SitesBLAST
Comparing WP_005351049.1 NCBI__GCF_000173975.1:WP_005351049.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
6xxyA Crystal structure of haemophilus influenzae 3-isopropylmalate dehydrogenase in complex with o-isobutenyl oxalylhydroxamate. (see paper)
58% identity, 100% coverage: 2:360/360 of query aligns to 3:358/358 of 6xxyA
- active site: Y144 (= Y146), K194 (= K195), D226 (= D227), D250 (= D251)
- binding magnesium ion: D250 (= D251), D254 (= D255)
- binding nicotinamide-adenine-dinucleotide: S74 (= S73), V75 (≠ I74), G76 (= G75), E90 (= E93), L94 (= L96), Y224 (≠ L225), N227 (= N228), M230 (= M231), M263 (≠ I264), G264 (= G265), E280 (= E281), G283 (≠ H284), G284 (= G285), S285 (= S286), A286 (= A287), P287 (= P288), D288 (= D289), I289 (= I290), N296 (= N297), D337 (= D338)
- binding 2-(2-methylprop-2-enoxyamino)-2-oxidanylidene-ethanoic acid: E90 (= E93), R108 (= R110), R137 (= R139), K194 (= K195), V197 (= V198), D226 (= D227), D250 (= D251)
1cnzA 3-isopropylmalate dehydrogenase (ipmdh) from salmonella typhimurium (see paper)
53% identity, 100% coverage: 2:360/360 of query aligns to 4:359/363 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)
53% identity, 100% coverage: 2:360/360 of query aligns to 4:359/363 of P37412
- D227 (= D227) binding Mn(2+)
- D251 (= D251) binding Mn(2+)
- D255 (= D255) binding Mn(2+)
1a05A Crystal structure of the complex of 3-isopropylmalate dehydrogenase from thiobacillus ferrooxidans with 3-isopropylmalate (see paper)
54% identity, 98% coverage: 4:356/360 of query aligns to 3:350/357 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)
54% identity, 98% coverage: 4:356/360 of query aligns to 3:350/358 of Q56268
- R95 (= R100) binding substrate
- R105 (= R110) binding substrate
- R133 (= R139) binding substrate
- D222 (= D227) binding Mg(2+); binding substrate
- D246 (= D251) binding Mg(2+)
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)
55% identity, 98% coverage: 3:353/360 of query aligns to 44:391/404 of Q9SA14
- L134 (= L97) 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)
54% identity, 98% coverage: 3:353/360 of query aligns to 47:394/409 of Q9FMT1
- F137 (≠ L97) Confers substrate specificity; mutation to L: Reduced activity toward 3-(2'-methylthio)-ethylmalate, but enhanced catalytic efficiency with 3-isopropylmalate.
- C232 (≠ T191) Essential for redox regulation; mutation to S: Reduced sensitivity to oxidation on enzyme activity regulation.
- C390 (= C349) Essential for redox regulation; mutation to S: Reduced sensitivity to oxidation on enzyme activity regulation.
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)
54% identity, 98% coverage: 3:353/360 of query aligns to 43:390/405 of P93832
- 114:129 (vs. 74:93, 40% identical) binding NAD(+)
- L132 (= L96) mutation to A: Reduced activity toward 3-isopropylmalate.
- L133 (= L97) 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 (= R100) binding substrate; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- R146 (= R110) binding substrate; mutation to A: Reduced activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- R174 (= R139) binding substrate; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- Y181 (= Y146) Important for catalysis; mutation Y->A,F,H: Reduced activity toward 3-isopropylmalate.
- K232 (= K195) Important for catalysis; mutation to M: Loss of activity toward 3-isopropylmalate.
- N234 (= N197) binding NAD(+); mutation N->A,D: Loss of activity toward 3-isopropylmalate.
- V235 (= V198) mutation to A: Reduced activity toward 3-isopropylmalate.
- D264 (= D227) binding Mg(2+); binding substrate; mutation to N: Loss of activity toward 3-isopropylmalate.
- N265 (= N228) binding NAD(+)
- D288 (= D251) binding Mg(2+); mutation to N: Loss of activity toward 3-isopropylmalate.
- D292 (= D255) binding Mg(2+); mutation to N: Reduced activity toward 3-isopropylmalate.
