SitesBLAST
Comparing 3607175 FitnessBrowser__Dino:3607175 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)
Q9JZG1 2-isopropylmalate synthase; Alpha-IPM synthase; Alpha-isopropylmalate synthase; EC 2.3.3.13 from Neisseria meningitidis serogroup B (strain MC58) (see 2 papers)
51% identity, 95% coverage: 5:503/525 of query aligns to 2:502/517 of Q9JZG1
- D16 (= D19) binding
- H204 (= H206) binding
- H206 (= H208) binding
- N240 (= N242) binding
Sites not aligning to the query:
- 366:517 Required for the condensation reaction. Not required to bind substrate
6e1jA Crystal structure of methylthioalkylmalate synthase (bjumam1.1) from brassica juncea (see paper)
48% identity, 72% coverage: 6:384/525 of query aligns to 14:408/409 of 6e1jA
- binding coenzyme a: Q30 (= Q22), F60 (= F52), S63 (≠ A55), I95 (≠ L78), R97 (= R80), F121 (= F104), K132 (≠ I114), L133 (≠ P115), S322 (= S301), G323 (= G302), I324 (= I303), D327 (= D306), K331 (= K310), L359 (≠ H335), R362 (= R338), H363 (≠ A339)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (= P173), T194 (= T175), H225 (= H206), H227 (= H208)
- binding manganese (ii) ion: D27 (= D19), V82 (= V74), E84 (vs. gap), H225 (= H206), H227 (= H208)
Q9FN52 Methylthioalkylmalate synthase 3, chloroplastic; 2-isopropylmalate synthase 2; Methylthioalkylmalate synthase-like; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
46% identity, 75% coverage: 7:398/525 of query aligns to 82:488/503 of Q9FN52
- G263 (= G177) mutation to E: In gsm2-1; loss of activity and lack of C6, C7 and C8 aliphatic glucosinolates.
Q9FG67 Methylthioalkylmalate synthase 1, chloroplastic; 2-isopropylmalate synthase 3; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
47% identity, 74% coverage: 6:396/525 of query aligns to 81:486/506 of Q9FG67
- S102 (≠ T27) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
- A290 (= A204) mutation to T: In gsm1-2; loss of conversion of C3 to C4 glucosinolates.
3rmjB Crystal structure of truncated alpha-isopropylmalate synthase from neisseria meningitidis (see paper)
51% identity, 61% coverage: 8:326/525 of query aligns to 2:308/308 of 3rmjB
6ktqA Crystal structure of catalytic domain of homocitrate synthase from sulfolobus acidocaldarius (sahcs(dram)) in complex with alpha- ketoglutarate/zn2+/coa (see paper)
36% identity, 68% coverage: 9:366/525 of query aligns to 21:371/399 of 6ktqA
- binding 2-oxoglutaric acid: R30 (= R18), R154 (≠ Q141), T156 (≠ S143), E158 (≠ M145), S184 (≠ N171), T188 (= T175), H216 (= H206), H218 (= H208)
- binding coenzyme a: V67 (≠ A55), R96 (≠ K84), A97 (≠ D85), F116 (= F104), H128 (≠ P115), E158 (≠ M145)
- binding zinc ion: E31 (≠ D19), H216 (= H206), H218 (= H208)
4ov9A Structure of isopropylmalate synthase binding with alpha- isopropylmalate (see paper)
31% identity, 71% coverage: 10:382/525 of query aligns to 4:379/380 of 4ov9A
4ov4A Isopropylmalate synthase binding with ketoisovalerate (see paper)
31% identity, 71% coverage: 10:382/525 of query aligns to 4:377/379 of 4ov4A
Q8F3Q1 (R)-citramalate synthase CimA; LiCMS; EC 2.3.3.21 from Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) (see 2 papers)
29% identity, 95% coverage: 7:504/525 of query aligns to 5:511/516 of Q8F3Q1
- R16 (= R18) mutation R->K,Q: Loss of activity.
