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Comparing WP_010875823.1 NCBI__GCF_000008645.1:WP_010875823.1 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)
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)
52% identity, 98% coverage: 2:327/331 of query aligns to 3:331/334 of Q72IW9
- E57 (≠ K56) 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 (≠ VTT 69:71) binding NADH
- S72 (≠ T71) 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 (≠ I80) 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 (≠ T81) 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 (= R83) binding in other chain
- R98 (= R93) binding in other chain
- R118 (= R114) binding in other chain
- Y125 (= Y121) binding in other chain; mutation to A: Reduces catalytic efficiency with isocitrate.
- V135 (≠ G131) mutation to M: Formation of homodimers instead of homotetramers. Increased affinity for isocitrate. Reduces enzyme activity with isocitrate.
- K171 (= K167) binding (2R,3S)-homoisocitrate
- N173 (= N169) binding (2R,3S)-homoisocitrate; binding NADH
- D204 (= D200) binding Mg(2+)
- M208 (= M204) 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 (= F213) 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 (= D224) binding Mg(2+)
- D232 (= D228) binding Mg(2+)
- V238 (≠ I234) 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 (≠ GSAPQ 257:261) binding NADH
- N273 (= N269) binding NADH
- R310 (≠ M306) 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
52% identity, 98% coverage: 2:327/331 of query aligns to 2:330/333 of 4yb4A
- active site: Y124 (= Y121), K170 (= K167), D203 (= D200), D227 (= D224), D231 (= D228)
- binding (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylic acid: S71 (≠ T71), R84 (≠ I80), R87 (= R83), R97 (= R93), R117 (= R114), Y124 (= Y121), D227 (= D224)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I12 (= I12), A69 (≠ V69), T70 (= T70), S71 (≠ T71), I201 (≠ Y198), N204 (≠ A201), L240 (= L237), E256 (= E253), H259 (= H256), G260 (= G257), S261 (= S258), A262 (= A259), D264 (≠ Q261), I265 (= I262), N272 (= N269), D312 (= D309)
3asjB Crystal structure of homoisocitrate dehydrogenase in complex with a designed inhibitor (see paper)
52% identity, 98% coverage: 2:327/331 of query aligns to 2:330/333 of 3asjB
- active site: Y124 (= Y121), K170 (= K167), D203 (= D200), D227 (= D224), D231 (= D228)
- binding (2Z)-3-[(carboxymethyl)sulfanyl]-2-hydroxyprop-2-enoic acid: R84 (≠ I80), R97 (= R93), R117 (= R114), Y124 (= Y121), D227 (= D224), D231 (= D228), V258 (= V255)
3asjA Crystal structure of homoisocitrate dehydrogenase in complex with a designed inhibitor (see paper)
52% identity, 98% coverage: 2:327/331 of query aligns to 2:330/333 of 3asjA
6m3sB Dimeric isocitrate dehydrogenase from xanthomonas campestris pv. Campestris 8004
47% identity, 98% coverage: 4:327/331 of query aligns to 8:338/338 of 6m3sB
- active site: Y128 (= Y121), K177 (= K167), D210 (= D200), D234 (= D224)
- binding isocitrate calcium complex: T75 (= T71), S83 (= S77), N85 (≠ I79), R89 (= R83), R99 (= R93), R121 (= R114), Y128 (= Y121), D234 (= D224), D238 (= D228)
- binding nicotinamide-adenine-dinucleotide: P72 (≠ A68), L73 (≠ V69), T75 (= T71), N85 (≠ I79), H266 (= H256), G267 (= G257), S268 (= S258), A269 (= A259), D271 (≠ Q261), I272 (= I262), N279 (= N269)
