SitesBLAST
Comparing WP_041532230.1 NCBI__GCF_000015045.1:WP_041532230.1 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)
4delA Active site loop dynamics of a class iia fructose 1,6-bisphosphate aldolase from m. Tuberculosis (see paper)
56% identity, 99% coverage: 2:338/341 of query aligns to 1:341/345 of 4delA
- active site: D94 (= D95), H95 (= H96), E168 (= E169), H211 (= H211), H251 (= H248), N273 (= N270)
- binding phosphoglycolohydroxamic acid: D94 (= D95), H95 (= H96), H211 (= H211), G212 (= G212), H251 (= H248), G252 (= G249), S254 (= S251), N273 (= N270), D275 (= D272), T276 (= T273)
- binding zinc ion: H95 (= H96), H211 (= H211), H251 (= H248)
Sites not aligning to the query:
3ekzA Structural characterization of tetrameric mycobacterium tuberculosis fructose 1,6-bisphosphate aldolase - substrate binding and catalysis mechanism of a class iia bacterial aldolase (see paper)
55% identity, 99% coverage: 2:338/341 of query aligns to 1:330/334 of 3ekzA
Sites not aligning to the query:
4a22A Structure of mycobacterium tuberculosis fructose 1,6-bisphosphate aldolase bound to n-(4-hydroxybutyl)- glycolohydroxamic acid bis- phosphate (see paper)
54% identity, 99% coverage: 2:338/341 of query aligns to 1:328/329 of 4a22A
- active site: D94 (= D95), H95 (= H96), H198 (= H211), H238 (= H248), N260 (= N270)
- binding 4-{hydroxy[(phosphonooxy)acetyl]amino}butyl dihydrogen phosphate: N26 (= N27), S52 (= S53), D94 (= D95), H95 (= H96), H198 (= H211), G199 (= G212), H238 (= H248), G239 (= G249), S241 (= S251), N260 (= N270), V261 (≠ I271), D262 (= D272), T263 (= T273)
- binding zinc ion: H95 (= H96), H198 (= H211), H238 (= H248)
3elfA Structural characterization of tetrameric mycobacterium tuberculosis fructose 1,6-bisphosphate aldolase - substrate binding and catalysis mechanism of a class iia bacterial aldolase (see paper)
54% identity, 99% coverage: 2:338/341 of query aligns to 1:328/332 of 3elfA
- active site: D94 (= D95), H95 (= H96), H198 (= H211), H238 (= H248), N260 (= N270)
- binding 1,6-fructose diphosphate (linear form): N26 (= N27), S52 (= S53), D94 (= D95), H95 (= H96), H198 (= H211), G199 (= G212), H238 (= H248), G239 (= G249), S241 (= S251), N260 (= N270), V261 (≠ I271), D262 (= D272), T263 (= T273)
- binding zinc ion: H95 (= H96), H198 (= H211), H238 (= H248)
Sites not aligning to the query:
4lv4A A noncompetitive inhibitor for m. Tuberculosis's class iia fructose 1, 6-bisphosphate aldolase (see paper)
51% identity, 99% coverage: 2:338/341 of query aligns to 1:316/320 of 4lv4A
Sites not aligning to the query:
P0AB71 Fructose-bisphosphate aldolase class 2; FBP aldolase; FBPA; Fructose-1,6-bisphosphate aldolase; Fructose-bisphosphate aldolase class II; Sedoheptulose bisphosphate aldolase; EC 4.1.2.13 from Escherichia coli (strain K12) (see 11 papers)
41% identity, 95% coverage: 10:332/341 of query aligns to 19:354/359 of P0AB71
- N36 (= N27) mutation to A: 1.5% of wild-type activity. 5-fold decrease in FBP affinity.
- Q60 (= Q51) mutation to A: 81% of wild-type activity. 1.3-fold decrease in FBP affinity.
- S62 (= S53) mutation to A: 8% of wild-type activity. 16-fold decrease in FBP affinity.; mutation to T: 60% of wild-type activity. 2.5-fold decrease in FBP affinity.
- K72 (≠ T63) modified: N6-succinyllysine
- H108 (= H93) mutation to A: Loss of activity.
- D110 (= D95) active site, Proton donor
- H111 (= H96) binding Zn(2+); mutation to A: Loss of activity.
- C112 (= C97) mutation to A: Partial loss of activity.
