SitesBLAST

Comparing AZOBR_RS11025 FitnessBrowser__azobra:AZOBR_RS11025 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Found 20 (the maximum) hits to proteins with known functional sites

2d1cA Crystal structure of tt0538 protein from thermus thermophilus hb8
44% identity, 98% coverage: 7:479/481 of query aligns to 21:489/495 of 2d1cA

• active site: Y143 (= Y128), K190 (= K175), D223 (= D208), D247 (= D232), D251 (= D236)
• binding nadp nicotinamide-adenine-dinucleotide phosphate: I29 (= I15), K84 (= K70), P86 (= P72), L87 (≠ I73), E88 (≠ T74), T89 (= T75), N99 (= N85), N192 (= N177), I221 (= I206), N224 (≠ I209), H227 (≠ A212), Q228 (≠ R213), K231 (≠ D216), L260 (≠ V245), G261 (= G246), E276 (= E261), V278 (≠ I263), H279 (= H264), G280 (= G265), S281 (= S266), A282 (= A267), K284 (≠ M269), Y285 (≠ I270), I291 (≠ A276), N292 (= N277), D333 (= D317), Y337 (≠ F319)

6lkyA Crystal structure of isocitrate dehydrogenase from methylococcus capsulatus
48% identity, 70% coverage: 7:343/481 of query aligns to 4:339/339 of 6lkyA

• active site: Y123 (= Y128), K174 (= K175), D207 (= D208), D231 (= D232)
• binding nicotinamide-adenine-dinucleotide: I12 (= I15), K66 (= K70), P68 (= P72), L69 (≠ I73), T70 (= T74), T71 (= T75), N81 (= N85), N176 (= N177), I205 (= I206), A208 (≠ I209), M211 (≠ A212), Q212 (≠ R213), L244 (≠ V245), G245 (= G246), E260 (= E261), V262 (≠ I263), H263 (= H264), G264 (= G265), S265 (= S266), A266 (= A267), P267 (= P268), D268 (≠ M269), I269 (= I270), A275 (= A276), N276 (= N277), D317 (≠ I318)

6m3sB Dimeric isocitrate dehydrogenase from xanthomonas campestris pv. Campestris 8004
47% identity, 70% coverage: 4:341/481 of query aligns to 5:338/338 of 6m3sB

• active site: Y128 (= Y128), K177 (= K175), D210 (= D208), D234 (= D232)
• binding isocitrate calcium complex: T75 (= T75), S83 (= S83), N85 (= N85), R89 (= R89), R99 (= R99), R121 (= R121), Y128 (= Y128), D234 (= D232), D238 (= D236)
• binding nicotinamide-adenine-dinucleotide: I16 (= I15), K70 (= K70), P72 (= P72), L73 (≠ I73), T74 (= T74), T75 (= T75), N85 (= N85), L247 (≠ V245), E263 (= E261), V265 (≠ I263), H266 (= H264), G267 (= G265), S268 (= S266), A269 (= A267), D271 (≠ M269), I272 (= I270), A278 (= A276), N279 (= N277), D320 (= D317)

6kdyA Crystal structure of the alpha bata heterodimer of human idh3 in complex with NAD. (see paper)
45% identity, 64% coverage: 7:312/481 of query aligns to 5:309/335 of 6kdyA

• active site: Y124 (= Y128), K171 (= K175), D204 (= D208), D228 (= D232)
• binding nicotinamide-adenine-dinucleotide: I13 (= I15), P69 (= P72), L70 (≠ I73), T72 (= T75), N82 (= N85), L241 (≠ V245), G242 (= G246), E258 (= E261), H261 (= H264), G262 (= G265), T263 (≠ S266), A264 (= A267), P265 (= P268), D266 (≠ M269), I267 (= I270), A273 (= A276), N274 (= N277)

Sites not aligning to the query:

• binding nicotinamide-adenine-dinucleotide: 315

6kdeA Crystal structure of the alpha beta heterodimer of human idh3 in complex with ca(2+) (see paper)
45% identity, 64% coverage: 7:312/481 of query aligns to 5:309/336 of 6kdeA

• active site: Y124 (= Y128), K171 (= K175), D204 (= D208), D228 (= D232)
• binding calcium ion: D228 (= D232), D232 (= D236)

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)
45% identity, 64% coverage: 7:312/481 of query aligns to 34:338/366 of P50213

• R115 (= R89) binding
• A122 (= A96) to T: in RP90; unknown pathological significance; dbSNP:rs756333430
• R125 (= R99) binding
• R146 (= R121) binding
• E152 (≠ L127) mutation to A: No significant effect on the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP.
• Y153 (= Y128) 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 (= K144) mutation to A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP.
• A175 (≠ G150) to V: in RP90; unknown pathological significance; dbSNP:rs765473830
• K200 (= K175) Critical for catalysis; mutation to A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate.
• N202 (= N177) mutation to A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate.
• M204 (= M179) to I: in RP90; unknown pathological significance
• D208 (= D183) mutation to A: Complete loss of the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP.
• D233 (= D208) binding
• M239 (≠ L214) to T: in RP90; unknown pathological significance; dbSNP:rs2074707744
• Y255 (= Y230) mutation to A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP.
• D257 (= D232) binding
• D261 (= D236) binding
• P304 (= P278) to H: in RP90; unknown pathological significance; dbSNP:rs756712426
• M313 (= M287) to T: in RP90; unknown pathological significance; dbSNP:rs149862950
• R316 (≠ V290) to C: in RP90; unknown pathological significance; dbSNP:rs770798851

