SitesBLAST
Comparing Dsui_3198 FitnessBrowser__PS:Dsui_3198 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)
4iwhA Crystal structure of a 3-isopropylmalate dehydrogenase from burkholderia pseudomallei
69% identity, 100% coverage: 1:354/354 of query aligns to 4:358/358 of 4iwhA
4xxvA Crystal structure of 3-isopropylmalate dehydrogenase from burkholderia thailandensis in complex with NAD
69% identity, 100% coverage: 1:354/354 of query aligns to 2:356/356 of 4xxvA
1a05A Crystal structure of the complex of 3-isopropylmalate dehydrogenase from thiobacillus ferrooxidans with 3-isopropylmalate (see paper)
64% identity, 100% coverage: 2:354/354 of query aligns to 3:354/357 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)
64% identity, 100% coverage: 2:354/354 of query aligns to 3:354/358 of Q56268
- R95 (= R90) binding substrate
- R105 (= R100) binding substrate
- R133 (= R128) binding substrate
- D222 (= D221) binding Mg(2+); binding substrate
- D246 (= D245) binding Mg(2+)
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, 99% coverage: 3:354/354 of query aligns to 46:398/404 of Q9SA14
- L134 (= L87) Confers substrate specificity; mutation to F: Enhanced activity toward 3-(2'-methylthio)-ethylmalate, but reduced catalytic efficiency with 3-isopropylmalate.
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)
59% identity, 99% coverage: 3:354/354 of query aligns to 45:397/405 of P93832
- 114:129 (vs. 68:83, 44% identical) binding NAD(+)
- L132 (= L86) mutation to A: Reduced activity toward 3-isopropylmalate.
- L133 (= L87) 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 (= R90) binding substrate; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- R146 (= R100) binding substrate; mutation to A: Reduced activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- R174 (= R128) binding substrate; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- Y181 (= Y135) 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 (= N222) 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. 275:291, 76% identical) binding NAD(+)
5j32A Isopropylmalate dehydrogenase in complex with isopropylmalate (see paper)
59% identity, 99% coverage: 3:354/354 of query aligns to 15:367/369 of 5j32A
5j33A Isopropylmalate dehydrogenase in complex with NAD+ (see paper)
59% identity, 99% coverage: 3:354/354 of query aligns to 5:357/360 of 5j33A
- active site: Y141 (= Y135), K192 (= K189), D224 (= D221), D248 (= D245), D252 (= D249)
- binding magnesium ion: D248 (= D245), D252 (= D249)
- binding nicotinamide-adenine-dinucleotide: I74 (≠ V68), E89 (= E83), L92 (= L86), I261 (= I258), E278 (= E275), H281 (= H278), G282 (= G279), S283 (= S280), A284 (= A281), I287 (= I284), N294 (= N291), D335 (= D332)
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)
57% identity, 99% coverage: 3:354/354 of query aligns to 49:401/409 of Q9FMT1
- F137 (≠ L87) Confers substrate specificity; mutation to L: Reduced activity toward 3-(2'-methylthio)-ethylmalate, but enhanced catalytic efficiency with 3-isopropylmalate.
- C232 (= C185) Essential for redox regulation; mutation to S: Reduced sensitivity to oxidation on enzyme activity regulation.
- C390 (≠ T343) Essential for redox regulation; mutation to S: Reduced sensitivity to oxidation on enzyme activity regulation.
1cnzA 3-isopropylmalate dehydrogenase (ipmdh) from salmonella typhimurium (see paper)
53% identity, 99% coverage: 2:350/354 of query aligns to 6:355/363 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)
53% identity, 99% coverage: 2:350/354 of query aligns to 6:355/363 of P37412
- D227 (= D221) binding Mn(2+)
- D251 (= D245) binding Mn(2+)
- D255 (= D249) binding Mn(2+)
6xxyA Crystal structure of haemophilus influenzae 3-isopropylmalate dehydrogenase in complex with o-isobutenyl oxalylhydroxamate. (see paper)
54% identity, 99% coverage: 3:354/354 of query aligns to 6:358/358 of 6xxyA
- active site: Y144 (= Y135), K194 (= K189), D226 (= D221), D250 (= D245)
- binding magnesium ion: D250 (= D245), D254 (= D249)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ A67), V75 (= V68), G76 (= G69), E90 (= E83), L94 (= L86), Y224 (≠ L219), N227 (= N222), M230 (= M225), M263 (≠ I258), G264 (= G259), E280 (= E275), G283 (≠ H278), G284 (= G279), S285 (= S280), A286 (= A281), P287 (= P282), D288 (= D283), I289 (= I284), N296 (= N291), D337 (= D332)
- binding 2-(2-methylprop-2-enoxyamino)-2-oxidanylidene-ethanoic acid: E90 (= E83), R108 (= R100), R137 (= R128), K194 (= K189), V197 (= V192), D226 (= D221), D250 (= D245)
2y42D Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with nadh and mn (see paper)
57% identity, 92% coverage: 1:326/354 of query aligns to 2:322/355 of 2y42D