SitesBLAST
Comparing WP_097070056.1 NCBI__GCF_900217815.1:WP_097070056.1 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)
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, 82% coverage: 12:329/386 of query aligns to 22:342/399 of 6ktqA
- binding 2-oxoglutaric acid: R30 (= R20), R154 (≠ S140), T156 (≠ G142), E158 (= E144), S184 (≠ R170), T188 (= T174), H216 (= H201), H218 (= H203)
- binding coenzyme a: V67 (≠ M57), R96 (= R82), A97 (≠ L83), F116 (≠ A102), H128 (≠ L114), E158 (= E144)
- binding zinc ion: E31 (≠ D21), H216 (= H201), H218 (= H203)
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)
33% identity, 94% coverage: 14:377/386 of query aligns to 9:383/517 of Q9JZG1
- D16 (= D21) binding Mn(2+)
- H204 (= H201) binding Mn(2+)
- H206 (= H203) binding Mn(2+)
- N240 (= N237) 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)
32% identity, 94% coverage: 16:376/386 of query aligns to 22:407/409 of 6e1jA
- binding coenzyme a: Q30 (= Q24), F60 (≠ I54), S63 (≠ M57), I95 (≠ R82), R97 (= R84), F121 (≠ A102), K132 (= K113), L133 (= L114), S322 (= S292), G323 (= G293), I324 (= I294), D327 (= D297), K331 (= K301), L359 (≠ H327), R362 (≠ A330), H363 (≠ A331)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (≠ A172), T194 (= T174), H225 (= H201), H227 (= H203)
- binding manganese (ii) ion: D27 (= D21), V82 (≠ A76), E84 (vs. gap), H225 (= H201), H227 (= H203)
Q9FG67 Methylthioalkylmalate synthase 1, chloroplastic; 2-isopropylmalate synthase 3; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
31% identity, 94% coverage: 16:376/386 of query aligns to 89:474/506 of Q9FG67
- S102 (≠ A29) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
- A290 (≠ E199) 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)
31% identity, 96% coverage: 9:378/386 of query aligns to 80:476/503 of Q9FN52
- G263 (= G176) mutation to E: In gsm2-1; loss of activity and lack of C6, C7 and C8 aliphatic glucosinolates.
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, 96% coverage: 12:380/386 of query aligns to 8:384/516 of Q8F3Q1
- R16 (= R20) mutation R->K,Q: Loss of activity.
- RD 16:17 (= RD 20:21) binding pyruvate
- D17 (= D21) 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 (≠ V79) 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 (≠ C81) mutation to A: 5-fold increase in Km for acetyl-CoA and 120-fold decrease in kcat.
- L104 (≠ A102) mutation to V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat.
- Y144 (≠ G142) 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 (= E144) mutation E->D,Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat.
- T179 (= T174) binding pyruvate; mutation to A: 16.4-fold increase in Km for pyruvate and 186-fold decrease in kcat.
- H302 (= H295) mutation H->A,N: Loss of activity.
- D304 (= D297) mutation to A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat.
- N310 (≠ D304) mutation to A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat.
- L311 (≠ T305) mutation to A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat.
- Y312 (= Y306) 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.
3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
32% identity, 82% coverage: 10:325/386 of query aligns to 28:344/400 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, 82% coverage: 10:325/386 of query aligns to 33:349/418 of Q9Y823
- R43 (= R20) binding 2-oxoglutarate; mutation R->A,K,Q: Abolishes the catalytic activity.
- E44 (≠ D21) binding 2-oxoglutarate; binding L-lysine; binding Zn(2+)
- Q47 (= Q24) mutation to A: Abolishes the catalytic activity.
- E74 (= E51) 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 (≠ W80) binding 2-oxoglutarate; mutation to A: Substantially impairs catalytic efficiency.
- D123 (≠ H100) binding L-lysine; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
- R163 (≠ S140) 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 (≠ G142) binding 2-oxoglutarate; mutation to A: Results in a moderate decrease in catalytic efficiency.
- E167 (= E144) mutation E->A,Q: Abolishes the catalytic activity.
- T197 (= T174) 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 (= E199) mutation to Q: Does not affect the catalytic activity but impairs L-lysine inhibition.
- H224 (= H201) binding 2-oxoglutarate; binding Zn(2+)
- H226 (= H203) binding 2-oxoglutarate; binding Zn(2+)
- R288 (≠ Q262) mutation to K: Does not affect the catalytic activity but impairs L-lysine inhibition.
- Y332 (= Y306) mutation to A: Abolishes the catalytic activity.; mutation to F: Results in a decrease in catalytic efficiency.
Sites not aligning to the query:
- 364 Q→R: Does not affect the catalytic activity but impairs L-lysine inhibition.
3mi3A Homocitrate synthase lys4 bound to lysine (see paper)
32% identity, 82% coverage: 10:325/386 of query aligns to 10:315/370 of 3mi3A
3ivsA Homocitrate synthase lys4 (see paper)
31% identity, 82% coverage: 10:325/386 of query aligns to 10:313/364 of 3ivsA
3rmjB Crystal structure of truncated alpha-isopropylmalate synthase from neisseria meningitidis (see paper)
33% identity, 72% coverage: 14:292/386 of query aligns to 6:296/308 of 3rmjB
3bliA Crystal structure of the catalytic domain of licms in complexed with pyruvate and acetyl-coa (see paper)
30% identity, 80% coverage: 12:320/386 of query aligns to 2:311/311 of 3bliA
2zyfA Crystal structure of homocitrate synthase from thermus thermophilus complexed with magnesuim ion and alpha-ketoglutarate (see paper)
33% identity, 81% coverage: 14:324/386 of query aligns to 6:313/314 of 2zyfA
O87198 Homocitrate synthase; HCS; EC 2.3.3.14 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see paper)
31% identity, 94% coverage: 14:376/386 of query aligns to 6:370/376 of O87198