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)
44% identity, 64% coverage: 7:312/481 of query aligns to 34:338/366 of Q9D6R2

• E229 (≠ H204) mutation to K: Homozygous mutant mice exhibit retinal degeneration.

5yvtA Crystal structure of the alpha gamma heterodimer of human idh3 in complex with mg(2+) and nadh (see paper)
45% identity, 64% coverage: 7:312/481 of query aligns to 4:306/332 of 5yvtA

• active site: Y121 (= Y128), K168 (= K175), D201 (= D208), D225 (= D232), D229 (= D236)
• binding magnesium ion: D225 (= D232), D229 (= D236)
• binding 1,4-dihydronicotinamide adenine dinucleotide: I12 (= I15), L69 (≠ I73), K70 (≠ T74), T71 (= T75), N79 (= N85), N170 (= N177), Y199 (≠ I206), D201 (= D208), T202 (≠ I209), L238 (≠ V245), E255 (= E261), V257 (≠ I263), H258 (= H264), G259 (= G265), T260 (≠ S266), A261 (= A267), D263 (≠ M269), I264 (= I270), A270 (= A276), N271 (= N277)

Sites not aligning to the query:

• binding 1,4-dihydronicotinamide adenine dinucleotide: 312

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)
45% identity, 64% coverage: 7:312/481 of query aligns to 4:297/325 of 6l59A

• active site: Y112 (= Y128), K159 (= K175), D192 (= D208), D216 (= D232)
• binding adenosine-5'-triphosphate: I12 (= I15), H249 (= H264), G250 (= G265), T251 (≠ S266), A252 (= A267), D254 (≠ M269), A261 (= A276), N262 (= N277)
• binding magnesium ion: D216 (= D232), D220 (= D236)

Sites not aligning to the query:

• binding adenosine-5'-triphosphate: 303

5greA Crystal structure of the alpha gamma heterodimer of human idh3 in complex with mg(2+), citrate and adp (see paper)
45% identity, 64% coverage: 7:312/481 of query aligns to 4:298/325 of 5greA

• active site: Y113 (= Y128), K160 (= K175), D193 (= D208), D217 (= D232), D221 (= D236)
• binding adenosine-5'-diphosphate: Y191 (≠ I206), T194 (≠ I209)
• binding magnesium ion: D217 (= D232), D221 (= D236)

3blvH Yeast isocitrate dehydrogenase with citrate bound in the regulatory subunits (see paper)
42% identity, 70% coverage: 7:341/481 of query aligns to 21:348/348 of 3blvH

• active site: Y136 (= Y128), K183 (= K175), D216 (= D208), D242 (= D232), D246 (= D236)
• binding citrate anion: K183 (= K175), T185 (≠ N177), D216 (= D208)

P51553 Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial; Isocitric dehydrogenase subunit gamma; NAD(+)-specific ICDH subunit gamma from Homo sapiens (Human) (see 2 papers)
40% identity, 67% coverage: 7:328/481 of query aligns to 57:376/393 of P51553

• N117 (≠ P72) mutation to A: No effect on the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate.
• T120 (= T75) binding ; mutation to A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate.
• S130 (= S83) mutation to A: No significant effect on the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate.
• N133 (≠ V86) binding ; mutation to A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate.
• R136 (= R89) binding ; mutation to A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate.
• R167 (= R121) binding ; mutation to A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate.
• E173 (≠ L127) mutation to A: No effect on the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP.
• Y174 (= Y128) mutation to F: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate.
• K190 (= K144) mutation to A: Complete loss of the activation of the heterotetramer and the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP.
• D229 (= D183) mutation to A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP.
• D254 (= D208) binding ; binding
• Y276 (= Y230) mutation to F: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP.
• R311 (≠ H264) mutation to A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate.
• N312 (≠ G265) binding ; mutation to A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by ADP.
• T313 (≠ S266) binding ; mutation to A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by ADP.
• K315 (≠ P268) mutation to A: No significant effect on the activation of the heterodimer composed of IDH3A and IDH3G subunits by ADP.
• N324 (= N277) binding ; mutation to A: Complete loss of the activation of the heterodimer composed of IDH3A and IDH3G subunits by ADP.

5yvtB Crystal structure of the alpha gamma heterodimer of human idh3 in complex with mg(2+) and nadh (see paper)
40% identity, 67% coverage: 7:328/481 of query aligns to 4:323/333 of 5yvtB