SitesBLAST
Comparing CCNA_00193 CCNA_00193 3-isopropylmalate dehydrogenase 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
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: I74 (≠ V69), E89 (= E84), L92 (= L87), I261 (≠ L257), E278 (= E275), H281 (= H278), G282 (= G279), S283 (= S280), A284 (= A281), I287 (= I284), 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: S74 (≠ A68), V75 (= V69), G76 (= G70), E90 (= E84), L94 (= L87), 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), N296 (= N291), D337 (= D332)
- binding 2-(2-methylprop-2-enoxyamino)-2-oxidanylidene-ethanoic acid: E90 (= E84), R108 (= R101), R137 (= R129), K194 (= K187), V197 (= V190), D226 (= D220), D250 (= D244)
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
2y42D Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with nadh and mn (see paper)
50% identity, 98% coverage: 6:347/350 of query aligns to 6:342/355 of 2y42D
- active site: Y140 (= Y136), K186 (= K187), D218 (= D220), D242 (= D244), D246 (= D248)
- binding manganese (ii) ion: D242 (= D244), D246 (= D248)
- binding nicotinamide-adenine-dinucleotide: I12 (= I12), D79 (≠ A75), H274 (= H278), G275 (= G279), A277 (= A281), D279 (= D283), I280 (= I284), N287 (= N291)
2y41A Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with ipm and mn (see paper)
50% identity, 99% coverage: 6:350/350 of query aligns to 6:345/346 of 2y41A
2ztwA Structure of 3-isopropylmalate dehydrogenase in complex with the inhibitor and NAD+ (see paper)
50% identity, 99% coverage: 6:350/350 of query aligns to 5:344/345 of 2ztwA
- active site: Y139 (= Y136), K185 (= K187), D217 (= D220), D241 (= D244), D245 (= D248)
- binding magnesium ion: G203 (≠ A206), Y206 (= Y209), V209 (= V212)
- binding nicotinamide-adenine-dinucleotide: I11 (= I12), H273 (= H278), G274 (= G279), A276 (= A281), D278 (= D283), I279 (= I284), A285 (= A290), N286 (= N291)
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)
50% identity, 99% coverage: 6:350/350 of query aligns to 5:344/345 of Q5SIY4
- 74:87 (vs. 71:84, 64% identical) binding
- Y139 (= Y136) mutation to F: Large decrease in activity and a small decrease in substrate affinity.
- 274:286 (vs. 279:291, 92% identical) binding
3vmkA 3-isopropylmalate dehydrogenase from shewanella benthica db21 mt-2 (see paper)
47% identity, 99% coverage: 4:350/350 of query aligns to 11:366/369 of 3vmkA
P18869 3-isopropylmalate dehydrogenase; 3-IPM-DH; IMDH; Beta-IPM dehydrogenase; EC 1.1.1.85 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
45% identity, 99% coverage: 4:350/350 of query aligns to 6:367/371 of P18869
- T55 (= T48) modified: Phosphothreonine
Q72IW9 Isocitrate/homoisocitrate dehydrogenase; Homoisocitrate dehydrogenase; HICDH; EC 1.1.1.286 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see 4 papers)
41% identity, 99% coverage: 4:350/350 of query aligns to 5:331/334 of Q72IW9
- E57 (= E56) mutation to V: Confers enzyme activity with 3-isopropylmalate; when associated with I-72; M-85; A-86; T-208; Y-217; M-238 and M-310.
- ATS 70:72 (≠ VGG 69:71) binding
- S72 (≠ G71) binding in other chain; mutation to I: Confers enzyme activity with 3-isopropylmalate; when associated with V-57; M-85; A-86; T-208; Y-217; M-238 and M-310.
- R85 (≠ L88) binding in other chain; mutation to M: Confers enzyme activity with 3-isopropylmalate; when associated with V-57; I-72; A-86; T-208; Y-217; M-238 and M-310.; mutation to V: Confers low enzyme activity with 3-isopropylmalate. Reduces activity with homoisocitrate. Abolishes activity with isocitrate.
- Y86 (≠ N89) mutation to A: Confers enzyme activity with 3-isopropylmalate; when associated with V-57; I-72; M-85; T-208; Y-217; M-238 and M-310.
- R88 (= R91) binding in other chain
- R98 (= R101) binding in other chain
- R118 (= R129) binding in other chain
- Y125 (= Y136) binding in other chain; mutation to A: Reduces catalytic efficiency with isocitrate.
- V135 (≠ L146) mutation to M: Formation of homodimers instead of homotetramers. Increased affinity for isocitrate. Reduces enzyme activity with isocitrate.
- K171 (= K187) binding
- N173 (= N189) binding ; binding
- D204 (= D220) binding
- M208 (= M224) mutation to T: Confers enzyme activity with 3-isopropylmalate; when associated with V-57; I-72; M-85; A-86; T-208; Y-217; M-238 and M-310.
- F217 (= F233) mutation to Y: Confers enzyme activity with 3-isopropylmalate; when associated with V-57; I-72; M-85; A-86; T-208; M-238 and M-310.
- D228 (= D244) binding
- D232 (= D248) binding
- V238 (≠ T254) mutation to M: Confers enzyme activity with 3-isopropylmalate; when associated with V-57; I-72; M-85; A-86; T-208; Y-217; and M-310.
- GSAPD 261:265 (= GSAPD 279:283) binding
- N273 (= N291) binding
- R310 (= R329) mutation to M: Confers enzyme activity with 3-isopropylmalate; when associated with V-57; I-72; M-85; A-86; T-208; Y-217; and M-238.
Query Sequence
>CCNA_00193 CCNA_00193 3-isopropylmalate dehydrogenase
MATLLLLPGDGIGPEVCAQVRRVAAALTPDLKVDEALYGGASYDTHGTPLTDEVREQALA
SDAVLMGAVGGPKWADAPRHLRPEAGLLNLRKAMDVFANLRPAYCFEALAGASSLKPELV
SGLDIMFVRELVGGVYFGQPRGIEDLADGQKKGFDTQVYTTSEIERVGRVAFELARGRTN
KVHSAEKSNVMESGLLWKQVITELHAREYPDVQLEHILADNCAMQLVRAPKQFDVIVTDN
LFGDILSDAAAMLTGSLGMLPSAALGAPGKPGLYEPIHGSAPDIAGKGLANPLAAILSFE
MALRWSLKQTEAADALLAAVKAALDNGARTRDLGGSLTTTQMGDAVLAAL
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory