SitesBLAST
Comparing WP_017598162.1 NCBI__GCF_000341125.1:WP_017598162.1 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)
65% identity, 97% coverage: 7:348/354 of query aligns to 3:335/337 of 2g4oA
3flkA Crystal structure of tartrate dehydrogenase from pseudomonas putida in complex with nadh, oxalate and metal ion (see paper)
45% identity, 96% coverage: 5:343/354 of query aligns to 1:349/359 of 3flkA
- active site: Y137 (= Y139), K188 (= K190), D221 (= D223), D245 (= D247), D249 (= D251)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I12 (= I16), A73 (= A76), V74 (= V77), G75 (= G78), D82 (≠ S84), L90 (= L92), N190 (= N192), I222 (≠ A224), R226 (≠ F228), I258 (= I260), H280 (= H282), G281 (= G283), S282 (= S284), A283 (= A285), I286 (= I288), N293 (≠ D295)
- binding oxalate ion: R94 (= R96), R104 (= R106), R130 (= R132), D245 (= D247)
6lkyA Crystal structure of isocitrate dehydrogenase from methylococcus capsulatus
41% identity, 90% coverage: 7:323/354 of query aligns to 3:304/339 of 6lkyA
- active site: Y123 (= Y139), K174 (= K190), D207 (= D223), D231 (= D247)
- binding nicotinamide-adenine-dinucleotide: P68 (≠ A76), L69 (≠ V77), T71 (≠ V82), N81 (≠ L92), H263 (= H282), G264 (= G283), S265 (= S284), A266 (= A285), D268 (= D287), I269 (= I288), N276 (≠ D295)
3vmkA 3-isopropylmalate dehydrogenase from shewanella benthica db21 mt-2 (see paper)
40% identity, 98% coverage: 5:352/354 of query aligns to 8:368/369 of 3vmkA
2y42D Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with nadh and mn (see paper)
43% identity, 91% coverage: 5:327/354 of query aligns to 1:320/355 of 2y42D
- active site: Y140 (= Y139), K186 (= K190), D218 (= D223), D242 (= D247), D246 (= D251)
- binding manganese (ii) ion: D242 (= D247), D246 (= D251)
- binding nicotinamide-adenine-dinucleotide: I12 (= I16), D79 (vs. gap), H274 (= H282), G275 (= G283), A277 (= A285), D279 (= D287), I280 (= I288), N287 (≠ D295)
2y41A Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with ipm and mn (see paper)
43% identity, 91% coverage: 5:327/354 of query aligns to 1:320/346 of 2y41A
2ztwA Structure of 3-isopropylmalate dehydrogenase in complex with the inhibitor and NAD+ (see paper)
43% identity, 91% coverage: 6:327/354 of query aligns to 1:319/345 of 2ztwA
- active site: Y139 (= Y139), K185 (= K190), D217 (= D223), D241 (= D247), D245 (= D251)
- binding magnesium ion: G203 (= G209), Y206 (= Y212), V209 (= V215)
- binding nicotinamide-adenine-dinucleotide: I11 (= I16), H273 (= H282), G274 (= G283), A276 (= A285), D278 (= D287), I279 (= I288), A285 (= A294), N286 (≠ D295)
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)
43% identity, 91% coverage: 6:327/354 of query aligns to 1:319/345 of Q5SIY4
- 74:87 (vs. 79:89, 14% identical) binding NAD(+)
- Y139 (= Y139) mutation to F: Large decrease in activity and a small decrease in substrate affinity.
- 274:286 (vs. 283:295, 77% identical) binding NAD(+)
1cnzA 3-isopropylmalate dehydrogenase (ipmdh) from salmonella typhimurium (see paper)
38% identity, 99% coverage: 3:352/354 of query aligns to 2:361/363 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)
38% identity, 99% coverage: 3:352/354 of query aligns to 2:361/363 of P37412
- D227 (= D223) binding Mn(2+)
- D251 (= D247) binding Mn(2+)
- D255 (= D251) binding Mn(2+)
6m3sB Dimeric isocitrate dehydrogenase from xanthomonas campestris pv. Campestris 8004
40% identity, 92% coverage: 5:330/354 of query aligns to 5:314/338 of 6m3sB
- active site: Y128 (= Y139), K177 (= K190), D210 (= D223), D234 (= D247)
- binding isocitrate calcium complex: T75 (≠ D79), S83 (≠ E88), N85 (≠ G90), R89 (= R94), R99 (= R106), R121 (= R132), Y128 (= Y139), D234 (= D247), D238 (= D251)
- binding nicotinamide-adenine-dinucleotide: P72 (≠ A76), L73 (≠ V77), T75 (≠ D79), N85 (≠ G90), H266 (= H282), G267 (= G283), S268 (= S284), A269 (= A285), D271 (= D287), I272 (= I288), N279 (≠ D295)
3vkzA 3-isopropylmalate dehydrogenase from shewanella oneidensis mr-1 at atmospheric pressure (see paper)
40% identity, 97% coverage: 5:347/354 of query aligns to 2:357/364 of 3vkzA
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)
42% identity, 90% coverage: 7:323/354 of query aligns to 4:301/334 of Q72IW9
- E57 (≠ D64) 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 (≠ VGD 77:79) binding NADH
- S72 (≠ D79) 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 (≠ L93) 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 (≠ R94) 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 (= R96) binding in other chain
- R98 (= R106) binding in other chain
- R118 (= R132) binding in other chain
- Y125 (= Y139) binding in other chain; mutation to A: Reduces catalytic efficiency with isocitrate.
- V135 (≠ I154) mutation to M: Formation of homodimers instead of homotetramers. Increased affinity for isocitrate. Reduces enzyme activity with isocitrate.
- K171 (= K190) binding (2R,3S)-homoisocitrate
- N173 (= N192) binding (2R,3S)-homoisocitrate; binding NADH
- D204 (= D223) binding Mg(2+)
- M208 (= M227) 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 (= F236) 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 (= D247) binding Mg(2+)
- D232 (= D251) binding Mg(2+)
- V238 (≠ T257) 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 283:287) binding NADH
- N273 (≠ D295) binding NADH
Sites not aligning to the query:
- 310 R→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
42% identity, 90% coverage: 7:323/354 of query aligns to 3:300/333 of 4yb4A