SitesBLAST

Comparing GFF1875 FitnessBrowser__Marino:GFF1875 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
66% identity, 97% coverage: 11:363/363 of query aligns to 4:356/356 of 4xxvA

• active site: Y136 (= Y147), K191 (= K198), D223 (= D230), D247 (= D254), D251 (= D258)
• binding nicotinamide-adenine-dinucleotide: N193 (= N200), Y221 (= Y228), N224 (= N231)

4iwhA Crystal structure of a 3-isopropylmalate dehydrogenase from burkholderia pseudomallei
66% identity, 97% coverage: 11:363/363 of query aligns to 6:358/358 of 4iwhA

• active site: Y138 (= Y147), K193 (= K198), D225 (= D230), D249 (= D254), D253 (= D258)
• binding magnesium ion: D249 (= D254), D253 (= D258)

1a05A Crystal structure of the complex of 3-isopropylmalate dehydrogenase from thiobacillus ferrooxidans with 3-isopropylmalate (see paper)
65% identity, 98% coverage: 9:363/363 of query aligns to 2:354/357 of 1a05A

• active site: Y140 (= Y147), K190 (= K198), D222 (= D230), D246 (= D254), D250 (= D258)
• binding 3-isopropylmalic acid: R95 (= R102), R105 (= R112), R133 (= R140), Y140 (= Y147), D246 (= D254)

Q56268 3-isopropylmalate dehydrogenase; 3-IPM-DH; Beta-IPM dehydrogenase; IMDH; EC 1.1.1.85 from Acidithiobacillus ferrooxidans (Thiobacillus ferrooxidans) (see paper)
65% identity, 98% coverage: 9:363/363 of query aligns to 2:354/358 of Q56268

• R95 (= R102) binding substrate
• R105 (= R112) binding substrate
• R133 (= R140) binding substrate
• D222 (= D230) binding Mg(2+); binding substrate
• D246 (= D254) 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)
62% identity, 98% coverage: 10:363/363 of query aligns to 44:397/405 of P93832

• 114:129 (vs. 80:95, 44% identical) binding NAD(+)
• L132 (= L98) mutation to A: Reduced activity toward 3-isopropylmalate.
• L133 (= L99) 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 (= R102) binding substrate; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
• R146 (= R112) binding substrate; mutation to A: Reduced activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
• R174 (= R140) binding substrate; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
• Y181 (= Y147) Important for catalysis; mutation Y->A,F,H: Reduced activity toward 3-isopropylmalate.
• K232 (= K198) Important for catalysis; mutation to M: Loss of activity toward 3-isopropylmalate.
• N234 (= N200) binding NAD(+); mutation N->A,D: Loss of activity toward 3-isopropylmalate.
• V235 (= V201) mutation to A: Reduced activity toward 3-isopropylmalate.
• D264 (= D230) binding Mg(2+); binding substrate; mutation to N: Loss of activity toward 3-isopropylmalate.
• N265 (= N231) binding NAD(+)
• D288 (= D254) binding Mg(2+); mutation to N: Loss of activity toward 3-isopropylmalate.
• D292 (= D258) binding Mg(2+); mutation to N: Reduced activity toward 3-isopropylmalate.
• 318:334 (vs. 284:300, 82% identical) binding NAD(+)

5j33A Isopropylmalate dehydrogenase in complex with NAD+ (see paper)
62% identity, 98% coverage: 10:363/363 of query aligns to 4:357/360 of 5j33A

• active site: Y141 (= Y147), K192 (= K198), D224 (= D230), D248 (= D254), D252 (= D258)
• binding magnesium ion: D248 (= D254), D252 (= D258)
• binding nicotinamide-adenine-dinucleotide: I74 (≠ V80), E89 (= E95), L92 (= L98), I261 (= I267), E278 (= E284), H281 (= H287), G282 (= G288), S283 (= S289), A284 (= A290), I287 (= I293), N294 (= N300), D335 (= D341)

5j32A Isopropylmalate dehydrogenase in complex with isopropylmalate (see paper)
62% identity, 98% coverage: 10:363/363 of query aligns to 14:367/369 of 5j32A

• active site: L18 (= L14), Y151 (= Y147), K202 (= K198), D234 (= D230), D258 (= D254), D262 (= D258)
• binding 3-isopropylmalic acid: R106 (= R102), R144 (= R140), Y151 (= Y147), D258 (= D254)
• binding magnesium ion: D258 (= D254), D262 (= D258)

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)
62% identity, 98% coverage: 10:363/363 of query aligns to 45:398/404 of Q9SA14

• L134 (= L99) Confers substrate specificity; mutation to F: Enhanced activity toward 3-(2'-methylthio)-ethylmalate, but reduced catalytic efficiency with 3-isopropylmalate.

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)
61% identity, 98% coverage: 10:363/363 of query aligns to 48:401/409 of Q9FMT1

• F137 (≠ L99) Confers substrate specificity; mutation to L: Reduced activity toward 3-(2'-methylthio)-ethylmalate, but enhanced catalytic efficiency with 3-isopropylmalate.
• C232 (= C194) Essential for redox regulation; mutation to S: Reduced sensitivity to oxidation on enzyme activity regulation.
• C390 (≠ T352) Essential for redox regulation; mutation to S: Reduced sensitivity to oxidation on enzyme activity regulation.

6xxyA Crystal structure of haemophilus influenzae 3-isopropylmalate dehydrogenase in complex with o-isobutenyl oxalylhydroxamate. (see paper)
56% identity, 98% coverage: 10:363/363 of query aligns to 5:358/358 of 6xxyA

• active site: Y144 (= Y147), K194 (= K198), D226 (= D230), D250 (= D254)
• binding magnesium ion: D250 (= D254), D254 (= D258)
• binding nicotinamide-adenine-dinucleotide: S74 (≠ A79), V75 (= V80), G76 (= G81), E90 (= E95), L94 (= L98), Y224 (= Y228), N227 (= N231), M230 (= M234), M263 (≠ I267), G264 (= G268), E280 (= E284), G283 (≠ H287), G284 (= G288), S285 (= S289), A286 (= A290), P287 (= P291), D288 (= D292), I289 (= I293), N296 (= N300), D337 (= D341)
• binding 2-(2-methylprop-2-enoxyamino)-2-oxidanylidene-ethanoic acid: E90 (= E95), R108 (= R112), R137 (= R140), K194 (= K198), V197 (= V201), D226 (= D230), D250 (= D254)

1cnzA 3-isopropylmalate dehydrogenase (ipmdh) from salmonella typhimurium (see paper)
54% identity, 96% coverage: 11:359/363 of query aligns to 7:355/363 of 1cnzA

• active site: Y145 (= Y147), K195 (= K198), D227 (= D230), D251 (= D254)
• binding manganese (ii) ion: D251 (= D254), D255 (= D258)

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)
54% identity, 96% coverage: 11:359/363 of query aligns to 7:355/363 of P37412

• D227 (= D230) binding Mn(2+)
• D251 (= D254) binding Mn(2+)
• D255 (= D258) binding Mn(2+)

3vmkA 3-isopropylmalate dehydrogenase from shewanella benthica db21 mt-2 (see paper)
55% identity, 97% coverage: 11:363/363 of query aligns to 11:366/369 of 3vmkA