6lkyA Crystal structure of isocitrate dehydrogenase from methylococcus capsulatus
46% identity, 99% coverage: 1:327/331 of query aligns to 1:337/339 of 6lkyA
- active site: Y123 (= Y121), K174 (= K167), D207 (= D200), D231 (= D224)
- binding nicotinamide-adenine-dinucleotide: P68 (≠ V69), L69 (≠ T70), T71 (≠ V72), N81 (≠ I79), H263 (= H256), G264 (= G257), S265 (= S258), A266 (= A259), D268 (≠ Q261), I269 (= I262), N276 (= N269)
2d1cA Crystal structure of tt0538 protein from thermus thermophilus hb8
46% identity, 98% coverage: 4:329/331 of query aligns to 21:356/495 of 2d1cA
- active site: Y143 (= Y121), K190 (= K167), D223 (= D200), D247 (= D224), D251 (= D228)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P86 (≠ A68), L87 (≠ V69), E88 (≠ T70), T89 (= T71), N99 (≠ I79), I221 (≠ Y198), N224 (≠ A201), Q228 (≠ Y205), L260 (= L237), G261 (= G238), H279 (= H256), G280 (= G257), S281 (= S258), A282 (= A259), K284 (≠ Q261), Y285 (≠ I262), I291 (≠ A268), N292 (= N269), D333 (= D309)
4y1pB Crystal structure of 3-isopropylmalate dehydrogenase (saci_0600) from sulfolobus acidocaldarius complex with 3-isopropylmalate and mg2+ (see paper)
43% identity, 98% coverage: 2:327/331 of query aligns to 2:335/336 of 4y1pB
P40495 Homoisocitrate dehydrogenase, mitochondrial; HIcDH; EC 1.1.1.87 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
45% identity, 97% coverage: 4:323/331 of query aligns to 26:367/371 of P40495
- Y150 (= Y121) mutation to F: Strongly reduced enzyme activity.
- K206 (= K167) mutation to M: Strongly reduced enzyme activity.
5hn6A Crystal structure of beta-decarboxylating dehydrogenase (tk0280) from thermococcus kodakarensis complexed with mn and 3-isopropylmalate (see paper)
44% identity, 99% coverage: 1:327/331 of query aligns to 1:319/329 of 5hn6A
5hn4A Crystal structure of beta-decarboxylating dehydrogenase (tk0280) from thermococcus kodakarensis complexed with mn and homoisocitrate (see paper)
44% identity, 99% coverage: 1:327/331 of query aligns to 1:319/329 of 5hn4A
- active site: Y118 (= Y121), K163 (= K167), D194 (= D200), D218 (= D224), D222 (= D228)
- binding (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylic acid: T71 (= T71), S80 (= S77), R86 (= R83), R96 (= R93), R111 (= R114), Y118 (= Y121), D218 (= D224)
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, 98% coverage: 4:327/331 of query aligns to 4:323/325 of 8grdA
3ty3A Crystal structure of homoisocitrate dehydrogenase from schizosaccharomyces pombe bound to glycyl-glycyl-glycine (see paper)
41% identity, 98% coverage: 4:327/331 of query aligns to 5:356/358 of 3ty3A
- active site: Y129 (= Y121), K192 (= K167), D228 (= D200), D252 (= D224), D256 (= D228)
- binding glycylglycylglycine: A74 (= A68), V75 (= V69), S77 (≠ T71), R93 (= R83), E281 (= E253), P282 (= P254), H284 (= H256)
O14104 Homoisocitrate dehydrogenase; HICDH; EC 1.1.1.87 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
41% identity, 98% coverage: 4:327/331 of query aligns to 9:360/362 of O14104
- S81 (≠ T71) modified: Phosphoserine
- S91 (= S77) modified: Phosphoserine
5greA Crystal structure of the alpha gamma heterodimer of human idh3 in complex with mg(2+), citrate and adp (see paper)
40% identity, 98% coverage: 4:327/331 of query aligns to 4:322/325 of 5greA
