SitesBLAST
Comparing 6938304 FitnessBrowser__SB2B:6938304 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)
6m3sB Dimeric isocitrate dehydrogenase from xanthomonas campestris pv. Campestris 8004
62% identity, 99% coverage: 4:335/336 of query aligns to 6:338/338 of 6m3sB
- active site: Y128 (= Y125), K177 (= K174), D210 (= D207), D234 (= D231)
- binding isocitrate calcium complex: T75 (= T73), S83 (= S81), N85 (= N83), R89 (= R87), R99 (= R97), R121 (= R118), Y128 (= Y125), D234 (= D231), D238 (= D235)
- binding nicotinamide-adenine-dinucleotide: P72 (= P70), L73 (= L71), T75 (= T73), N85 (= N83), H266 (= H263), G267 (= G264), S268 (= S265), A269 (= A266), D271 (= D268), I272 (= I269), N279 (= N276)
6lkyA Crystal structure of isocitrate dehydrogenase from methylococcus capsulatus
54% identity, 98% coverage: 6:335/336 of query aligns to 4:337/339 of 6lkyA
- active site: Y123 (= Y125), K174 (= K174), D207 (= D207), D231 (= D231)
- binding nicotinamide-adenine-dinucleotide: P68 (= P70), L69 (= L71), T71 (= T73), N81 (= N83), H263 (= H263), G264 (= G264), S265 (= S265), A266 (= A266), D268 (= D268), I269 (= I269), N276 (= N276)
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)
47% identity, 99% coverage: 4:335/336 of query aligns to 32:362/366 of Q9D6R2
- E229 (= E203) mutation to K: Homozygous mutant mice exhibit retinal degeneration.
6kdyA Crystal structure of the alpha bata heterodimer of human idh3 in complex with NAD. (see paper)
47% identity, 99% coverage: 4:335/336 of query aligns to 3:333/335 of 6kdyA
- active site: Y124 (= Y125), K171 (= K174), D204 (= D207), D228 (= D231)
- binding nicotinamide-adenine-dinucleotide: P69 (= P70), L70 (= L71), T72 (= T73), N82 (= N83), H261 (= H263), G262 (= G264), T263 (≠ S265), A264 (= A266), D266 (= D268), I267 (= I269), N274 (= N276), D315 (= D317)
6kdeA Crystal structure of the alpha beta heterodimer of human idh3 in complex with ca(2+) (see paper)
47% identity, 99% coverage: 4:335/336 of query aligns to 3:333/336 of 6kdeA
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)
47% identity, 99% coverage: 4:335/336 of query aligns to 32:362/366 of P50213
- R115 (= R87) binding
- A122 (= A94) to T: in RP90; unknown pathological significance; dbSNP:rs756333430
- R125 (= R97) binding
- R146 (= R118) binding
- E152 (≠ M124) mutation to A: No significant effect on the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP.
- Y153 (= Y125) 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 (≠ S143) mutation to A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP.
- A175 (≠ G149) to V: in RP90; unknown pathological significance; dbSNP:rs765473830
- K200 (= K174) Critical for catalysis; mutation to A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate.
- N202 (= N176) mutation to A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate.
- M204 (= M178) to I: in RP90; unknown pathological significance
- D208 (≠ S182) mutation to A: Complete loss of the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP.
- D233 (= D207) binding
- M239 (≠ L213) to T: in RP90; unknown pathological significance; dbSNP:rs2074707744
- Y255 (≠ F229) mutation to A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP.
