SitesBLAST
Comparing WP_012674645.1 NCBI__GCF_000021545.1:WP_012674645.1 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)
6ktqA Crystal structure of catalytic domain of homocitrate synthase from sulfolobus acidocaldarius (sahcs(dram)) in complex with alpha- ketoglutarate/zn2+/coa (see paper)
31% identity, 70% coverage: 1:374/533 of query aligns to 18:378/399 of 6ktqA
- binding 2-oxoglutaric acid: R30 (= R13), R154 (≠ I142), T156 (≠ D144), E158 (= E146), S184 (≠ I175), T188 (= T179), H216 (= H207), H218 (= H209)
- binding coenzyme a: V67 (≠ S50), R96 (= R79), A97 (≠ S80), F116 (= F104), H128 (≠ L116), E158 (= E146)
- binding zinc ion: E31 (≠ D14), 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)
29% identity, 83% coverage: 4:448/533 of query aligns to 6:440/517 of Q9JZG1
- D16 (= D14) 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)
30% identity, 69% coverage: 5:371/533 of query aligns to 18:394/409 of 6e1jA
- binding coenzyme a: Q30 (= Q17), F60 (≠ W47), S63 (= S50), I95 (≠ T77), R97 (= R79), F121 (= F104), K132 (≠ A115), L133 (= L116), S322 (≠ G301), G323 (= G302), I324 (≠ V303), D327 (≠ S306), K331 (≠ R310), L359 (= L334), R362 (≠ K337), H363 (≠ S338)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (≠ C177), T194 (= T179), H225 (= H207), H227 (= H209)
- binding manganese (ii) ion: D27 (= D14), V82 (≠ L64), E84 (≠ L66), 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)
29% identity, 68% coverage: 5:368/533 of query aligns to 85:458/506 of Q9FG67
- S102 (= S22) 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, 68% coverage: 5:368/533 of query aligns to 85:458/503 of Q9FN52
- G263 (= G181) mutation to E: In gsm2-1; loss of activity and lack of C6, C7 and C8 aliphatic glucosinolates.
O87198 Homocitrate synthase; HCS; EC 2.3.3.14 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see paper)
30% identity, 69% coverage: 7:372/533 of query aligns to 6:359/376 of O87198
- R12 (= R13) binding 2-oxoglutarate
- E13 (≠ D14) 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 (≠ I101) binding L-lysine
- R133 (≠ I142) 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+)
3rmjB Crystal structure of truncated alpha-isopropylmalate synthase from neisseria meningitidis (see paper)
32% identity, 56% coverage: 4:300/533 of query aligns to 3:295/308 of 3rmjB
4ov9A Structure of isopropylmalate synthase binding with alpha- isopropylmalate (see paper)
28% identity, 69% coverage: 3:370/533 of query aligns to 2:367/380 of 4ov9A
3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
27% identity, 68% coverage: 7:370/533 of query aligns to 32:381/400 of 3ivtB
Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
27% identity, 68% coverage: 7:370/533 of query aligns to 37:386/418 of Q9Y823
- R43 (= R13) binding 2-oxoglutarate; mutation R->A,K,Q: Abolishes the catalytic activity.
- E44 (≠ D14) binding 2-oxoglutarate; binding L-lysine; binding Zn(2+)
- 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 (≠ S81) binding 2-oxoglutarate; mutation to A: Substantially impairs catalytic efficiency.
- D123 (≠ I101) binding L-lysine; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
- R163 (≠ I142) 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 (≠ D144) 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 (≠ G205) 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 (≠ K271) 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.
