SitesBLAST
Comparing GFF1775 PGA1_c17990 D-malate dehydrogenase 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)
57% identity, 99% coverage: 4:354/354 of query aligns to 1:357/359 of 3flkA
- active site: Y137 (= Y138), K188 (= K189), D221 (= D222), D245 (= D246), D249 (= D250)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I12 (= I15), A73 (= A75), V74 (= V76), G75 (= G77), P77 (= P79), D82 (= D83), L90 (= L91), N190 (= N191), H219 (= H220), I222 (= I223), R226 (≠ N227), I258 (= I259), G259 (= G260), E277 (= E278), V279 (= V280), H280 (= H281), G281 (= G282), S282 (= S283), A283 (= A284), P284 (= P285), I286 (= I287), A292 (= A293), N293 (= N294), D338 (= D335)
- binding ammonium ion: G72 (= G74), A73 (= A75), E277 (= E278), P278 (= P279), H280 (= H281)
- binding oxalate ion: R94 (= R95), R104 (= R105), R130 (= R131), K188 (= K189), D221 (= D222), D245 (= D246)
2g4oD Anomalous substructure of 3-isopropylmalate dehydrogenase (see paper)
42% identity, 94% coverage: 6:337/354 of query aligns to 3:330/337 of 2g4oD
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, 99% coverage: 5:354/354 of query aligns to 3:332/334 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 (≠ VGF 76:78) binding
- S72 (≠ F78) 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 (≠ I92) 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 (≠ P93) 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 (= R95) binding in other chain
- R98 (= R105) binding in other chain
- R118 (= R131) binding in other chain
- Y125 (= Y138) binding in other chain; mutation to A: Reduces catalytic efficiency with isocitrate.
- V135 (≠ A153) mutation to M: Formation of homodimers instead of homotetramers. Increased affinity for isocitrate. Reduces enzyme activity with isocitrate.
- K171 (= K189) binding
- N173 (= N191) binding ; binding
- D204 (= D222) binding
- M208 (≠ A226) 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 (= F235) 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 (= D246) binding
- D232 (= D250) binding
- V238 (≠ A256) 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 282:286) binding
- N273 (= N294) binding
- R310 (≠ K332) 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, 99% coverage: 5:354/354 of query aligns to 2:331/333 of 4yb4A
- active site: Y124 (= Y138), K170 (= K189), D203 (= D222), D227 (= D246), D231 (= D250)
- binding (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylic acid: S71 (≠ F78), R84 (≠ I92), R87 (= R95), R97 (= R105), R117 (= R131), Y124 (= Y138), K170 (= K189), N172 (= N191), V173 (≠ G192), D203 (= D222), D227 (= D246)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I12 (= I15), F66 (≠ L73), A68 (= A75), A69 (≠ V76), T70 (≠ G77), S71 (≠ F78), I83 (≠ L91), N172 (= N191), I201 (≠ H220), N204 (≠ I223), M207 (≠ A226), L240 (≠ I259), G241 (= G260), E256 (= E278), V258 (= V280), H259 (= H281), G260 (= G282), S261 (= S283), A262 (= A284), D264 (= D286), I265 (= I287), A271 (= A293), N272 (= N294), D312 (= D335)
3asjA Crystal structure of homoisocitrate dehydrogenase in complex with a designed inhibitor (see paper)
38% identity, 99% coverage: 5:354/354 of query aligns to 2:331/333 of 3asjA
- active site: Y124 (= Y138), K170 (= K189), D203 (= D222), D227 (= D246), D231 (= D250)
- binding (2Z)-3-[(carboxymethyl)sulfanyl]-2-hydroxyprop-2-enoic acid: K170 (= K189), D203 (= D222)
- binding 3-[(carboxymethyl)sulfanyl]-2-oxopropanoic acid: R84 (≠ I92), R87 (= R95), R97 (= R105), R117 (= R131), Y124 (= Y138), D227 (= D246), D231 (= D250), V258 (= V280)
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: 3:342/354 of query aligns to 22:360/371 of P40495
- Y150 (= Y138) mutation to F: Strongly reduced enzyme activity.
