SitesBLAST
Comparing WP_012755403.1 NCBI__GCF_000023185.1:WP_012755403.1 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)
3flkA Crystal structure of tartrate dehydrogenase from pseudomonas putida in complex with nadh, oxalate and metal ion (see paper)
53% identity, 88% coverage: 3:307/347 of query aligns to 1:310/359 of 3flkA
- active site: Y137 (= Y135), K188 (= K185), D221 (= D218), D245 (= D242), D249 (= D246)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I12 (= I14), A73 (= A74), V74 (= V75), G75 (= G76), D82 (= D83), L90 (= L91), N190 (= N187), I222 (≠ A219), R226 (= R223), I258 (≠ L255), H280 (= H277), G281 (= G278), S282 (= S279), A283 (= A280), I286 (= I283), N293 (= N290)
- binding oxalate ion: R94 (= R95), R104 (= R105), R130 (= R128), D245 (= D242)
2g4oA Anomalous substructure of 3-isopropylmalate dehydrogenase (see paper)
46% identity, 97% coverage: 5:342/347 of query aligns to 3:337/337 of 2g4oA
3vkzA 3-isopropylmalate dehydrogenase from shewanella oneidensis mr-1 at atmospheric pressure (see paper)
39% identity, 95% coverage: 3:332/347 of query aligns to 2:336/364 of 3vkzA
1cnzA 3-isopropylmalate dehydrogenase (ipmdh) from salmonella typhimurium (see paper)
39% identity, 94% coverage: 2:326/347 of query aligns to 3:334/363 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)
39% identity, 94% coverage: 2:326/347 of query aligns to 3:334/363 of P37412
- D227 (= D218) binding Mn(2+)
- D251 (= D242) binding Mn(2+)
- D255 (= D246) binding Mn(2+)
3vmkA 3-isopropylmalate dehydrogenase from shewanella benthica db21 mt-2 (see paper)
37% identity, 98% coverage: 3:343/347 of query aligns to 8:358/369 of 3vmkA
2y41A Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with ipm and mn (see paper)
38% identity, 99% coverage: 3:346/347 of query aligns to 1:345/346 of 2y41A
2ztwA Structure of 3-isopropylmalate dehydrogenase in complex with the inhibitor and NAD+ (see paper)
38% identity, 99% coverage: 5:346/347 of query aligns to 2:344/345 of 2ztwA
- active site: Y139 (= Y135), K185 (= K185), D217 (= D218), D241 (= D242), D245 (= D246)
- binding magnesium ion: G203 (≠ S204), Y206 (= Y207), V209 (≠ I210)
- binding nicotinamide-adenine-dinucleotide: I11 (= I14), H273 (= H277), G274 (= G278), A276 (= A280), D278 (= D282), I279 (= I283), A285 (= A289), N286 (= N290)
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)
38% identity, 99% coverage: 5:346/347 of query aligns to 2:344/345 of Q5SIY4
- 74:87 (vs. 77:88, 14% identical) binding NAD(+)
- Y139 (= Y135) mutation to F: Large decrease in activity and a small decrease in substrate affinity.
- 274:286 (vs. 278:290, 85% identical) binding NAD(+)
2y42D Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with nadh and mn (see paper)
38% identity, 98% coverage: 3:343/347 of query aligns to 1:342/355 of 2y42D
- active site: Y140 (= Y135), K186 (= K185), D218 (= D218), D242 (= D242), D246 (= D246)
- binding manganese (ii) ion: D242 (= D242), D246 (= D246)
- binding nicotinamide-adenine-dinucleotide: I12 (= I14), D79 (vs. gap), H274 (= H277), G275 (= G278), A277 (= A280), D279 (= D282), I280 (= I283), N287 (= N290)
6xxyA Crystal structure of haemophilus influenzae 3-isopropylmalate dehydrogenase in complex with o-isobutenyl oxalylhydroxamate. (see paper)
37% identity, 94% coverage: 1:325/347 of query aligns to 1:332/358 of 6xxyA
- active site: Y144 (= Y135), K194 (= K185), D226 (= D218), D250 (= D242)
- binding magnesium ion: D250 (= D242), D254 (= D246)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ A74), V75 (= V75), G76 (= G76), E90 (≠ L87), L94 (= L91), Y224 (≠ H216), N227 (≠ A219), M230 (≠ A222), M263 (≠ L255), G264 (= G256), E280 (= E274), G283 (≠ H277), G284 (= G278), S285 (= S279), A286 (= A280), P287 (= P281), D288 (= D282), I289 (= I283), N296 (= N290)
- binding 2-(2-methylprop-2-enoxyamino)-2-oxidanylidene-ethanoic acid: E90 (≠ L87), R108 (= R105), R137 (= R128), K194 (= K185), V197 (≠ A188), D226 (= D218), D250 (= D242)
Sites not aligning to the query:
6lkyA Crystal structure of isocitrate dehydrogenase from methylococcus capsulatus
38% identity, 94% coverage: 4:330/347 of query aligns to 2:316/339 of 6lkyA
- active site: Y123 (= Y135), K174 (= K185), D207 (= D218), D231 (= D242)
- binding nicotinamide-adenine-dinucleotide: P68 (= P78), L69 (≠ R79), T71 (≠ V81), N81 (≠ L91), H263 (= H277), G264 (= G278), S265 (= S279), A266 (= A280), D268 (= D282), I269 (= I283), N276 (= N290)
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)
39% identity, 90% coverage: 2:314/347 of query aligns to 45:363/409 of Q9FMT1
- F137 (≠ L92) Confers substrate specificity; mutation to L: Reduced activity toward 3-(2'-methylthio)-ethylmalate, but enhanced catalytic efficiency with 3-isopropylmalate.