- 318:334 (vs. 281:297, 88% identical) binding NAD(+)
3vmkA 3-isopropylmalate dehydrogenase from shewanella benthica db21 mt-2 (see paper)
52% identity, 100% coverage: 2:360/360 of query aligns to 8:366/369 of 3vmkA
5j32A Isopropylmalate dehydrogenase in complex with isopropylmalate (see paper)
54% identity, 98% coverage: 3:353/360 of query aligns to 13:360/369 of 5j32A
5j33A Isopropylmalate dehydrogenase in complex with NAD+ (see paper)
54% identity, 98% coverage: 3:353/360 of query aligns to 3:350/360 of 5j33A
- active site: Y141 (= Y146), K192 (= K195), D224 (= D227), D248 (= D251), D252 (= D255)
- binding magnesium ion: D248 (= D251), D252 (= D255)
- binding nicotinamide-adenine-dinucleotide: I74 (= I74), E89 (= E93), L92 (= L96), I261 (= I264), E278 (= E281), H281 (= H284), G282 (= G285), S283 (= S286), A284 (= A287), I287 (= I290), N294 (= N297), D335 (= D338)
4iwhA Crystal structure of a 3-isopropylmalate dehydrogenase from burkholderia pseudomallei
53% identity, 98% coverage: 4:356/360 of query aligns to 5:354/358 of 4iwhA
4xxvA Crystal structure of 3-isopropylmalate dehydrogenase from burkholderia thailandensis in complex with NAD
53% identity, 98% coverage: 4:356/360 of query aligns to 3:352/356 of 4xxvA
3vkzA 3-isopropylmalate dehydrogenase from shewanella oneidensis mr-1 at atmospheric pressure (see paper)
51% identity, 100% coverage: 2:360/360 of query aligns to 2:360/364 of 3vkzA
2y41A Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with ipm and mn (see paper)
50% identity, 91% coverage: 2:330/360 of query aligns to 1:320/346 of 2y41A
2y42D Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with nadh and mn (see paper)
50% identity, 91% coverage: 2:330/360 of query aligns to 1:320/355 of 2y42D
- active site: Y140 (= Y146), K186 (= K195), D218 (= D227), D242 (= D251), D246 (= D255)
- binding manganese (ii) ion: D242 (= D251), D246 (= D255)
- binding nicotinamide-adenine-dinucleotide: I12 (= I13), D79 (≠ Y84), H274 (= H284), G275 (= G285), A277 (= A287), D279 (= D289), I280 (= I290), N287 (= N297)
2ztwA Structure of 3-isopropylmalate dehydrogenase in complex with the inhibitor and NAD+ (see paper)
50% identity, 91% coverage: 4:330/360 of query aligns to 2:319/345 of 2ztwA
- active site: Y139 (= Y146), K185 (= K195), D217 (= D227), D241 (= D251), D245 (= D255)
- binding magnesium ion: G203 (≠ A213), Y206 (= Y216), V209 (= V219)
- binding nicotinamide-adenine-dinucleotide: I11 (= I13), H273 (= H284), G274 (= G285), A276 (= A287), D278 (= D289), I279 (= I290), A285 (= A296), N286 (= N297)
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, 91% coverage: 4:330/360 of query aligns to 2:319/345 of Q5SIY4
- 74:87 (vs. 76:93, 39% identical) binding NAD(+)
- Y139 (= Y146) mutation to F: Large decrease in activity and a small decrease in substrate affinity.
- 274:286 (vs. 285:297, 85% identical) binding NAD(+)
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, 95% coverage: 4:345/360 of query aligns to 5:356/371 of P18869
- T55 (≠ K53) 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, 96% coverage: 1:346/360 of query aligns to 1:321/334 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.
- ATS 70:72 (≠ TTS 79:81) binding NADH
- S72 (= S81) 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 (≠ L97) 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 (≠ A98) 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 (= R100) binding in other chain
- R98 (= R110) binding in other chain
- R118 (= R139) binding in other chain
- Y125 (= Y146) binding in other chain; mutation to A: Reduces catalytic efficiency with isocitrate.
- V135 (≠ D156) mutation to M: Formation of homodimers instead of homotetramers. Increased affinity for isocitrate. Reduces enzyme activity with isocitrate.
- K171 (= K195) binding (2R,3S)-homoisocitrate
- N173 (= N197) binding (2R,3S)-homoisocitrate; binding NADH
- D204 (= D227) binding Mg(2+)
- M208 (= M231) 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 (= F240) 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 (= D251) binding Mg(2+)
- D232 (= D255) binding Mg(2+)
- V238 (≠ T261) 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 285:289) binding NADH
- N273 (= N297) binding NADH
- R310 (= R335) 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_005351049.1 NCBI__GCF_000173975.1:WP_005351049.1
MSYKVGVIRGDGIGPEIVAEALKVLDKVAEKYNETFDYTDILLGGASIDATGKPLTEEAL
ETAKSCDAVLMGSIGGNTTTSPWYKLPANLRPEAGLLAIRKGLGLFANMRPAYLYEELKD
ACPLREDIIGDGFDLVVMRELTGGLYFGERKTFEEDGVTKAVDTLTYSEEEIRRIAIRGF
DIAMKRRKKVTSVDKANVLDSSRLWRKVVNEVAKDYPEVELEHMLVDNCAMQLVRDPKQF
DVILTENMFGDILSDEASMVTGSIGMLSSASLKEGSFGLYEPSHGSAPDIAGQDIANPIA
TILSASMLLRYSFNMDEAADAVDNAVKQVLKDGYRTVDIMSEGMTKVGCKEMGTLIAERI
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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