- K206 (= K189) mutation to M: Strongly reduced enzyme activity.
6m3sB Dimeric isocitrate dehydrogenase from xanthomonas campestris pv. Campestris 8004
37% identity, 100% coverage: 1:353/354 of query aligns to 4:338/338 of 6m3sB
- active site: Y128 (= Y138), K177 (= K189), D210 (= D222), D234 (= D246)
- binding isocitrate calcium complex: T75 (≠ V81), S83 (≠ G89), N85 (≠ L91), R89 (= R95), R99 (= R105), R121 (= R131), Y128 (= Y138), D234 (= D246), D238 (= D250)
- binding nicotinamide-adenine-dinucleotide: I16 (= I15), K70 (≠ P79), P72 (vs. gap), L73 (vs. gap), T74 (vs. gap), T75 (≠ V81), N85 (≠ L91), L247 (≠ I259), E263 (= E278), V265 (= V280), H266 (= H281), G267 (= G282), S268 (= S283), A269 (= A284), D271 (= D286), I272 (= I287), A278 (= A293), N279 (= N294), D320 (= D335)
6xxyA Crystal structure of haemophilus influenzae 3-isopropylmalate dehydrogenase in complex with o-isobutenyl oxalylhydroxamate. (see paper)
37% identity, 94% coverage: 3:336/354 of query aligns to 2:338/358 of 6xxyA
- active site: Y144 (= Y138), K194 (= K189), D226 (= D222), D250 (= D246)
- binding magnesium ion: D250 (= D246), D254 (= D250)
- binding nicotinamide-adenine-dinucleotide: I14 (= I15), S74 (≠ A75), V75 (= V76), G76 (= G77), G77 (≠ F78), E90 (≠ L87), L94 (= L91), N196 (= N191), Y224 (≠ H220), N227 (≠ I223), M230 (≠ A226), M263 (≠ I259), G264 (= G260), E280 (= E278), G283 (≠ H281), G284 (= G282), S285 (= S283), A286 (= A284), P287 (= P285), D288 (= D286), I289 (= I287), A295 (= A293), N296 (= N294), D337 (= D335)
- binding 2-(2-methylprop-2-enoxyamino)-2-oxidanylidene-ethanoic acid: E90 (≠ L87), L94 (= L91), L95 (≠ I92), R98 (= R95), R108 (= R105), R137 (= R131), K194 (= K189), V197 (≠ I193), D226 (= D222), D250 (= D246), A282 (≠ V280)
O14104 Homoisocitrate dehydrogenase; HICDH; EC 1.1.1.87 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
36% identity, 100% coverage: 1:353/354 of query aligns to 1:360/362 of O14104
- S81 (≠ F78) modified: Phosphoserine
- S91 (≠ G89) modified: Phosphoserine
1cnzA 3-isopropylmalate dehydrogenase (ipmdh) from salmonella typhimurium (see paper)
36% identity, 92% coverage: 1:326/354 of query aligns to 1:330/363 of 1cnzA
P37412 3-isopropylmalate dehydrogenase; 3-IPM-DH; Beta-IPM dehydrogenase; IMDH; EC 1.1.1.85 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
36% identity, 92% coverage: 1:326/354 of query aligns to 1:330/363 of P37412
- D227 (= D222) binding
- D251 (= D246) binding
- D255 (= D250) binding
2y41A Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with ipm and mn (see paper)
36% identity, 99% coverage: 4:354/354 of query aligns to 1:346/346 of 2y41A
- active site: Y140 (= Y138), K186 (= K189), D218 (= D222), D242 (= D246), D246 (= D250)
- binding 3-isopropylmalic acid: E88 (≠ W88), R95 (= R95), R105 (= R105), R133 (= R131), Y140 (= Y138), K186 (= K189), N188 (= N191), V189 (≠ I193), D218 (= D222), D242 (= D246)
- binding manganese (ii) ion: D242 (= D246), D246 (= D250)
2y42D Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with nadh and mn (see paper)
36% identity, 98% coverage: 4:350/354 of query aligns to 1:342/355 of 2y42D