SitesBLAST
Comparing WP_013707830.1 NCBI__GCF_000195295.1:WP_013707830.1 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)
2g4oA Anomalous substructure of 3-isopropylmalate dehydrogenase (see paper)
52% identity, 97% coverage: 4:347/355 of query aligns to 3:334/337 of 2g4oA
3flkA Crystal structure of tartrate dehydrogenase from pseudomonas putida in complex with nadh, oxalate and metal ion (see paper)
46% identity, 86% coverage: 2:308/355 of query aligns to 1:310/359 of 3flkA
- active site: Y137 (= Y136), K188 (= K188), D221 (= D221), D245 (= D245), D249 (= D249)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I12 (≠ T13), A73 (= A73), V74 (≠ I74), G75 (= G75), D82 (≠ G82), L90 (= L89), N190 (= N190), I222 (≠ A222), R226 (≠ W226), I258 (≠ M258), H280 (≠ G278), G281 (= G279), S282 (= S280), A283 (= A281), I286 (≠ Y284), N293 (= N291)
- binding oxalate ion: R94 (= R93), R104 (= R103), R130 (= R129), D245 (= D245)
6xxyA Crystal structure of haemophilus influenzae 3-isopropylmalate dehydrogenase in complex with o-isobutenyl oxalylhydroxamate. (see paper)
39% identity, 98% coverage: 2:348/355 of query aligns to 3:356/358 of 6xxyA
- active site: Y144 (= Y136), K194 (= K188), D226 (= D221), D250 (= D245)
- binding magnesium ion: D250 (= D245), D254 (= D249)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ A73), V75 (≠ I74), G76 (= G75), E90 (= E85), L94 (= L89), Y224 (≠ H219), N227 (≠ A222), M230 (= M225), M263 (= M258), G264 (= G259), E280 (= E275), G283 (= G278), G284 (= G279), S285 (= S280), A286 (= A281), P287 (= P282), D288 (≠ K283), I289 (≠ Y284), N296 (= N291), D337 (vs. gap)
- binding 2-(2-methylprop-2-enoxyamino)-2-oxidanylidene-ethanoic acid: E90 (= E85), R108 (= R103), R137 (= R129), K194 (= K188), V197 (= V191), D226 (= D221), D250 (= D245)
1cnzA 3-isopropylmalate dehydrogenase (ipmdh) from salmonella typhimurium (see paper)
36% identity, 98% coverage: 2:349/355 of query aligns to 4:358/363 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)
36% identity, 98% coverage: 2:349/355 of query aligns to 4:358/363 of P37412
- D227 (= D221) binding Mn(2+)
- D251 (= D245) binding Mn(2+)
- D255 (= D249) binding Mn(2+)
6lkyA Crystal structure of isocitrate dehydrogenase from methylococcus capsulatus
40% identity, 90% coverage: 3:322/355 of query aligns to 2:307/339 of 6lkyA
- active site: Y123 (= Y136), K174 (= K188), D207 (= D221), D231 (= D245)
- binding nicotinamide-adenine-dinucleotide: P68 (≠ A73), L69 (≠ I74), T71 (≠ H76), N81 (≠ L89), H263 (≠ G278), G264 (= G279), S265 (= S280), A266 (= A281), D268 (≠ K283), I269 (≠ Y284), N276 (= N291)
3vmkA 3-isopropylmalate dehydrogenase from shewanella benthica db21 mt-2 (see paper)
36% identity, 98% coverage: 2:348/355 of query aligns to 8:364/369 of 3vmkA
3vkzA 3-isopropylmalate dehydrogenase from shewanella oneidensis mr-1 at atmospheric pressure (see paper)
36% identity, 97% coverage: 2:347/355 of query aligns to 2:357/364 of 3vkzA
2y41A Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with ipm and mn (see paper)
36% identity, 90% coverage: 2:319/355 of query aligns to 1:316/346 of 2y41A
2y42D Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with nadh and mn (see paper)
36% identity, 90% coverage: 2:319/355 of query aligns to 1:316/355 of 2y42D
- active site: Y140 (= Y136), K186 (= K188), D218 (= D221), D242 (= D245), D246 (= D249)
- binding manganese (ii) ion: D242 (= D245), D246 (= D249)
- binding nicotinamide-adenine-dinucleotide: I12 (≠ T13), D79 (vs. gap), H274 (≠ G278), G275 (= G279), A277 (= A281), D279 (≠ K283), I280 (≠ Y284), N287 (= N291)
2ztwA Structure of 3-isopropylmalate dehydrogenase in complex with the inhibitor and NAD+ (see paper)
36% identity, 89% coverage: 4:319/355 of query aligns to 2:315/345 of 2ztwA
- active site: Y139 (= Y136), K185 (= K188), D217 (= D221), D241 (= D245), D245 (= D249)
- binding magnesium ion: G203 (≠ A207), Y206 (= Y210), V209 (≠ I213)
- binding nicotinamide-adenine-dinucleotide: I11 (≠ T13), H273 (≠ G278), G274 (= G279), A276 (= A281), D278 (≠ K283), I279 (≠ Y284), A285 (≠ I290), N286 (= N291)
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)
36% identity, 89% coverage: 4:319/355 of query aligns to 2:315/345 of Q5SIY4
- 74:87 (vs. 76:85, 18% identical) binding NAD(+)
- Y139 (= Y136) mutation to F: Large decrease in activity and a small decrease in substrate affinity.
