SitesBLAST
Comparing Echvi_2061 FitnessBrowser__Cola:Echvi_2061 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)
Q8F3Q1 (R)-citramalate synthase CimA; LiCMS; EC 2.3.3.21 from Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) (see 2 papers)
53% identity, 99% coverage: 1:497/504 of query aligns to 11:512/516 of Q8F3Q1
- R16 (= R6) mutation R->K,Q: Loss of activity.
- RD 16:17 (= RD 6:7) binding
- D17 (= D7) 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 (= L71) 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 (= F73) mutation to A: 5-fold increase in Km for acetyl-CoA and 120-fold decrease in kcat.
- L104 (= L94) mutation to V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat.
- Y144 (= Y134) 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 (= E136) mutation E->D,Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat.
- T179 (= T169) binding ; mutation to A: 16.4-fold increase in Km for pyruvate and 186-fold decrease in kcat.
- H302 (= H292) mutation H->A,N: Loss of activity.
- D304 (= D294) mutation to A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat.
- N310 (= N300) mutation to A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat.
- L311 (= L301) mutation to A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat.
- Y312 (= Y302) mutation to A: Loss of activity.
- Y430 (≠ F421) mutation to L: No change in Km for acetyl-CoA and 2.3-fold decrease in kcat. Severely impairs inhibition by isoleucine.
- D431 (= D422) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 5-fold decrease in kcat.
- L451 (= L442) mutation to V: 1.5-fold increase in Km for acetyl-CoA and 4.3 decrease in kcat.
- Y454 (≠ F445) 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 (= I449) mutation to A: 1.3-fold decrease in Km for acetyl-CoA and 14-fold decrease in kcat. Abolishes inhibition by isoleucine.
- T464 (= T455) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 4.3-fold decrease in kcat.
- V468 (= V459) 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 (≠ S478) mutation to A: 1.5-fold decrease in Km for acetyl-CoA and 2.6-fold decrease in kcat.
- Q495 (= Q480) mutation to A: 1.6-fold decrease in Km for acetyl-CoA and 2.8-fold decrease in kcat.
3bliA Crystal structure of the catalytic domain of licms in complexed with pyruvate and acetyl-coa (see paper)
56% identity, 63% coverage: 1:315/504 of query aligns to 5:311/311 of 3bliA
6ktqA Crystal structure of catalytic domain of homocitrate synthase from sulfolobus acidocaldarius (sahcs(dram)) in complex with alpha- ketoglutarate/zn2+/coa (see paper)
34% identity, 70% coverage: 1:351/504 of query aligns to 25:369/399 of 6ktqA
- binding 2-oxoglutaric acid: R30 (= R6), R154 (≠ N132), T156 (≠ Y134), E158 (= E136), S184 (≠ M165), T188 (= T169), H216 (= H197), H218 (= H199)
- binding coenzyme a: V67 (= V44), R96 (≠ V74), A97 (≠ D75), F116 (≠ L94), H128 (≠ L106), E158 (= E136)
- binding zinc ion: E31 (≠ D7), H216 (= H197), H218 (= H199)
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)
30% identity, 98% coverage: 1:496/504 of query aligns to 10:503/517 of Q9JZG1
- D16 (= D7) binding
- H204 (= H197) binding
- H206 (= H199) binding
- N240 (= N233) binding
Sites not aligning to the query:
- 366:517 Required for the condensation reaction. Not required to bind substrate
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)
32% identity, 73% coverage: 1:370/504 of query aligns to 88:474/503 of Q9FN52
- G263 (= G171) mutation to E: In gsm2-1; loss of activity and lack of C6, C7 and C8 aliphatic glucosinolates.
6e1jA Crystal structure of methylthioalkylmalate synthase (bjumam1.1) from brassica juncea (see paper)
32% identity, 74% coverage: 1:371/504 of query aligns to 21:408/409 of 6e1jA
- binding coenzyme a: Q30 (= Q10), F60 (≠ S41), S63 (≠ V44), I95 (≠ L71), R97 (≠ F73), F121 (≠ L94), K132 (≠ Q105), L133 (= L106), S322 (≠ A289), G323 (= G290), I324 (= I291), D327 (= D294), K331 (= K298), L359 (≠ T322), R362 (≠ K325), H363 (≠ A326)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (= P167), T194 (= T169), H225 (= H197), H227 (= H199)
- binding manganese (ii) ion: D27 (= D7), V82 (vs. gap), E84 (vs. gap), H225 (= H197), H227 (= H199)
Q9FG67 Methylthioalkylmalate synthase 1, chloroplastic; 2-isopropylmalate synthase 3; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
32% identity, 80% coverage: 1:402/504 of query aligns to 88:502/506 of Q9FG67
- S102 (= S15) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
- A290 (≠ D195) 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)
31% identity, 57% coverage: 1:287/504 of query aligns to 7:294/308 of 3rmjB
O87198 Homocitrate synthase; HCS; EC 2.3.3.14 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see paper)
28% identity, 74% coverage: 1:372/504 of query aligns to 7:372/376 of O87198
- R12 (= R6) binding
- E13 (≠ D7) binding
- H72 (= H57) 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 (≠ N92) binding
- R133 (≠ Y134) binding
- S135 (≠ E136) binding
- T166 (= T169) binding ; binding
- H195 (= H197) binding
- H197 (= H199) binding
3f6hB Crystal structure of the regulatory domain of licms in complexed with isoleucine - type iii (see paper)
45% identity, 23% coverage: 381:497/504 of query aligns to 1:121/125 of 3f6hB
3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
28% identity, 71% coverage: 1:356/504 of query aligns to 33:381/400 of 3ivtB
Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
29% identity, 71% coverage: 1:356/504 of query aligns to 38:386/418 of Q9Y823
- R43 (= R6) binding ; mutation R->A,K,Q: Abolishes the catalytic activity.
