SitesBLAST
Comparing WP_011813628.1 NCBI__GCF_000015585.1:WP_011813628.1 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)
39% identity, 96% coverage: 7:381/389 of query aligns to 1:356/359 of 3flkA
- active site: Y137 (= Y147), K188 (= K217), D221 (= D250), D245 (= D274), D249 (= D278)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I12 (= I18), A73 (= A76), V74 (≠ L77), G75 (= G78), D82 (= D93), L90 (= L100), N190 (= N219), I222 (≠ A251), R226 (≠ K255), I258 (≠ M287), H280 (= H310), G281 (= G311), S282 (= S312), A283 (= A313), I286 (= I316), N293 (≠ H323)
- binding oxalate ion: R94 (= R104), R104 (= R114), R130 (= R140), D245 (= D274)
2g4oA Anomalous substructure of 3-isopropylmalate dehydrogenase (see paper)
36% identity, 95% coverage: 9:378/389 of query aligns to 3:334/337 of 2g4oA
6lkyA Crystal structure of isocitrate dehydrogenase from methylococcus capsulatus
33% identity, 96% coverage: 9:382/389 of query aligns to 3:338/339 of 6lkyA
- active site: Y123 (= Y147), K174 (= K217), D207 (= D250), D231 (= D274)
- binding nicotinamide-adenine-dinucleotide: P68 (≠ V95), L69 (≠ S96), T71 (≠ A98), N81 (vs. gap), H263 (= H310), G264 (= G311), S265 (= S312), A266 (= A313), D268 (= D315), I269 (= I316), N276 (≠ H323)
6m3sB Dimeric isocitrate dehydrogenase from xanthomonas campestris pv. Campestris 8004
33% identity, 96% coverage: 7:381/389 of query aligns to 5:338/338 of 6m3sB
- active site: Y128 (= Y147), K177 (= K217), D210 (= D250), D234 (= D274)
- binding isocitrate calcium complex: T75 (≠ D79), S83 (≠ A98), N85 (≠ L100), R89 (= R104), R99 (= R114), R121 (= R140), Y128 (= Y147), D234 (= D274), D238 (= D278)
- binding nicotinamide-adenine-dinucleotide: P72 (≠ A76), L73 (= L77), T75 (≠ D79), N85 (≠ L100), H266 (= H310), G267 (= G311), S268 (= S312), A269 (= A313), D271 (= D315), I272 (= I316), N279 (≠ H323)
2y42D Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with nadh and mn (see paper)
37% identity, 92% coverage: 7:362/389 of query aligns to 1:318/355 of 2y42D
- active site: Y140 (= Y147), K186 (= K217), D218 (= D250), D242 (= D274), D246 (= D278)
- binding manganese (ii) ion: D242 (= D274), D246 (= D278)
- binding nicotinamide-adenine-dinucleotide: I12 (= I18), D79 (= D85), H274 (= H310), G275 (= G311), A277 (= A313), D279 (= D315), I280 (= I316), N287 (≠ H323)
2y41A Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with ipm and mn (see paper)
37% identity, 92% coverage: 7:362/389 of query aligns to 1:318/346 of 2y41A
2ztwA Structure of 3-isopropylmalate dehydrogenase in complex with the inhibitor and NAD+ (see paper)
37% identity, 91% coverage: 9:362/389 of query aligns to 2:317/345 of 2ztwA
- active site: Y139 (= Y147), K185 (= K217), D217 (= D250), D241 (= D274), D245 (= D278)
- binding magnesium ion: G203 (≠ A236), Y206 (= Y239), V209 (≠ I242)
- binding nicotinamide-adenine-dinucleotide: I11 (= I18), H273 (= H310), G274 (= G311), A276 (= A313), D278 (= D315), I279 (= I316), A285 (= A322), N286 (≠ H323)
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)
37% identity, 91% coverage: 9:362/389 of query aligns to 2:317/345 of Q5SIY4
- 74:87 (vs. 81:93, 36% identical) binding NAD(+)
- Y139 (= Y147) mutation to F: Large decrease in activity and a small decrease in substrate affinity.
