SitesBLAST
Comparing CA265_RS15850 FitnessBrowser__Pedo557:CA265_RS15850 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)
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)
51% identity, 99% coverage: 2:360/363 of query aligns to 43:402/404 of Q9SA14
- L134 (= L94) Confers substrate specificity; mutation to F: Enhanced activity toward 3-(2'-methylthio)-ethylmalate, but reduced catalytic efficiency with 3-isopropylmalate.
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)
50% identity, 100% coverage: 2:363/363 of query aligns to 42:404/405 of P93832
- 114:129 (vs. 74:90, 47% 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 (= K189) Important for catalysis; mutation to M: Loss of activity toward 3-isopropylmalate.
- N234 (= N191) binding ; mutation N->A,D: Loss of activity toward 3-isopropylmalate.
- V235 (= V192) mutation to A: Reduced activity toward 3-isopropylmalate.
- D264 (= D221) binding ; binding ; mutation to N: Loss of activity toward 3-isopropylmalate.
- N265 (= N222) binding
- D288 (= D245) binding ; mutation to N: Loss of activity toward 3-isopropylmalate.
- D292 (= D249) binding ; mutation to N: Reduced activity toward 3-isopropylmalate.
- 318:334 (vs. 274:290, 82% identical) binding
5j33A Isopropylmalate dehydrogenase in complex with NAD+ (see paper)
51% identity, 97% coverage: 2:354/363 of query aligns to 2:355/360 of 5j33A
- active site: Y141 (= Y142), K192 (= K189), D224 (= D221), D248 (= D245), D252 (= D249)
- binding magnesium ion: D248 (= D245), D252 (= D249)
- binding nicotinamide-adenine-dinucleotide: I74 (= I74), E89 (= E90), L92 (= L93), I261 (≠ M258), E278 (= E274), H281 (= H277), G282 (= G278), S283 (= S279), A284 (= A280), I287 (= I283), N294 (= N290), D335 (= D331)
5j32A Isopropylmalate dehydrogenase in complex with isopropylmalate (see paper)
51% identity, 97% coverage: 2:354/363 of query aligns to 12:365/369 of 5j32A
1a05A Crystal structure of the complex of 3-isopropylmalate dehydrogenase from thiobacillus ferrooxidans with 3-isopropylmalate (see paper)
50% identity, 98% coverage: 3:359/363 of query aligns to 2:357/357 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)
50% identity, 98% coverage: 3:359/363 of query aligns to 2:357/358 of Q56268
- R95 (= R97) binding
- R105 (= R107) binding
- R133 (= R135) binding
- D222 (= D221) binding ; binding
- D246 (= D245) 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)
50% identity, 99% coverage: 2:360/363 of query aligns to 46:405/409 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 (= C185) Essential for redox regulation; mutation to S: Reduced sensitivity to oxidation on enzyme activity regulation.
- C390 (≠ T345) 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)
51% identity, 97% coverage: 4:354/363 of query aligns to 5:356/358 of 6xxyA
- active site: Y144 (= Y142), K194 (= K189), D226 (= D221), D250 (= D245)
- binding magnesium ion: D250 (= D245), D254 (= D249)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ A73), V75 (≠ I74), G76 (= G75), E90 (= E90), L94 (= L93), Y224 (≠ F219), N227 (= N222), M230 (= M225), M263 (= M258), G264 (= G259), E280 (= E274), G283 (≠ H277), G284 (= G278), S285 (= S279), A286 (= A280), P287 (≠ H281), D288 (= D282), I289 (= I283), N296 (= N290), D337 (= D331)
- binding 2-(2-methylprop-2-enoxyamino)-2-oxidanylidene-ethanoic acid: E90 (= E90), R108 (= R107), R137 (= R135), K194 (= K189), V197 (= V192), D226 (= D221), D250 (= D245)
4xxvA Crystal structure of 3-isopropylmalate dehydrogenase from burkholderia thailandensis in complex with NAD
50% identity, 97% coverage: 5:356/363 of query aligns to 4:356/356 of 4xxvA
4iwhA Crystal structure of a 3-isopropylmalate dehydrogenase from burkholderia pseudomallei
50% identity, 97% coverage: 5:356/363 of query aligns to 6:358/358 of 4iwhA