- E44 (≠ D7) binding ; binding ; binding
- Q47 (= Q10) mutation to A: Abolishes the catalytic activity.
- E74 (= E38) 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 (≠ Y64) binding ; mutation to A: Substantially impairs catalytic efficiency.
- D123 (≠ K89) binding ; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
- R163 (≠ N132) binding ; mutation R->A,Q: Abolishes the catalytic activity.; mutation to K: Severely diminishes affinity for 2-oxoglutarate and substantially impairs catalytic efficiency.
- S165 (≠ Y134) binding ; mutation to A: Results in a moderate decrease in catalytic efficiency.
- E167 (= E136) mutation E->A,Q: Abolishes the catalytic activity.
- T197 (= T169) 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 (= E191) mutation to Q: Does not affect the catalytic activity but impairs L-lysine inhibition.
- H224 (= H193) binding ; binding
- H226 (= H199) binding ; binding
- R288 (≠ Y259) mutation to K: Does not affect the catalytic activity but impairs L-lysine inhibition.
- Y332 (≠ F303) mutation to A: Abolishes the catalytic activity.; mutation to F: Results in a decrease in catalytic efficiency.
- Q364 (vs. gap) mutation to R: Does not affect the catalytic activity but impairs L-lysine inhibition.
3mi3A Homocitrate synthase lys4 bound to lysine (see paper)
27% identity, 71% coverage: 1:356/504 of query aligns to 15:352/370 of 3mi3A
4ov9A Structure of isopropylmalate synthase binding with alpha- isopropylmalate (see paper)
27% identity, 68% coverage: 2:342/504 of query aligns to 8:350/380 of 4ov9A
3ivsA Homocitrate synthase lys4 (see paper)
26% identity, 70% coverage: 1:351/504 of query aligns to 15:345/364 of 3ivsA
3a9iA Crystal structure of homocitrate synthase from thermus thermophilus complexed with lys (see paper)
28% identity, 74% coverage: 1:372/504 of query aligns to 6:343/347 of 3a9iA
4ov4A Isopropylmalate synthase binding with ketoisovalerate (see paper)
27% identity, 68% coverage: 2:342/504 of query aligns to 8:348/379 of 4ov4A
2zyfA Crystal structure of homocitrate synthase from thermus thermophilus complexed with magnesuim ion and alpha-ketoglutarate (see paper)
27% identity, 63% coverage: 1:316/504 of query aligns to 7:310/314 of 2zyfA
2ztjA Crystal structure of homocitrate synthase from thermus thermophilus complexed with alpha-ketoglutarate (see paper)
27% identity, 63% coverage: 1:316/504 of query aligns to 7:308/312 of 2ztjA
Q53WI0 4-hydroxy-2-oxovalerate aldolase; HOA; 4-hydroxy-2-keto-pentanoic acid aldolase; 4-hydroxy-2-oxohexanoate aldolase; 4-hydroxy-2-oxopentanoate aldolase; EC 4.1.3.39; EC 4.1.3.43 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
26% identity, 48% coverage: 1:243/504 of query aligns to 14:247/347 of Q53WI0
Sites not aligning to the query:
- 324 A→G: Increases the channeling efficiency of propanaldehyde from 57% to 94%.
Query Sequence
>Echvi_2061 FitnessBrowser__Cola:Echvi_2061
MDTTLRDGEQTSGVSFLPSEKLQIAKLLLEELRVDRIEVASARVSEGELEGVKKITHWAA
EKGYLDCVEVLGFVDTPASVDWLTEAGAKVLNLLTKGSLNHLTHQLKKTPVEHFAAIEKC
IHYANEKGISVNVYLEDWSSGMRHSRDYTLELIAFLADQNVKRVMLPDTLGLLKPAEVAE
YVGLVSEQFPEVHFDFHAHNDYDLSVANVMEAINHGISGIHTTVNGLGERAGNAPLESVV
ATLSDFTTVKLNVQENKIYRISKLVEQFSGLHIPSNKPVVGENVFTQTAGIHADGDNKKN
LYFNDLLPERFGRTRKYALGKTSGKANILKNLLELGIKLEPEELSKVTQKIIELGDRKER
VTTEDLPYIISDVLQNNSIKKDISIEGYHMTHSKGLKPTVQLKLKFKDQFYEAHASGNGQ
FDSFMLALQKIYKSLNKKLPKLTDFSVSIPPGGKTDAFVETVITWDYGRIIKTKGLDSDQ
TVAAMMATEKMLNIIEQIDSGNRA
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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