SitesBLAST
Comparing Echvi_4068 FitnessBrowser__Cola:Echvi_4068 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)
2d1cA Crystal structure of tt0538 protein from thermus thermophilus hb8
43% identity, 99% coverage: 4:487/487 of query aligns to 18:494/495 of 2d1cA
- active site: Y143 (= Y128), K190 (= K175), D223 (= D208), D247 (= D232), D251 (= D236)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P86 (= P72), L87 (≠ I73), E88 (≠ T74), T89 (= T75), N99 (= N85), I221 (= I206), N224 (≠ I209), Q228 (≠ L213), L260 (≠ V245), G261 (= G246), H279 (= H264), G280 (= G265), S281 (= S266), A282 (= A267), K284 (≠ D269), Y285 (≠ I270), I291 (≠ A276), N292 (= N277), D333 (= D317)
6lkyA Crystal structure of isocitrate dehydrogenase from methylococcus capsulatus
43% identity, 69% coverage: 6:343/487 of query aligns to 3:339/339 of 6lkyA
- active site: Y123 (= Y128), K174 (= K175), D207 (= D208), D231 (= D232)
- binding nicotinamide-adenine-dinucleotide: P68 (= P72), L69 (≠ I73), T71 (= T75), N81 (= N85), H263 (= H264), G264 (= G265), S265 (= S266), A266 (= A267), D268 (= D269), I269 (= I270), N276 (= N277)
6m3sB Dimeric isocitrate dehydrogenase from xanthomonas campestris pv. Campestris 8004
45% identity, 69% coverage: 5:341/487 of query aligns to 6:338/338 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: P72 (= P72), L73 (≠ I73), T75 (= T75), N85 (= N85), H266 (= H264), G267 (= G265), S268 (= S266), A269 (= A267), D271 (= D269), I272 (= I270), N279 (= N277)
3blwF Yeast isocitrate dehydrogenase with citrate and amp bound in the regulatory subunits (see paper)
42% identity, 70% coverage: 3:341/487 of query aligns to 15:347/347 of 3blwF
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)
41% identity, 63% coverage: 5:312/487 of query aligns to 32:338/366 of Q9D6R2
- E229 (≠ H204) 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)
41% identity, 63% coverage: 5:312/487 of query aligns to 3:309/335 of 6kdyA
- active site: Y124 (= Y128), K171 (= K175), D204 (= D208), D228 (= D232)
- binding nicotinamide-adenine-dinucleotide: P69 (= P72), L70 (≠ I73), T72 (= T75), N82 (= N85), H261 (= H264), G262 (= G265), T263 (≠ S266), A264 (= A267), D266 (= D269), I267 (= I270), N274 (= N277)
Sites not aligning to the query:
6kdeA Crystal structure of the alpha beta heterodimer of human idh3 in complex with ca(2+) (see paper)
41% identity, 63% coverage: 5:312/487 of query aligns to 3:309/336 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)
41% identity, 63% coverage: 5:312/487 of query aligns to 32:338/366 of P50213
- R115 (= R89) binding
- A122 (= A96) to T: in RP90; uncertain 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; uncertain 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; uncertain 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 (≠ I214) to T: in RP90; uncertain 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; uncertain significance; dbSNP:rs756712426
- M313 (= M287) to T: in RP90; uncertain significance; dbSNP:rs149862950
- R316 (≠ V290) to C: in RP90; uncertain significance; dbSNP:rs770798851
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)
41% identity, 63% coverage: 5:312/487 of query aligns to 2:297/325 of 6l59A
Sites not aligning to the query:
5greA Crystal structure of the alpha gamma heterodimer of human idh3 in complex with mg(2+), citrate and adp (see paper)
41% identity, 63% coverage: 5:312/487 of query aligns to 2:298/325 of 5greA
5yvtA Crystal structure of the alpha gamma heterodimer of human idh3 in complex with mg(2+) and nadh (see paper)
41% identity, 63% coverage: 5:312/487 of query aligns to 2:306/332 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: L69 (≠ I73), T71 (= T75), N79 (= N85), N170 (= N177), D201 (= D208), E255 (= E261), V257 (≠ I263), H258 (= H264), G259 (= G265), I264 (= I270), N271 (= N277)
Sites not aligning to the query:
8grdA Crystal structure of a constitutively active mutant of the alpha beta heterodimer of human idh3 in complex with adp and mg (see paper)
40% identity, 63% coverage: 5:312/487 of query aligns to 2:299/325 of 8grdA
3blwA Yeast isocitrate dehydrogenase with citrate and amp bound in the regulatory subunits (see paper)
40% identity, 69% coverage: 7:341/487 of query aligns to 5:326/329 of 3blwA
- active site: F116 (≠ Y128), K163 (= K175), D197 (= D208), T221 (≠ D232), N225 (≠ D236)
- binding adenosine monophosphate: G257 (≠ A267), N267 (= N277), D308 (= D317)
