SitesBLAST
Comparing WP_011384529.1 NCBI__GCF_000009985.1:WP_011384529.1 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)
27% identity, 99% coverage: 4:541/546 of query aligns to 6:504/517 of Q9JZG1
- D16 (= D14) binding
- H204 (= H206) binding
- H206 (= H208) binding
- N240 (= N242) binding
Sites not aligning to the query:
- 366:517 Required for the condensation reaction. Not required to bind substrate
6ktqA Crystal structure of catalytic domain of homocitrate synthase from sulfolobus acidocaldarius (sahcs(dram)) in complex with alpha- ketoglutarate/zn2+/coa (see paper)
33% identity, 71% coverage: 4:390/546 of query aligns to 21:399/399 of 6ktqA
- binding 2-oxoglutaric acid: R30 (= R13), R154 (≠ M140), T156 (≠ D142), E158 (= E144), S184 (≠ V173), T188 (= T177), H216 (= H206), H218 (= H208)
- binding coenzyme a: V67 (≠ A50), R96 (= R80), A97 (≠ S81), F116 (≠ M101), H128 (≠ L114), E158 (= E144)
- binding zinc ion: E31 (≠ D14), H216 (= H206), H218 (= H208)
6e1jA Crystal structure of methylthioalkylmalate synthase (bjumam1.1) from brassica juncea (see paper)
28% identity, 64% coverage: 5:355/546 of query aligns to 18:380/409 of 6e1jA
- binding coenzyme a: Q30 (= Q17), F60 (≠ W47), S63 (≠ A50), I95 (≠ P95), R97 (= R97), F121 (vs. gap), K132 (≠ A113), L133 (= L114), S322 (≠ G301), G323 (= G302), I324 (≠ L303), D327 (≠ S306), K331 (= K310), L359 (≠ Q334), R362 (= R337), H363 (≠ S338)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (≠ C175), T194 (= T177), H225 (= H206), H227 (= H208)
- binding manganese (ii) ion: D27 (= D14), V82 (≠ A82), E84 (≠ N84), H225 (= H206), H227 (= H208)
Q9FG67 Methylthioalkylmalate synthase 1, chloroplastic; 2-isopropylmalate synthase 3; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
27% identity, 64% coverage: 5:355/546 of query aligns to 85:447/506 of Q9FG67
- S102 (≠ D22) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
- A290 (≠ G204) 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, 54% coverage: 4:300/546 of query aligns to 3:295/308 of 3rmjB
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)
27% identity, 64% coverage: 5:355/546 of query aligns to 85:447/503 of Q9FN52
- G263 (= G179) 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)
24% identity, 98% coverage: 4:540/546 of query aligns to 7:511/516 of Q8F3Q1
- R16 (= R13) mutation R->K,Q: Loss of activity.
- RD 16:17 (= RD 13:14) binding
- 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 (≠ V102) mutation to V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat.
- Y144 (≠ D142) 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 (= E144) mutation E->D,Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat.
- T179 (= T177) binding ; mutation to A: 16.4-fold increase in Km for pyruvate and 186-fold decrease in kcat.
- H302 (= H304) mutation H->A,N: Loss of activity.
- D304 (≠ S306) mutation to A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat.
- N310 (≠ P312) mutation to A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat.
- L311 (≠ K313) mutation to A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat.
- Y312 (≠ C314) mutation to A: Loss of activity.
- Y430 (≠ V460) mutation to L: No change in Km for acetyl-CoA and 2.3-fold decrease in kcat. Severely impairs inhibition by isoleucine.
- D431 (≠ H461) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 5-fold decrease in kcat.
- L451 (= L483) mutation to V: 1.5-fold increase in Km for acetyl-CoA and 4.3 decrease in kcat.
- Y454 (= Y486) 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 (= I490) mutation to A: 1.3-fold decrease in Km for acetyl-CoA and 14-fold decrease in kcat. Abolishes inhibition by isoleucine.
- T464 (= T491) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 4.3-fold decrease in kcat.
- V468 (= V495) 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 (≠ T522) mutation to A: 1.5-fold decrease in Km for acetyl-CoA and 2.6-fold decrease in kcat.
- Q495 (≠ V524) mutation to A: 1.6-fold decrease in Km for acetyl-CoA and 2.8-fold decrease in kcat.
