SitesBLAST
Comparing WP_029767971.1 NCBI__GCF_000527155.1:WP_029767971.1 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)
2g4oA Anomalous substructure of 3-isopropylmalate dehydrogenase (see paper)
65% identity, 98% coverage: 1:338/344 of query aligns to 1:335/337 of 2g4oA
3flkA Crystal structure of tartrate dehydrogenase from pseudomonas putida in complex with nadh, oxalate and metal ion (see paper)
42% identity, 99% coverage: 4:344/344 of query aligns to 4:359/359 of 3flkA
- active site: Y137 (= Y131), K188 (= K181), D221 (= D214), D245 (= D238), D249 (= D242)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I12 (= I12), A73 (= A68), V74 (= V69), G75 (= G70), D82 (≠ P76), L90 (= L84), N190 (= N183), I222 (≠ A215), R226 (≠ F219), I258 (= I251), H280 (= H273), G281 (= G274), S282 (= S275), A283 (= A276), I286 (= I279), N293 (≠ D286)
- binding oxalate ion: R94 (= R88), R104 (= R98), R130 (= R124), D245 (= D238)
3vkzA 3-isopropylmalate dehydrogenase from shewanella oneidensis mr-1 at atmospheric pressure (see paper)
41% identity, 92% coverage: 4:320/344 of query aligns to 5:330/364 of 3vkzA
2y42D Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with nadh and mn (see paper)
41% identity, 96% coverage: 3:331/344 of query aligns to 3:336/355 of 2y42D
- active site: Y140 (= Y131), K186 (= K181), D218 (= D214), D242 (= D238), D246 (= D242)
- binding manganese (ii) ion: D242 (= D238), D246 (= D242)
- binding nicotinamide-adenine-dinucleotide: I12 (= I12), D79 (vs. gap), H274 (= H273), G275 (= G274), A277 (= A276), D279 (= D278), I280 (= I279), N287 (≠ D286)
2y41A Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with ipm and mn (see paper)
41% identity, 96% coverage: 3:331/344 of query aligns to 3:336/346 of 2y41A
2ztwA Structure of 3-isopropylmalate dehydrogenase in complex with the inhibitor and NAD+ (see paper)
41% identity, 96% coverage: 3:331/344 of query aligns to 2:335/345 of 2ztwA
- active site: Y139 (= Y131), K185 (= K181), D217 (= D214), D241 (= D238), D245 (= D242)
- binding magnesium ion: G203 (≠ A200), Y206 (= Y203), V209 (= V206)
- binding nicotinamide-adenine-dinucleotide: I11 (= I12), H273 (= H273), G274 (= G274), A276 (= A276), D278 (= D278), I279 (= I279), A285 (= A285), N286 (≠ D286)
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)
41% identity, 96% coverage: 3:331/344 of query aligns to 2:335/345 of Q5SIY4
- 74:87 (vs. 71:81, 14% identical) binding NAD(+)
- Y139 (= Y131) mutation to F: Large decrease in activity and a small decrease in substrate affinity.
- 274:286 (vs. 274:286, 85% identical) binding NAD(+)
3vmkA 3-isopropylmalate dehydrogenase from shewanella benthica db21 mt-2 (see paper)
38% identity, 99% coverage: 4:342/344 of query aligns to 11:368/369 of 3vmkA
1cnzA 3-isopropylmalate dehydrogenase (ipmdh) from salmonella typhimurium (see paper)
38% identity, 99% coverage: 4:342/344 of query aligns to 7:361/363 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: 4:342/344 of query aligns to 7:361/363 of P37412
- D227 (= D214) binding Mn(2+)
- D251 (= D238) binding Mn(2+)
- D255 (= D242) binding Mn(2+)
6lkyA Crystal structure of isocitrate dehydrogenase from methylococcus capsulatus
38% identity, 98% coverage: 1:336/344 of query aligns to 1:337/339 of 6lkyA
- active site: Y123 (= Y131), K174 (= K181), D207 (= D214), D231 (= D238)
- binding nicotinamide-adenine-dinucleotide: P68 (≠ A68), L69 (≠ V69), T71 (≠ V74), N81 (≠ L84), H263 (= H273), G264 (= G274), S265 (= S275), A266 (= A276), D268 (= D278), I269 (= I279), N276 (≠ D286)
4iwhA Crystal structure of a 3-isopropylmalate dehydrogenase from burkholderia pseudomallei
38% identity, 98% coverage: 3:338/344 of query aligns to 5:356/358 of 4iwhA
4xxvA Crystal structure of 3-isopropylmalate dehydrogenase from burkholderia thailandensis in complex with NAD
38% identity, 98% coverage: 3:338/344 of query aligns to 3:354/356 of 4xxvA
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)
37% identity, 99% coverage: 3:344/344 of query aligns to 48:405/409 of Q9FMT1
- F137 (≠ L85) Confers substrate specificity; mutation to L: Reduced activity toward 3-(2'-methylthio)-ethylmalate, but enhanced catalytic efficiency with 3-isopropylmalate.
- C232 (≠ T177) Essential for redox regulation; mutation to S: Reduced sensitivity to oxidation on enzyme activity regulation.
- C390 (≠ T329) Essential for redox regulation; mutation to S: Reduced sensitivity to oxidation on enzyme activity regulation.
