SitesBLAST
Comparing WP_029001951.1 NCBI__GCF_000430725.1:WP_029001951.1 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)
6m3sB Dimeric isocitrate dehydrogenase from xanthomonas campestris pv. Campestris 8004
42% identity, 99% coverage: 3:351/354 of query aligns to 8:335/338 of 6m3sB
- active site: Y128 (= Y133), K177 (= K186), D210 (= D219), D234 (= D243)
- binding isocitrate calcium complex: T75 (≠ Y77), S83 (≠ N86), N85 (≠ S88), R89 (= R92), R99 (= R102), R121 (= R126), Y128 (= Y133), D234 (= D243), D238 (= D247)
- binding nicotinamide-adenine-dinucleotide: P72 (≠ H74), L73 (≠ A75), T75 (≠ Y77), N85 (≠ S88), H266 (= H275), G267 (= G276), S268 (= S277), A269 (= A278), D271 (= D280), I272 (= I281), N279 (= N288)
4yb4A Crystal structure of homoisocitrate dehydrogenase from thermus thermophilus in complex with homoisocitrate, magnesium ion (ii) and nadh
43% identity, 100% coverage: 2:354/354 of query aligns to 3:330/333 of 4yb4A
- active site: Y124 (= Y133), K170 (= K186), D203 (= D219), D227 (= D243), D231 (= D247)
- binding (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylic acid: S71 (≠ H74), R84 (≠ A89), R87 (= R92), R97 (= R102), R117 (= R126), Y124 (= Y133), D227 (= D243)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I12 (= I11), A69 (≠ Q72), T70 (≠ S73), S71 (≠ H74), I201 (≠ L217), N204 (≠ A220), L240 (= L256), E256 (≠ Q272), H259 (= H275), G260 (= G276), S261 (= S277), A262 (= A278), D264 (= D280), I265 (= I281), N272 (= N288), D312 (= D336)
3asjB Crystal structure of homoisocitrate dehydrogenase in complex with a designed inhibitor (see paper)
43% identity, 100% coverage: 2:354/354 of query aligns to 3:330/333 of 3asjB
- active site: Y124 (= Y133), K170 (= K186), D203 (= D219), D227 (= D243), D231 (= D247)
- binding (2Z)-3-[(carboxymethyl)sulfanyl]-2-hydroxyprop-2-enoic acid: R84 (≠ A89), R97 (= R102), R117 (= R126), Y124 (= Y133), D227 (= D243), D231 (= D247), V258 (≠ Q274)
3asjA Crystal structure of homoisocitrate dehydrogenase in complex with a designed inhibitor (see paper)
43% identity, 100% coverage: 2:354/354 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)
43% identity, 100% coverage: 2:354/354 of query aligns to 4:331/334 of Q72IW9
- E57 (≠ Q59) 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 (≠ QSH 72:74) binding NADH
- S72 (≠ H74) 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 (≠ A89) 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 (≠ G90) 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 (= R92) binding in other chain
- R98 (= R102) binding in other chain
- R118 (= R126) binding in other chain
- Y125 (= Y133) binding in other chain; mutation to A: Reduces catalytic efficiency with isocitrate.
- V135 (≠ M151) mutation to M: Formation of homodimers instead of homotetramers. Increased affinity for isocitrate. Reduces enzyme activity with isocitrate.
- K171 (= K186) binding (2R,3S)-homoisocitrate
- N173 (= N188) binding (2R,3S)-homoisocitrate; binding NADH
- D204 (= D219) binding Mg(2+)
- M208 (≠ A223) 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 (= F232) 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 (= D243) binding Mg(2+)
- D232 (= D247) binding Mg(2+)
- V238 (≠ S253) 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 276:280) binding NADH
- N273 (= N288) binding NADH
- R310 (= R333) 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.
