SitesBLAST
Comparing RR42_RS16500 FitnessBrowser__Cup4G11:RR42_RS16500 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)
3mmtA Crystal structure of fructose bisphosphate aldolase from bartonella henselae, bound to fructose bisphosphate (see paper)
59% identity, 94% coverage: 14:331/340 of query aligns to 14:336/341 of 3mmtA
- active site: D25 (= D25), K138 (= K137), E180 (= E178), E182 (= E180), K225 (= K220), S294 (= S289)
- binding 1,6-fructose diphosphate (linear form): A23 (= A23), D25 (= D25), E26 (= E26), S27 (= S27), T30 (= T30), K99 (= K98), K138 (= K137), R140 (= R139), E180 (= E178), K225 (= K220), L265 (= L260), S266 (= S261), G267 (= G262), S294 (= S289), Y295 (= Y290), G296 (= G291), R297 (= R292)
Q9SJQ9 Fructose-bisphosphate aldolase 6, cytosolic; AtFBA6; Cytosolic aldolase 2; cAld2; EC 4.1.2.13 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
54% identity, 96% coverage: 6:332/340 of query aligns to 11:338/358 of Q9SJQ9
- C68 (= C63) modified: S-glutathionyl cysteine; transient
- C173 (= C168) modified: S-glutathionyl cysteine; transient; alternate; modified: S-nitrosocysteine; transient; alternate
6rngB Dipeptide gly-pro binds to a glycolytic enzyme fructose bisphosphate aldolase
54% identity, 96% coverage: 6:332/340 of query aligns to 6:333/334 of 6rngB
- active site: D25 (= D25), K137 (= K137), E178 (= E178), E180 (= E180), K220 (= K220), S290 (= S289)
- binding glycine: S261 (= S261), G262 (= G262), R293 (= R292)
- binding proline: R34 (= R34), L260 (= L260), S261 (= S261), G262 (= G262), G292 (= G291), R293 (= R292)
P07764 Fructose-bisphosphate aldolase; EC 4.1.2.13 from Drosophila melanogaster (Fruit fly) (see 2 papers)
53% identity, 96% coverage: 4:331/340 of query aligns to 13:342/361 of P07764
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylthreonine
5tklA Crystal structure of fbp aldolase from toxoplasma gondii, condensation intermediate (see paper)
53% identity, 96% coverage: 6:331/340 of query aligns to 15:343/350 of 5tklA
- active site: D34 (= D25), K146 (= K137), E189 (= E178), E191 (= E180), K231 (= K220), S301 (= S289)
- binding glyceraldehyde-3-phosphate: D34 (= D25), S36 (= S27), T39 (= T30), K107 (= K98), K146 (= K137), R148 (= R139), E189 (= E178), K231 (= K220)
- binding 1,6-di-O-phosphono-D-fructose: A32 (= A23), D34 (= D25), S36 (= S27), T39 (= T30), K107 (= K98), K146 (= K137), R148 (= R139), E189 (= E178), K231 (= K220), L272 (= L260), S273 (= S261), G274 (= G262), S301 (= S289), Y302 (= Y290), G303 (= G291), R304 (= R292)
Sites not aligning to the query:
4tr9A Ternary co-crystal structure of fructose-bisphosphate aldolase from plasmodium falciparum in complex with trap and a small molecule inhibitor (see paper)
49% identity, 97% coverage: 2:332/340 of query aligns to 12:345/347 of 4tr9A
- active site: D35 (= D25), K147 (= K137), E190 (= E178), E192 (= E180), K232 (= K220), S302 (= S289)
- binding N'-[(E)-(2,4-dichlorophenyl)methylidene]-3,4-dihydroxybenzohydrazide: D35 (= D25), S37 (= S27), T40 (= T30), K108 (= K98), K147 (= K137), R149 (= R139), E190 (= E178), K232 (= K220)
