SitesBLAST
Comparing Echvi_3833 FitnessBrowser__Cola:Echvi_3833 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, 96% coverage: 5:379/390 of query aligns to 6:382/517 of Q9JZG1
- D16 (= D15) binding
- H204 (= H203) binding
- H206 (= H205) binding
- N240 (= N239) 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, 97% coverage: 2:379/390 of query aligns to 14:407/409 of 6e1jA
- binding coenzyme a: Q30 (= Q18), F60 (= F48), S63 (= S51), I95 (≠ L74), R97 (= R76), F121 (≠ G100), K132 (= K111), L133 (≠ F112), S322 (= S297), G323 (= G298), I324 (= I299), D327 (= D302), K331 (= K306), L359 (≠ R331), R362 (= R334), H363 (≠ A335)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (= P170), T194 (= T172), H225 (= H203), H227 (= H205)
- binding manganese (ii) ion: D27 (= D15), V82 (vs. gap), E84 (vs. gap), H225 (= H203), H227 (= H205)
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)
48% identity, 97% coverage: 3:379/390 of query aligns to 82:474/503 of Q9FN52
- G263 (= G174) 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)
48% identity, 98% coverage: 2:382/390 of query aligns to 81:477/506 of Q9FG67
- S102 (≠ K23) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
- A290 (≠ S201) 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, 81% coverage: 5:320/390 of query aligns to 3:306/308 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)
37% identity, 90% coverage: 5:356/390 of query aligns to 21:365/399 of 6ktqA
- binding 2-oxoglutaric acid: R30 (= R14), R154 (≠ E138), T156 (≠ Y140), E158 (= E142), S184 (≠ N168), T188 (= T172), H216 (= H203), H218 (= H205)
- binding coenzyme a: V67 (≠ S51), R96 (= R76), A97 (≠ G77), F116 (≠ G100), H128 (≠ F112), E158 (= E142)
- binding zinc ion: E31 (≠ D15), H216 (= H203), H218 (= H205)
4ov4A Isopropylmalate synthase binding with ketoisovalerate (see paper)
34% identity, 95% coverage: 4:375/390 of query aligns to 2:374/379 of 4ov4A
4ov9A Structure of isopropylmalate synthase binding with alpha- isopropylmalate (see paper)
35% identity, 95% coverage: 4:375/390 of query aligns to 2:376/380 of 4ov9A
3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
30% identity, 94% coverage: 8:373/390 of query aligns to 32:389/400 of 3ivtB
Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
30% identity, 94% coverage: 8:373/390 of query aligns to 37:394/418 of Q9Y823
- R43 (= R14) binding ; mutation R->A,K,Q: Abolishes the catalytic activity.
- E44 (≠ D15) binding ; binding ; binding
- Q47 (= Q18) mutation to A: Abolishes the catalytic activity.
- E74 (= E45) 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 (≠ L74) binding ; mutation to A: Substantially impairs catalytic efficiency.
- D123 (≠ H98) binding ; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
- R163 (≠ E138) binding ; mutation R->A,Q: Abolishes the catalytic activity.; mutation to K: Severely diminishes affinity for 2-oxoglutarate and substantially impairs catalytic efficiency.
- S165 (≠ Y140) binding ; mutation to A: Results in a moderate decrease in catalytic efficiency.
- E167 (= E142) mutation E->A,Q: Abolishes the catalytic activity.
- T197 (= T172) 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 (≠ S201) mutation to Q: Does not affect the catalytic activity but impairs L-lysine inhibition.
- H224 (= H203) binding ; binding
- H226 (= H205) binding ; binding
- R288 (≠ N267) mutation to K: Does not affect the catalytic activity but impairs L-lysine inhibition.
- Y332 (= Y311) mutation to A: Abolishes the catalytic activity.; mutation to F: Results in a decrease in catalytic efficiency.
- Q364 (≠ K343) mutation to R: Does not affect the catalytic activity but impairs L-lysine inhibition.
O87198 Homocitrate synthase; HCS; EC 2.3.3.14 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see paper)
31% identity, 97% coverage: 4:380/390 of query aligns to 2:371/376 of O87198
- R12 (= R14) binding
- E13 (≠ D15) binding
- H72 (≠ D81) 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 (vs. gap) binding
- R133 (≠ E138) binding
- S135 (≠ Y140) binding
- T166 (= T172) binding ; binding
- H195 (= H203) binding
- H197 (= H205) binding
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, 94% coverage: 8:375/390 of query aligns to 10:376/516 of Q8F3Q1
- R16 (= R14) mutation R->K,Q: Loss of activity.
