SitesBLAST
Comparing WP_016197539.1 NCBI__GCF_000403135.1:WP_016197539.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
47% identity, 97% coverage: 4:346/354 of query aligns to 3:347/357 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)
47% identity, 97% coverage: 4:346/354 of query aligns to 3:347/358 of Q56268
- R95 (= R97) binding substrate
- R105 (= R107) binding substrate
- R133 (= R135) binding substrate
- D222 (= D221) binding Mg(2+); binding substrate
- D246 (= D245) binding Mg(2+)
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)
48% identity, 98% coverage: 2:347/354 of query aligns to 42:391/405 of P93832
- 114:129 (vs. 74:90, 47% 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 (= K189) Important for catalysis; mutation to M: Loss of activity toward 3-isopropylmalate.
- N234 (= N191) binding NAD(+); mutation N->A,D: Loss of activity toward 3-isopropylmalate.
- V235 (= V192) mutation to A: Reduced activity toward 3-isopropylmalate.
- D264 (= D221) binding Mg(2+); binding substrate; mutation to N: Loss of activity toward 3-isopropylmalate.
- N265 (≠ A222) binding NAD(+)
- D288 (= D245) binding Mg(2+); mutation to N: Loss of activity toward 3-isopropylmalate.
- D292 (= D249) binding Mg(2+); mutation to N: Reduced activity toward 3-isopropylmalate.
- 318:334 (vs. 274:290, 71% identical) binding NAD(+)
5j32A Isopropylmalate dehydrogenase in complex with isopropylmalate (see paper)
48% identity, 98% coverage: 2:347/354 of query aligns to 12:361/369 of 5j32A
5j33A Isopropylmalate dehydrogenase in complex with NAD+ (see paper)
48% identity, 98% coverage: 2:347/354 of query aligns to 2:351/360 of 5j33A
- active site: Y141 (= Y142), K192 (= K189), D224 (= D221), D248 (= D245), D252 (= D249)
- binding magnesium ion: D248 (= D245), D252 (= D249)
- binding nicotinamide-adenine-dinucleotide: I74 (= I74), E89 (= E90), L92 (= L93), I261 (≠ M258), E278 (= E274), H281 (= H277), G282 (= G278), S283 (= S279), A284 (≠ Y280), I287 (≠ A283), N294 (= N290), D335 (= D331)
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)
47% identity, 98% coverage: 2:347/354 of query aligns to 43:392/404 of Q9SA14
- L134 (= L94) Confers substrate specificity; mutation to F: Enhanced activity toward 3-(2'-methylthio)-ethylmalate, but reduced catalytic efficiency with 3-isopropylmalate.
4xxvA Crystal structure of 3-isopropylmalate dehydrogenase from burkholderia thailandensis in complex with NAD
46% identity, 99% coverage: 3:353/354 of query aligns to 2:356/356 of 4xxvA
4iwhA Crystal structure of a 3-isopropylmalate dehydrogenase from burkholderia pseudomallei
46% identity, 99% coverage: 3:353/354 of query aligns to 4:358/358 of 4iwhA
6xxyA Crystal structure of haemophilus influenzae 3-isopropylmalate dehydrogenase in complex with o-isobutenyl oxalylhydroxamate. (see paper)
48% identity, 93% coverage: 4:332/354 of query aligns to 5:338/358 of 6xxyA
- active site: Y144 (= Y142), K194 (= K189), D226 (= D221), D250 (= D245)
- binding magnesium ion: D250 (= D245), D254 (= D249)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ A73), V75 (≠ I74), G76 (= G75), E90 (= E90), L94 (= L93), Y224 (≠ F219), N227 (≠ A222), M230 (= M225), M263 (= M258), G264 (= G259), E280 (= E274), G283 (≠ H277), G284 (= G278), S285 (= S279), A286 (≠ Y280), P287 (= P281), D288 (≠ Q282), I289 (≠ A283), N296 (= N290), D337 (= D331)
- binding 2-(2-methylprop-2-enoxyamino)-2-oxidanylidene-ethanoic acid: E90 (= E90), R108 (= R107), R137 (= R135), K194 (= K189), V197 (= V192), D226 (= D221), D250 (= D245)
2ztwA Structure of 3-isopropylmalate dehydrogenase in complex with the inhibitor and NAD+ (see paper)
49% identity, 91% coverage: 3:325/354 of query aligns to 1:321/345 of 2ztwA
- active site: Y139 (= Y142), K185 (= K189), D217 (= D221), D241 (= D245), D245 (= D249)
- binding magnesium ion: G203 (≠ E207), Y206 (= Y210), V209 (= V213)
- binding nicotinamide-adenine-dinucleotide: I11 (= I13), H273 (= H277), G274 (= G278), A276 (≠ Y280), D278 (≠ Q282), I279 (≠ A283), A285 (= A289), N286 (= N290)
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, 91% coverage: 3:325/354 of query aligns to 1:321/345 of Q5SIY4
- 74:87 (vs. 76:90, 40% identical) binding NAD(+)
- Y139 (= Y142) mutation to F: Large decrease in activity and a small decrease in substrate affinity.
- 274:286 (vs. 278:290, 62% identical) binding NAD(+)
2y41A Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with ipm and mn (see paper)
49% identity, 91% coverage: 3:325/354 of query aligns to 2:322/346 of 2y41A
2y42D Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with nadh and mn (see paper)
49% identity, 91% coverage: 3:325/354 of query aligns to 2:322/355 of 2y42D