- binding citrate anion: T63 (= T75), S72 (= S83), N74 (= N85), V75 (= V86), R78 (= R89), R109 (= R121), F116 (≠ Y128), T221 (≠ D232), R254 (vs. gap)
3blvC Yeast isocitrate dehydrogenase with citrate bound in the regulatory subunits (see paper)
40% identity, 69% coverage: 7:341/487 of query aligns to 20:341/344 of 3blvC
2iv0A Thermal stability of isocitrate dehydrogenase from archaeoglobus fulgidus studied by crystal structure analysis and engineering of chimers (see paper)
35% identity, 68% coverage: 12:341/487 of query aligns to 35:409/412 of 2iv0A
6l57B Crystal structure of the alpha gamma heterodimer of human idh3 in complex with cit , mg and atp binding at allosteric site. (see paper)
35% identity, 67% coverage: 4:328/487 of query aligns to 1:323/332 of 6l57B
- active site: Y121 (= Y128), K168 (= K175), D201 (= D208), N225 (≠ D232)
- binding adenosine-5'-triphosphate: I12 (= I15), P238 (≠ V245), N259 (≠ G265), T260 (≠ S266), G261 (≠ A267), K262 (≠ P268), S263 (≠ D269), I264 (= I270), N271 (= N277), D312 (= D317)
- binding magnesium ion: N64 (≠ P72), R258 (≠ H264)
5yvtB Crystal structure of the alpha gamma heterodimer of human idh3 in complex with mg(2+) and nadh (see paper)
35% identity, 67% coverage: 4:328/487 of query aligns to 1:323/333 of 5yvtB
- active site: Y121 (= Y128), K168 (= K175), D201 (= D208), N225 (≠ D232), N229 (≠ D236)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I12 (= I15), E66 (≠ T74), T67 (= T75), P238 (≠ V245), G239 (= G246), R258 (≠ H264), N259 (≠ G265), T260 (≠ S266), G261 (≠ A267), S263 (≠ D269), I264 (= I270), A270 (= A276), N271 (= N277), D312 (= D317)
P51553 Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial; Isocitric dehydrogenase subunit gamma; NAD(+)-specific ICDH subunit gamma from Homo sapiens (Human) (see 2 papers)
35% identity, 67% coverage: 4:328/487 of query aligns to 54:376/393 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.
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)
38% identity, 69% coverage: 6:341/487 of query aligns to 4:331/334 of Q72IW9
- E57 (≠ W59) 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 (≠ SPI 71:73) binding
- S72 (≠ I73) 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 (≠ V86) 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 (≠ T87) 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 (= R89) binding in other chain
- R98 (= R99) binding in other chain
- R118 (= R121) binding in other chain
- Y125 (= Y128) binding in other chain; mutation to A: Reduces catalytic efficiency with isocitrate.
- V135 (= V139) mutation to M: Formation of homodimers instead of homotetramers. Increased affinity for isocitrate. Reduces enzyme activity with isocitrate.
- K171 (= K175) binding
- N173 (= N177) binding ; binding
- D204 (= D208) binding
- M208 (≠ A212) 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 (= F221) 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 (= D232) binding
- D232 (= D236) binding
- V238 (≠ T242) 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 265:269) binding
- N273 (= N277) binding
- R310 (≠ H314) 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
38% identity, 69% coverage: 6:341/487 of query aligns to 3:330/333 of 4yb4A
- active site: Y124 (= Y128), K170 (= K175), D203 (= D208), D227 (= D232), D231 (= D236)
- binding (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylic acid: S71 (≠ I73), R84 (≠ V86), R87 (= R89), R97 (= R99), R117 (= R121), Y124 (= Y128), D227 (= D232)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I12 (= I15), A69 (≠ S71), T70 (≠ P72), S71 (≠ I73), I201 (= I206), N204 (≠ I209), L240 (≠ V245), E256 (= E261), H259 (= H264), G260 (= G265), S261 (= S266), A262 (= A267), D264 (= D269), I265 (= I270), N272 (= N277), D312 (= D317)
Query Sequence
>Echvi_4068 FitnessBrowser__Cola:Echvi_4068
MSSKRKITVAYGDGIGPEIMKATLEILEAAGAQIEPEVIEIGEQVYLKGISSGIEPKAWD
SLRETKIFLKSPITTPQGGGFKSLNVTTRKTLGLYANVRPCKAYSPYIRTHFPETDMVIV
RENEEDLYAGIEHRQTDDVYQCLKLISRPGSEKIIRYAFEYAKKYNRKKVTCMTKDNIMK
LADGLFHKVFNDVAKEYPEIEADHKIIDIGTALIADKPEMFDVIVTLNLYGDIISDVAAQ
ITGSVGLGGSSNVGEDVAMFEAIHGSAPDIAGQNIANPSGLLNGAIMMLVHIGQPEVAEK
VSNAWMKTLEDGIHTGDIYQEGVSSQLVGTKEFAQAVIDRLGQKPEKMVPAEFKKGDGAD
DNMGAIKLADRKPCKKDLIGLDVFIDWKENDRDANVIGDKLRAVDADGLKMQLITNRGVK
VYPDGMKETFCSDHWRVRFFNADQSTITHGQVLDVLKQVEDLGFDFIKTENLYTFDGERG
FSLAQGE
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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