SitesBLAST
Comparing 351385 FitnessBrowser__Btheta:351385 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)
1cnzA 3-isopropylmalate dehydrogenase (ipmdh) from salmonella typhimurium (see paper)
46% identity, 100% coverage: 2:353/353 of query aligns to 4:362/363 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)
46% identity, 100% coverage: 2:353/353 of query aligns to 4:362/363 of P37412
- D227 (= D219) binding Mn(2+)
- D251 (= D243) binding Mn(2+)
- D255 (= D247) binding Mn(2+)
2y41A Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with ipm and mn (see paper)
49% identity, 92% coverage: 2:327/353 of query aligns to 1:324/346 of 2y41A
2y42D Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with nadh and mn (see paper)
49% identity, 92% coverage: 2:327/353 of query aligns to 1:324/355 of 2y42D
- active site: Y140 (= Y142), K186 (= K187), D218 (= D219), D242 (= D243), D246 (= D247)
- binding manganese (ii) ion: D242 (= D243), D246 (= D247)
- binding nicotinamide-adenine-dinucleotide: I12 (= I13), D79 (= D80), H274 (= H275), G275 (= G276), A277 (≠ W278), D279 (≠ Q280), I280 (≠ A281), N287 (= N288)
2ztwA Structure of 3-isopropylmalate dehydrogenase in complex with the inhibitor and NAD+ (see paper)
49% identity, 92% coverage: 3:327/353 of query aligns to 1:323/345 of 2ztwA
- active site: Y139 (= Y142), K185 (= K187), D217 (= D219), D241 (= D243), D245 (= D247)
- binding magnesium ion: G203 (≠ A205), Y206 (= Y208), V209 (= V211)
- binding nicotinamide-adenine-dinucleotide: I11 (= I13), H273 (= H275), G274 (= G276), A276 (≠ W278), D278 (≠ Q280), I279 (≠ A281), A285 (= A287), N286 (= N288)
Q5SIY4 3-isopropylmalate dehydrogenase; 3-IPM-DH; Beta-IPM dehydrogenase; IMDH; EC 1.1.1.85 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see 2 papers)
49% identity, 92% coverage: 3:327/353 of query aligns to 1:323/345 of Q5SIY4
- 74:87 (vs. 76:90, 53% identical) binding NAD(+)
- Y139 (= Y142) mutation to F: Large decrease in activity and a small decrease in substrate affinity.
- 274:286 (vs. 276:288, 54% identical) binding NAD(+)
Q56268 3-isopropylmalate dehydrogenase; 3-IPM-DH; Beta-IPM dehydrogenase; IMDH; EC 1.1.1.85 from Acidithiobacillus ferrooxidans (Thiobacillus ferrooxidans) (see paper)
46% identity, 99% coverage: 4:351/353 of query aligns to 3:355/358 of Q56268
- R95 (= R97) binding substrate
- R105 (= R107) binding substrate
- R133 (= R135) binding substrate
- D222 (= D219) binding Mg(2+); binding substrate
- D246 (= D243) binding Mg(2+)
1a05A Crystal structure of the complex of 3-isopropylmalate dehydrogenase from thiobacillus ferrooxidans with 3-isopropylmalate (see paper)
46% identity, 99% coverage: 4:351/353 of query aligns to 3:355/357 of 1a05A
6xxyA Crystal structure of haemophilus influenzae 3-isopropylmalate dehydrogenase in complex with o-isobutenyl oxalylhydroxamate. (see paper)
47% identity, 99% coverage: 3:350/353 of query aligns to 4:358/358 of 6xxyA
- active site: Y144 (= Y142), K194 (= K187), D226 (= D219), D250 (= D243)
- binding magnesium ion: D250 (= D243), D254 (= D247)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ A73), V75 (= V74), G76 (= G75), E90 (= E90), L94 (= L93), Y224 (≠ F217), N227 (= N220), M230 (= M223), M263 (= M256), G264 (= G257), E280 (= E272), G283 (≠ H275), G284 (= G276), S285 (= S277), A286 (≠ W278), P287 (= P279), D288 (≠ Q280), I289 (≠ A281), N296 (= N288), D337 (≠ E328)
- binding 2-(2-methylprop-2-enoxyamino)-2-oxidanylidene-ethanoic acid: E90 (= E90), R108 (= R107), R137 (= R135), K194 (= K187), V197 (= V190), D226 (= D219), D250 (= D243)
5j33A Isopropylmalate dehydrogenase in complex with NAD+ (see paper)
45% identity, 99% coverage: 3:350/353 of query aligns to 3:357/360 of 5j33A
- active site: Y141 (= Y142), K192 (= K187), D224 (= D219), D248 (= D243), D252 (= D247)
- binding magnesium ion: D248 (= D243), D252 (= D247)
- binding nicotinamide-adenine-dinucleotide: I74 (≠ V74), E89 (= E90), L92 (= L93), I261 (≠ M256), E278 (= E272), H281 (= H275), G282 (= G276), S283 (= S277), A284 (≠ W278), I287 (≠ A281), N294 (= N288), D335 (≠ E328)
P93832 3-isopropylmalate dehydrogenase 2, chloroplastic; 3-IPM-DH 2; AtIMDH2; AtIMDH3; IMDH 2; Beta-IPM dehydrogenase 2; Isopropylmalate dehydrogenase 2; AtIMD2; EC 1.1.1.85 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
45% identity, 99% coverage: 3:350/353 of query aligns to 43:397/405 of P93832
- 114:129 (vs. 74:90, 41% identical) binding NAD(+)
- L132 (= L93) mutation to A: Reduced activity toward 3-isopropylmalate.
- L133 (= L94) Confers substrate specificity; mutation to A: Reduced activity toward 3-isopropylmalate.; mutation to F: Enhanced activity toward 3-(2'-methylthio)-ethylmalate, but reduced catalytic efficiency with 3-isopropylmalate.
- R136 (= R97) binding substrate; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- R146 (= R107) binding substrate; mutation to A: Reduced activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- R174 (= R135) binding substrate; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- Y181 (= Y142) Important for catalysis; mutation Y->A,F,H: Reduced activity toward 3-isopropylmalate.
- K232 (= K187) Important for catalysis; mutation to M: Loss of activity toward 3-isopropylmalate.
- N234 (= N189) binding NAD(+); mutation N->A,D: Loss of activity toward 3-isopropylmalate.
- V235 (= V190) mutation to A: Reduced activity toward 3-isopropylmalate.
- D264 (= D219) binding Mg(2+); binding substrate; mutation to N: Loss of activity toward 3-isopropylmalate.
- N265 (= N220) binding NAD(+)
- D288 (= D243) binding Mg(2+); mutation to N: Loss of activity toward 3-isopropylmalate.
- D292 (= D247) binding Mg(2+); mutation to N: Reduced activity toward 3-isopropylmalate.
- 318:334 (vs. 272:288, 59% identical) binding NAD(+)
5j32A Isopropylmalate dehydrogenase in complex with isopropylmalate (see paper)
45% identity, 99% coverage: 3:350/353 of query aligns to 13:367/369 of 5j32A
3vkzA 3-isopropylmalate dehydrogenase from shewanella oneidensis mr-1 at atmospheric pressure (see paper)
44% identity, 99% coverage: 3:351/353 of query aligns to 3:361/364 of 3vkzA