SitesBLAST
Comparing WP_011386420.1 NCBI__GCF_000009985.1:WP_011386420.1 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)
1a05A Crystal structure of the complex of 3-isopropylmalate dehydrogenase from thiobacillus ferrooxidans with 3-isopropylmalate (see paper)
57% identity, 98% coverage: 4:365/369 of query aligns to 2:355/357 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)
57% identity, 98% coverage: 4:365/369 of query aligns to 2:355/358 of Q56268
- R95 (= R97) binding
- R105 (= R107) binding
- R133 (= R135) binding
- D222 (= D226) binding ; binding
- D246 (= D250) binding
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)
57% identity, 98% coverage: 5:365/369 of query aligns to 45:399/404 of Q9SA14
- L134 (= L94) Confers substrate specificity; mutation to F: Enhanced activity toward 3-(2'-methylthio)-ethylmalate, but reduced catalytic efficiency with 3-isopropylmalate.
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)
57% identity, 98% coverage: 6:365/369 of query aligns to 45:398/405 of P93832
- 114:129 (vs. 75:90, 44% 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 (= R135) binding ; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- Y181 (= Y142) 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 (= D226) binding ; binding ; mutation to N: Loss of activity toward 3-isopropylmalate.
- N265 (= N227) binding
- D288 (= D250) binding ; mutation to N: Loss of activity toward 3-isopropylmalate.
- D292 (= D254) binding ; mutation to N: Reduced activity toward 3-isopropylmalate.
- 318:334 (vs. 285:301, 82% identical) binding
5j33A Isopropylmalate dehydrogenase in complex with NAD+ (see paper)
57% identity, 98% coverage: 6:365/369 of query aligns to 5:358/360 of 5j33A
- active site: Y141 (= Y142), K192 (= K193), D224 (= D226), D248 (= D250), D252 (= D254)
- binding magnesium ion: D248 (= D250), D252 (= D254)
- binding nicotinamide-adenine-dinucleotide: I74 (≠ V75), E89 (= E90), L92 (= L93), I261 (≠ L263), E278 (= E285), H281 (= H288), G282 (= G289), S283 (= S290), A284 (= A291), I287 (= I294), N294 (= N301), D335 (= D342)
5j32A Isopropylmalate dehydrogenase in complex with isopropylmalate (see paper)
57% identity, 98% coverage: 6:365/369 of query aligns to 15:368/369 of 5j32A
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)
55% identity, 98% coverage: 5:365/369 of query aligns to 48:402/409 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 (= C189) Essential for redox regulation; mutation to S: Reduced sensitivity to oxidation on enzyme activity regulation.
- C390 (≠ T353) Essential for redox regulation; mutation to S: Reduced sensitivity to oxidation on enzyme activity regulation.
4iwhA Crystal structure of a 3-isopropylmalate dehydrogenase from burkholderia pseudomallei
56% identity, 98% coverage: 5:364/369 of query aligns to 5:358/358 of 4iwhA
4xxvA Crystal structure of 3-isopropylmalate dehydrogenase from burkholderia thailandensis in complex with NAD
56% identity, 98% coverage: 5:364/369 of query aligns to 3:356/356 of 4xxvA
6xxyA Crystal structure of haemophilus influenzae 3-isopropylmalate dehydrogenase in complex with o-isobutenyl oxalylhydroxamate. (see paper)
50% identity, 99% coverage: 1:364/369 of query aligns to 1:358/358 of 6xxyA
- active site: Y144 (= Y142), K194 (= K193), D226 (= D226), D250 (= D250)
- binding magnesium ion: D250 (= D250), D254 (= D254)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ A74), V75 (= V75), G76 (= G76), E90 (= E90), L94 (= L93), Y224 (= Y224), N227 (= N227), M230 (= M230), M263 (≠ L263), G264 (= G264), E280 (= E285), G283 (≠ H288), G284 (= G289), S285 (= S290), A286 (= A291), P287 (= P292), D288 (= D293), I289 (= I294), N296 (= N301), D337 (= D342)
- binding 2-(2-methylprop-2-enoxyamino)-2-oxidanylidene-ethanoic acid: E90 (= E90), R108 (= R107), R137 (= R135), K194 (= K193), V197 (= V196), D226 (= D226), D250 (= D250)