6lkyA Crystal structure of isocitrate dehydrogenase from methylococcus capsulatus
40% identity, 97% coverage: 2:343/354 of query aligns to 3:324/339 of 6lkyA
- active site: Y123 (= Y133), K174 (= K186), D207 (= D219), D231 (= D243)
- binding nicotinamide-adenine-dinucleotide: P68 (≠ T71), L69 (≠ Q72), T71 (≠ A79), N81 (≠ S88), H263 (= H275), G264 (= G276), S265 (= S277), A266 (= A278), D268 (= D280), I269 (= I281), N276 (= N288)
2y41A Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with ipm and mn (see paper)
38% identity, 99% coverage: 1:352/354 of query aligns to 2:343/346 of 2y41A
2ztwA Structure of 3-isopropylmalate dehydrogenase in complex with the inhibitor and NAD+ (see paper)
38% identity, 99% coverage: 1:352/354 of query aligns to 1:342/345 of 2ztwA
- active site: Y139 (= Y133), K185 (= K186), D217 (= D219), D241 (= D243), D245 (= D247)
- binding magnesium ion: G203 (≠ A205), Y206 (≠ F208), V209 (= V211)
- binding nicotinamide-adenine-dinucleotide: I11 (= I11), H273 (= H275), G274 (= G276), A276 (= A278), D278 (= D280), I279 (= I281), A285 (= A287), N286 (= N288)
2y42D Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with nadh and mn (see paper)
38% identity, 99% coverage: 1:352/354 of query aligns to 2:343/355 of 2y42D
- active site: Y140 (= Y133), K186 (= K186), D218 (= D219), D242 (= D243), D246 (= D247)
- binding manganese (ii) ion: D242 (= D243), D246 (= D247)
- binding nicotinamide-adenine-dinucleotide: I12 (= I11), D79 (≠ P78), H274 (= H275), G275 (= G276), A277 (= A278), D279 (= D280), I280 (= I281), N287 (= N288)
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: 1:352/354 of query aligns to 1:342/345 of Q5SIY4
- 74:87 (vs. 74:81, 14% identical) binding NAD(+)
- Y139 (= Y133) mutation to F: Large decrease in activity and a small decrease in substrate affinity.
- 274:286 (vs. 276:288, 69% identical) binding NAD(+)
O14104 Homoisocitrate dehydrogenase; HICDH; EC 1.1.1.87 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
35% identity, 98% coverage: 5:350/354 of query aligns to 11:356/362 of O14104
- S81 (≠ L69) modified: Phosphoserine
- S91 (≠ A79) modified: Phosphoserine
3ty3A Crystal structure of homoisocitrate dehydrogenase from schizosaccharomyces pombe bound to glycyl-glycyl-glycine (see paper)
35% identity, 98% coverage: 5:350/354 of query aligns to 7:352/358 of 3ty3A
- active site: Y129 (= Y133), K192 (= K186), D228 (= D219), D252 (= D243), D256 (= D247)
- binding glycylglycylglycine: A74 (≠ G66), V75 (≠ I67), S77 (≠ L69), R93 (= R92), E281 (≠ Q272), P282 (≠ A273), H284 (= H275)
Q56268 3-isopropylmalate dehydrogenase; 3-IPM-DH; Beta-IPM dehydrogenase; IMDH; EC 1.1.1.85 from Acidithiobacillus ferrooxidans (Thiobacillus ferrooxidans) (see paper)
39% identity, 100% coverage: 2:354/354 of query aligns to 3:354/358 of Q56268
- R95 (= R92) binding substrate
- R105 (= R102) binding substrate
- R133 (= R126) binding substrate
- D222 (= D219) binding Mg(2+); binding substrate
- D246 (= D243) binding Mg(2+)
1a05A Crystal structure of the complex of 3-isopropylmalate dehydrogenase from thiobacillus ferrooxidans with 3-isopropylmalate (see paper)
39% identity, 100% coverage: 2:354/354 of query aligns to 3:354/357 of 1a05A
3vmkA 3-isopropylmalate dehydrogenase from shewanella benthica db21 mt-2 (see paper)
37% identity, 93% coverage: 2:329/354 of query aligns to 10:336/369 of 3vmkA
4y1pB Crystal structure of 3-isopropylmalate dehydrogenase (saci_0600) from sulfolobus acidocaldarius complex with 3-isopropylmalate and mg2+ (see paper)
35% identity, 95% coverage: 3:340/354 of query aligns to 4:321/336 of 4y1pB
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)
37% identity, 99% coverage: 3:354/354 of query aligns to 45:397/405 of P93832
- 114:129 (vs. 72:81, 13% identical) binding NAD(+)
- L132 (≠ G84) mutation to A: Reduced activity toward 3-isopropylmalate.