- D257 (= D231) binding
- D261 (= D235) binding
- P304 (= P277) to H: in RP90; unknown pathological significance; dbSNP:rs756712426
- M313 (≠ Q286) to T: in RP90; unknown pathological significance; dbSNP:rs149862950
- R316 (≠ E289) to C: in RP90; unknown pathological significance; dbSNP:rs770798851
5yvtA Crystal structure of the alpha gamma heterodimer of human idh3 in complex with mg(2+) and nadh (see paper)
47% identity, 99% coverage: 4:335/336 of query aligns to 2:330/332 of 5yvtA
- active site: Y121 (= Y125), K168 (= K174), D201 (= D207), D225 (= D231), D229 (= D235)
- binding magnesium ion: D225 (= D231), D229 (= D235)
- binding 1,4-dihydronicotinamide adenine dinucleotide: L69 (= L71), T71 (= T73), N79 (= N83), N170 (= N176), D201 (= D207), E255 (= E260), V257 (= V262), H258 (= H263), G259 (= G264), I264 (= I269), N271 (= N276), D312 (= D317)
8grdA Crystal structure of a constitutively active mutant of the alpha beta heterodimer of human idh3 in complex with adp and mg (see paper)
48% identity, 99% coverage: 4:335/336 of query aligns to 2:323/325 of 8grdA
6l59A Crystal structure of the alpha gamma heterodimer of human idh3 in complex with cit, mg and atp binding at allosteric site and mg, atp binding at active site. (see paper)
47% identity, 99% coverage: 4:335/336 of query aligns to 2:321/325 of 6l59A
- active site: Y112 (= Y125), K159 (= K174), D192 (= D207), D216 (= D231)
- binding adenosine-5'-triphosphate: I12 (= I14), H249 (= H263), G250 (= G264), T251 (≠ S265), A252 (= A266), N262 (= N276), D303 (= D317)
- binding magnesium ion: D216 (= D231), D220 (= D235)
5greA Crystal structure of the alpha gamma heterodimer of human idh3 in complex with mg(2+), citrate and adp (see paper)
47% identity, 99% coverage: 4:335/336 of query aligns to 2:322/325 of 5greA
2d1cA Crystal structure of tt0538 protein from thermus thermophilus hb8
48% identity, 99% coverage: 3:335/336 of query aligns to 18:354/495 of 2d1cA
- active site: Y143 (= Y125), K190 (= K174), D223 (= D207), D247 (= D231), D251 (= D235)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P86 (= P70), L87 (= L71), E88 (≠ T72), T89 (= T73), N99 (= N83), I221 (= I205), N224 (≠ A208), Q228 (≠ K212), L260 (= L244), G261 (= G245), H279 (= H263), G280 (= G264), S281 (= S265), A282 (= A266), K284 (≠ D268), Y285 (≠ I269), I291 (≠ A275), N292 (= N276), D333 (= D317)
3blwF Yeast isocitrate dehydrogenase with citrate and amp bound in the regulatory subunits (see paper)
45% identity, 99% coverage: 3:335/336 of query aligns to 18:347/347 of 3blwF
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)
45% identity, 98% coverage: 6:335/336 of query aligns to 5:331/334 of Q72IW9
- E57 (≠ D58) 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 (≠ LTT 71:73) binding
- S72 (≠ T73) 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 (≠ V84) 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 (≠ T85) 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 (= R87) binding in other chain
- R98 (= R97) binding in other chain
- R118 (= R118) binding in other chain
- Y125 (= Y125) binding in other chain; mutation to A: Reduces catalytic efficiency with isocitrate.
- V135 (≠ T138) mutation to M: Formation of homodimers instead of homotetramers. Increased affinity for isocitrate. Reduces enzyme activity with isocitrate.
- K171 (= K174) binding
- N173 (= N176) binding ; binding
- D204 (= D207) binding
- M208 (= M211) 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 (= F220) 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 (= D231) binding
- D232 (= D235) binding
- V238 (= V241) 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 (= GSAPD 264:268) binding
- N273 (= N276) binding
- R310 (= R313) 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.
4yb4A Crystal structure of homoisocitrate dehydrogenase from thermus thermophilus in complex with homoisocitrate, magnesium ion (ii) and nadh
45% identity, 98% coverage: 6:335/336 of query aligns to 4:330/333 of 4yb4A