1cnzA 3-isopropylmalate dehydrogenase (ipmdh) from salmonella typhimurium (see paper)
51% identity, 97% coverage: 5:362/369 of query aligns to 6:357/363 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)
51% identity, 97% coverage: 5:362/369 of query aligns to 6:357/363 of P37412
- D227 (= D226) binding
- D251 (= D250) binding
- D255 (= D254) binding
3vkzA 3-isopropylmalate dehydrogenase from shewanella oneidensis mr-1 at atmospheric pressure (see paper)
47% identity, 97% coverage: 2:360/369 of query aligns to 1:356/364 of 3vkzA
3vmkA 3-isopropylmalate dehydrogenase from shewanella benthica db21 mt-2 (see paper)
46% identity, 98% coverage: 2:364/369 of query aligns to 7:366/369 of 3vmkA
2ztwA Structure of 3-isopropylmalate dehydrogenase in complex with the inhibitor and NAD+ (see paper)
50% identity, 89% coverage: 5:334/369 of query aligns to 2:319/345 of 2ztwA
- active site: Y139 (= Y142), K185 (= K193), D217 (= D226), D241 (= D250), D245 (= D254)
- binding magnesium ion: G203 (≠ Q211), Y206 (≠ F215), V209 (= V218)
- binding nicotinamide-adenine-dinucleotide: I11 (= I14), H273 (= H288), G274 (= G289), A276 (= A291), D278 (= D293), I279 (= I294), A285 (= A300), N286 (= N301)
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, 89% coverage: 5:334/369 of query aligns to 2:319/345 of Q5SIY4
- 74:87 (vs. 77:90, 64% identical) binding
- Y139 (= Y142) mutation to F: Large decrease in activity and a small decrease in substrate affinity.
- 274:286 (vs. 289:301, 85% identical) binding
2y42D Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with nadh and mn (see paper)
50% identity, 89% coverage: 5:334/369 of query aligns to 3:320/355 of 2y42D
- active site: Y140 (= Y142), K186 (= K193), D218 (= D226), D242 (= D250), D246 (= D254)
- binding manganese (ii) ion: D242 (= D250), D246 (= D254)
- binding nicotinamide-adenine-dinucleotide: I12 (= I14), D79 (= D81), H274 (= H288), G275 (= G289), A277 (= A291), D279 (= D293), I280 (= I294), N287 (= N301)
2y41A Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with ipm and mn (see paper)
50% identity, 89% coverage: 5:334/369 of query aligns to 3:320/346 of 2y41A
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)
44% identity, 99% coverage: 1:367/369 of query aligns to 1:370/371 of P18869
- T55 (= T54) 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)
38% identity, 99% coverage: 3:367/369 of query aligns to 2:334/334 of Q72IW9
- E57 (= E62) 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 75:77) binding
- S72 (≠ G77) 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 (vs. gap) 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 (vs. gap) 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 (= R135) binding in other chain
- Y125 (= Y142) binding in other chain; mutation to A: Reduces catalytic efficiency with isocitrate.
- V135 (≠ L152) 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 (= D226) binding
- M208 (= M230) 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 (= F239) 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 (= D250) binding
- D232 (= D254) binding
- V238 (≠ T260) 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 289:293) binding
- N273 (= N301) binding
- R310 (= R339) 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
>WP_011386420.1 NCBI__GCF_000009985.1:WP_011386420.1
MAAKKLLILPGDGIGVEVMAQVRRIIDWMGRKRKIEFEITEGLLGGAAYDVHGTPYPAET
LEAALAADAVLLGAVGGPKWDDLPFDKKPERGLLGIRKDMGLFANLRPATVLEALADAST
LKAEVVSGLDIMILRELTGGLYFGQPRGIDTLPDGTRKGYNTLVYTTPEIQRIGRVAFDL
ARKRNKKLCSVDKANVLECTVLWREEMIKLQKEEFPDVELTHMYVDNAAMQLVRNPKQFD
VMVTENMFGDILSDCAAMLTGSLGMLPSASLGEADAQGKRKALYEPVHGSAPDIAGKDMA
NPLATIMSFAMCLRYSFDMAAEADLIETAVKNVLKGGLRTADIMQPGKAKVSTTVMGEAV
VRELDKLNA
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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