- L133 (≠ R85) 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 (≠ S88) binding substrate; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- R146 (= R102) binding substrate; mutation to A: Reduced activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- R174 (= R126) binding substrate; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- Y181 (= Y133) Important for catalysis; mutation Y->A,F,H: Reduced activity toward 3-isopropylmalate.
- K232 (= K186) Important for catalysis; mutation to M: Loss of activity toward 3-isopropylmalate.
- N234 (= N188) binding NAD(+); mutation N->A,D: Loss of activity toward 3-isopropylmalate.
- V235 (≠ S189) mutation to A: Reduced activity toward 3-isopropylmalate.
- D264 (= D219) binding Mg(2+); binding substrate; mutation to N: Loss of activity toward 3-isopropylmalate.
- N265 (≠ A220) binding NAD(+)
- D288 (= D243) binding Mg(2+); mutation to N: Loss of activity toward 3-isopropylmalate.
- D292 (= D247) binding Mg(2+); mutation to N: Reduced activity toward 3-isopropylmalate.
- 318:334 (vs. 272:288, 76% identical) binding NAD(+)
5j33A Isopropylmalate dehydrogenase in complex with NAD+ (see paper)
37% identity, 99% coverage: 3:354/354 of query aligns to 5:357/360 of 5j33A
- active site: Y141 (= Y133), K192 (= K186), D224 (= D219), D248 (= D243), D252 (= D247)
- binding magnesium ion: D248 (= D243), D252 (= D247)
- binding nicotinamide-adenine-dinucleotide: I74 (vs. gap), E89 (= E81), L92 (≠ G84), I261 (≠ L256), E278 (≠ Q272), H281 (= H275), G282 (= G276), S283 (= S277), A284 (= A278), I287 (= I281), N294 (= N288), D335 (= D336)
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)
38% identity, 99% coverage: 3:354/354 of query aligns to 49:401/409 of Q9FMT1
- F137 (= F91) Confers substrate specificity; mutation to L: Reduced activity toward 3-(2'-methylthio)-ethylmalate, but enhanced catalytic efficiency with 3-isopropylmalate.
- C232 (≠ T182) Essential for redox regulation; mutation to S: Reduced sensitivity to oxidation on enzyme activity regulation.
- C390 (= C343) Essential for redox regulation; mutation to S: Reduced sensitivity to oxidation on enzyme activity regulation.
5j32A Isopropylmalate dehydrogenase in complex with isopropylmalate (see paper)
36% identity, 99% coverage: 3:354/354 of query aligns to 15:367/369 of 5j32A
Query Sequence
>WP_029001951.1 NCBI__GCF_000430725.1:WP_029001951.1
MKILVLPGDGIGPEIVEASVGVLRAADAKYKLGLEFDYDDVGFASLEKHGTTLREEVLQK
ARGYDGIILGTQSHADYPAPEKGGRNVSAGFRIGLDLYANVRPARTRPFLESNMKPGKRM
DLVIMREATEGFYPDRNMARGWGEVMPSPDMALSTRKITRHCSERIARRAFELAMTRRRK
VTAIHKANSFHMTDGLFLEAVRHVAKDFPEVQLDDLLVDASTAHLVRSPERFDVIVATNF
YGDIISDLASELSGSLGLAGSMMASDTHCCAQAQHGSAPDIQGQDKANPVSMILSVAMLV
QWMGEHHRAPALSEAGAAIHAAVDRVLENPATRTADLGGTLGCKAFGEAVARAV
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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