SitesBLAST
Comparing AZOBR_RS14130 FitnessBrowser__azobra:AZOBR_RS14130 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)
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)
55% identity, 99% coverage: 2:367/371 of query aligns to 39:399/404 of Q9SA14
- L134 (= L96) 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)
54% identity, 99% coverage: 2:367/371 of query aligns to 38:398/405 of P93832
- 114:129 (vs. 76:92, 53% identical) binding
- L132 (= L95) mutation to A: Reduced activity toward 3-isopropylmalate.
- L133 (= L96) 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 (= R99) binding ; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- R146 (= R109) binding ; mutation to A: Reduced activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- R174 (= R137) binding ; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- Y181 (= Y144) Important for catalysis; mutation Y->A,F,H: Reduced activity toward 3-isopropylmalate.
- K232 (= K195) Important for catalysis; mutation to M: Loss of activity toward 3-isopropylmalate.
- N234 (= N197) binding ; mutation N->A,D: Loss of activity toward 3-isopropylmalate.
- V235 (= V198) mutation to A: Reduced activity toward 3-isopropylmalate.
- D264 (= D228) binding ; binding ; mutation to N: Loss of activity toward 3-isopropylmalate.
- N265 (= N229) binding
- D288 (= D252) binding ; mutation to N: Loss of activity toward 3-isopropylmalate.
- D292 (= D256) binding ; mutation to N: Reduced activity toward 3-isopropylmalate.
- 318:334 (vs. 287:303, 82% identical) binding
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)
54% identity, 99% coverage: 2:367/371 of query aligns to 42:402/409 of Q9FMT1
- F137 (≠ L96) Confers substrate specificity; mutation to L: Reduced activity toward 3-(2'-methylthio)-ethylmalate, but enhanced catalytic efficiency with 3-isopropylmalate.
- C232 (≠ H191) Essential for redox regulation; mutation to S: Reduced sensitivity to oxidation on enzyme activity regulation.
- C390 (≠ T355) Essential for redox regulation; mutation to S: Reduced sensitivity to oxidation on enzyme activity regulation.
5j33A Isopropylmalate dehydrogenase in complex with NAD+ (see paper)
55% identity, 97% coverage: 7:367/371 of query aligns to 5:358/360 of 5j33A
- active site: Y141 (= Y144), K192 (= K195), D224 (= D228), D248 (= D252), D252 (= D256)
- binding magnesium ion: D248 (= D252), D252 (= D256)
- binding nicotinamide-adenine-dinucleotide: I74 (≠ V76), E89 (= E92), L92 (= L95), I261 (≠ L265), E278 (= E287), H281 (= H290), G282 (= G291), S283 (= S292), A284 (= A293), I287 (= I296), N294 (= N303), D335 (= D344)
5j32A Isopropylmalate dehydrogenase in complex with isopropylmalate (see paper)
55% identity, 97% coverage: 7:367/371 of query aligns to 15:368/369 of 5j32A
1a05A Crystal structure of the complex of 3-isopropylmalate dehydrogenase from thiobacillus ferrooxidans with 3-isopropylmalate (see paper)
55% identity, 98% coverage: 5:367/371 of query aligns to 2:355/357 of 1a05A
Q56268 3-isopropylmalate dehydrogenase; 3-IPM-DH; Beta-IPM dehydrogenase; IMDH; EC 1.1.1.85 from Acidithiobacillus ferrooxidans (Thiobacillus ferrooxidans) (see paper)
55% identity, 98% coverage: 5:367/371 of query aligns to 2:355/358 of Q56268
- R95 (= R99) binding
- R105 (= R109) binding
- R133 (= R137) binding
- D222 (= D228) binding ; binding
- D246 (= D252) binding
4xxvA Crystal structure of 3-isopropylmalate dehydrogenase from burkholderia thailandensis in complex with NAD
53% identity, 97% coverage: 6:366/371 of query aligns to 3:356/356 of 4xxvA
4iwhA Crystal structure of a 3-isopropylmalate dehydrogenase from burkholderia pseudomallei
53% identity, 97% coverage: 6:366/371 of query aligns to 5:358/358 of 4iwhA
6xxyA Crystal structure of haemophilus influenzae 3-isopropylmalate dehydrogenase in complex with o-isobutenyl oxalylhydroxamate. (see paper)
51% identity, 96% coverage: 10:366/371 of query aligns to 9:358/358 of 6xxyA
- active site: Y144 (= Y144), K194 (= K195), D226 (= D228), D250 (= D252)
- binding magnesium ion: D250 (= D252), D254 (= D256)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ A75), V75 (= V76), G76 (= G77), E90 (= E92), L94 (= L95), Y224 (= Y226), N227 (= N229), M230 (= M232), M263 (≠ L265), G264 (= G266), E280 (= E287), G283 (≠ H290), G284 (= G291), S285 (= S292), A286 (= A293), P287 (= P294), D288 (= D295), I289 (= I296), N296 (= N303), D337 (= D344)
