SitesBLAST
Comparing WP_020565007.1 NCBI__GCF_000372865.1:WP_020565007.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
50% identity, 97% coverage: 8:507/514 of query aligns to 8:512/516 of Q8F3Q1
- R16 (= R16) mutation R->K,Q: Loss of activity.
- RD 16:17 (= RD 16:17) binding pyruvate
- D17 (= D17) 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 (= L81) 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 (= F83) mutation to A: 5-fold increase in Km for acetyl-CoA and 120-fold decrease in kcat.
- L104 (= L104) mutation to V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat.
- Y144 (= Y144) 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 (= H302) mutation H->A,N: Loss of activity.
- D304 (= D304) mutation to A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat.
- N310 (≠ G310) mutation to A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat.
- L311 (= L311) mutation to A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat.
- Y312 (= Y312) mutation to A: Loss of activity.
- Y430 (≠ F430) mutation to L: No change in Km for acetyl-CoA and 2.3-fold decrease in kcat. Severely impairs inhibition by isoleucine.
- D431 (= D431) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 5-fold decrease in kcat.
- L451 (= L451) mutation to V: 1.5-fold increase in Km for acetyl-CoA and 4.3 decrease in kcat.
- Y454 (= Y454) 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 (= I458) mutation to A: 1.3-fold decrease in Km for acetyl-CoA and 14-fold decrease in kcat. Abolishes inhibition by isoleucine.
- T464 (= T464) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 4.3-fold decrease in kcat.
- V468 (≠ T468) 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 (≠ A488) mutation to A: 1.5-fold decrease in Km for acetyl-CoA and 2.6-fold decrease in kcat.
- Q495 (= Q490) 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)
51% identity, 62% coverage: 8:325/514 of query aligns to 2:311/311 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)
35% identity, 69% coverage: 8:363/514 of query aligns to 22:371/399 of 6ktqA
- binding 2-oxoglutaric acid: R30 (= R16), R154 (≠ N142), T156 (≠ Y144), E158 (= E146), S184 (≠ M175), T188 (= T179), H216 (= H207), H218 (= H209)
- binding coenzyme a: V67 (= V54), R96 (= R88), A97 (≠ S89), F116 (≠ L104), H128 (≠ L116), E158 (= E146)
- binding zinc ion: E31 (≠ D17), H216 (= H207), H218 (= H209)
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)
31% identity, 85% coverage: 3:437/514 of query aligns to 2:439/517 of Q9JZG1
- D16 (= D17) 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)
31% identity, 73% coverage: 7:380/514 of query aligns to 17:407/409 of 6e1jA
- binding coenzyme a: Q30 (= Q20), F60 (≠ S51), S63 (≠ V54), I95 (≠ V84), R97 (≠ H86), F121 (≠ L104), K132 (≠ Q115), L133 (= L116), S322 (≠ A299), G323 (= G300), I324 (= I301), D327 (= D304), K331 (= K308), L359 (≠ M332), R362 (≠ K335), H363 (≠ A336)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (= P177), T194 (= T179), H225 (= H207), H227 (= H209)
- binding manganese (ii) ion: D27 (= D17), V82 (≠ G73), E84 (≠ D75), H225 (= H207), H227 (= H209)
Q9FG67 Methylthioalkylmalate synthase 1, chloroplastic; 2-isopropylmalate synthase 3; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
32% identity, 73% coverage: 7:380/514 of query aligns to 84:474/506 of Q9FG67
- S102 (= S25) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
- A290 (≠ D205) 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)
32% identity, 73% coverage: 7:382/514 of query aligns to 84:476/503 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)
32% identity, 56% coverage: 10:297/514 of query aligns to 6:294/308 of 3rmjB
3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
25% identity, 72% coverage: 10:380/514 of query aligns to 32:394/400 of 3ivtB
Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
25% identity, 72% coverage: 10:380/514 of query aligns to 37:399/418 of Q9Y823
- R43 (= R16) binding 2-oxoglutarate; mutation R->A,K,Q: Abolishes the catalytic activity.
- E44 (≠ D17) binding 2-oxoglutarate; binding L-lysine; binding Zn(2+)
- Q47 (= Q20) mutation to A: Abolishes the catalytic activity.
- E74 (= E48) 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 (≠ G82) binding 2-oxoglutarate; mutation to A: Substantially impairs catalytic efficiency.
- D123 (≠ N102) binding L-lysine; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
- R163 (≠ N142) 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 (≠ Y144) binding 2-oxoglutarate; mutation to A: Results in a moderate decrease in catalytic efficiency.