- RD 16:17 (= RD 14:15) binding
- D17 (= D15) 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 (≠ C72) 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 (≠ L74) mutation to A: 5-fold increase in Km for acetyl-CoA and 120-fold decrease in kcat.
- L104 (≠ A92) mutation to V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat.
- Y144 (= Y140) 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 (= E142) mutation E->D,Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat.
- T179 (= T172) binding ; mutation to A: 16.4-fold increase in Km for pyruvate and 186-fold decrease in kcat.
- H302 (= H300) mutation H->A,N: Loss of activity.
- D304 (= D302) mutation to A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat.
- N310 (≠ R308) mutation to A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat.
- L311 (≠ E309) mutation to A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat.
- Y312 (≠ T310) mutation to A: Loss of activity.
Sites not aligning to the query:
- 430 Y→L: No change in Km for acetyl-CoA and 2.3-fold decrease in kcat. Severely impairs inhibition by isoleucine.
- 431 D→A: 1.8-fold decrease in Km for acetyl-CoA and 5-fold decrease in kcat.
- 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.
3mi3A Homocitrate synthase lys4 bound to lysine (see paper)
30% identity, 94% coverage: 8:373/390 of query aligns to 14:360/370 of 3mi3A
3ivsA Homocitrate synthase lys4 (see paper)
30% identity, 86% coverage: 8:344/390 of query aligns to 14:329/364 of 3ivsA
2zyfA Crystal structure of homocitrate synthase from thermus thermophilus complexed with magnesuim ion and alpha-ketoglutarate (see paper)
33% identity, 83% coverage: 4:327/390 of query aligns to 2:313/314 of 2zyfA
2ztjA Crystal structure of homocitrate synthase from thermus thermophilus complexed with alpha-ketoglutarate (see paper)
33% identity, 83% coverage: 4:327/390 of query aligns to 2:311/312 of 2ztjA
3a9iA Crystal structure of homocitrate synthase from thermus thermophilus complexed with lys (see paper)
33% identity, 82% coverage: 4:321/390 of query aligns to 1:306/347 of 3a9iA
3bliA Crystal structure of the catalytic domain of licms in complexed with pyruvate and acetyl-coa (see paper)
29% identity, 75% coverage: 8:300/390 of query aligns to 4:296/311 of 3bliA
P9WQB3 2-isopropylmalate synthase; Alpha-IPM synthase; Alpha-isopropylmalate synthase; EC 2.3.3.13 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
27% identity, 86% coverage: 4:339/390 of query aligns to 70:439/644 of P9WQB3
- R80 (= R14) binding
- T254 (= T172) binding
- H285 (= H203) binding
- H287 (= H205) binding
- 369:424 (vs. 290:324, 25% identical) Subdomain I
- 425:433 (vs. 325:333, 33% identical) Linker
Sites not aligning to the query:
- 51:368 N-terminal domain
- 426:644 Required for the condensation reaction. Not required to bind substrate
- 434:490 Subdomain II
- 491:644 Regulatory domain
- 532 binding
- 536 binding
- 563 binding
- 565 binding
- 625 binding
- 627 binding
3hpzB Crystal structure of mycobacterium tuberculosis leua complexed with bromopyruvate
25% identity, 92% coverage: 4:362/390 of query aligns to 53:454/576 of 3hpzB
Query Sequence
>Echvi_3833 FitnessBrowser__Cola:Echvi_3833
MDKRQVLIFDTTLRDGEQVPGCKLNTPQKIEIARQLESLGVDVIEAGFPISSPGDFKSVV
EISKSVSEPIICGLSRGVAKDIEVAAEALKYAKRPRIHTGIGTSPSHIKYKFKSTPDQIL
ERAVAAVKHAKSFVEDVEFYAEDAGRTDNEYLARICEAVVKAGATVLNIPDTTGYCLPDE
YGAKIKYLMDNVKGIENVIISAHCHNDLGLATANSISAVMNGARQIECTINGIGERAGNT
SLEEVAMIMKQHPRLNVYNKINSRLLNPISRLVSERMGMHVQPNKAIVGSNAFAHSSGIH
QDGVIKNRETYEIIDPEEVGVTESMIVLTARSGRAALAFRLHKIGYTITKLQLDDIYQLF
LEHADMKKEITDEDLHEIMKVSSVPGNVEA
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