SitesBLAST
Comparing WP_007726777.1 NCBI__GCF_002893965.1:WP_007726777.1 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)
82% identity, 99% coverage: 2:343/345 of query aligns to 1:342/345 of 4delA
- active site: D94 (= D95), H95 (= H96), E168 (= E169), H211 (= H212), H251 (= H252), N273 (= N274)
- binding phosphoglycolohydroxamic acid: D94 (= D95), H95 (= H96), H211 (= H212), G212 (= G213), H251 (= H252), G252 (= G253), S254 (= S255), N273 (= N274), D275 (= D276), T276 (= T277)
- binding zinc ion: H95 (= H96), H211 (= H212), H251 (= H252)
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)
80% identity, 99% coverage: 2:343/345 of query aligns to 1:331/334 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)
79% identity, 99% coverage: 2:343/345 of query aligns to 1:329/329 of 4a22A
- active site: D94 (= D95), H95 (= H96), H198 (= H212), H238 (= H252), N260 (= N274)
- binding 4-{hydroxy[(phosphonooxy)acetyl]amino}butyl dihydrogen phosphate: N26 (= N27), S52 (= S53), D94 (= D95), H95 (= H96), H198 (= H212), G199 (= G213), H238 (= H252), G239 (= G253), S241 (= S255), N260 (= N274), V261 (= V275), D262 (= D276), T263 (= T277)
- binding zinc ion: H95 (= H96), H198 (= H212), H238 (= H252)
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)
79% identity, 99% coverage: 2:343/345 of query aligns to 1:329/332 of 3elfA
- active site: D94 (= D95), H95 (= H96), H198 (= H212), H238 (= H252), N260 (= N274)
- binding 1,6-fructose diphosphate (linear form): N26 (= N27), S52 (= S53), D94 (= D95), H95 (= H96), H198 (= H212), G199 (= G213), H238 (= H252), G239 (= G253), S241 (= S255), N260 (= N274), V261 (= V275), D262 (= D276), T263 (= T277)
- binding zinc ion: H95 (= H96), H198 (= H212), H238 (= H252)
Sites not aligning to the query:
4lv4A A noncompetitive inhibitor for m. Tuberculosis's class iia fructose 1, 6-bisphosphate aldolase (see paper)
75% identity, 99% coverage: 2:343/345 of query aligns to 1:317/320 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)
42% identity, 93% coverage: 16:337/345 of query aligns to 25:355/359 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 (≠ L63) 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 (= H212) binding Zn(2+)
- K231 (= K216) modified: N6-succinyllysine
- K251 (≠ A236) modified: N6-succinyllysine
- H265 (= H252) binding Zn(2+)
- K319 (vs. gap) modified: N6-succinyllysine
- K326 (= K308) modified: N6-succinyllysine; mutation to A: 6% of wild-type activity. 2.2-fold decrease in FBP affinity.
- K348 (≠ E330) 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)
41% identity, 93% coverage: 16:337/345 of query aligns to 24:354/358 of 1dosA
1b57A Class ii fructose-1,6-bisphosphate aldolase in complex with phosphoglycolohydroxamate (see paper)
41% identity, 93% coverage: 16:337/345 of query aligns to 24:342/346 of 1b57A
- active site: D109 (= D95), H110 (= H96), E182 (= E169), H214 (= H212), H252 (= H252), N274 (= N274)
- binding phosphoglycolohydroxamic acid: D109 (= D95), H110 (= H96), H214 (= H212), G215 (= G213), H252 (= H252), G253 (= G253), S255 (= S255), N274 (= N274), I275 (≠ V275), D276 (= D276), T277 (= T277)
- binding zinc ion: H91 (≠ E77), H110 (= H96), H129 (≠ R116), D144 (= D131), E174 (= E161), E181 (= E168), H214 (= H212), H252 (= H252)
3qm3A 1.85 angstrom resolution crystal structure of fructose-bisphosphate aldolase (fba) from campylobacter jejuni
40% identity, 94% coverage: 16:341/345 of query aligns to 25:350/350 of 3qm3A
5vjeA Class ii fructose-1,6-bisphosphate aldolase of escherichia coli with d-glucitol 1,6-bisphosphate (see paper)
39% identity, 93% coverage: 16:337/345 of query aligns to 24:335/339 of 5vjeA
- active site: D109 (= D95), H110 (= H96), H207 (= H212), H245 (= H252), N267 (= N274)
- binding D-Glucitol-1,6-bisphosphate: S61 (= S53), D109 (= D95), H110 (= H96), H207 (= H212), G208 (= G213), H245 (= H252), G246 (= G253), S248 (= S255), N267 (= N274), D269 (= D276), T270 (= T277)
5gk5C Apo structure of fructose 1,6-bisphosphate aldolase from escherichia coli at 1.9 angstrom resolution
38% identity, 93% coverage: 16:337/345 of query aligns to 24:331/335 of 5gk5C
- active site: D109 (= D95), H110 (= H96), H210 (= H212), H241 (= H252), N263 (= N274)
- binding zinc ion: H110 (= H96), H110 (= H96), E174 (= E161), H210 (= H212), H210 (= H212), H241 (= H252), H241 (= H252)
1gynA Class ii fructose 1,6-bisphosphate aldolase with cadmium (not zinc) in the active site (see paper)
37% identity, 93% coverage: 16:337/345 of query aligns to 24:329/333 of 1gynA
- active site: D109 (= D95), H110 (= H96), H239 (= H252), N261 (= N274)
- binding cadmium ion: H91 (≠ E77), H110 (= H96), H129 (≠ R116), D144 (= D131), E174 (= E161), E221 (≠ K232), H231 (≠ S242), H239 (= H252)
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)
38% identity, 94% coverage: 11:335/345 of query aligns to 19:352/358 of P36580
- T289 (= T277) modified: Phosphothreonine
- T312 (≠ K300) modified: Phosphothreonine
- T340 (≠ G323) modified: Phosphothreonine
- T342 (= T325) modified: Phosphothreonine
7rgnA Crystal structure of putative fructose-1,6-bisphosphate aldolase from candida auris
36% identity, 93% coverage: 11:331/345 of query aligns to 18:330/340 of 7rgnA