- RD 16:17 (= RD 18:19) binding
- D17 (= D19) mutation to A: 34-fold increase in Km for pyruvate and 315-fold decrease in kcat.; mutation to N: 4.4-fold increase in Km for pyruvate and 480-fold decrease in kcat.
- L81 (≠ A81) mutation to A: 4.7-fold increase in Km for pyruvate and 15.7-fold decrease in kcat.; mutation to V: 3.3-fold increase in Km for pyruvate and 10.1-fold decrease in kcat.
- F83 (= F83) mutation to A: 5-fold increase in Km for acetyl-CoA and 120-fold decrease in kcat.
- L104 (≠ I105) mutation to V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat.
- Y144 (≠ Q141) binding ; mutation to L: 259-fold increase in Km for pyruvate and 76-fold decrease in kcat.; mutation to V: 114-fold increase in Km for pyruvate and 5.3-fold decrease in kcat.
- E146 (vs. gap) mutation E->D,Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat.
- T179 (= T175) binding ; mutation to A: 16.4-fold increase in Km for pyruvate and 186-fold decrease in kcat.
- H302 (= H304) mutation H->A,N: Loss of activity.
- D304 (= D306) mutation to A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat.
- N310 (≠ A312) mutation to A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat.
- L311 (≠ E313) mutation to A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat.
- Y312 (≠ T314) mutation to A: Loss of activity.
- Y430 (≠ V433) mutation to L: No change in Km for acetyl-CoA and 2.3-fold decrease in kcat. Severely impairs inhibition by isoleucine.
- D431 (= D434) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 5-fold decrease in kcat.
- L451 (vs. gap) mutation to V: 1.5-fold increase in Km for acetyl-CoA and 4.3 decrease in kcat.
- Y454 (= Y453) mutation to A: 1.4 decrease in Km for acetyl-CoA and 17-fold decrease in kcat. Still inhibited by isoleucine and weakly inhibited by leucine.
- I458 (≠ V458) mutation to A: 1.3-fold decrease in Km for acetyl-CoA and 14-fold decrease in kcat. Abolishes inhibition by isoleucine.
- T464 (≠ A464) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 4.3-fold decrease in kcat.
- V468 (= V468) mutation to A: No change in Km for acetyl-CoA and 2-fold decrease in kcat. Increases inhibition by isoleucine and leucine becomes an effective inhibitor.
- P493 (≠ T486) mutation to A: 1.5-fold decrease in Km for acetyl-CoA and 2.6-fold decrease in kcat.
- Q495 (≠ T488) mutation to A: 1.6-fold decrease in Km for acetyl-CoA and 2.8-fold decrease in kcat.
3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
32% identity, 68% coverage: 12:369/525 of query aligns to 32:381/400 of 3ivtB
Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
32% identity, 68% coverage: 12:369/525 of query aligns to 37:386/418 of Q9Y823
- R43 (= R18) binding ; mutation R->A,K,Q: Abolishes the catalytic activity.
- E44 (≠ D19) binding ; binding ; binding
- Q47 (= Q22) mutation to A: Abolishes the catalytic activity.
- E74 (= E49) mutation to A: Abolishes the catalytic activity.; mutation to Q: Results in a moderate decrease in the turnover number and a slight increase in the Km value for each substrate.
- H103 (≠ L78) binding ; mutation to A: Substantially impairs catalytic efficiency.
- D123 (≠ H102) binding ; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
- R163 (≠ Q141) binding ; mutation R->A,Q: Abolishes the catalytic activity.; mutation to K: Severely diminishes affinity for 2-oxoglutarate and substantially impairs catalytic efficiency.
- S165 (= S143) binding ; mutation to A: Results in a moderate decrease in catalytic efficiency.
- E167 (≠ M145) mutation E->A,Q: Abolishes the catalytic activity.
- T197 (= T175) binding ; binding ; mutation to A: Exhibits a 25-fold decrease in catalytic efficiency.; mutation to S: Results in a modest decrease in catalytic efficiency.; mutation to V: Abolishes the catalytic activity.
- E222 (≠ A204) mutation to Q: Does not affect the catalytic activity but impairs L-lysine inhibition.
