SitesBLAST
Comparing WP_011842036.1 NCBI__GCF_000015985.1:WP_011842036.1 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)
64% identity, 99% coverage: 6:357/357 of query aligns to 2:357/359 of 3flkA
- active site: Y137 (= Y141), K188 (= K192), D221 (= D225), D245 (= D249), D249 (= D253)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I12 (= I16), A73 (= A77), V74 (= V78), G75 (= G79), D82 (= D86), L90 (= L94), N190 (= N194), I222 (= I226), R226 (≠ H230), I258 (= I262), H280 (= H284), G281 (= G285), S282 (= S286), A283 (= A287), I286 (= I290), N293 (= N297)
- binding oxalate ion: R94 (= R98), R104 (= R108), R130 (= R134), D245 (= D249)
2g4oA Anomalous substructure of 3-isopropylmalate dehydrogenase (see paper)
45% identity, 93% coverage: 7:339/357 of query aligns to 3:329/337 of 2g4oA
4yb4A Crystal structure of homoisocitrate dehydrogenase from thermus thermophilus in complex with homoisocitrate, magnesium ion (ii) and nadh
40% identity, 98% coverage: 7:356/357 of query aligns to 3:330/333 of 4yb4A
- active site: Y124 (= Y141), K170 (= K192), D203 (= D225), D227 (= D249), D231 (= D253)
- binding (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylic acid: S71 (≠ W80), R84 (≠ I95), R87 (= R98), R97 (= R108), R117 (= R134), Y124 (= Y141), D227 (= D249)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I12 (= I16), A69 (≠ V78), T70 (≠ G79), S71 (≠ W80), I201 (≠ H223), N204 (≠ I226), L240 (≠ I262), E256 (= E281), H259 (= H284), G260 (= G285), S261 (= S286), A262 (= A287), D264 (= D289), I265 (= I290), N272 (= N297), D312 (= D338)
3asjB Crystal structure of homoisocitrate dehydrogenase in complex with a designed inhibitor (see paper)
40% identity, 98% coverage: 7:356/357 of query aligns to 3:330/333 of 3asjB
- active site: Y124 (= Y141), K170 (= K192), D203 (= D225), D227 (= D249), D231 (= D253)
- binding (2Z)-3-[(carboxymethyl)sulfanyl]-2-hydroxyprop-2-enoic acid: R84 (≠ I95), R97 (= R108), R117 (= R134), Y124 (= Y141), D227 (= D249), D231 (= D253), V258 (= V283)
3asjA Crystal structure of homoisocitrate dehydrogenase in complex with a designed inhibitor (see paper)
40% identity, 98% coverage: 7:356/357 of query aligns to 3:330/333 of 3asjA
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)
40% identity, 98% coverage: 7:356/357 of query aligns to 4:331/334 of Q72IW9
- E57 (= E65) 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 (≠ VGW 78:80) binding NADH
- S72 (≠ W80) 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 (≠ I95) 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 (≠ Q96) 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 (= R98) binding in other chain
- R98 (= R108) binding in other chain
- R118 (= R134) binding in other chain
- Y125 (= Y141) binding in other chain; mutation to A: Reduces catalytic efficiency with isocitrate.
- V135 (≠ I156) mutation to M: Formation of homodimers instead of homotetramers. Increased affinity for isocitrate. Reduces enzyme activity with isocitrate.
- K171 (= K192) binding (2R,3S)-homoisocitrate
- N173 (= N194) binding (2R,3S)-homoisocitrate; binding NADH
- D204 (= D225) binding Mg(2+)
- M208 (≠ A229) 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 (= F238) 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 (= D249) binding Mg(2+)
- D232 (= D253) binding Mg(2+)
- V238 (≠ T259) 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.
6xxyA Crystal structure of haemophilus influenzae 3-isopropylmalate dehydrogenase in complex with o-isobutenyl oxalylhydroxamate. (see paper)
39% identity, 98% coverage: 7:356/357 of query aligns to 5:358/358 of 6xxyA
- active site: Y144 (= Y141), K194 (= K192), D226 (= D225), D250 (= D249)
- binding magnesium ion: D250 (= D249), D254 (= D253)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ A77), V75 (= V78), G76 (= G79), E90 (≠ L90), L94 (= L94), Y224 (≠ H223), N227 (≠ I226), M230 (≠ A229), M263 (≠ I262), G264 (= G263), 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 (≠ L90), R108 (= R108), R137 (= R134), K194 (= K192), V197 (≠ G195), D226 (= D225), D250 (= D249)
2y42D Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with nadh and mn (see paper)
39% identity, 95% coverage: 6:345/357 of query aligns to 2:334/355 of 2y42D
- active site: Y140 (= Y141), K186 (= K192), D218 (= D225), D242 (= D249), D246 (= D253)
- binding manganese (ii) ion: D242 (= D249), D246 (= D253)
- binding nicotinamide-adenine-dinucleotide: I12 (= I16), D79 (vs. gap), H274 (= H284), G275 (= G285), A277 (= A287), D279 (= D289), I280 (= I290), N287 (= N297)
2y41A Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with ipm and mn (see paper)
39% identity, 95% coverage: 6:345/357 of query aligns to 2:334/346 of 2y41A
6lkyA Crystal structure of isocitrate dehydrogenase from methylococcus capsulatus
36% identity, 97% coverage: 7:354/357 of query aligns to 3:335/339 of 6lkyA
- active site: Y123 (= Y141), K174 (= K192), D207 (= D225), D231 (= D249)
- binding nicotinamide-adenine-dinucleotide: P68 (= P81), L69 (≠ A82), T71 (≠ V84), N81 (≠ L94), H263 (= H284), G264 (= G285), S265 (= S286), A266 (= A287), D268 (= D289), I269 (= I290), N276 (= N297)
2ztwA Structure of 3-isopropylmalate dehydrogenase in complex with the inhibitor and NAD+ (see paper)
39% identity, 95% coverage: 6:345/357 of query aligns to 1:333/345 of 2ztwA
- active site: Y139 (= Y141), K185 (= K192), D217 (= D225), D241 (= D249), D245 (= D253)
- binding magnesium ion: G203 (≠ A211), Y206 (= Y214), V209 (= V217)
- binding nicotinamide-adenine-dinucleotide: I11 (= I16), 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)
39% identity, 95% coverage: 6:345/357 of query aligns to 1:333/345 of Q5SIY4
- 74:87 (vs. 80:91, 14% identical) binding NAD(+)
- Y139 (= Y141) mutation to F: Large decrease in activity and a small decrease in substrate affinity.