- 274:286 (vs. 279:291, 62% identical) binding NAD(+)
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, 89% coverage: 3:319/355 of query aligns to 43:363/405 of P93832
- 114:129 (vs. 74:85, 21% identical) binding NAD(+)
- L132 (= L88) mutation to A: Reduced activity toward 3-isopropylmalate.
- L133 (= L89) 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 (= R93) binding substrate; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- R146 (= R103) binding substrate; mutation to A: Reduced activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- R174 (= R129) binding substrate; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- Y181 (= Y136) Important for catalysis; mutation Y->A,F,H: Reduced activity toward 3-isopropylmalate.
- K232 (= K188) Important for catalysis; mutation to M: Loss of activity toward 3-isopropylmalate.
- N234 (= N190) binding NAD(+); mutation N->A,D: Loss of activity toward 3-isopropylmalate.
- V235 (= V191) mutation to A: Reduced activity toward 3-isopropylmalate.
- D264 (= D221) binding Mg(2+); binding substrate; mutation to N: Loss of activity toward 3-isopropylmalate.
- N265 (≠ A222) binding NAD(+)
- D288 (= D245) binding Mg(2+); mutation to N: Loss of activity toward 3-isopropylmalate.
- D292 (= D249) binding Mg(2+); mutation to N: Reduced activity toward 3-isopropylmalate.
- 318:334 (vs. 275:291, 53% identical) binding NAD(+)
2d1cA Crystal structure of tt0538 protein from thermus thermophilus hb8
39% identity, 89% coverage: 5:319/355 of query aligns to 21:320/495 of 2d1cA
- active site: Y143 (= Y136), K190 (= K188), D223 (= D221), D247 (= D245), D251 (= D249)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P86 (≠ A73), L87 (≠ I74), E88 (≠ G75), T89 (≠ H76), N99 (≠ L89), I221 (≠ H219), N224 (≠ A222), Q228 (≠ W226), L260 (≠ M258), G261 (= G259), H279 (≠ G278), G280 (= G279), S281 (= S280), A282 (= A281), K284 (= K283), Y285 (= Y284), I291 (= I290), N292 (= N291)
Sites not aligning to the query:
5j33A Isopropylmalate dehydrogenase in complex with NAD+ (see paper)
37% identity, 89% coverage: 3:319/355 of query aligns to 3:323/360 of 5j33A
- active site: Y141 (= Y136), K192 (= K188), D224 (= D221), D248 (= D245), D252 (= D249)
- binding magnesium ion: D248 (= D245), D252 (= D249)
- binding nicotinamide-adenine-dinucleotide: I74 (= I74), E89 (= E85), L92 (= L88), I261 (≠ M258), E278 (= E275), H281 (≠ G278), G282 (= G279), S283 (= S280), A284 (= A281), I287 (≠ Y284), N294 (= N291)
Sites not aligning to the query:
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)
36% identity, 92% coverage: 3:329/355 of query aligns to 47:377/409 of Q9FMT1
- F137 (≠ L90) Confers substrate specificity; mutation to L: Reduced activity toward 3-(2'-methylthio)-ethylmalate, but enhanced catalytic efficiency with 3-isopropylmalate.
- C232 (≠ T184) 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.
5j32A Isopropylmalate dehydrogenase in complex with isopropylmalate (see paper)
37% identity, 89% coverage: 3:319/355 of query aligns to 13:333/369 of 5j32A
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)
36% identity, 92% coverage: 3:329/355 of query aligns to 44:374/404 of Q9SA14
- L134 (= L89) Confers substrate specificity; mutation to F: Enhanced activity toward 3-(2'-methylthio)-ethylmalate, but reduced catalytic efficiency with 3-isopropylmalate.
6m3sB Dimeric isocitrate dehydrogenase from xanthomonas campestris pv. Campestris 8004
37% identity, 90% coverage: 1:319/355 of query aligns to 4:307/338 of 6m3sB
- active site: Y128 (= Y136), K177 (= K188), D210 (= D221), D234 (= D245)
- binding isocitrate calcium complex: T75 (≠ H76), S83 (≠ E85), N85 (≠ G87), R89 (= R91), R99 (= R103), R121 (= R129), Y128 (= Y136), D234 (= D245), D238 (= D249)
- binding nicotinamide-adenine-dinucleotide: P72 (≠ A73), L73 (≠ I74), T75 (≠ H76), N85 (≠ G87), H266 (≠ G278), G267 (= G279), S268 (= S280), A269 (= A281), D271 (≠ K283), I272 (≠ Y284), N279 (= N291)
4iwhA Crystal structure of a 3-isopropylmalate dehydrogenase from burkholderia pseudomallei
36% identity, 97% coverage: 4:346/355 of query aligns to 5:354/358 of 4iwhA
Query Sequence
>WP_013707830.1 NCBI__GCF_000195295.1:WP_013707830.1
MTHKIAVLPGDGTGPEVVAEGIKVLNAIAGPAGLKFEFIHYDLGGERYKRTGEILPDSVL
KELRGFRSIYLGAIGHPDVKPGILEKGLLLRLRFELDQYINLRPVILYPGVYTPLRDKGP
EDINFVVVRENTEGLYAGAGGVLKYGTPDEVAVQESINTRKGVDRCLKYAFELTRKRNKN
KKLTLVGKTNVLTFAFDLWERAFHAMAQSYPDIATDYAHVDATCMWMVKNPEWFDVLVTD
NMFGDIITDLGAMIQGGMGIAAGGNINPEGVSMFEPIGGSAPKYTGKNIINPLAAIAAAQ
MLLDHLGEVKAAAAIEEAIKTVCAKHLKSLQAGKMGYSTSEVGDLVAQYAIDNLK
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