SitesBLAST
Comparing WP_085545223.1 NCBI__GCF_900177735.1:WP_085545223.1 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)
2g4oA Anomalous substructure of 3-isopropylmalate dehydrogenase (see paper)
39% identity, 96% coverage: 6:369/380 of query aligns to 4:335/337 of 2g4oA
3flkA Crystal structure of tartrate dehydrogenase from pseudomonas putida in complex with nadh, oxalate and metal ion (see paper)
34% identity, 97% coverage: 6:373/380 of query aligns to 4:358/359 of 3flkA
- active site: Y137 (= Y137), K188 (= K209), D221 (= D241), D245 (= D265), D249 (= D269)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I12 (= I14), A73 (= A74), V74 (≠ I75), G75 (= G76), D82 (≠ G83), L90 (= L90), N190 (= N211), I222 (≠ A242), R226 (≠ H246), I258 (≠ L278), H280 (= H297), G281 (= G298), S282 (= S299), A283 (= A300), I286 (= I303), N293 (= N310)
- binding oxalate ion: R94 (= R94), R104 (= R104), R130 (= R130), D245 (= D265)
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)
36% identity, 97% coverage: 6:372/380 of query aligns to 5:332/334 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 (≠ IGD 75:77) binding NADH
- S72 (≠ D77) 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 (≠ L91) 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 (≠ T92) 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 (= R94) binding in other chain
- R98 (= R104) binding in other chain
- R118 (= R130) binding in other chain
- Y125 (= Y137) binding in other chain; mutation to A: Reduces catalytic efficiency with isocitrate.
- V135 (≠ M173) mutation to M: Formation of homodimers instead of homotetramers. Increased affinity for isocitrate. Reduces enzyme activity with isocitrate.
- K171 (= K209) binding (2R,3S)-homoisocitrate
- N173 (= N211) binding (2R,3S)-homoisocitrate; binding NADH
- D204 (= D241) binding Mg(2+)
- M208 (≠ Y245) 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 (= F254) 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 (= D265) binding Mg(2+)
- D232 (= D269) binding Mg(2+)
- V238 (≠ T275) 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 298:302) binding NADH
- N273 (= N310) binding NADH
- R310 (= R349) 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.
4yb4A Crystal structure of homoisocitrate dehydrogenase from thermus thermophilus in complex with homoisocitrate, magnesium ion (ii) and nadh
36% identity, 97% coverage: 6:372/380 of query aligns to 4:331/333 of 4yb4A
- active site: Y124 (= Y137), K170 (= K209), D203 (= D241), D227 (= D265), D231 (= D269)
- binding (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylic acid: S71 (≠ D77), R84 (≠ L91), R87 (= R94), R97 (= R104), R117 (= R130), Y124 (= Y137), D227 (= D265)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I12 (= I14), A69 (≠ I75), T70 (≠ G76), S71 (≠ D77), I201 (≠ N239), N204 (≠ A242), L240 (= L278), E256 (= E294), H259 (= H297), G260 (= G298), S261 (= S299), A262 (= A300), D264 (= D302), I265 (= I303), N272 (= N310), D312 (≠ E353)
3asjB Crystal structure of homoisocitrate dehydrogenase in complex with a designed inhibitor (see paper)
36% identity, 97% coverage: 6:372/380 of query aligns to 4:331/333 of 3asjB
- active site: Y124 (= Y137), K170 (= K209), D203 (= D241), D227 (= D265), D231 (= D269)
- binding (2Z)-3-[(carboxymethyl)sulfanyl]-2-hydroxyprop-2-enoic acid: R84 (≠ L91), R97 (= R104), R117 (= R130), Y124 (= Y137), D227 (= D265), D231 (= D269), V258 (≠ I296)
3asjA Crystal structure of homoisocitrate dehydrogenase in complex with a designed inhibitor (see paper)
36% identity, 97% coverage: 6:372/380 of query aligns to 4:331/333 of 3asjA
P40495 Homoisocitrate dehydrogenase, mitochondrial; HIcDH; EC 1.1.1.87 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
34% identity, 96% coverage: 5:369/380 of query aligns to 25:369/371 of P40495
- Y150 (= Y137) mutation to F: Strongly reduced enzyme activity.
- K206 (= K209) mutation to M: Strongly reduced enzyme activity.
Q56268 3-isopropylmalate dehydrogenase; 3-IPM-DH; Beta-IPM dehydrogenase; IMDH; EC 1.1.1.85 from Acidithiobacillus ferrooxidans (Thiobacillus ferrooxidans) (see paper)
35% identity, 90% coverage: 3:344/380 of query aligns to 1:326/358 of Q56268
- R95 (= R94) binding substrate
- R105 (= R104) binding substrate
- R133 (= R130) binding substrate
- D222 (= D241) binding Mg(2+); binding substrate
- D246 (= D265) binding Mg(2+)
1a05A Crystal structure of the complex of 3-isopropylmalate dehydrogenase from thiobacillus ferrooxidans with 3-isopropylmalate (see paper)
35% identity, 90% coverage: 3:344/380 of query aligns to 1:326/357 of 1a05A
2y42D Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with nadh and mn (see paper)
34% identity, 95% coverage: 6:367/380 of query aligns to 4:341/355 of 2y42D
- active site: Y140 (= Y137), K186 (= K209), D218 (= D241), D242 (= D265), D246 (= D269)
- binding manganese (ii) ion: D242 (= D265), D246 (= D269)
- binding nicotinamide-adenine-dinucleotide: I12 (= I14), D79 (≠ G83), H274 (= H297), G275 (= G298), A277 (= A300), D279 (= D302), I280 (= I303), N287 (= N310)
2ztwA Structure of 3-isopropylmalate dehydrogenase in complex with the inhibitor and NAD+ (see paper)
34% identity, 95% coverage: 6:367/380 of query aligns to 3:340/345 of 2ztwA
- active site: Y139 (= Y137), K185 (= K209), D217 (= D241), D241 (= D265), D245 (= D269)
- binding magnesium ion: G203 (≠ A228), Y206 (≠ Q231), V209 (≠ M233)
- binding nicotinamide-adenine-dinucleotide: I11 (= I14), H273 (= H297), G274 (= G298), A276 (= A300), D278 (= D302), I279 (= I303), A285 (= A309), N286 (= N310)
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)
34% identity, 95% coverage: 6:367/380 of query aligns to 3:340/345 of Q5SIY4
- 74:87 (vs. 77:89, 31% identical) binding NAD(+)
- Y139 (= Y137) mutation to F: Large decrease in activity and a small decrease in substrate affinity.
- 274:286 (vs. 298:310, 77% identical) binding NAD(+)
2y41A Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with ipm and mn (see paper)
34% identity, 95% coverage: 6:367/380 of query aligns to 4:341/346 of 2y41A