SitesBLAST
Comparing GFF1875 FitnessBrowser__Marino:GFF1875 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)
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
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
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
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
- R105 (= R112) binding
- R133 (= R140) binding
- D222 (= D230) binding ; binding
- D246 (= D254) binding
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
- 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 ; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- R146 (= R112) binding ; mutation to A: Reduced activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- R174 (= R140) binding ; 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 ; mutation N->A,D: Loss of activity toward 3-isopropylmalate.
- V235 (= V201) mutation to A: Reduced activity toward 3-isopropylmalate.
- D264 (= D230) binding ; binding ; mutation to N: Loss of activity toward 3-isopropylmalate.
- N265 (= N231) binding
- D288 (= D254) binding ; mutation to N: Loss of activity toward 3-isopropylmalate.
- D292 (= D258) binding ; mutation to N: Reduced activity toward 3-isopropylmalate.
- 318:334 (vs. 284:300, 82% identical) binding
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
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
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
- D251 (= D254) binding
- D255 (= D258) binding
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
3vkzA 3-isopropylmalate dehydrogenase from shewanella oneidensis mr-1 at atmospheric pressure (see paper)
53% identity, 97% coverage: 11:363/363 of query aligns to 5:360/364 of 3vkzA
2y41A Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with ipm and mn (see paper)
55% identity, 89% coverage: 11:333/363 of query aligns to 4:320/346 of 2y41A
2y42D Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with nadh and mn (see paper)
55% identity, 89% coverage: 11:333/363 of query aligns to 4:320/355 of 2y42D
- active site: Y140 (= Y147), K186 (= K198), D218 (= D230), D242 (= D254), D246 (= D258)
- binding manganese (ii) ion: D242 (= D254), D246 (= D258)
- binding nicotinamide-adenine-dinucleotide: I12 (= I19), D79 (= D86), H274 (= H287), G275 (= G288), A277 (= A290), D279 (= D292), I280 (= I293), N287 (= N300)
2ztwA Structure of 3-isopropylmalate dehydrogenase in complex with the inhibitor and NAD+ (see paper)
55% identity, 89% coverage: 11:333/363 of query aligns to 3:319/345 of 2ztwA
- active site: Y139 (= Y147), K185 (= K198), D217 (= D230), D241 (= D254), D245 (= D258)
- binding magnesium ion: G203 (≠ R216), Y206 (= Y219), V209 (= V222)
- binding nicotinamide-adenine-dinucleotide: I11 (= I19), H273 (= H287), G274 (= G288), A276 (= A290), D278 (= D292), I279 (= I293), A285 (= A299), N286 (= N300)
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)
55% identity, 89% coverage: 11:333/363 of query aligns to 3:319/345 of Q5SIY4
- 74:87 (vs. 82:95, 64% identical) binding
- Y139 (= Y147) mutation to F: Large decrease in activity and a small decrease in substrate affinity.
- 274:286 (vs. 288:300, 92% identical) binding
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)
47% identity, 98% coverage: 9:363/363 of query aligns to 4:367/371 of P18869
- T55 (= T59) 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)
40% identity, 98% coverage: 7:363/363 of query aligns to 1:331/334 of Q72IW9
- E57 (= E67) 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 80:82) binding
- S72 (≠ G82) 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 (= R102) binding in other chain
- R98 (= R112) binding in other chain
- R118 (= R140) binding in other chain
- Y125 (= Y147) binding in other chain; mutation to A: Reduces catalytic efficiency with isocitrate.
- V135 (≠ S159) mutation to M: Formation of homodimers instead of homotetramers. Increased affinity for isocitrate. Reduces enzyme activity with isocitrate.
- K171 (= K198) binding
- N173 (= N200) binding ; binding
- D204 (= D230) binding
- M208 (= M234) 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 (= F243) 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 (= D254) binding
- D232 (= D258) binding
- V238 (≠ T264) 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 288:292) binding
- N273 (= N300) binding
- R310 (= R338) 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
>GFF1875 FitnessBrowser__Marino:GFF1875
MEQGKNMPRTILMLPGDGIGPEIVAEAEKVLNKINDQFNLGLSFESGLVGGAAIDETDTP
LPDETLEKATRADAILLGAVGGPQWDSLPMAKRPEKGLLGLRSNLELFANLRPAILYPQL
ASASSLKPEVVSGLDIMIVRELTGGIYFGQPRGVRELESGERQGYNTYAYTESEIRRIGR
VAFEAAQQRGKKLCSVDKANVLEVTVLWREIMNDLRREYPDVELSHMYVDNAAMQLVRAP
KQFDVIVTGNMFGDILSDEAAMLTGSIGMLPSASLNSEKQGMYEPCHGSAPDIAGQGIAN
PLATILSAAMMLRYSLNEEKAAEAIEAAVSKVLDQGLRTADIMSEGAKKVSTREMGEAVL
AAL
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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