2y42D Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with nadh and mn (see paper)
50% identity, 89% coverage: 4:325/363 of query aligns to 3:322/355 of 2y42D
- active site: Y140 (= Y142), K186 (= K189), D218 (= D221), D242 (= D245), D246 (= D249)
- binding manganese (ii) ion: D242 (= D245), D246 (= D249)
- binding nicotinamide-adenine-dinucleotide: I12 (= I13), D79 (= D80), H274 (= H277), G275 (= G278), A277 (= A280), D279 (= D282), I280 (= I283), N287 (= N290)
2y41A Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with ipm and mn (see paper)
50% identity, 89% coverage: 4:325/363 of query aligns to 3:322/346 of 2y41A
2ztwA Structure of 3-isopropylmalate dehydrogenase in complex with the inhibitor and NAD+ (see paper)
50% identity, 89% coverage: 4:325/363 of query aligns to 2:321/345 of 2ztwA
- active site: Y139 (= Y142), K185 (= K189), D217 (= D221), D241 (= D245), D245 (= D249)
- binding magnesium ion: G203 (≠ A207), Y206 (= Y210), V209 (= V213)
- binding nicotinamide-adenine-dinucleotide: I11 (= I13), H273 (= H277), G274 (= G278), A276 (= A280), D278 (= D282), I279 (= I283), A285 (= A289), N286 (= N290)
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: 4:325/363 of query aligns to 2:321/345 of Q5SIY4
- 74:87 (vs. 76:90, 47% identical) binding
- Y139 (= Y142) mutation to F: Large decrease in activity and a small decrease in substrate affinity.
- 274:286 (vs. 278:290, 77% identical) binding
1cnzA 3-isopropylmalate dehydrogenase (ipmdh) from salmonella typhimurium (see paper)
46% identity, 99% coverage: 1:358/363 of query aligns to 1:361/363 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)
46% identity, 99% coverage: 1:358/363 of query aligns to 1:361/363 of P37412
- D227 (= D221) binding
- D251 (= D245) binding
- D255 (= D249) binding
3vkzA 3-isopropylmalate dehydrogenase from shewanella oneidensis mr-1 at atmospheric pressure (see paper)
46% identity, 96% coverage: 4:352/363 of query aligns to 4:356/364 of 3vkzA
3vmkA 3-isopropylmalate dehydrogenase from shewanella benthica db21 mt-2 (see paper)
43% identity, 98% coverage: 4:358/363 of query aligns to 10:368/369 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)
42% identity, 99% coverage: 3:360/363 of query aligns to 4:371/371 of P18869
- T55 (≠ E53) 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)
39% identity, 93% coverage: 1:338/363 of query aligns to 1:320/334 of Q72IW9
- E57 (= E61) 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.
- A------TS 70:72 (≠ IGHAKYDND 74:82) binding
- S72 (≠ D82) 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 (≠ K95) 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 (≠ R152) mutation to M: Formation of homodimers instead of homotetramers. Increased affinity for isocitrate. Reduces enzyme activity with isocitrate.
- K171 (= K189) binding
- N173 (= N191) binding ; binding
- D204 (= D221) binding
- M208 (= M225) 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 (= F234) 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 (= D245) binding
- D232 (= D249) binding
- V238 (≠ A255) 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 (≠ GSAHD 278:282) binding
- N273 (= N290) binding
- R310 (= R328) 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
>CA265_RS15850 FitnessBrowser__Pedo557:CA265_RS15850
MKKNILVIPGDGIGPEVTTWGKAALEKIAEIFGHEFAFEEALMGHAAIEVTGEPLPDETL
EKARQSDAILFGAIGHAKYDNDPSLKVRPEQGLLKIRKELGLFANLRPILLFDELLQASS
IKPEILRGTDILFFRELTGDVYFGEKTRSEDRNTASDLMIYHRYEVERIAHKAYQAAQQR
NKRLCSVDKANVLESSRLWRETVQEIAKQYPDVETEHMFIDNAAMQLIKNPKKFDVVLTA
NLFGDILTDEASQIAGSMGMLASASVGESTGFFEPIHGSAHDIAGKDLANPLASILSAAL
MLEIGFGLKEEAKLLVDTIDQVLKEGFRTHDIADQSTNRFKVLGTAEMGKLVLKFLSQKL
ITS
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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