- 274:286 (vs. 285:297, 92% identical) binding NAD(+)
3vkzA 3-isopropylmalate dehydrogenase from shewanella oneidensis mr-1 at atmospheric pressure (see paper)
39% identity, 98% coverage: 7:356/357 of query aligns to 4:360/364 of 3vkzA
6m3sB Dimeric isocitrate dehydrogenase from xanthomonas campestris pv. Campestris 8004
35% identity, 98% coverage: 8:356/357 of query aligns to 8:338/338 of 6m3sB
- active site: Y128 (= Y141), K177 (= K192), D210 (= D225), D234 (= D249)
- binding isocitrate calcium complex: T75 (≠ V84), S83 (≠ G92), N85 (≠ L94), R89 (= R98), R99 (= R108), R121 (= R134), Y128 (= Y141), D234 (= D249), D238 (= D253)
- binding nicotinamide-adenine-dinucleotide: P72 (= P81), L73 (≠ A82), T75 (≠ V84), N85 (≠ L94), H266 (= H284), G267 (= G285), S268 (= S286), A269 (= A287), D271 (= D289), I272 (= I290), N279 (= N297)
3vmkA 3-isopropylmalate dehydrogenase from shewanella benthica db21 mt-2 (see paper)
38% identity, 98% coverage: 7:356/357 of query aligns to 10:366/369 of 3vmkA
1cnzA 3-isopropylmalate dehydrogenase (ipmdh) from salmonella typhimurium (see paper)
39% identity, 97% coverage: 1:347/357 of query aligns to 1:347/363 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, 97% coverage: 1:347/357 of query aligns to 1:347/363 of P37412
- D227 (= D225) binding Mn(2+)
- D251 (= D249) binding Mn(2+)
- D255 (= D253) binding Mn(2+)
P40495 Homoisocitrate dehydrogenase, mitochondrial; HIcDH; EC 1.1.1.87 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
35% identity, 96% coverage: 2:345/357 of query aligns to 20:360/371 of P40495
- Y150 (= Y141) mutation to F: Strongly reduced enzyme activity.
- K206 (= K192) mutation to M: Strongly reduced enzyme activity.
2d1cA Crystal structure of tt0538 protein from thermus thermophilus hb8
34% identity, 100% coverage: 1:357/357 of query aligns to 14:355/495 of 2d1cA
- active site: Y143 (= Y141), K190 (= K192), D223 (= D225), D247 (= D249), D251 (= D253)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P86 (= P81), L87 (≠ A82), E88 (≠ T83), T89 (≠ V84), N99 (≠ L94), I221 (≠ H223), N224 (≠ I226), Q228 (≠ H230), L260 (≠ I262), G261 (= G263), H279 (= H284), G280 (= G285), S281 (= S286), A282 (= A287), K284 (≠ D289), Y285 (≠ I290), I291 (≠ A296), N292 (= N297), D333 (= D338)
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)
35% identity, 97% coverage: 8:354/357 of query aligns to 46:392/404 of Q9SA14
- L134 (≠ I95) Confers substrate specificity; mutation to F: Enhanced activity toward 3-(2'-methylthio)-ethylmalate, but reduced catalytic efficiency with 3-isopropylmalate.
Query Sequence
>WP_011842036.1 NCBI__GCF_000015985.1:WP_011842036.1
MADNHLKIAVIAGDGIGKEVVPEGLRVLEAVAGRHRIDLRFEEFDFASCDYYARHGQMMP
DDWQERVGGHDALFFGAVGWPATVPDHVSLWGSLIQFRRQFDQYVNLRPARLMPGVPSPL
AGRGPGDIDMWIVRENTEGEYSAIGGRMYPGTEREIVLQETVMSRHGIDRVLRYAFELAN
RRERRRLTSATKSNGISITMPYWDERVEAMAQDYPDVAWDKYHIDILAAHFVLNPDRFDV
VVASNLFGDILSDLGPACTGTIGIAPSGNINPERAFPSLFEPVHGSAPDIAGQGIANPVG
QIWAGAMMLEHLGHAEAAAEIMAAIERVLADPRLRTRDLAGAADTVTCGKAIVEALG
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