SitesBLAST

Comparing Pf1N1B4_12 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_12 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Found 20 (the maximum) hits to proteins with known functional sites

4xxvA Crystal structure of 3-isopropylmalate dehydrogenase from burkholderia thailandensis in complex with NAD
67% identity, 98% coverage: 4:357/360 of query aligns to 3:356/356 of 4xxvA

• active site: Y136 (= Y141), K191 (= K192), D223 (= D224), D247 (= D248), D251 (= D252)
• binding nicotinamide-adenine-dinucleotide: N193 (= N194), Y221 (= Y222), N224 (= N225)

4iwhA Crystal structure of a 3-isopropylmalate dehydrogenase from burkholderia pseudomallei
67% identity, 98% coverage: 4:357/360 of query aligns to 5:358/358 of 4iwhA

• active site: Y138 (= Y141), K193 (= K192), D225 (= D224), D249 (= D248), D253 (= D252)
• binding magnesium ion: D249 (= D248), D253 (= D252)

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)
60% identity, 98% coverage: 5:357/360 of query aligns to 45:397/405 of P93832

• 114:129 (vs. 74:89, 56% identical) binding NAD(+)
• L132 (= L92) mutation to A: Reduced activity toward 3-isopropylmalate.
• L133 (= L93) 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 (= R96) binding substrate; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
• R146 (= R106) binding substrate; mutation to A: Reduced activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
• R174 (= R134) binding substrate; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
• Y181 (= Y141) 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. 278:294, 76% identical) binding NAD(+)

5j32A Isopropylmalate dehydrogenase in complex with isopropylmalate (see paper)
60% identity, 98% coverage: 5:357/360 of query aligns to 15:367/369 of 5j32A

• active site: L18 (= L8), Y151 (= Y141), K202 (= K192), D234 (= D224), D258 (= D248), D262 (= D252)
• binding 3-isopropylmalic acid: R106 (= R96), R144 (= R134), Y151 (= Y141), D258 (= D248)
• binding magnesium ion: D258 (= D248), D262 (= D252)

5j33A Isopropylmalate dehydrogenase in complex with NAD+ (see paper)
60% identity, 98% coverage: 5:357/360 of query aligns to 5:357/360 of 5j33A

• active site: Y141 (= Y141), K192 (= K192), D224 (= D224), D248 (= D248), D252 (= D252)
• binding magnesium ion: D248 (= D248), D252 (= D252)
• binding nicotinamide-adenine-dinucleotide: I74 (≠ V74), E89 (= E89), L92 (= L92), I261 (= I261), E278 (= E278), H281 (= H281), G282 (= G282), S283 (= S283), A284 (= A284), I287 (= I287), N294 (= N294), D335 (= D335)

Q56268 3-isopropylmalate dehydrogenase; 3-IPM-DH; Beta-IPM dehydrogenase; IMDH; EC 1.1.1.85 from Acidithiobacillus ferrooxidans (Thiobacillus ferrooxidans) (see paper)
61% identity, 99% coverage: 3:357/360 of query aligns to 2:354/358 of Q56268

• R95 (= R96) binding substrate
• R105 (= R106) binding substrate
• R133 (= R134) binding substrate
• D222 (= D224) binding Mg(2+); binding substrate
• D246 (= D248) 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)
60% identity, 98% coverage: 4:357/360 of query aligns to 45:398/404 of Q9SA14

• L134 (= L93) 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)
61% identity, 99% coverage: 3:357/360 of query aligns to 2:354/357 of 1a05A

• active site: Y140 (= Y141), K190 (= K192), D222 (= D224), D246 (= D248), D250 (= D252)
• binding 3-isopropylmalic acid: R95 (= R96), R105 (= R106), R133 (= R134), Y140 (= Y141), D246 (= 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)
58% identity, 99% coverage: 4:359/360 of query aligns to 48:403/409 of Q9FMT1

• F137 (≠ L93) Confers substrate specificity; mutation to L: Reduced activity toward 3-(2'-methylthio)-ethylmalate, but enhanced catalytic efficiency with 3-isopropylmalate.
• C232 (= C188) Essential for redox regulation; mutation to S: Reduced sensitivity to oxidation on enzyme activity regulation.
• C390 (≠ T346) 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)
56% identity, 98% coverage: 1:353/360 of query aligns to 1:355/363 of 1cnzA

• active site: Y145 (= Y141), K195 (= K192), D227 (= D224), D251 (= D248)
• binding manganese (ii) ion: D251 (= D248), D255 (= D252)

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)
56% identity, 98% coverage: 1:353/360 of query aligns to 1:355/363 of P37412

• D227 (= D224) binding Mn(2+)
• D251 (= D248) binding Mn(2+)
• D255 (= D252) binding Mn(2+)

6xxyA Crystal structure of haemophilus influenzae 3-isopropylmalate dehydrogenase in complex with o-isobutenyl oxalylhydroxamate. (see paper)
56% identity, 99% coverage: 2:357/360 of query aligns to 3:358/358 of 6xxyA

• active site: Y144 (= Y141), K194 (= K192), D226 (= D224), D250 (= D248)
• binding magnesium ion: D250 (= D248), D254 (= D252)
• binding nicotinamide-adenine-dinucleotide: S74 (≠ A73), V75 (= V74), G76 (= G75), E90 (= E89), L94 (= L92), Y224 (= Y222), N227 (= N225), M230 (= M228), M263 (≠ I261), G264 (= G262), E280 (= E278), G283 (≠ H281), G284 (= G282), S285 (= S283), A286 (= A284), P287 (= P285), D288 (= D286), I289 (= I287), N296 (= N294), D337 (= D335)
• binding 2-(2-methylprop-2-enoxyamino)-2-oxidanylidene-ethanoic acid: E90 (= E89), R108 (= R106), R137 (= R134), K194 (= K192), V197 (= V195), D226 (= D224), D250 (= D248)

3vmkA 3-isopropylmalate dehydrogenase from shewanella benthica db21 mt-2 (see paper)
56% identity, 99% coverage: 2:357/360 of query aligns to 8:366/369 of 3vmkA