SitesBLAST
Comparing CCNA_00193 FitnessBrowser__Caulo:CCNA_00193 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)
53% identity, 99% coverage: 3:350/350 of query aligns to 44:397/405 of P93832
- 114:129 (vs. 69:84, 56% identical) binding
- L132 (= L87) mutation to A: Reduced activity toward 3-isopropylmalate.
- L133 (= L88) 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 (= R91) binding ; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- R146 (= R101) binding ; mutation to A: Reduced activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- R174 (= R129) binding ; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- Y181 (= Y136) 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 ; mutation N->A,D: Loss of activity toward 3-isopropylmalate.
- V235 (= V190) mutation to A: Reduced activity toward 3-isopropylmalate.
- D264 (= D220) binding ; binding ; mutation to N: Loss of activity toward 3-isopropylmalate.
- N265 (= N221) binding
- D288 (= D244) binding ; mutation to N: Loss of activity toward 3-isopropylmalate.
- D292 (= D248) binding ; mutation to N: Reduced activity toward 3-isopropylmalate.
- 318:334 (vs. 275:291, 82% identical) binding
5j32A Isopropylmalate dehydrogenase in complex with isopropylmalate (see paper)
53% identity, 99% coverage: 3:350/350 of query aligns to 14:367/369 of 5j32A
- active site: L18 (= L7), Y151 (= Y136), K202 (= K187), D234 (= D220), D258 (= D244), D262 (= D248)
- binding 3-isopropylmalic acid: R106 (= R91), R144 (= R129), Y151 (= Y136), K202 (= K187), D234 (= D220), D258 (= D244)
- binding magnesium ion: D258 (= D244), D262 (= D248)
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)
53% identity, 99% coverage: 3:350/350 of query aligns to 45:398/404 of Q9SA14
- L134 (= L88) Confers substrate specificity; mutation to F: Enhanced activity toward 3-(2'-methylthio)-ethylmalate, but reduced catalytic efficiency with 3-isopropylmalate.
5j33A Isopropylmalate dehydrogenase in complex with NAD+ (see paper)
53% identity, 99% coverage: 3:350/350 of query aligns to 4:357/360 of 5j33A
- active site: Y141 (= Y136), K192 (= K187), D224 (= D220), D248 (= D244), D252 (= D248)
- binding magnesium ion: D248 (= D244), D252 (= D248)
- binding nicotinamide-adenine-dinucleotide: I13 (= I12), A73 (= A68), I74 (≠ V69), G75 (= G70), E89 (= E84), L92 (= L87), N194 (= N189), Y222 (≠ L218), D224 (= D220), N225 (= N221), I261 (≠ L257), G262 (= G258), E278 (= E275), H281 (= H278), G282 (= G279), S283 (= S280), A284 (= A281), P285 (= P282), D286 (= D283), I287 (= I284), A293 (= A290), N294 (= N291), D335 (= D332)
4iwhA Crystal structure of a 3-isopropylmalate dehydrogenase from burkholderia pseudomallei
53% identity, 99% coverage: 4:350/350 of query aligns to 6:358/358 of 4iwhA
4xxvA Crystal structure of 3-isopropylmalate dehydrogenase from burkholderia thailandensis in complex with NAD
53% identity, 99% coverage: 4:350/350 of query aligns to 4:356/356 of 4xxvA
1a05A Crystal structure of the complex of 3-isopropylmalate dehydrogenase from thiobacillus ferrooxidans with 3- isopropylmalate (see paper)
53% identity, 100% coverage: 1:350/350 of query aligns to 1:354/357 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)
53% identity, 100% coverage: 1:350/350 of query aligns to 1:354/358 of Q56268
- R95 (= R91) binding
- R105 (= R101) binding
- R133 (= R129) binding
- D222 (= D220) binding ; binding
- D246 (= D244) binding
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)
52% identity, 99% coverage: 3:350/350 of query aligns to 48:401/409 of Q9FMT1
- F137 (≠ L88) Confers substrate specificity; mutation to L: Reduced activity toward 3-(2'-methylthio)-ethylmalate, but enhanced catalytic efficiency with 3-isopropylmalate.
- C232 (≠ H183) Essential for redox regulation; mutation to S: Reduced sensitivity to oxidation on enzyme activity regulation.
- C390 (≠ T339) 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)
49% identity, 98% coverage: 4:346/350 of query aligns to 7:355/363 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)
49% identity, 98% coverage: 4:346/350 of query aligns to 7:355/363 of P37412
- D227 (= D220) binding
- D251 (= D244) binding
- D255 (= D248) binding
6xxyA Crystal structure of haemophilus influenzae 3-isopropylmalate dehydrogenase in complex with o-isobutenyl oxalylhydroxamate. (see paper)
49% identity, 99% coverage: 3:350/350 of query aligns to 5:358/358 of 6xxyA
- active site: Y144 (= Y136), K194 (= K187), D226 (= D220), D250 (= D244)
- binding magnesium ion: D250 (= D244), D254 (= D248)
- binding nicotinamide-adenine-dinucleotide: I14 (= I12), S74 (≠ A68), V75 (= V69), G76 (= G70), G77 (= G71), E90 (= E84), L94 (= L87), N196 (= N189), Y224 (≠ L218), N227 (= N221), M230 (= M224), M263 (≠ L257), G264 (= G258), E280 (= E275), G283 (≠ H278), G284 (= G279), S285 (= S280), A286 (= A281), P287 (= P282), D288 (= D283), I289 (= I284), A295 (= A290), N296 (= N291), D337 (= D332)
- binding 2-(2-methylprop-2-enoxyamino)-2-oxidanylidene-ethanoic acid: E90 (= E84), L94 (= L87), L95 (= L88), R98 (= R91), R108 (= R101), R137 (= R129), K194 (= K187), V197 (= V190), D226 (= D220), D250 (= D244), A282 (≠ I277)
3vkzA 3-isopropylmalate dehydrogenase from shewanella oneidensis mr-1 at atmospheric pressure (see paper)
48% identity, 99% coverage: 4:350/350 of query aligns to 5:360/364 of 3vkzA