- C232 (≠ A181) Essential for redox regulation; mutation to S: Reduced sensitivity to oxidation on enzyme activity regulation.
Sites not aligning to the query:
- 390 Essential for redox regulation; C→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)
38% identity, 90% coverage: 2:314/347 of query aligns to 41:359/405 of P93832
- 114:129 (vs. 75:87, 13% identical) binding NAD(+)
- L132 (= L90) mutation to A: Reduced activity toward 3-isopropylmalate.
- L133 (= L91) 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 (= R95) binding substrate; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- R146 (= R105) binding substrate; mutation to A: Reduced activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- R174 (= R128) binding substrate; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- Y181 (= Y135) Important for catalysis; mutation Y->A,F,H: Reduced activity toward 3-isopropylmalate.
- K232 (= K185) Important for catalysis; mutation to M: Loss of activity toward 3-isopropylmalate.
- N234 (= N187) binding NAD(+); mutation N->A,D: Loss of activity toward 3-isopropylmalate.
- V235 (≠ A188) mutation to A: Reduced activity toward 3-isopropylmalate.
- D264 (= D218) binding Mg(2+); binding substrate; mutation to N: Loss of activity toward 3-isopropylmalate.
- N265 (≠ A219) binding NAD(+)
- D288 (= D242) binding Mg(2+); mutation to N: Loss of activity toward 3-isopropylmalate.
- D292 (= D246) binding Mg(2+); mutation to N: Reduced activity toward 3-isopropylmalate.
- 318:334 (vs. 274:290, 71% identical) binding NAD(+)
5j32A Isopropylmalate dehydrogenase in complex with isopropylmalate (see paper)
38% identity, 90% coverage: 2:314/347 of query aligns to 11:329/369 of 5j32A
5j33A Isopropylmalate dehydrogenase in complex with NAD+ (see paper)
38% identity, 90% coverage: 2:314/347 of query aligns to 1:319/360 of 5j33A
- active site: Y141 (= Y135), K192 (= K185), D224 (= D218), D248 (= D242), D252 (= D246)
- binding magnesium ion: D248 (= D242), D252 (= D246)
- binding nicotinamide-adenine-dinucleotide: I74 (≠ V75), E89 (≠ L87), L92 (= L90), I261 (≠ L255), E278 (= E274), H281 (= H277), G282 (= G278), S283 (= S279), A284 (= A280), I287 (= I283), N294 (= N290)
Sites not aligning to the query:
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)
39% identity, 90% coverage: 2:314/347 of query aligns to 42:360/404 of Q9SA14
- L134 (= L91) Confers substrate specificity; mutation to F: Enhanced activity toward 3-(2'-methylthio)-ethylmalate, but reduced catalytic efficiency with 3-isopropylmalate.
4yb4A Crystal structure of homoisocitrate dehydrogenase from thermus thermophilus in complex with homoisocitrate, magnesium ion (ii) and nadh
38% identity, 99% coverage: 4:346/347 of query aligns to 2:330/333 of 4yb4A
- active site: Y124 (= Y135), K170 (= K185), D203 (= D218), D227 (= D242), D231 (= D246)
- binding (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylic acid: S71 (≠ W77), R84 (≠ L92), R87 (= R95), R97 (= R105), R117 (= R128), Y124 (= Y135), D227 (= D242)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I12 (= I14), A69 (≠ V75), T70 (≠ G76), S71 (≠ W77), I201 (≠ H216), N204 (≠ A219), L240 (= L255), E256 (= E274), H259 (= H277), G260 (= G278), S261 (= S279), A262 (= A280), D264 (= D282), I265 (= I283), N272 (= N290), D312 (≠ A328)
3asjB Crystal structure of homoisocitrate dehydrogenase in complex with a designed inhibitor (see paper)
38% identity, 99% coverage: 4:346/347 of query aligns to 2:330/333 of 3asjB
- active site: Y124 (= Y135), K170 (= K185), D203 (= D218), D227 (= D242), D231 (= D246)
- binding (2Z)-3-[(carboxymethyl)sulfanyl]-2-hydroxyprop-2-enoic acid: R84 (≠ L92), R97 (= R105), R117 (= R128), Y124 (= Y135), D227 (= D242), D231 (= D246), V258 (= V276)
3asjA Crystal structure of homoisocitrate dehydrogenase in complex with a designed inhibitor (see paper)
38% identity, 99% coverage: 4:346/347 of query aligns to 2:330/333 of 3asjA
Query Sequence
>WP_012755403.1 NCBI__GCF_000023185.1:WP_012755403.1
MKTYKIALLPGDGIGRDVTAAAWAVLEKTARLNGFSLDATSYPWSCDYYLENGSMMPADG
IETLRSFDAILLGAVGWPRKVPDSVSLHGLLLPIRKAFVQYANIRPHRLLPGVQGPLRSD
GFDILCIRENTEGEYSGAGGRVHQGTDNEVAVETSIFTRTGVERILRFGFEQARTRRGKL
ASVTKSNAQKYSMVFWDEITQKLSLEYPDIEVTSYHIDAMAARMVMAPDSLDVVVASNLF
GDILTDLGAAIQGGLGFAASANINPDRSAPSMFEPVHGSAPDIAELGIANPIAAIWSGAM
MLEHLGETAAAARVMASIEATTARGIGAIPGKDKTDAITASVLSALG
Or try a new SitesBLAST search
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