5yvtA Crystal structure of the alpha gamma heterodimer of human idh3 in complex with mg(2+) and nadh (see paper)
39% identity, 98% coverage: 4:327/331 of query aligns to 4:330/332 of 5yvtA
- active site: Y121 (= Y121), K168 (= K167), D201 (= D200), D225 (= D224), D229 (= D228)
- binding magnesium ion: D225 (= D224), D229 (= D228)
- binding 1,4-dihydronicotinamide adenine dinucleotide: L69 (≠ V69), T71 (= T71), N79 (≠ I79), N170 (= N169), D201 (= D200), E255 (= E253), V257 (= V255), H258 (= H256), G259 (= G257), I264 (= I262), N271 (= N269), D312 (= D309)
6kdeA Crystal structure of the alpha beta heterodimer of human idh3 in complex with ca(2+) (see paper)
39% identity, 98% coverage: 4:327/331 of query aligns to 5:333/336 of 6kdeA
6kdyA Crystal structure of the alpha bata heterodimer of human idh3 in complex with NAD. (see paper)
39% identity, 98% coverage: 4:327/331 of query aligns to 5:333/335 of 6kdyA
- active site: Y124 (= Y121), K171 (= K167), D204 (= D200), D228 (= D224)
- binding nicotinamide-adenine-dinucleotide: P69 (≠ A68), L70 (≠ V69), T72 (= T71), N82 (≠ I79), H261 (= H256), G262 (= G257), T263 (≠ S258), A264 (= A259), D266 (≠ Q261), I267 (= I262), N274 (= N269), D315 (= D309)
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)
39% identity, 98% coverage: 4:327/331 of query aligns to 34:362/366 of P50213
- R115 (= R83) binding substrate
- A122 (= A90) to T: in RP90; uncertain significance; dbSNP:rs756333430
- R125 (= R93) binding substrate
- R146 (= R114) binding substrate
- E152 (≠ L120) mutation to A: No significant effect on the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP.
- Y153 (= Y121) 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 (≠ R136) mutation to A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP.
- A175 (= A142) to V: in RP90; uncertain significance; dbSNP:rs765473830
- K200 (= K167) Critical for catalysis; mutation to A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate.
- N202 (= N169) mutation to A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate.
- M204 (≠ L171) to I: in RP90; uncertain significance
- D208 (= D175) mutation to A: Complete loss of the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP.
- D233 (= D200) binding Mg(2+)
- M239 (≠ L206) to T: in RP90; uncertain significance; dbSNP:rs2074707744
- Y255 (≠ F222) mutation to A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP.
- D257 (= D224) binding Mg(2+)
- D261 (= D228) binding Mg(2+)
- P304 (= P270) to H: in RP90; uncertain significance; dbSNP:rs756712426
- M313 (≠ L279) to T: in RP90; uncertain significance; dbSNP:rs149862950
- R316 (≠ K282) to C: in RP90; uncertain 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)
39% identity, 98% coverage: 4:327/331 of query aligns to 34:362/366 of Q9D6R2
- E229 (≠ D196) mutation to K: Homozygous mutant mice exhibit retinal degeneration.
Query Sequence
>WP_010875823.1 NCBI__GCF_000008645.1:WP_010875823.1
MYRITVIPGDGIGVEVMEAALHVLQALEIEFEFTHAEAGNECFRRCGDTLPEETLKLVRK
ADATLFGAVTTVPGQKSAIITLRRELDLFANLRPVKSLPGVPCLYPDLDFVIVRENTEDL
YVGDEEYTPEGAVAKRIITRTASRRISQFAFQYAQKEGMQKVTAVHKANVLKKTDGIFRD
EFYKVASEYPQMEANDYYVDATAMYLITQPQEFQTIVTTNLFGDILSDEAAGLIGGLGLA
PSANIGEKNALFEPVHGSAPQIAGKNIANPTAMILTTTLMLKHLNKKQEAQKIEKALQKT
LMRGIMTPDLGGTASTMEMAEAIKEEIVKGE
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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