SitesBLAST
Comparing 7026627 Shewana3_3760 3-isopropylmalate dehydrogenase (RefSeq) 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)
3vkzA 3-isopropylmalate dehydrogenase from shewanella oneidensis mr-1 at atmospheric pressure (see paper)
98% identity, 100% coverage: 2:364/364 of query aligns to 2:364/364 of 3vkzA
3vmkA 3-isopropylmalate dehydrogenase from shewanella benthica db21 mt-2 (see paper)
85% identity, 99% coverage: 2:363/364 of query aligns to 8:369/369 of 3vmkA
1cnzA 3-isopropylmalate dehydrogenase (ipmdh) from salmonella typhimurium (see paper)
70% identity, 100% coverage: 2:364/364 of query aligns to 4:363/363 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)
70% identity, 100% coverage: 2:364/364 of query aligns to 4:363/363 of P37412
- D227 (= D225) binding
- D251 (= D249) binding
- D255 (= D253) binding
6xxyA Crystal structure of haemophilus influenzae 3-isopropylmalate dehydrogenase in complex with o-isobutenyl oxalylhydroxamate. (see paper)
67% identity, 99% coverage: 2:360/364 of query aligns to 3:358/358 of 6xxyA
- active site: Y144 (= Y143), K194 (= K193), D226 (= D225), D250 (= D249)
- binding magnesium ion: D250 (= D249), D254 (= D253)
- binding nicotinamide-adenine-dinucleotide: S74 (= S73), V75 (= V74), G76 (= G75), E90 (= E89), L94 (= L93), Y224 (= Y223), N227 (= N226), M230 (= M229), M263 (= M262), G264 (= G263), E280 (= E279), G283 (= G282), G284 (= G283), S285 (= S284), A286 (= A285), P287 (= P286), D288 (= D287), I289 (= I288), N296 (= N295), D337 (≠ E336)
- binding 2-(2-methylprop-2-enoxyamino)-2-oxidanylidene-ethanoic acid: E90 (= E89), R108 (= R107), R137 (= R136), K194 (= K193), V197 (= V196), D226 (= D225), D250 (= D249)
2y41A Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with ipm and mn (see paper)
57% identity, 90% coverage: 2:328/364 of query aligns to 1:320/346 of 2y41A
2y42D Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with nadh and mn (see paper)
57% identity, 90% coverage: 2:328/364 of query aligns to 1:320/355 of 2y42D
- active site: Y140 (= Y143), K186 (= K193), D218 (= D225), D242 (= D249), D246 (= D253)
- binding manganese (ii) ion: D242 (= D249), D246 (= D253)
- binding nicotinamide-adenine-dinucleotide: I12 (= I13), D79 (≠ E80), H274 (≠ G282), G275 (= G283), A277 (= A285), D279 (= D287), I280 (= I288), N287 (= N295)
2ztwA Structure of 3-isopropylmalate dehydrogenase in complex with the inhibitor and NAD+ (see paper)
58% identity, 89% coverage: 4:328/364 of query aligns to 2:319/345 of 2ztwA
- active site: Y139 (= Y143), K185 (= K193), D217 (= D225), D241 (= D249), D245 (= D253)
- binding magnesium ion: G203 (≠ A211), Y206 (≠ F214), V209 (= V217)
- binding nicotinamide-adenine-dinucleotide: I11 (= I13), H273 (≠ G282), G274 (= G283), A276 (= A285), D278 (= D287), I279 (= I288), A285 (= A294), N286 (= N295)
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)
58% identity, 89% coverage: 4:328/364 of query aligns to 2:319/345 of Q5SIY4
- 74:87 (vs. 76:89, 57% identical) binding
- Y139 (= Y143) mutation to F: Large decrease in activity and a small decrease in substrate affinity.
- 274:286 (vs. 283:295, 100% identical) binding
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, 92% coverage: 4:337/364 of query aligns to 3:333/358 of Q56268
- R95 (= R97) binding
- R105 (= R107) binding
- R133 (= R136) binding
- D222 (= D225) binding ; binding
- D246 (= D249) binding
1a05A Crystal structure of the complex of 3-isopropylmalate dehydrogenase from thiobacillus ferrooxidans with 3-isopropylmalate (see paper)
53% identity, 92% coverage: 4:337/364 of query aligns to 3:333/357 of 1a05A
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)
49% identity, 99% coverage: 3:364/364 of query aligns to 43:401/405 of P93832
- 114:129 (vs. 74:89, 38% identical) binding
- L132 (= L93) mutation to A: Reduced activity toward 3-isopropylmalate.
- L133 (= L94) 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 (= R97) binding ; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- R146 (= R107) binding ; mutation to A: Reduced activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- R174 (= R136) binding ; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- Y181 (= Y143) Important for catalysis; mutation Y->A,F,H: Reduced activity toward 3-isopropylmalate.