O87198 Homocitrate synthase; HCS; EC 2.3.3.14 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see paper)
29% identity, 67% coverage: 7:371/546 of query aligns to 6:357/376 of O87198
- R12 (= R13) binding
- E13 (≠ D14) binding
- H72 (≠ A71) 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 (≠ N89) binding
- R133 (≠ M140) binding
- S135 (≠ D142) binding
- T166 (= T177) binding ; binding
- H195 (= H206) binding
- H197 (= H208) binding
4ov9A Structure of isopropylmalate synthase binding with alpha- isopropylmalate (see paper)
26% identity, 68% coverage: 5:377/546 of query aligns to 4:373/380 of 4ov9A
4ov4A Isopropylmalate synthase binding with ketoisovalerate (see paper)
26% identity, 68% coverage: 5:377/546 of query aligns to 4:371/379 of 4ov4A
2zyfA Crystal structure of homocitrate synthase from thermus thermophilus complexed with magnesuim ion and alpha-ketoglutarate (see paper)
29% identity, 60% coverage: 7:332/546 of query aligns to 6:314/314 of 2zyfA
2ztjA Crystal structure of homocitrate synthase from thermus thermophilus complexed with alpha-ketoglutarate (see paper)
28% identity, 60% coverage: 7:332/546 of query aligns to 6:312/312 of 2ztjA
3a9iA Crystal structure of homocitrate synthase from thermus thermophilus complexed with lys (see paper)
29% identity, 58% coverage: 7:324/546 of query aligns to 5:305/347 of 3a9iA
3mi3A Homocitrate synthase lys4 bound to lysine (see paper)
26% identity, 65% coverage: 7:362/546 of query aligns to 14:347/370 of 3mi3A
3bliA Crystal structure of the catalytic domain of licms in complexed with pyruvate and acetyl-coa (see paper)
26% identity, 57% coverage: 4:315/546 of query aligns to 1:307/311 of 3bliA
3ivsA Homocitrate synthase lys4 (see paper)
25% identity, 65% coverage: 7:362/546 of query aligns to 14:342/364 of 3ivsA
3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
26% identity, 65% coverage: 7:362/546 of query aligns to 32:376/400 of 3ivtB
Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
26% identity, 65% coverage: 7:362/546 of query aligns to 37:381/418 of Q9Y823
- R43 (= R13) binding ; mutation R->A,K,Q: Abolishes the catalytic activity.
- E44 (≠ D14) binding ; binding ; binding
- 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 (vs. gap) binding ; mutation to A: Substantially impairs catalytic efficiency.
- D123 (≠ T111) binding ; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
- R163 (≠ M140) binding ; mutation R->A,Q: Abolishes the catalytic activity.; mutation to K: Severely diminishes affinity for 2-oxoglutarate and substantially impairs catalytic efficiency.
- S165 (≠ D142) binding ; mutation to A: Results in a moderate decrease in catalytic efficiency.
- E167 (= E144) mutation E->A,Q: Abolishes the catalytic activity.
- T197 (= T177) 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 (≠ G204) mutation to Q: Does not affect the catalytic activity but impairs L-lysine inhibition.
- H224 (= H206) binding ; binding
- H226 (= H208) binding ; binding
- R288 (= R275) mutation to K: Does not affect the catalytic activity but impairs L-lysine inhibition.
- Y332 (= Y315) mutation to A: Abolishes the catalytic activity.; mutation to F: Results in a decrease in catalytic efficiency.
- Q364 (≠ E346) mutation to R: Does not affect the catalytic activity but impairs L-lysine inhibition.
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)
25% identity, 58% coverage: 9:323/546 of query aligns to 15:313/347 of Q53WI0
Sites not aligning to the query:
- 324 A→G: Increases the channeling efficiency of propanaldehyde from 57% to 94%.
3hpzB Crystal structure of mycobacterium tuberculosis leua complexed with bromopyruvate
27% identity, 49% coverage: 203:470/546 of query aligns to 265:513/576 of 3hpzB
Sites not aligning to the query:
Query Sequence
>WP_011384529.1 NCBI__GCF_000009985.1:WP_011384529.1
MAERVYLYDTTLRDGAQTQGVDFSAADKVRIARELDRIGIDYVEGGWPGANPTDDAFFAD
PPAFKRSRLTAFGMTRRAGRSADNDPGLNALLVTPARVATMVGKSWDFQVTVALGIELDE
NLRMVADSVQHARTKVEEVMFDAEHFFDGYKANPAYALAAAKAAYDAGARWVVLCDTNGG
TLPHEMRRIVGEVIKGGIPGSHLGVHCHNDSDTAVANSLAAVEAGVRQIQGTLNGLGERC
GNANLISIIPALMLKMGFDTGIAPEDLKNLVSVSRALDEVLDRTPNRGQPYVGKSAFAHK
GGLHVSAVAKDPKCYEHVDPASVGNMRHIVMSDQAGRSNLVARLTEIGIDLDSVKRESLV
RVVDQMQVTFDAREATDLVDLVKRLEHEGYAYDQAAASFELLVRRALGEVPEYFALERYR
VIDERRRNAHGEWITLSEATVKVEVGGTEYMEVGEGTGPVHAFDVALRKVLTRVYPALTA
LELKDYRVRITESTVGTAAKTRVTIESEDDKGHRWTTVGVHTNVLEASLEALQDSITFML
FRFKDE
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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