SitesBLAST
Comparing WP_084275692.1 NCBI__GCF_900176045.1:WP_084275692.1 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)
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)
61% identity, 97% coverage: 2:346/356 of query aligns to 41:390/405 of P93832
- 114:129 (vs. 75:90, 50% 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 (= K188) Important for catalysis; mutation to M: Loss of activity toward 3-isopropylmalate.
- N234 (= N190) binding NAD(+); mutation N->A,D: Loss of activity toward 3-isopropylmalate.
- V235 (= V191) mutation to A: Reduced activity toward 3-isopropylmalate.
- D264 (= D220) binding Mg(2+); binding substrate; mutation to N: Loss of activity toward 3-isopropylmalate.
- N265 (= N221) binding NAD(+)
- D288 (= D244) binding Mg(2+); mutation to N: Loss of activity toward 3-isopropylmalate.
- D292 (= D248) binding Mg(2+); mutation to N: Reduced activity toward 3-isopropylmalate.
- 318:334 (vs. 273:289, 88% identical) binding NAD(+)
5j32A Isopropylmalate dehydrogenase in complex with isopropylmalate (see paper)
61% identity, 97% coverage: 2:346/356 of query aligns to 11:360/369 of 5j32A
5j33A Isopropylmalate dehydrogenase in complex with NAD+ (see paper)
61% identity, 97% coverage: 2:346/356 of query aligns to 1:350/360 of 5j33A
- active site: Y141 (= Y142), K192 (= K188), D224 (= D220), D248 (= D244), D252 (= D248)
- binding magnesium ion: D248 (= D244), D252 (= D248)
- binding nicotinamide-adenine-dinucleotide: I74 (= I75), E89 (= E90), L92 (= L93), I261 (= I257), E278 (= E273), H281 (= H276), G282 (= G277), S283 (= S278), A284 (= A279), I287 (= I282), N294 (= N289), D335 (= D330)
6xxyA Crystal structure of haemophilus influenzae 3-isopropylmalate dehydrogenase in complex with o-isobutenyl oxalylhydroxamate. (see paper)
56% identity, 99% coverage: 1:351/356 of query aligns to 1:356/358 of 6xxyA
- active site: Y144 (= Y142), K194 (= K188), D226 (= D220), D250 (= D244)
- binding magnesium ion: D250 (= D244), D254 (= D248)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ A74), V75 (≠ I75), G76 (= G76), E90 (= E90), L94 (= L93), Y224 (= Y218), N227 (= N221), M230 (= M224), M263 (≠ I257), G264 (= G258), E280 (= E273), G283 (≠ H276), G284 (= G277), S285 (= S278), A286 (= A279), P287 (= P280), D288 (= D281), I289 (= I282), N296 (= N289), D337 (= D330)
- binding 2-(2-methylprop-2-enoxyamino)-2-oxidanylidene-ethanoic acid: E90 (= E90), R108 (= R107), R137 (= R135), K194 (= K188), V197 (= V191), D226 (= D220), D250 (= D244)
Q9SA14 3-isopropylmalate dehydrogenase 3, chloroplastic; 3-IPM-DH 3; AtIMDH2; AtIMDH3; IMDH 3; Beta-IPM dehydrogenase 3; Isopropylmalate dehydrogenase 3; AtIMD3; EC 1.1.1.85 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
59% identity, 97% coverage: 2:346/356 of query aligns to 42:391/404 of Q9SA14
- L134 (= L94) Confers substrate specificity; mutation to F: Enhanced activity toward 3-(2'-methylthio)-ethylmalate, but reduced catalytic efficiency with 3-isopropylmalate.
1a05A Crystal structure of the complex of 3-isopropylmalate dehydrogenase from thiobacillus ferrooxidans with 3-isopropylmalate (see paper)
56% identity, 97% coverage: 6:349/356 of query aligns to 4:350/357 of 1a05A
Q56268 3-isopropylmalate dehydrogenase; 3-IPM-DH; Beta-IPM dehydrogenase; IMDH; EC 1.1.1.85 from Acidithiobacillus ferrooxidans (Thiobacillus ferrooxidans) (see paper)
56% identity, 97% coverage: 6:349/356 of query aligns to 4:350/358 of Q56268
- R95 (= R97) binding substrate
- R105 (= R107) binding substrate
- R133 (= R135) binding substrate
- D222 (= D220) binding Mg(2+); binding substrate
- D246 (= D244) binding Mg(2+)
Q9FMT1 3-isopropylmalate dehydrogenase 1, chloroplastic; 3-IPM-DH 1; AtIMDH1; IMDH 1; Beta-IPM dehydrogenase 1; Isopropylmalate dehydrogenase 1; AtIMD1; Methylthioalkylmalate dehydrogenase 1; EC 1.1.1.85 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
59% identity, 97% coverage: 2:346/356 of query aligns to 45:394/409 of Q9FMT1
- F137 (≠ L94) Confers substrate specificity; mutation to L: Reduced activity toward 3-(2'-methylthio)-ethylmalate, but enhanced catalytic efficiency with 3-isopropylmalate.
- C232 (≠ V184) Essential for redox regulation; mutation to S: Reduced sensitivity to oxidation on enzyme activity regulation.
- C390 (≠ T342) Essential for redox regulation; mutation to S: Reduced sensitivity to oxidation on enzyme activity regulation.
4iwhA Crystal structure of a 3-isopropylmalate dehydrogenase from burkholderia pseudomallei
56% identity, 97% coverage: 6:350/356 of query aligns to 6:356/358 of 4iwhA
4xxvA Crystal structure of 3-isopropylmalate dehydrogenase from burkholderia thailandensis in complex with NAD
56% identity, 97% coverage: 6:350/356 of query aligns to 4:354/356 of 4xxvA
1cnzA 3-isopropylmalate dehydrogenase (ipmdh) from salmonella typhimurium (see paper)
52% identity, 99% coverage: 2:355/356 of query aligns to 3:361/363 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)
52% identity, 99% coverage: 2:355/356 of query aligns to 3:361/363 of P37412
- D227 (= D220) binding Mn(2+)
- D251 (= D244) binding Mn(2+)
- D255 (= D248) binding Mn(2+)
2y41A Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with ipm and mn (see paper)
55% identity, 96% coverage: 6:348/356 of query aligns to 4:345/346 of 2y41A