAD dependent isocitrate dehydrogenase from acidithiobacillus thiooxidans (see paper)
51% identity, 99% coverage: 5:472/473 of query aligns to 3:427/427 of 2d4vA
- active site: Y158 (= Y160), K228 (= K237), D294 (= D338), D318 (= D362), D322 (= D366)
- binding citrate anion: T103 (= T105), S111 (= S113), N113 (= N115), R117 (= R119), R127 (= R129), R151 (= R153), Y158 (= Y160), K228 (= K237), I231 (= I240), D318 (= D362)
- binding nicotinamide-adenine-dinucleotide: I35 (≠ T37), P100 (= P102), L101 (= L103), E102 (≠ T104), T103 (= T105), N113 (= N115), N230 (= N239), I292 (= I336), N295 (≠ S339), I331 (≠ L375), E347 (= E391), T349 (= T393), H350 (= H394), G351 (= G395), T352 (= T396), A353 (= A397), D355 (≠ K399), A362 (≠ I406), N363 (= N407), D403 (= D447)
2iv0A Thermal stability of isocitrate dehydrogenase from archaeoglobus fulgidus studied by crystal structure analysis and engineering of chimers (see paper)
49% identity, 100% coverage: 2:472/473 of query aligns to 3:409/412 of 2iv0A
6c0eA Crystal structure of isocitrate dehydrogenase from legionella pneumophila with bound NADPH with an alpha-ketoglutarate adduct
47% identity, 100% coverage: 2:472/473 of query aligns to 4:419/419 of 6c0eA
- active site: Y163 (= Y160), K233 (= K237), D286 (= D338), D310 (= D362)
- 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 (= P102), L106 (= L103), T108 (= T105), S116 (= S113), N118 (= N115), R122 (= R119), R132 (= R129), R156 (= R153), N235 (= N239), I284 (= I336), Q291 (= Q343), R295 (= R347), D310 (= D362), I323 (≠ L375), E339 (= E391), H342 (= H394), G343 (= G395), T344 (= T396), A345 (= A397), K347 (= K399), Y348 (≠ H400), V354 (≠ I406), N355 (= N407), Y394 (= Y446), D395 (= D447)
- binding glycine: S23 (≠ P21), L24 (≠ I22), H25 (vs. gap)
1tyoA Isocitrate dehydrogenase from the hyperthermophile aeropyrum pernix in complex with etheno-NADP (see paper)
43% identity, 99% coverage: 3:472/473 of query aligns to 7:416/427 of 1tyoA
1xkdA Ternary complex of isocitrate dehydrogenase from the hyperthermophile aeropyrum pernix (see paper)
42% identity, 99% coverage: 3:472/473 of query aligns to 8:413/427 of 1xkdA
- active site: Y158 (= Y160), K225 (= K237), D279 (= D338), D303 (= D362), D307 (= D366)
- binding calcium ion: D303 (= D362), D307 (= D366)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P105 (= P102), L106 (= L103), T108 (= T105), N114 (= N115), I277 (= I336), N280 (≠ S339), Q283 (= Q342), Q284 (= Q343), R288 (= R347), G317 (= G376), E332 (= E391), H335 (= H394), G336 (= G395), T337 (= T396), A338 (= A397), Y341 (≠ H400), I347 (= I406), N348 (= N407), D389 (= D447), R392 (= R450)
2e5mA Crystal structure of isocitrate dehydrogenase from sulfolobus tokodaii strain 7 (see paper)
42% identity, 98% coverage: 8:470/473 of query aligns to 6:398/403 of 2e5mA
- active site: Y150 (= Y160), K217 (= K237), D268 (= D338), D292 (= D362), D296 (= D366)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L99 (= L103), T101 (= T105), N105 (= N115), E321 (= E391), H324 (= H394), G325 (= G395), K329 (= K399), Y330 (≠ H400), N337 (= N407)
Query Sequence
>WP_012411727.1 NCBI__GCF_000020025.1:WP_012411727.1
MYEKITPPAAGAKIAFKNGEPIVPDNPIIPFIRGDGTGIDIWPATQKVLDAAVAKAYKGQ
RQISWFKVYAGDEACDLYGTYQYLPQDTLTAIEEYGVAIKGPLTTPVGGGIRSLNVALRQ
IFDLYACVRPCRYYAGTPSPHKNPEKLDVIVYRENTEDIYLGIEWRQGSEIGDRLIKILN
EELIPATPEHGKKRIPLDSGIGIKPISKTGSQRLVRRAIKHALLLPKNKQQVTLVHKGNI
MKYTEGAFRDWGYELATSEFRQETVTEQESWILSNKEKNPNISLEENARQIEPGFDNLTP
DKKAQVVKEVETVLNTIWATHGDGKWKEKVLVNDRIADSIFQQIQTRPDEYSILATMNLN
GDYLSDAAAAIVGGLGMGPGANIGDSSAIFEATHGTAPKHAGLDRINPGSVILSGVMMLE
FLGWQEAADLIKKGLSDAIANSQVTYDLARLLEPPVEPLKCSEFADAIIQHFG
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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