- 274:286 (vs. 311:323, 69% identical) binding NAD(+)
4yb4A Crystal structure of homoisocitrate dehydrogenase from thermus thermophilus in complex with homoisocitrate, magnesium ion (ii) and nadh
36% identity, 86% coverage: 7:340/389 of query aligns to 1:289/333 of 4yb4A
- active site: Y124 (= Y147), K170 (= K217), D203 (= D250), D227 (= D274), D231 (= D278)
- binding (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylic acid: S71 (≠ D79), R84 (= R88), R87 (= R104), R97 (= R114), R117 (= R140), Y124 (= Y147), D227 (= D274)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I12 (= I18), A69 (≠ L77), T70 (≠ G78), S71 (≠ D79), I201 (≠ L248), N204 (≠ A251), L240 (≠ M287), E256 (= E307), H259 (= H310), G260 (= G311), S261 (= S312), A262 (= A313), D264 (= D315), I265 (= I316), N272 (≠ H323)
Sites not aligning to the query:
3asjB Crystal structure of homoisocitrate dehydrogenase in complex with a designed inhibitor (see paper)
36% identity, 86% coverage: 7:340/389 of query aligns to 1:289/333 of 3asjB
- active site: Y124 (= Y147), K170 (= K217), D203 (= D250), D227 (= D274), D231 (= D278)
- binding (2Z)-3-[(carboxymethyl)sulfanyl]-2-hydroxyprop-2-enoic acid: R84 (= R88), R97 (= R114), R117 (= R140), Y124 (= Y147), D227 (= D274), D231 (= D278), V258 (≠ T309)
3asjA Crystal structure of homoisocitrate dehydrogenase in complex with a designed inhibitor (see paper)
36% identity, 86% coverage: 7:340/389 of query aligns to 1:289/333 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)
36% identity, 86% coverage: 7:340/389 of query aligns to 2:290/334 of Q72IW9
- E57 (≠ G64) 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 (≠ LGD 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 (= R88) 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 (= Y89) 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 (= R104) binding in other chain
- R98 (= R114) binding in other chain
- R118 (= R140) binding in other chain
- Y125 (= Y147) binding in other chain; mutation to A: Reduces catalytic efficiency with isocitrate.
- V135 (≠ T162) mutation to M: Formation of homodimers instead of homotetramers. Increased affinity for isocitrate. Reduces enzyme activity with isocitrate.
- K171 (= K217) binding (2R,3S)-homoisocitrate
- N173 (= N219) binding (2R,3S)-homoisocitrate; binding NADH
- D204 (= D250) binding Mg(2+)
- M208 (= M254) 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 (= F263) 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 (= D274) binding Mg(2+)
- D232 (= D278) binding Mg(2+)
- V238 (≠ A284) 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 311:315) binding NADH
- N273 (≠ H323) 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.
8grdA Crystal structure of a constitutively active mutant of the alpha beta heterodimer of human idh3 in complex with adp and mg (see paper)
31% identity, 96% coverage: 10:382/389 of query aligns to 4:324/325 of 8grdA
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)
31% identity, 97% coverage: 5:381/389 of query aligns to 41:398/404 of Q9SA14
- L134 (= L101) Confers substrate specificity; mutation to F: Enhanced activity toward 3-(2'-methylthio)-ethylmalate, but reduced catalytic efficiency with 3-isopropylmalate.
