SitesBLAST
Comparing WP_012566191.1 NCBI__GCF_000016185.1:WP_012566191.1 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)
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, 92% coverage: 1:503/547 of query aligns to 1:476/517 of Q9JZG1
- D16 (= D16) binding Mn(2+)
- H204 (= H207) binding Mn(2+)
- H206 (= H209) binding Mn(2+)
- N240 (= N243) 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)
29% identity, 64% coverage: 1:352/547 of query aligns to 12:376/409 of 6e1jA
- binding coenzyme a: Q30 (= Q19), F60 (≠ W49), S63 (≠ A52), I95 (≠ P80), R97 (= R82), F121 (≠ V104), K132 (≠ A115), L133 (= L116), S322 (≠ G302), G323 (= G303), I324 (≠ L304), D327 (≠ S307), K331 (= K311), L359 (≠ Q335), R362 (= R338), H363 (≠ S339)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (≠ C177), T194 (= T179), H225 (= H207), H227 (= H209)
- binding manganese (ii) ion: D27 (= D16), V82 (vs. gap), E84 (vs. gap), H225 (= H207), H227 (= H209)
6ktqA Crystal structure of catalytic domain of homocitrate synthase from sulfolobus acidocaldarius (sahcs(dram)) in complex with alpha- ketoglutarate/zn2+/coa (see paper)
30% identity, 66% coverage: 6:367/547 of query aligns to 21:370/399 of 6ktqA
- binding 2-oxoglutaric acid: R30 (= R15), R154 (≠ L142), T156 (≠ D144), E158 (= E146), S184 (≠ V175), T188 (= T179), H216 (= H207), H218 (= H209)
- binding coenzyme a: V67 (≠ A52), R96 (= R82), A97 (≠ S83), F116 (≠ V104), H128 (≠ L116), E158 (= E146)
- binding zinc ion: E31 (≠ D16), H216 (= H207), H218 (= H209)
Q9FG67 Methylthioalkylmalate synthase 1, chloroplastic; 2-isopropylmalate synthase 3; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
30% identity, 64% coverage: 5:353/547 of query aligns to 83:444/506 of Q9FG67
- S102 (≠ D24) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
- A290 (≠ G205) 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)
29% identity, 71% coverage: 5:394/547 of query aligns to 83:493/503 of Q9FN52
- G263 (= G181) 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)
33% identity, 54% coverage: 4:301/547 of query aligns to 1:295/308 of 3rmjB
4ov9A Structure of isopropylmalate synthase binding with alpha- isopropylmalate (see paper)
29% identity, 67% coverage: 7:370/547 of query aligns to 4:366/380 of 4ov9A
4ov4A Isopropylmalate synthase binding with ketoisovalerate (see paper)
29% identity, 67% coverage: 7:370/547 of query aligns to 4:364/379 of 4ov4A
O87198 Homocitrate synthase; HCS; EC 2.3.3.14 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see paper)
29% identity, 66% coverage: 9:369/547 of query aligns to 6:358/376 of O87198
- R12 (= R15) binding 2-oxoglutarate
- E13 (≠ D16) binding Mg(2+)
- H72 (≠ A73) binding 2-oxoglutarate; 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 (≠ A91) binding L-lysine
- R133 (= R137) binding 2-oxoglutarate
- S135 (≠ D144) binding L-lysine
- T166 (= T179) binding 2-oxoglutarate; binding L-lysine
- H195 (= H207) binding Mg(2+)
- H197 (= H209) binding Mg(2+)
Q8F3Q1 (R)-citramalate synthase CimA; LiCMS; EC 2.3.3.21 from Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) (see 2 papers)
27% identity, 63% coverage: 6:350/547 of query aligns to 7:347/516 of Q8F3Q1
- R16 (= R15) mutation R->K,Q: Loss of activity.
- RD 16:17 (= RD 15:16) binding pyruvate
- D17 (= D16) 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 (≠ S83) 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 (≠ A85) mutation to A: 5-fold increase in Km for acetyl-CoA and 120-fold decrease in kcat.
- L104 (≠ V104) mutation to V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat.
- Y144 (≠ D144) 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 (= E146) mutation E->D,Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat.
- T179 (= T179) binding pyruvate; mutation to A: 16.4-fold increase in Km for pyruvate and 186-fold decrease in kcat.
- H302 (= H305) mutation H->A,N: Loss of activity.
- D304 (≠ S307) mutation to A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat.
- N310 (≠ P313) mutation to A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat.
- L311 (≠ A314) mutation to A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat.
- Y312 (≠ C315) 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.
2zyfA Crystal structure of homocitrate synthase from thermus thermophilus complexed with magnesuim ion and alpha-ketoglutarate (see paper)
29% identity, 59% coverage: 9:333/547 of query aligns to 6:314/314 of 2zyfA
2ztjA Crystal structure of homocitrate synthase from thermus thermophilus complexed with alpha-ketoglutarate (see paper)
29% identity, 59% coverage: 9:333/547 of query aligns to 6:312/312 of 2ztjA