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Comparing Ac3H11_635 FitnessBrowser__acidovorax_3H11:Ac3H11_635 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)
3flkA Crystal structure of tartrate dehydrogenase from pseudomonas putida in complex with nadh, oxalate and metal ion (see paper)
49% identity, 96% coverage: 3:349/363 of query aligns to 1:352/359 of 3flkA
- active site: Y137 (= Y138), K188 (= K189), D221 (= D222), D245 (= D246), D249 (= D250)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I12 (= I14), A73 (≠ S75), V74 (≠ A76), G75 (= G77), D82 (= D83), L90 (≠ R91), N190 (= N191), I222 (≠ A223), R226 (= R227), I258 (≠ L259), H280 (= H281), G281 (= G282), S282 (= S283), A283 (= A284), I286 (= I287), N293 (= N294)
- binding oxalate ion: R94 (≠ C95), R104 (= R105), R130 (= R131), D245 (= D246)
2g4oA Anomalous substructure of 3-isopropylmalate dehydrogenase (see paper)
42% identity, 92% coverage: 5:337/363 of query aligns to 3:330/337 of 2g4oA
4yb4A Crystal structure of homoisocitrate dehydrogenase from thermus thermophilus in complex with homoisocitrate, magnesium ion (ii) and nadh
39% identity, 97% coverage: 4:355/363 of query aligns to 2:332/333 of 4yb4A
- active site: Y124 (= Y138), K170 (= K189), D203 (= D222), D227 (= D246), D231 (= D250)
- binding (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylic acid: S71 (≠ D78), R84 (≠ L92), R87 (≠ C95), R97 (= R105), R117 (= R131), Y124 (= Y138), D227 (= D246)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I12 (= I14), A69 (= A76), T70 (≠ G77), S71 (≠ D78), I201 (≠ L220), N204 (≠ A223), L240 (= L259), E256 (= E278), H259 (= H281), G260 (= G282), S261 (= S283), A262 (= A284), D264 (= D286), I265 (= I287), N272 (= N294), D312 (= D335)
3asjB Crystal structure of homoisocitrate dehydrogenase in complex with a designed inhibitor (see paper)
39% identity, 97% coverage: 4:355/363 of query aligns to 2:332/333 of 3asjB
- active site: Y124 (= Y138), K170 (= K189), D203 (= D222), D227 (= D246), D231 (= D250)
- binding (2Z)-3-[(carboxymethyl)sulfanyl]-2-hydroxyprop-2-enoic acid: R84 (≠ L92), R97 (= R105), R117 (= R131), Y124 (= Y138), D227 (= D246), D231 (= D250), V258 (≠ I280)
3asjA Crystal structure of homoisocitrate dehydrogenase in complex with a designed inhibitor (see paper)
39% identity, 97% coverage: 4:355/363 of query aligns to 2:332/333 of 3asjA
Q72IW9 Isocitrate/homoisocitrate dehydrogenase; Homoisocitrate dehydrogenase; HICDH; EC 1.1.1.286 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see 4 papers)
39% identity, 97% coverage: 4:355/363 of query aligns to 3:333/334 of Q72IW9
- E57 (≠ D63) mutation to V: Confers enzyme activity with 3-isopropylmalate; when associated with I-72; M-85; A-86; T-208; Y-217; M-238 and M-310.
- ATS 70:72 (≠ AGD 76:78) binding
- S72 (≠ D78) binding in other chain; mutation to I: Confers enzyme activity with 3-isopropylmalate; when associated with V-57; M-85; A-86; T-208; Y-217; M-238 and M-310.
- R85 (≠ L92) binding in other chain; mutation to M: Confers enzyme activity with 3-isopropylmalate; when associated with V-57; I-72; A-86; T-208; Y-217; M-238 and M-310.; mutation to V: Confers low enzyme activity with 3-isopropylmalate. Reduces activity with homoisocitrate. Abolishes activity with isocitrate.
- Y86 (≠ K93) mutation to A: Confers enzyme activity with 3-isopropylmalate; when associated with V-57; I-72; M-85; T-208; Y-217; M-238 and M-310.
- R88 (≠ C95) binding in other chain
- R98 (= R105) binding in other chain
- R118 (= R131) binding in other chain
- Y125 (= Y138) binding in other chain; mutation to A: Reduces catalytic efficiency with isocitrate.
- V135 (≠ A153) mutation to M: Formation of homodimers instead of homotetramers. Increased affinity for isocitrate. Reduces enzyme activity with isocitrate.
- K171 (= K189) binding
- N173 (= N191) binding ; binding
- D204 (= D222) binding
- M208 (≠ A226) mutation to T: Confers enzyme activity with 3-isopropylmalate; when associated with V-57; I-72; M-85; A-86; T-208; Y-217; M-238 and M-310.