5j32A Isopropylmalate dehydrogenase in complex with isopropylmalate (see paper)
32% identity, 98% coverage: 2:381/389 of query aligns to 7:367/369 of 5j32A
1cnzA 3-isopropylmalate dehydrogenase (ipmdh) from salmonella typhimurium (see paper)
34% identity, 95% coverage: 6:373/389 of query aligns to 3:346/363 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)
34% identity, 95% coverage: 6:373/389 of query aligns to 3:346/363 of P37412
- D227 (= D250) binding Mn(2+)
- D251 (= D274) binding Mn(2+)
- D255 (= D278) binding Mn(2+)
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)
32% identity, 97% coverage: 5:381/389 of query aligns to 40:397/405 of P93832
- 114:129 (vs. 77:93, 12% identical) binding NAD(+)
- L132 (= L100) mutation to A: Reduced activity toward 3-isopropylmalate.
- L133 (= L101) 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 (= R104) binding substrate; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- R146 (= R114) binding substrate; mutation to A: Reduced activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- R174 (= R140) binding substrate; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- Y181 (= Y147) Important for catalysis; mutation Y->A,F,H: Reduced activity toward 3-isopropylmalate.
- K232 (= K217) Important for catalysis; mutation to M: Loss of activity toward 3-isopropylmalate.
- N234 (= N219) binding NAD(+); mutation N->A,D: Loss of activity toward 3-isopropylmalate.
- V235 (≠ A220) mutation to A: Reduced activity toward 3-isopropylmalate.
- D264 (= D250) binding Mg(2+); binding substrate; mutation to N: Loss of activity toward 3-isopropylmalate.
- N265 (≠ A251) binding NAD(+)
- D288 (= D274) binding Mg(2+); mutation to N: Loss of activity toward 3-isopropylmalate.
- D292 (= D278) binding Mg(2+); mutation to N: Reduced activity toward 3-isopropylmalate.
- 318:334 (vs. 307:323, 76% identical) binding NAD(+)
5j33A Isopropylmalate dehydrogenase in complex with NAD+ (see paper)
32% identity, 96% coverage: 8:381/389 of query aligns to 3:357/360 of 5j33A
- active site: Y141 (= Y147), K192 (= K217), D224 (= D250), D248 (= D274), D252 (= D278)
- binding magnesium ion: D248 (= D274), D252 (= D278)
- binding nicotinamide-adenine-dinucleotide: I74 (≠ L77), E89 (≠ D93), L92 (= L100), I261 (≠ M287), E278 (= E307), H281 (= H310), G282 (= G311), S283 (= S312), A284 (= A313), I287 (= I316), N294 (≠ H323), D335 (= D359)
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)
31% identity, 97% coverage: 5:383/389 of query aligns to 44:403/409 of Q9FMT1
- F137 (≠ L101) Confers substrate specificity; mutation to L: Reduced activity toward 3-(2'-methylthio)-ethylmalate, but enhanced catalytic efficiency with 3-isopropylmalate.
- C232 (= C213) Essential for redox regulation; mutation to S: Reduced sensitivity to oxidation on enzyme activity regulation.
- C390 (= C370) Essential for redox regulation; mutation to S: Reduced sensitivity to oxidation on enzyme activity regulation.
Query Sequence
>WP_011813628.1 NCBI__GCF_000015585.1:WP_011813628.1
MEQNQESWQVAVMPGDGIGPEVMAATRHALEALPGPALVLTELGWPAHAWHRDHGEMMPA
DWRGQLAGYDALLLGALGDPGPSHDAQRYCLPDGVSLAPLLQLRKGLDLWACERPAVPLA
GAPMPLSDPRALHTDLLVIRENSEGEYVDQGGRLAAGTPRETATQLEVFTRAGTERIIRH
AFERAARRAEERRQGLRAPRYAAADGAADAAVCVVTKRNAVQYAGELWSEVFAEVAAEYP
GIATHHELIDACCMKFVSQPWQFDVVVASNLHGDILTDLAAVLAGGMGVAPSANLNPADR
SVPPLFEPTHGSAPDIAGADRAHPAAMLLTAAAMLEWMGEVDPVAARSAVQLQRAVAEDI
AEHGMGGRGCAEVGRAVAQRIRTAGAPSA
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