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)
38% identity, 99% coverage: 3:344/344 of query aligns to 45:402/404 of Q9SA14
- L134 (= L84) 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)
36% identity, 99% coverage: 3:344/344 of query aligns to 44:401/405 of P93832
- 114:129 (vs. 69:80, 16% identical) binding NAD(+)
- L132 (= L83) mutation to A: Reduced activity toward 3-isopropylmalate.
- L133 (= L84) 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 (= R88) binding substrate; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- R146 (= R98) binding substrate; mutation to A: Reduced activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- R174 (= R124) binding substrate; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- Y181 (= Y131) Important for catalysis; mutation Y->A,F,H: Reduced activity toward 3-isopropylmalate.
- K232 (= K181) Important for catalysis; mutation to M: Loss of activity toward 3-isopropylmalate.
- N234 (= N183) binding NAD(+); mutation N->A,D: Loss of activity toward 3-isopropylmalate.
- V235 (= V184) mutation to A: Reduced activity toward 3-isopropylmalate.
- D264 (= D214) binding Mg(2+); binding substrate; mutation to N: Loss of activity toward 3-isopropylmalate.
- N265 (≠ A215) binding NAD(+)
- D288 (= D238) binding Mg(2+); mutation to N: Loss of activity toward 3-isopropylmalate.
- D292 (= D242) binding Mg(2+); mutation to N: Reduced activity toward 3-isopropylmalate.
- 318:334 (vs. 270:286, 76% identical) binding NAD(+)
6xxyA Crystal structure of haemophilus influenzae 3-isopropylmalate dehydrogenase in complex with o-isobutenyl oxalylhydroxamate. (see paper)
37% identity, 92% coverage: 3:320/344 of query aligns to 5:331/358 of 6xxyA
- active site: Y144 (= Y131), K194 (= K181), D226 (= D214), D250 (= D238)
- binding magnesium ion: D250 (= D238), D254 (= D242)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ A68), V75 (= V69), G76 (= G70), E90 (= E80), L94 (= L84), Y224 (≠ H212), N227 (≠ A215), M230 (= M218), M263 (≠ I251), G264 (= G252), E280 (= E270), G283 (≠ H273), G284 (= G274), S285 (= S275), A286 (= A276), P287 (= P277), D288 (= D278), I289 (= I279), N296 (≠ D286)
- binding 2-(2-methylprop-2-enoxyamino)-2-oxidanylidene-ethanoic acid: E90 (= E80), R108 (= R98), R137 (= R124), K194 (= K181), V197 (= V184), D226 (= D214), D250 (= D238)
Sites not aligning to the query:
5j33A Isopropylmalate dehydrogenase in complex with NAD+ (see paper)
36% identity, 99% coverage: 3:343/344 of query aligns to 4:360/360 of 5j33A
- active site: Y141 (= Y131), K192 (= K181), D224 (= D214), D248 (= D238), D252 (= D242)
- binding magnesium ion: D248 (= D238), D252 (= D242)
- binding nicotinamide-adenine-dinucleotide: I74 (≠ V69), E89 (= E80), L92 (= L83), I261 (= I251), E278 (= E270), H281 (= H273), G282 (= G274), S283 (= S275), A284 (= A276), I287 (= I279), N294 (≠ D286), D335 (vs. gap)
5j32A Isopropylmalate dehydrogenase in complex with isopropylmalate (see paper)
38% identity, 91% coverage: 3:314/344 of query aligns to 14:333/369 of 5j32A
6m3sB Dimeric isocitrate dehydrogenase from xanthomonas campestris pv. Campestris 8004
36% identity, 93% coverage: 3:321/344 of query aligns to 7:314/338 of 6m3sB
- active site: Y128 (= Y131), K177 (= K181), D210 (= D214), D234 (= D238)
- binding isocitrate calcium complex: T75 (≠ V74), S83 (≠ G82), N85 (≠ L84), R89 (= R88), R99 (= R98), R121 (= R124), Y128 (= Y131), D234 (= D238), D238 (= D242)
- binding nicotinamide-adenine-dinucleotide: P72 (≠ A68), L73 (≠ V69), T75 (≠ V74), N85 (≠ L84), H266 (= H273), G267 (= G274), S268 (= S275), A269 (= A276), D271 (= D278), I272 (= I279), N279 (≠ D286)
Query Sequence
>WP_029767971.1 NCBI__GCF_000527155.1:WP_029767971.1
MSSIAVIPGDGIGKEVIDQAMKVVRLVLPDWEAVEYDLGASRYHATGEVLPDSVLSELDT
HDAILLGAVGDPSVPPGVLERGLLLRLRFEFDQYVNLRPSRLYPGVASPLAKVQPGEVDF
IVVREGTEGLYAGAGGNLHTGTAAEIATEESLNTRYGVERVVRDAFERARSRRGRLTLVH
KTNVLSHAGGLWNRAFADVAEEYRDVVTDYQHVDAAAMFMVNRPQDYDVVVTDNLFGDII
TDIAAAVTGGIGLAASGCVNPDRTHPSMFEPVHGSAPDIAGQGIADPIAAIMSASLLLEH
VGEAKAATVVQESIERELSSRSPGQAVGTEAVGDRVASDVEQRL
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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