- F217 (≠ L235) mutation to Y: Confers enzyme activity with 3-isopropylmalate; when associated with V-57; I-72; M-85; A-86; T-208; M-238 and M-310.
- D228 (= D246) binding
- D232 (= D250) binding
- V238 (≠ A256) mutation to M: Confers enzyme activity with 3-isopropylmalate; when associated with V-57; I-72; M-85; A-86; T-208; Y-217; and M-310.
- GSAPD 261:265 (≠ GSAFD 282:286) binding
- N273 (= N294) binding
- R310 (≠ H332) mutation to M: Confers enzyme activity with 3-isopropylmalate; when associated with V-57; I-72; M-85; A-86; T-208; Y-217; and M-238.
6lkyA Crystal structure of isocitrate dehydrogenase from methylococcus capsulatus
36% identity, 95% coverage: 4:349/363 of query aligns to 2:333/339 of 6lkyA
- active site: Y123 (= Y138), K174 (= K189), D207 (= D222), D231 (= D246)
- binding nicotinamide-adenine-dinucleotide: P68 (≠ D78), L69 (≠ P79), T71 (≠ I81), N81 (≠ R91), H263 (= H281), G264 (= G282), S265 (= S283), A266 (= A284), D268 (= D286), I269 (= I287), N276 (= N294)
P40495 Homoisocitrate dehydrogenase, mitochondrial; HIcDH; EC 1.1.1.87 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
36% identity, 95% coverage: 6:351/363 of query aligns to 26:369/371 of P40495
- Y150 (= Y138) mutation to F: Strongly reduced enzyme activity.
- K206 (= K189) mutation to M: Strongly reduced enzyme activity.
3ty3A Crystal structure of homoisocitrate dehydrogenase from schizosaccharomyces pombe bound to glycyl-glycyl-glycine (see paper)
35% identity, 96% coverage: 6:353/363 of query aligns to 5:356/358 of 3ty3A
- active site: Y129 (= Y138), K192 (= K189), D228 (= D222), D252 (= D246), D256 (= D250)
- binding glycylglycylglycine: A74 (≠ S75), V75 (≠ A76), S77 (≠ D78), R93 (= R91), E281 (= E278), P282 (= P279), H284 (= H281)
O14104 Homoisocitrate dehydrogenase; HICDH; EC 1.1.1.87 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
35% identity, 96% coverage: 6:353/363 of query aligns to 9:360/362 of O14104
- S81 (≠ D78) modified: Phosphoserine
- S91 (≠ T86) modified: Phosphoserine
6kdyA Crystal structure of the alpha bata heterodimer of human idh3 in complex with NAD. (see paper)
33% identity, 95% coverage: 6:350/363 of query aligns to 5:330/335 of 6kdyA
- active site: Y124 (= Y138), K171 (= K189), D204 (= D222), D228 (= D246)
- binding nicotinamide-adenine-dinucleotide: P69 (≠ S75), L70 (≠ A76), T72 (≠ D78), N82 (≠ R91), H261 (= H281), G262 (= G282), T263 (≠ S283), A264 (= A284), D266 (= D286), I267 (= I287), N274 (= N294), D315 (= D335)
6kdeA Crystal structure of the alpha beta heterodimer of human idh3 in complex with ca(2+) (see paper)
33% identity, 95% coverage: 6:350/363 of query aligns to 5:330/336 of 6kdeA
2y42D Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with nadh and mn (see paper)
36% identity, 96% coverage: 3:350/363 of query aligns to 1:342/355 of 2y42D
- active site: Y140 (= Y138), K186 (= K189), D218 (= D222), D242 (= D246), D246 (= D250)
- binding manganese (ii) ion: D242 (= D246), D246 (= D250)
- binding nicotinamide-adenine-dinucleotide: I12 (= I14), D79 (vs. gap), H274 (= H281), G275 (= G282), A277 (= A284), D279 (= D286), I280 (= I287), N287 (= N294)
2y41A Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with ipm and mn (see paper)
36% identity, 96% coverage: 3:350/363 of query aligns to 1:342/346 of 2y41A
P50213 Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial; Isocitric dehydrogenase subunit alpha; NAD(+)-specific ICDH subunit alpha; EC 1.1.1.41 from Homo sapiens (Human) (see 5 papers)
33% identity, 95% coverage: 6:350/363 of query aligns to 34:359/366 of P50213
- R115 (≠ C95) binding
- A122 (= A102) to T: in RP90; uncertain significance; dbSNP:rs756333430
- R125 (= R105) binding
- R146 (= R131) binding
- E152 (= E137) mutation to A: No significant effect on the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP.
