SitesBLAST
Comparing WP_012991633.1 NCBI__GCF_000025605.1:WP_012991633.1 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)
1a05A Crystal structure of the complex of 3-isopropylmalate dehydrogenase from thiobacillus ferrooxidans with 3-isopropylmalate (see paper)
57% identity, 98% coverage: 5:357/361 of query aligns to 3:355/357 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)
57% identity, 98% coverage: 5:357/361 of query aligns to 3:355/358 of Q56268
- R95 (= R97) binding substrate
- R105 (= R107) binding substrate
- R133 (= R135) binding substrate
- D222 (= D224) binding Mg(2+); binding substrate
- D246 (= D248) binding Mg(2+)
4iwhA Crystal structure of a 3-isopropylmalate dehydrogenase from burkholderia pseudomallei
56% identity, 98% coverage: 4:356/361 of query aligns to 4:358/358 of 4iwhA
4xxvA Crystal structure of 3-isopropylmalate dehydrogenase from burkholderia thailandensis in complex with NAD
56% identity, 98% coverage: 4:356/361 of query aligns to 2:356/356 of 4xxvA
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)
57% identity, 98% coverage: 4:357/361 of query aligns to 43:398/405 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 (= K192) Important for catalysis; mutation to M: Loss of activity toward 3-isopropylmalate.
- N234 (= N194) binding NAD(+); mutation N->A,D: Loss of activity toward 3-isopropylmalate.
- V235 (= V195) mutation to A: Reduced activity toward 3-isopropylmalate.
- D264 (= D224) binding Mg(2+); binding substrate; mutation to N: Loss of activity toward 3-isopropylmalate.
- N265 (= N225) binding NAD(+)
- D288 (= D248) binding Mg(2+); mutation to N: Loss of activity toward 3-isopropylmalate.
- D292 (= D252) binding Mg(2+); mutation to N: Reduced activity toward 3-isopropylmalate.
- 318:334 (vs. 277:293, 76% identical) binding NAD(+)
5j33A Isopropylmalate dehydrogenase in complex with NAD+ (see paper)
57% identity, 98% coverage: 4:357/361 of query aligns to 3:358/360 of 5j33A
- active site: Y141 (= Y142), K192 (= K192), D224 (= D224), D248 (= D248), D252 (= D252)
- binding magnesium ion: D248 (= D248), D252 (= D252)
- binding nicotinamide-adenine-dinucleotide: I74 (≠ V75), E89 (= E90), L92 (= L93), I261 (≠ L261), E278 (= E277), H281 (= H280), G282 (= G281), S283 (= S282), A284 (= A283), I287 (= I286), N294 (= N293), D335 (= D334)
5j32A Isopropylmalate dehydrogenase in complex with isopropylmalate (see paper)
57% identity, 98% coverage: 4:357/361 of query aligns to 13:368/369 of 5j32A
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)
54% identity, 98% coverage: 4:357/361 of query aligns to 44:399/404 of Q9SA14
- L134 (= L94) Confers substrate specificity; mutation to F: Enhanced activity toward 3-(2'-methylthio)-ethylmalate, but reduced catalytic efficiency with 3-isopropylmalate.
6xxyA Crystal structure of haemophilus influenzae 3-isopropylmalate dehydrogenase in complex with o-isobutenyl oxalylhydroxamate. (see paper)
53% identity, 99% coverage: 1:356/361 of query aligns to 1:358/358 of 6xxyA
- active site: Y144 (= Y142), K194 (= K192), D226 (= D224), D250 (= D248)
- binding magnesium ion: D250 (= D248), D254 (= D252)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ A74), V75 (= V75), G76 (= G76), E90 (= E90), L94 (= L93), Y224 (= Y222), N227 (= N225), M230 (= M228), M263 (≠ L261), G264 (= G262), E280 (= E277), G283 (≠ H280), G284 (= G281), S285 (= S282), A286 (= A283), P287 (= P284), D288 (= D285), I289 (= I286), N296 (= N293), D337 (= D334)
- binding 2-(2-methylprop-2-enoxyamino)-2-oxidanylidene-ethanoic acid: E90 (= E90), R108 (= R107), R137 (= R135), K194 (= K192), V197 (= V195), D226 (= D224), D250 (= D248)
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)
53% identity, 98% coverage: 4:357/361 of query aligns to 47:402/409 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 (≠ T188) Essential for redox regulation; mutation to S: Reduced sensitivity to oxidation on enzyme activity regulation.
- C390 (≠ T345) Essential for redox regulation; mutation to S: Reduced sensitivity to oxidation on enzyme activity regulation.
2y41A Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with ipm and mn (see paper)
56% identity, 98% coverage: 4:356/361 of query aligns to 2:345/346 of 2y41A
2ztwA Structure of 3-isopropylmalate dehydrogenase in complex with the inhibitor and NAD+ (see paper)
56% identity, 98% coverage: 4:356/361 of query aligns to 1:344/345 of 2ztwA
- active site: Y139 (= Y142), K185 (= K192), D217 (= D224), D241 (= D248), D245 (= D252)
- binding magnesium ion: G203 (≠ S210), Y206 (≠ F213), V209 (= V216)
- binding nicotinamide-adenine-dinucleotide: I11 (= I14), H273 (= H280), G274 (= G281), A276 (= A283), D278 (= D285), I279 (= I286), A285 (= A292), N286 (= N293)
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)
56% identity, 98% coverage: 4:356/361 of query aligns to 1:344/345 of Q5SIY4