4ov4A Isopropylmalate synthase binding with ketoisovalerate (see paper)
27% identity, 69% coverage: 3:370/533 of query aligns to 2:365/379 of 4ov4A
3mi3A Homocitrate synthase lys4 bound to lysine (see paper)
27% identity, 68% coverage: 7:370/533 of query aligns to 14:352/370 of 3mi3A
2ztjA Crystal structure of homocitrate synthase from thermus thermophilus complexed with alpha-ketoglutarate (see paper)
29% identity, 61% coverage: 7:332/533 of query aligns to 6:312/312 of 2ztjA
2zyfA Crystal structure of homocitrate synthase from thermus thermophilus complexed with magnesuim ion and alpha-ketoglutarate (see paper)
29% identity, 61% coverage: 7:332/533 of query aligns to 6:314/314 of 2zyfA
3ivsA Homocitrate synthase lys4 (see paper)
26% identity, 65% coverage: 7:355/533 of query aligns to 14:337/364 of 3ivsA
3a9iA Crystal structure of homocitrate synthase from thermus thermophilus complexed with lys (see paper)
30% identity, 60% coverage: 7:324/533 of query aligns to 5:305/347 of 3a9iA
Q8F3Q1 (R)-citramalate synthase CimA; LiCMS; EC 2.3.3.21 from Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) (see 2 papers)
26% identity, 92% coverage: 1:488/533 of query aligns to 4:471/516 of Q8F3Q1
- R16 (= R13) mutation R->K,Q: Loss of activity.
- RD 16:17 (= RD 13:14) binding pyruvate
- 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 (≠ F104) 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 (= 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 (≠ R313) mutation to A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat.
- Y312 (≠ S314) mutation to A: Loss of activity.
- Y430 (≠ V440) mutation to L: No change in Km for acetyl-CoA and 2.3-fold decrease in kcat. Severely impairs inhibition by isoleucine.
- D431 (≠ N441) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 5-fold decrease in kcat.
- L451 (= L463) mutation to V: 1.5-fold increase in Km for acetyl-CoA and 4.3 decrease in kcat.
- Y454 (= Y466) 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 (= I470) mutation to A: 1.3-fold decrease in Km for acetyl-CoA and 14-fold decrease in kcat. Abolishes inhibition by isoleucine.
- T464 (≠ I481) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 4.3-fold decrease in kcat.
- V468 (≠ I485) 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.
Sites not aligning to the query:
- 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.
3bliA Crystal structure of the catalytic domain of licms in complexed with pyruvate and acetyl-coa (see paper)
27% identity, 60% coverage: 7:327/533 of query aligns to 4:311/311 of 3bliA
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, 66% coverage: 3:355/533 of query aligns to 9:341/347 of Q53WI0
- A324 (= A335) mutation to G: Increases the channeling efficiency of propanaldehyde from 57% to 94%.
3hpzB Crystal structure of mycobacterium tuberculosis leua complexed with bromopyruvate
23% identity, 59% coverage: 204:515/533 of query aligns to 265:572/576 of 3hpzB
Sites not aligning to the query:
Query Sequence
>WP_012674645.1 NCBI__GCF_000021545.1:WP_012674645.1
MEKQVLIYDTTLRDGTQAEGVSVSVEDKLRIAEKLADFGVHYIEGGWPGSNPKDMTFFKE
VKKLNLKNTKITAFGSTRRSSLKVEEDPQIQDLIKAETPVITIFGKSWDLHVTQALKTTL
EKNLEMIYDSISYLKKYVDEVIFDAEHFFDGFKENPDYAIEVLKVAQQGGADFLILCDTN
GGSLPTDIEKAFKAVKEAGITAKLGIHAHNDSDTAVWNSIVAVLHGAIQVHGTINGIGER
CGNANLCSIIPNLSLKLGYETVPRENIKRLKEISNFVSDILNMPVPKNMPYVGDSAFAHK
GGVHASAVLRNPRSYEHILPQEVGNRRKVLVSDLAGKSNIIYKAKEIGIEIDEKDERLTK
LVQEIKELENQGYHFEAAEASLELLIRKHLGTLPKYFDLDAYRVLIARRYTDKSPISEAT
VRIKIENHYEHTASLGYGPVNALDKALKKALTAVYPSLAEVELIDYKVRIVNESGGTAAK
IRVLIESRDKSKKWGTVGVSDNIIEASWQAVVDSIVYKLVKDGIKPAGGNKDA
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