- binding 2-(2-methylprop-2-enoxyamino)-2-oxidanylidene-ethanoic acid: E90 (= E92), R108 (= R109), R137 (= R137), K194 (= K195), V197 (= V198), D226 (= D228), D250 (= D252)
1cnzA 3-isopropylmalate dehydrogenase (ipmdh) from salmonella typhimurium (see paper)
49% identity, 98% coverage: 1:364/371 of query aligns to 1:357/363 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)
49% identity, 98% coverage: 1:364/371 of query aligns to 1:357/363 of P37412
- D227 (= D228) binding
- D251 (= D252) binding
- D255 (= D256) binding
2y41A Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with ipm and mn (see paper)
51% identity, 89% coverage: 6:336/371 of query aligns to 3:320/346 of 2y41A
2y42D Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with nadh and mn (see paper)
51% identity, 89% coverage: 6:336/371 of query aligns to 3:320/355 of 2y42D
- active site: Y140 (= Y144), K186 (= K195), D218 (= D228), D242 (= D252), D246 (= D256)
- binding manganese (ii) ion: D242 (= D252), D246 (= D256)
- binding nicotinamide-adenine-dinucleotide: I12 (= I15), D79 (= D82), H274 (= H290), G275 (= G291), A277 (= A293), D279 (= D295), I280 (= I296), N287 (= N303)
2ztwA Structure of 3-isopropylmalate dehydrogenase in complex with the inhibitor and NAD+ (see paper)
51% identity, 89% coverage: 6:336/371 of query aligns to 2:319/345 of 2ztwA
- active site: Y139 (= Y144), K185 (= K195), D217 (= D228), D241 (= D252), D245 (= D256)
- binding magnesium ion: G203 (≠ H213), Y206 (≠ F217), V209 (= V220)
- binding nicotinamide-adenine-dinucleotide: I11 (= I15), H273 (= H290), G274 (= G291), A276 (= A293), D278 (= D295), I279 (= I296), A285 (= A302), N286 (= N303)
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)
51% identity, 89% coverage: 6:336/371 of query aligns to 2:319/345 of Q5SIY4
- 74:87 (vs. 78:92, 53% identical) binding
- Y139 (= Y144) mutation to F: Large decrease in activity and a small decrease in substrate affinity.
- 274:286 (vs. 291:303, 77% identical) binding
3vmkA 3-isopropylmalate dehydrogenase from shewanella benthica db21 mt-2 (see paper)
46% identity, 98% coverage: 3:366/371 of query aligns to 7:366/369 of 3vmkA
3vkzA 3-isopropylmalate dehydrogenase from shewanella oneidensis mr-1 at atmospheric pressure (see paper)
47% identity, 97% coverage: 3:362/371 of query aligns to 1:356/364 of 3vkzA
P18869 3-isopropylmalate dehydrogenase; 3-IPM-DH; IMDH; Beta-IPM dehydrogenase; EC 1.1.1.85 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
43% identity, 98% coverage: 5:369/371 of query aligns to 4:370/371 of P18869
- T55 (≠ V55) modified: Phosphothreonine
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, 92% coverage: 6:345/371 of query aligns to 4:314/334 of Q72IW9
- E57 (≠ A63) 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 (≠ VGG 76:78) binding
- S72 (≠ G78) 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 (≠ L96) 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 (≠ S97) 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 (= R99) binding in other chain
- R98 (= R109) binding in other chain
- R118 (= R137) binding in other chain
- Y125 (= Y144) binding in other chain; mutation to A: Reduces catalytic efficiency with isocitrate.
- V135 (≠ I154) mutation to M: Formation of homodimers instead of homotetramers. Increased affinity for isocitrate. Reduces enzyme activity with isocitrate.
- K171 (= K195) binding
- N173 (= N197) binding ; binding
- D204 (= D228) binding
- M208 (= M232) 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 (= F241) 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 (= D252) binding
- D232 (= D256) binding
- V238 (≠ T262) 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 291:295) binding
- N273 (= N303) binding
- R310 (= R341) 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.
Query Sequence
>AZOBR_RS14130 FitnessBrowser__azobra:AZOBR_RS14130
MPANKKLLFLPGDGIGPEVMRQVRRVIDWLDRKRNVTFDVTEGLVGGAAIDAYGVPLKDE
TLADALAADAVMLGAVGGPKWDNPTDYTKRPEAGLLSLRKELNLFANLRPAVVFDALVDA
STLKADVIKGLDILIVRELTGGVYFGEPRGITDIGNGERRGVNTQVYTTSEIRRVARVAF
ELARKRGNKLHSMEKANVMESGLLWRQEVTKLHQEEFSDVTLEHMYADNGAMQLLKNPKQ
FDVIVTDNLFGDILSDEAAMMTGSLGMLPSASLGAPDANGQRKALYEPVHGSAPDIAGRD
LANPCATLLSFAMCLRYSFNMDEEAKMLEKAVQNVLSGGMRTADIMAPGMARCSTTVMGD
SILRELDKLAS
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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