- E167 (= E146) mutation E->A,Q: Abolishes the catalytic activity.
- T197 (= T179) 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 (≠ D205) mutation to Q: Does not affect the catalytic activity but impairs L-lysine inhibition.
- H224 (= H207) binding 2-oxoglutarate; binding Zn(2+)
- H226 (= H209) binding 2-oxoglutarate; binding Zn(2+)
- R288 (≠ V269) mutation to K: Does not affect the catalytic activity but impairs L-lysine inhibition.
- Y332 (≠ K313) mutation to A: Abolishes the catalytic activity.; mutation to F: Results in a decrease in catalytic efficiency.
- Q364 (≠ L344) 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)
25% identity, 73% coverage: 9:382/514 of query aligns to 5:372/376 of O87198
- R12 (= R16) binding 2-oxoglutarate
- E13 (≠ D17) binding Mg(2+)
- H72 (≠ F74) 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 (≠ N102) binding L-lysine
- R133 (≠ Y144) binding 2-oxoglutarate
- S135 (≠ D147) binding L-lysine
- T166 (= T179) binding 2-oxoglutarate; binding L-lysine
- H195 (= H207) binding Mg(2+)
- H197 (= H209) binding Mg(2+)
3mi3A Homocitrate synthase lys4 bound to lysine (see paper)
25% identity, 72% coverage: 10:380/514 of query aligns to 14:365/370 of 3mi3A
3f6hB Crystal structure of the regulatory domain of licms in complexed with isoleucine - type iii (see paper)
43% identity, 22% coverage: 396:507/514 of query aligns to 7:121/125 of 3f6hB
3ivsA Homocitrate synthase lys4 (see paper)
25% identity, 72% coverage: 10:380/514 of query aligns to 14:359/364 of 3ivsA
4ov9A Structure of isopropylmalate synthase binding with alpha- isopropylmalate (see paper)
26% identity, 72% coverage: 8:376/514 of query aligns to 4:376/380 of 4ov9A
4ov4A Isopropylmalate synthase binding with ketoisovalerate (see paper)
26% identity, 72% coverage: 8:376/514 of query aligns to 4:374/379 of 4ov4A
2zyfA Crystal structure of homocitrate synthase from thermus thermophilus complexed with magnesuim ion and alpha-ketoglutarate (see paper)
26% identity, 62% coverage: 9:325/514 of query aligns to 5:309/314 of 2zyfA
2ztjA Crystal structure of homocitrate synthase from thermus thermophilus complexed with alpha-ketoglutarate (see paper)
25% identity, 62% coverage: 9:325/514 of query aligns to 5:307/312 of 2ztjA
3a9iA Crystal structure of homocitrate synthase from thermus thermophilus complexed with lys (see paper)
27% identity, 57% coverage: 9:302/514 of query aligns to 4:285/347 of 3a9iA
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, 53% coverage: 10:280/514 of query aligns to 13:270/347 of Q53WI0
Sites not aligning to the query:
- 324 A→G: Increases the channeling efficiency of propanaldehyde from 57% to 94%.
Query Sequence
>WP_020565007.1 NCBI__GCF_000372865.1:WP_020565007.1
MATKSRFIQLMDTTLRDGEQTQGVSFTPAEKVNIAKALLQSLRVDRIEVASARVSAGEKE
AVTNINQWAKQEGFDGCVEVLGFVDHTRSVDWILETGGSVINLLTKGSEKHCREQLGKTR
EQHTADILQTVDYALSRSLKVNVYLEDWSNGYQNSPDYVYALMDSLKEAGISHFMLPDTL
GVMSPDEVFTSFSDMCRCYPALQFDFHPHNDYGLATANVMAAVRAGATAVHCTVNCLGER
AGNASLAEVAVVLRDKMNMQLSIDETHIVRLSNMVENFSGKRVAANAPIVGSDVFTQTAG
IHADGDHKGGLYKSRLSPERFSRSRSYALGKMSGKASLKKNLELLEIDLSEENQKKVLAR
IVSLGDSKQTITTDDLPFIIADVLESKNYQHIKLLNCFITSGLHLESTASLRLDVNGAKH
VISGAGNGGFDAFIDAVNKAMKEHDYTVPPLADYEVRIPKGGHTDALTECVITWNCGSEL
RKTRGVHANQVFAAIMATLKIINMQLHELNQNTA
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