- K115 (= K101) modified: N6-succinyllysine
- D145 (= D131) binding Zn(2+)
- E175 (= E161) binding Zn(2+)
- H227 (= H211) binding Zn(2+)
- K231 (= K215) modified: N6-succinyllysine
- K251 (≠ T235) modified: N6-succinyllysine
- H265 (= H248) binding Zn(2+)
- K319 (vs. gap) modified: N6-succinyllysine
- K326 (= K304) modified: N6-succinyllysine; mutation to A: 6% of wild-type activity. 2.2-fold decrease in FBP affinity.
- K348 (≠ R326) modified: N6-succinyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 9 modified: N6-acetyllysine; alternate; modified: N6-malonyllysine; alternate; modified: N6-succinyllysine; alternate
1dosA Structure of fructose-bisphosphate aldolase (see paper)
40% identity, 95% coverage: 10:332/341 of query aligns to 18:353/358 of 1dosA
1b57A Class ii fructose-1,6-bisphosphate aldolase in complex with phosphoglycolohydroxamate (see paper)
39% identity, 95% coverage: 10:332/341 of query aligns to 18:341/346 of 1b57A
- active site: D109 (= D95), H110 (= H96), E182 (= E169), H214 (= H211), H252 (= H248), N274 (= N270)
- binding phosphoglycolohydroxamic acid: D109 (= D95), H110 (= H96), H214 (= H211), G215 (= G212), H252 (= H248), G253 (= G249), S255 (= S251), N274 (= N270), I275 (= I271), D276 (= D272), T277 (= T273)
- binding zinc ion: H91 (≠ E77), H110 (= H96), H129 (≠ R116), D144 (= D131), E174 (= E161), E181 (= E168), H214 (= H211), H252 (= H248)
3qm3A 1.85 angstrom resolution crystal structure of fructose-bisphosphate aldolase (fba) from campylobacter jejuni
40% identity, 96% coverage: 10:337/341 of query aligns to 19:350/350 of 3qm3A
5vjeA Class ii fructose-1,6-bisphosphate aldolase of escherichia coli with d-glucitol 1,6-bisphosphate (see paper)
38% identity, 96% coverage: 10:335/341 of query aligns to 18:337/339 of 5vjeA
- active site: D109 (= D95), H110 (= H96), H207 (= H211), H245 (= H248), N267 (= N270)
- binding D-Glucitol-1,6-bisphosphate: S61 (= S53), D109 (= D95), H110 (= H96), H207 (= H211), G208 (= G212), H245 (= H248), G246 (= G249), S248 (= S251), N267 (= N270), D269 (= D272), T270 (= T273)
5gk5C Apo structure of fructose 1,6-bisphosphate aldolase from escherichia coli at 1.9 angstrom resolution
36% identity, 96% coverage: 10:335/341 of query aligns to 18:333/335 of 5gk5C
- active site: D109 (= D95), H110 (= H96), H210 (= H211), H241 (= H248), N263 (= N270)
- binding zinc ion: H110 (= H96), H110 (= H96), E174 (= E161), H210 (= H211), H210 (= H211), H241 (= H248), H241 (= H248)
1gynA Class ii fructose 1,6-bisphosphate aldolase with cadmium (not zinc) in the active site (see paper)
36% identity, 96% coverage: 10:335/341 of query aligns to 18:331/333 of 1gynA
- active site: D109 (= D95), H110 (= H96), H239 (= H248), N261 (= N270)
- binding cadmium ion: H91 (≠ E77), H110 (= H96), H129 (≠ R116), D144 (= D131), E174 (= E161), E221 (≠ D231), H231 (≠ A240), H239 (= H248)
P36580 Fructose-bisphosphate aldolase; FBP aldolase; FBPA; Fructose-1,6-bisphosphate aldolase; EC 4.1.2.13 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
36% identity, 96% coverage: 11:336/341 of query aligns to 19:357/358 of P36580
- T289 (= T273) modified: Phosphothreonine
- T312 (≠ K296) modified: Phosphothreonine
- T340 (≠ A319) modified: Phosphothreonine
- T342 (≠ A321) modified: Phosphothreonine
7rgnA Crystal structure of putative fructose-1,6-bisphosphate aldolase from candida auris
36% identity, 96% coverage: 10:335/341 of query aligns to 17:338/340 of 7rgnA