- K232 (= K193) Important for catalysis; mutation to M: Loss of activity toward 3-isopropylmalate.
- N234 (= N195) binding ; mutation N->A,D: Loss of activity toward 3-isopropylmalate.
- V235 (= V196) mutation to A: Reduced activity toward 3-isopropylmalate.
- D264 (= D225) binding ; binding ; mutation to N: Loss of activity toward 3-isopropylmalate.
- N265 (= N226) binding
- D288 (= D249) binding ; mutation to N: Loss of activity toward 3-isopropylmalate.
- D292 (= D253) binding ; mutation to N: Reduced activity toward 3-isopropylmalate.
- 318:334 (vs. 279:295, 71% identical) binding
5j32A Isopropylmalate dehydrogenase in complex with isopropylmalate (see paper)
50% identity, 94% coverage: 3:343/364 of query aligns to 13:352/369 of 5j32A
5j33A Isopropylmalate dehydrogenase in complex with NAD+ (see paper)
50% identity, 94% coverage: 3:343/364 of query aligns to 3:342/360 of 5j33A
- active site: Y141 (= Y143), K192 (= K193), D224 (= D225), D248 (= D249), D252 (= D253)
- binding magnesium ion: D248 (= D249), D252 (= D253)
- binding nicotinamide-adenine-dinucleotide: I74 (≠ V74), E89 (= E89), L92 (= L93), I261 (≠ M262), E278 (= E279), H281 (≠ G282), G282 (= G283), S283 (= S284), A284 (= A285), I287 (= I288), N294 (= N295), D335 (≠ E336)
4xxvA Crystal structure of 3-isopropylmalate dehydrogenase from burkholderia thailandensis in complex with NAD
51% identity, 98% coverage: 4:360/364 of query aligns to 3:356/356 of 4xxvA
4iwhA Crystal structure of a 3-isopropylmalate dehydrogenase from burkholderia pseudomallei
51% identity, 98% coverage: 4:360/364 of query aligns to 5:358/358 of 4iwhA
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)
50% identity, 99% coverage: 3:364/364 of query aligns to 47:405/409 of Q9FMT1
- F137 (≠ L94) Confers substrate specificity; mutation to L: Reduced activity toward 3-(2'-methylthio)-ethylmalate, but enhanced catalytic efficiency with 3-isopropylmalate.
- C232 (≠ T189) Essential for redox regulation; mutation to S: Reduced sensitivity to oxidation on enzyme activity regulation.
- C390 (≠ T349) Essential for redox regulation; mutation to S: Reduced sensitivity to oxidation on enzyme activity regulation.
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)
50% identity, 99% coverage: 3:364/364 of query aligns to 44:402/404 of Q9SA14
- L134 (= L94) Confers substrate specificity; mutation to F: Enhanced activity toward 3-(2'-methylthio)-ethylmalate, but reduced catalytic efficiency with 3-isopropylmalate.
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)
43% identity, 98% coverage: 4:358/364 of query aligns to 5:365/371 of P18869
- T55 (≠ C53) 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, 93% coverage: 1:337/364 of query aligns to 1:314/334 of Q72IW9
- E57 (≠ K61) 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 74:76) binding
- S72 (≠ G76) 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 (≠ L94) 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 (≠ P95) 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 (= R97) binding in other chain
- R98 (= R107) binding in other chain
- R118 (= R136) binding in other chain
- Y125 (= Y143) binding in other chain; mutation to A: Reduces catalytic efficiency with isocitrate.
- V135 (≠ E158) mutation to M: Formation of homodimers instead of homotetramers. Increased affinity for isocitrate. Reduces enzyme activity with isocitrate.
- K171 (= K193) binding
- N173 (= N195) binding ; binding
- D204 (= D225) binding
- M208 (= M229) 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 (= F238) 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 (= D249) binding
- D232 (= D253) binding
- V238 (≠ T259) 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 283:287) binding
- N273 (= N295) binding
- R310 (≠ L333) 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
>7026627 Shewana3_3760 3-isopropylmalate dehydrogenase (RefSeq)
MSYQIAVLAGDGIGPEVMAEARKVLKAVEARFGLNIEYSEYDVGGIAIDNHGCPLPEATL
KGCEAADAILFGSVGGPKWEKLPPNEQPERGALLPLRGHFELFCNLRPAKLHDGLEHMSP
LRSDISARGFDVLCVRELTGGIYFGKPKGRQGEGESEEAFDTMRYSRREIARIARIAFEA
ARGRRKKVTSVDKANVLACSVLWRQVVEEVAVDFPDVELEHIYIDNATMQLLRRPDEFDV
MLCSNLFGDILSDEIAMLTGSMGLLSSASMNSTGFGLFEPAGGSAPDIAGKGIANPIAQI
LSAALMLRHSLKQEEAASAIERAVSKALNSGYLTGELLSSDQRHKAKSTVEMGNFIADAV
KAGV
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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