- H224 (= H206) binding ; binding
- H226 (= H208) binding ; binding
- R288 (= R268) mutation to K: Does not affect the catalytic activity but impairs L-lysine inhibition.
- Y332 (≠ F315) mutation to A: Abolishes the catalytic activity.; mutation to F: Results in a decrease in catalytic efficiency.
- Q364 (≠ D347) mutation to R: Does not affect the catalytic activity but impairs L-lysine inhibition.
3mi3A Homocitrate synthase lys4 bound to lysine (see paper)
31% identity, 68% coverage: 12:369/525 of query aligns to 14:352/370 of 3mi3A
O87198 Homocitrate synthase; HCS; EC 2.3.3.14 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see paper)
31% identity, 70% coverage: 12:377/525 of query aligns to 6:365/376 of O87198
- R12 (= R18) binding
- E13 (≠ D19) binding
- H72 (≠ S73) binding ; mutation to L: Significant decrease in sensitivity to lysine inhibition. Large decrease in affinity for 2-oxoglutarate. Almost no effect on affinity for acetyl-CoA and on turnover number.
- D92 (≠ H102) binding
- R133 (vs. gap) binding
- S135 (= S143) binding
- T166 (= T175) binding ; binding
- H195 (= H206) binding
- H197 (= H208) binding
3ivsA Homocitrate synthase lys4 (see paper)
30% identity, 70% coverage: 12:380/525 of query aligns to 14:358/364 of 3ivsA
3a9iA Crystal structure of homocitrate synthase from thermus thermophilus complexed with lys (see paper)
31% identity, 70% coverage: 12:377/525 of query aligns to 5:336/347 of 3a9iA
2zyfA Crystal structure of homocitrate synthase from thermus thermophilus complexed with magnesuim ion and alpha-ketoglutarate (see paper)
32% identity, 61% coverage: 12:331/525 of query aligns to 6:313/314 of 2zyfA
2ztjA Crystal structure of homocitrate synthase from thermus thermophilus complexed with alpha-ketoglutarate (see paper)
32% identity, 61% coverage: 12:331/525 of query aligns to 6:311/312 of 2ztjA
3bliA Crystal structure of the catalytic domain of licms in complexed with pyruvate and acetyl-coa (see paper)
31% identity, 56% coverage: 9:304/525 of query aligns to 1:296/311 of 3bliA
3hq1A Crystal structure of mycobacterium tuberculosis leua complexed with citrate and mn2+
26% identity, 96% coverage: 1:502/525 of query aligns to 41:571/573 of 3hq1A
1sr9A Crystal structure of leua from mycobacterium tuberculosis (see paper)
26% identity, 96% coverage: 1:502/525 of query aligns to 41:571/573 of 1sr9A
Query Sequence
>3607175 FitnessBrowser__Dino:3607175
MTDKTDQDRVLIFDTTLRDGEQSPGATMTHDEKLEIAALLDEMGVDIIEAGFPIASDGDF
AAVSEIAKNSVNSVICGLARANFKDIDRCWEAVRHARQPRIHTFIGTSPLHRAIPNLTMD
EMADRIHDTVTHARNLCDNVQWSPMDATRTEYDYLCRVIEIAIKAGATTINIPDTVGYTA
PRESADLIARLIADVPGAEDVTFATHCHNDLGMATANALAAVDAGARQVECTINGLGERA
GNTALEEVVMALRVRNDIMPYQTRIDTRKIMNISRRVAAVSGFAVQFNKAIVGKNAFAHE
SGIHQDGMLKNAETFEIMRPEDIGLSETNLVMGKHSGRAALRAKLKDLGYELADNQLKDV
FVRFKALADRKKEIYDEDLVALMSESSSDPARERLSVKFLRVICGTEAPQSADLTLSIDG
VDKQVTAQGDGPVDATFNAVKALFPHTARLQLYQVHAVTEGTDAQATVTVRMEEDGRIVS
GQAADTDTVVASAKAYVAALNRLILRREKSPLGSDRKEVSYKDVS
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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