SitesBLAST
Comparing 351389 FitnessBrowser__Btheta:351389 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)
44% identity, 99% coverage: 3:497/498 of query aligns to 5:503/517 of Q9JZG1
- D16 (= D14) binding Mn(2+)
- H204 (= H202) binding Mn(2+)
- H206 (= H204) binding Mn(2+)
- N240 (= N238) binding Mn(2+)
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)
47% identity, 75% coverage: 3:377/498 of query aligns to 16:406/409 of 6e1jA
- binding coenzyme a: Q30 (= Q17), F60 (= F47), S63 (= S50), I95 (≠ L73), R97 (= R75), F121 (≠ G99), K132 (= K110), L133 (≠ F111), S322 (= S296), G323 (= G297), I324 (= I298), D327 (= D301), K331 (= K305), L359 (≠ R330), R362 (= R333), H363 (≠ A334)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (= P169), T194 (= T171), H225 (= H202), H227 (= H204)
- binding manganese (ii) ion: D27 (= D14), V82 (vs. gap), E84 (vs. gap), H225 (= H202), H227 (= H204)
Q9FG67 Methylthioalkylmalate synthase 1, chloroplastic; 2-isopropylmalate synthase 3; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
45% identity, 80% coverage: 3:399/498 of query aligns to 83:491/506 of Q9FG67
- S102 (≠ Q22) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
- A290 (≠ S200) mutation to T: In gsm1-2; loss of conversion of C3 to C4 glucosinolates.
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)
45% identity, 77% coverage: 3:383/498 of query aligns to 83:481/503 of Q9FN52
- G263 (= G173) mutation to E: In gsm2-1; loss of activity and lack of C6, C7 and C8 aliphatic glucosinolates.
3rmjB Crystal structure of truncated alpha-isopropylmalate synthase from neisseria meningitidis (see paper)
50% identity, 64% coverage: 3:319/498 of query aligns to 2:306/308 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, 70% coverage: 7:355/498 of query aligns to 24:365/399 of 6ktqA
- binding 2-oxoglutaric acid: R30 (= R13), R154 (≠ E137), T156 (≠ Y139), E158 (= E141), S184 (≠ N167), T188 (= T171), H216 (= H202), H218 (= H204)
- binding coenzyme a: V67 (≠ S50), R96 (= R75), A97 (= A76), F116 (≠ G99), H128 (≠ F111), E158 (= E141)
- binding zinc ion: E31 (≠ D14), H216 (= H202), H218 (= H204)
4ov4A Isopropylmalate synthase binding with ketoisovalerate (see paper)
34% identity, 75% coverage: 5:378/498 of query aligns to 4:378/379 of 4ov4A
4ov9A Structure of isopropylmalate synthase binding with alpha- isopropylmalate (see paper)
34% identity, 75% coverage: 5:378/498 of query aligns to 4:380/380 of 4ov9A
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, 88% coverage: 1:439/498 of query aligns to 4:443/516 of Q8F3Q1
- R16 (= R13) mutation R->K,Q: Loss of activity.
- RD 16:17 (= RD 13:14) binding pyruvate
- D17 (= D14) 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 (vs. gap) 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 (vs. gap) mutation to A: 5-fold increase in Km for acetyl-CoA and 120-fold decrease in kcat.
- L104 (≠ G99) mutation to V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat.
- Y144 (= Y139) binding pyruvate; 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 (= E141) mutation E->D,Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat.
- T179 (= T171) binding pyruvate; mutation to A: 16.4-fold increase in Km for pyruvate and 186-fold decrease in kcat.
- H302 (= H299) mutation H->A,N: Loss of activity.
- D304 (= D301) mutation to A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat.
- N310 (≠ V307) mutation to A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat.
- L311 (≠ E308) mutation to A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat.
- Y312 (≠ T309) mutation to A: Loss of activity.
- Y430 (≠ V426) mutation to L: No change in Km for acetyl-CoA and 2.3-fold decrease in kcat. Severely impairs inhibition by isoleucine.
- D431 (= D427) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 5-fold decrease in kcat.
Sites not aligning to the query:
- 451 L→V: 1.5-fold increase in Km for acetyl-CoA and 4.3 decrease in kcat.
- 454 Y→A: 1.4 decrease in Km for acetyl-CoA and 17-fold decrease in kcat. Still inhibited by isoleucine and weakly inhibited by leucine.
- 458 I→A: 1.3-fold decrease in Km for acetyl-CoA and 14-fold decrease in kcat. Abolishes inhibition by isoleucine.
- 464 T→A: 1.8-fold decrease in Km for acetyl-CoA and 4.3-fold decrease in kcat.
- 468 V→A: No change in Km for acetyl-CoA and 2-fold decrease in kcat. Increases inhibition by isoleucine and leucine becomes an effective inhibitor.
- 493 P→A: 1.5-fold decrease in Km for acetyl-CoA and 2.6-fold decrease in kcat.
- 495 Q→A: 1.6-fold decrease in Km for acetyl-CoA and 2.8-fold decrease in kcat.
Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
31% identity, 78% coverage: 3:391/498 of query aligns to 33:415/418 of Q9Y823
- R43 (= R13) binding 2-oxoglutarate; mutation R->A,K,Q: Abolishes the catalytic activity.
- E44 (≠ D14) binding 2-oxoglutarate; binding L-lysine; binding Zn(2+)
- Q47 (= Q17) mutation to A: Abolishes the catalytic activity.
- E74 (= E44) 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 (≠ L73) binding 2-oxoglutarate; mutation to A: Substantially impairs catalytic efficiency.
- D123 (≠ H97) binding L-lysine; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
- R163 (≠ E137) binding 2-oxoglutarate; mutation R->A,Q: Abolishes the catalytic activity.; mutation to K: Severely diminishes affinity for 2-oxoglutarate and substantially impairs catalytic efficiency.
- S165 (≠ Y139) binding 2-oxoglutarate; mutation to A: Results in a moderate decrease in catalytic efficiency.
- E167 (= E141) mutation E->A,Q: Abolishes the catalytic activity.
- T197 (= T171) binding 2-oxoglutarate; binding L-lysine; 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 (≠ S200) mutation to Q: Does not affect the catalytic activity but impairs L-lysine inhibition.
- H224 (= H202) binding 2-oxoglutarate; binding Zn(2+)
- H226 (= H204) binding 2-oxoglutarate; binding Zn(2+)
- R288 (≠ Y266) mutation to K: Does not affect the catalytic activity but impairs L-lysine inhibition.
- Y332 (= Y310) mutation to A: Abolishes the catalytic activity.; mutation to F: Results in a decrease in catalytic efficiency.
- Q364 (≠ L342) mutation to R: Does not affect the catalytic activity but impairs L-lysine inhibition.
3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
31% identity, 74% coverage: 3:372/498 of query aligns to 28:389/400 of 3ivtB