SitesBLAST
Comparing Ac3H11_375 FitnessBrowser__acidovorax_3H11:Ac3H11_375 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)
64% identity, 98% coverage: 5:362/364 of query aligns to 3:357/359 of 3flkA
- active site: Y137 (= Y144), K188 (= K195), D221 (= D228), D245 (= D252), D249 (= D256)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I12 (= I14), A73 (= A75), V74 (= V76), G75 (= G77), D82 (= D84), L90 (= L92), N190 (= N197), I222 (= I229), R226 (≠ H233), I258 (= I265), H280 (= H287), G281 (= G288), S282 (= S289), A283 (= A290), I286 (= I293), N293 (= N300)
- binding oxalate ion: R94 (= R96), R104 (= R106), R130 (= R137), D245 (= D252)
4yb4A Crystal structure of homoisocitrate dehydrogenase from thermus thermophilus in complex with homoisocitrate, magnesium ion (ii) and nadh
39% identity, 99% coverage: 4:364/364 of query aligns to 2:333/333 of 4yb4A
- active site: Y124 (= Y144), K170 (= K195), D203 (= D228), D227 (= D252), D231 (= D256)
- binding (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylic acid: S71 (≠ W78), R84 (≠ L93), R87 (= R96), R97 (= R106), R117 (= R137), Y124 (= Y144), D227 (= D252)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I12 (= I14), A69 (≠ V76), T70 (≠ G77), S71 (≠ W78), I201 (≠ H226), N204 (≠ I229), L240 (≠ I265), E256 (= E284), H259 (= H287), G260 (= G288), S261 (= S289), A262 (= A290), D264 (= D292), I265 (= I293), N272 (= N300), D312 (= D343)
3asjB Crystal structure of homoisocitrate dehydrogenase in complex with a designed inhibitor (see paper)
39% identity, 99% coverage: 4:364/364 of query aligns to 2:333/333 of 3asjB
- active site: Y124 (= Y144), K170 (= K195), D203 (= D228), D227 (= D252), D231 (= D256)
- binding (2Z)-3-[(carboxymethyl)sulfanyl]-2-hydroxyprop-2-enoic acid: R84 (≠ L93), R97 (= R106), R117 (= R137), Y124 (= Y144), D227 (= D252), D231 (= D256), V258 (= V286)
3asjA Crystal structure of homoisocitrate dehydrogenase in complex with a designed inhibitor (see paper)
39% identity, 99% coverage: 4:364/364 of query aligns to 2:333/333 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, 99% coverage: 4:364/364 of query aligns to 3:334/334 of Q72IW9
- E57 (= E63) 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 (≠ VGW 76:78) binding NADH
- S72 (≠ W78) 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 (≠ L93) 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 (≠ L94) 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 (= R96) binding in other chain
- R98 (= R106) binding in other chain
- R118 (= R137) binding in other chain
- Y125 (= Y144) binding in other chain; mutation to A: Reduces catalytic efficiency with isocitrate.
- V135 (≠ I159) mutation to M: Formation of homodimers instead of homotetramers. Increased affinity for isocitrate. Reduces enzyme activity with isocitrate.
- K171 (= K195) binding (2R,3S)-homoisocitrate
- N173 (= N197) binding (2R,3S)-homoisocitrate; binding NADH
- D204 (= D228) binding Mg(2+)
- M208 (≠ A232) 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 (= F241) 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 (= D252) binding Mg(2+)
- D232 (= D256) binding Mg(2+)
- V238 (≠ T262) 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 288:292) binding NADH
- N273 (= N300) binding NADH
- R310 (= R340) 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.
2g4oA Anomalous substructure of 3-isopropylmalate dehydrogenase (see paper)
42% identity, 98% coverage: 5:361/364 of query aligns to 3:337/337 of 2g4oA
6xxyA Crystal structure of haemophilus influenzae 3-isopropylmalate dehydrogenase in complex with o-isobutenyl oxalylhydroxamate. (see paper)
39% identity, 98% coverage: 4:361/364 of query aligns to 4:358/358 of 6xxyA
- active site: Y144 (= Y144), K194 (= K195), D226 (= D228), D250 (= D252)
- binding magnesium ion: D250 (= D252), D254 (= D256)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ A75), V75 (= V76), G76 (= G77), E90 (≠ L88), L94 (= L92), Y224 (≠ H226), N227 (≠ I229), M230 (≠ A232), M263 (≠ I265), G264 (= G266), E280 (= E284), G283 (≠ H287), G284 (= G288), S285 (= S289), A286 (= A290), P287 (= P291), D288 (= D292), I289 (= I293), N296 (= N300), D337 (= D343)
- binding 2-(2-methylprop-2-enoxyamino)-2-oxidanylidene-ethanoic acid: E90 (≠ L88), R108 (= R106), R137 (= R137), K194 (= K195), V197 (≠ G198), D226 (= D228), D250 (= D252)
3vkzA 3-isopropylmalate dehydrogenase from shewanella oneidensis mr-1 at atmospheric pressure (see paper)
40% identity, 91% coverage: 2:333/364 of query aligns to 1:329/364 of 3vkzA
3vmkA 3-isopropylmalate dehydrogenase from shewanella benthica db21 mt-2 (see paper)
37% identity, 99% coverage: 2:362/364 of query aligns to 7:367/369 of 3vmkA
P40495 Homoisocitrate dehydrogenase, mitochondrial; HIcDH; EC 1.1.1.87 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
36% identity, 96% coverage: 6:353/364 of query aligns to 26:363/371 of P40495
- Y150 (= Y144) mutation to F: Strongly reduced enzyme activity.
- K206 (= K195) mutation to M: Strongly reduced enzyme activity.
6m3sB Dimeric isocitrate dehydrogenase from xanthomonas campestris pv. Campestris 8004
35% identity, 98% coverage: 4:361/364 of query aligns to 6:338/338 of 6m3sB
- active site: Y128 (= Y144), K177 (= K195), D210 (= D228), D234 (= D252)
- binding isocitrate calcium complex: T75 (≠ W78), S83 (≠ L88), N85 (≠ G90), R89 (= R96), R99 (= R106), R121 (= R137), Y128 (= Y144), D234 (= D252), D238 (= D256)
- binding nicotinamide-adenine-dinucleotide: P72 (≠ A75), L73 (≠ V76), T75 (≠ W78), N85 (≠ G90), H266 (= H287), G267 (= G288), S268 (= S289), A269 (= A290), D271 (= D292), I272 (= I293), N279 (= N300)
O14104 Homoisocitrate dehydrogenase; HICDH; EC 1.1.1.87 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
35% identity, 97% coverage: 6:357/364 of query aligns to 9:356/362 of O14104
- S81 (≠ W78) modified: Phosphoserine
- S91 (= S87) modified: Phosphoserine
2y42D Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with nadh and mn (see paper)
36% identity, 95% coverage: 5:351/364 of query aligns to 3:335/355 of 2y42D