- Y153 (= Y138) Critical for catalysis; mutation to F: Complete loss of activity of the heterotetramer, heterodimer composed of IDH3A and IDH3B subunits and the heterodimer composed of IDH3A and IDH3G subunits with no effect on their oligomeric states.
- K169 (≠ S158) mutation to A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP.
- A175 (≠ G164) to V: in RP90; uncertain significance; dbSNP:rs765473830
- K200 (= K189) Critical for catalysis; mutation to A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate.
- N202 (= N191) mutation to A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate.
- M204 (≠ Q193) to I: in RP90; uncertain significance
- D208 (≠ M197) mutation to A: Complete loss of the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP.
- D233 (= D222) binding
- M239 (= M228) to T: in RP90; uncertain significance; dbSNP:rs2074707744
- Y255 (≠ H244) mutation to A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP.
- D257 (= D246) binding
- D261 (= D250) binding
- P304 (= P295) to H: in RP90; uncertain significance; dbSNP:rs756712426
- M313 (= M304) to T: in RP90; uncertain significance; dbSNP:rs149862950
- R316 (≠ E307) to C: in RP90; uncertain significance; dbSNP:rs770798851
5yvtA Crystal structure of the alpha gamma heterodimer of human idh3 in complex with mg(2+) and nadh (see paper)
33% identity, 95% coverage: 6:350/363 of query aligns to 4:327/332 of 5yvtA
- active site: Y121 (= Y138), K168 (= K189), D201 (= D222), D225 (= D246), D229 (= D250)
- binding magnesium ion: D225 (= D246), D229 (= D250)
- binding 1,4-dihydronicotinamide adenine dinucleotide: L69 (≠ A76), T71 (≠ D78), N79 (≠ R91), N170 (= N191), D201 (= D222), E255 (= E278), V257 (≠ I280), H258 (= H281), G259 (= G282), I264 (= I287), N271 (= N294), D312 (= D335)
2ztwA Structure of 3-isopropylmalate dehydrogenase in complex with the inhibitor and NAD+ (see paper)
36% identity, 95% coverage: 5:350/363 of query aligns to 2:341/345 of 2ztwA
- active site: Y139 (= Y138), K185 (= K189), D217 (= D222), D241 (= D246), D245 (= D250)
- binding magnesium ion: G203 (≠ A208), Y206 (≠ F211), V209 (= V214)
- binding nicotinamide-adenine-dinucleotide: I11 (= I14), H273 (= H281), G274 (= G282), A276 (= A284), D278 (= D286), I279 (= I287), A285 (= A293), N286 (= N294)
Q5SIY4 3-isopropylmalate dehydrogenase; 3-IPM-DH; Beta-IPM dehydrogenase; IMDH; EC 1.1.1.85 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see 2 papers)
36% identity, 95% coverage: 5:350/363 of query aligns to 2:341/345 of Q5SIY4
- 74:87 (vs. 78:88, 21% identical) binding
- Y139 (= Y138) mutation to F: Large decrease in activity and a small decrease in substrate affinity.
- 274:286 (vs. 282:294, 77% identical) binding
Q9D6R2 Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial; Isocitric dehydrogenase subunit alpha; NAD(+)-specific ICDH subunit alpha; EC 1.1.1.41 from Mus musculus (Mouse) (see paper)
33% identity, 95% coverage: 6:350/363 of query aligns to 34:359/366 of Q9D6R2
- E229 (≠ K218) mutation to K: Homozygous mutant mice exhibit retinal degeneration.
3vkzA 3-isopropylmalate dehydrogenase from shewanella oneidensis mr-1 at atmospheric pressure (see paper)
36% identity, 89% coverage: 2:324/363 of query aligns to 1:326/364 of 3vkzA
Query Sequence
>Ac3H11_635 FitnessBrowser__acidovorax_3H11:Ac3H11_635
MTTYQIATIPGDGIGKEVIPAGQRVLEALAARHPGLQFQFENFGWGGDWYRAHGVMMPAD
GLDALRGKDAILFGSAGDPDIPDHITLWGLRLKICQGFDQYANVRPTRILPGIDAPLKRC
TPKDLDWVIVRENSEGEYSGVGGRVHQGHPIEAATDVSIMTRVGVERILRFAFRLAQSRP
RKLLTVITKSNAQRHAMVMWDEIAAQVAAEFPDVKWDKELVDAATARMVNRPATLDTIVA
TNLHADILSDLAAALAGSLGIAPTGNIDPERRYPSMFEPIHGSAFDIMGKGLANPIGTFW
SVVMLLEHLGEMDAARAVMQAIEQVTANPALHTRDLGGTATTAQVTDAVCALIGSAPAAR
KAA
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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