- binding : A33 (= A23), E36 (= E26), R44 (= R34), E192 (= E180), F253 (≠ M240), V256 (= V243), R257 (≠ Q244), R260 (≠ K247), L273 (= L260), S274 (= S261), G275 (= G262), G276 (= G263), A291 (≠ R278), L292 (= L279), G293 (≠ A280), P294 (= P281), G304 (= G291), R305 (= R292), Q308 (= Q295), A309 (≠ E296)
2ephD Crystal structure of fructose-bisphosphate aldolase from plasmodium falciparum in complex with trap-tail determined at 2.7 angstrom resolution (see paper)
49% identity, 97% coverage: 2:332/340 of query aligns to 14:347/351 of 2ephD
- active site: D37 (= D25), K149 (= K137), E192 (= E178), E194 (= E180), K234 (= K220), S304 (= S289)
- binding : D37 (= D25), E38 (= E26), T42 (= T30), R46 (= R34), K149 (= K137), R151 (= R139), R307 (= R292), Q310 (= Q295), A311 (≠ E296)
P04075 Fructose-bisphosphate aldolase A; Lung cancer antigen NY-LU-1; Muscle-type aldolase; EC 4.1.2.13 from Homo sapiens (Human) (see 11 papers)
51% identity, 97% coverage: 2:331/340 of query aligns to 11:343/364 of P04075
- K99 (≠ A89) modified: N6-(2-hydroxyisobutyryl)lysine
- K111 (= K101) modified: N6-malonyllysine; alternate
- D129 (= D119) to G: in GSD12; thermolabile; dbSNP:rs121909533
- K147 (= K137) modified: N6-(2-hydroxyisobutyryl)lysine
- E207 (= E197) to K: in GSD12; reduces thermal stability; 3-fold decrease in catalytic efficiency mostly due to reduced substrate affinity; dbSNP:rs121909534
- K312 (≠ L300) modified: N6-malonyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 347 G → S: in GSD12; likely benign variant; does not affect thermal stability; 4-fold decrease in catalytic efficiency due to reduced enzyme activity; dbSNP:rs138824667
4aldA Human muscle fructose 1,6-bisphosphate aldolase complexed with fructose 1,6-bisphosphate (see paper)
51% identity, 97% coverage: 2:331/340 of query aligns to 10:342/363 of 4aldA
- active site: D33 (= D25), K146 (= K137), E187 (= E178), E189 (= E180), K229 (= K220), S300 (= S289)
- binding 1,6-fructose diphosphate (linear form): D33 (= D25), E34 (= E26), S35 (= S27), S38 (≠ T30), K107 (= K98), K146 (= K137), R148 (= R139), E187 (= E178), K229 (= K220), L270 (= L260), S271 (= S261), G272 (= G262), S300 (= S289), Y301 (= Y290), G302 (= G291), R303 (= R292)
Sites not aligning to the query:
2ot0A Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with a c-terminal peptide of wiskott-aldrich syndrome protein (see paper)
50% identity, 99% coverage: 2:337/340 of query aligns to 10:348/356 of 2ot0A
- active site: D33 (= D25), K146 (= K137), E187 (= E178), E189 (= E180), K229 (= K220), S300 (= S289)
- binding : E34 (= E26), S38 (≠ T30), K41 (= K33), R42 (= R34), K146 (= K137), R148 (= R139), E187 (= E178), G272 (= G262), G273 (= G263), R303 (= R292), Q306 (= Q295), A307 (≠ E296), L310 (= L299)
Sites not aligning to the query:
5tlzA Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with the inhibitor naphthalene 2,6-bisphosphate (see paper)
51% identity, 97% coverage: 2:331/340 of query aligns to 7:339/346 of 5tlzA
- active site: D30 (= D25), K143 (= K137), E184 (= E178), E186 (= E180), K226 (= K220), S297 (= S289)
- binding naphthalene-2,6-diyl bis[dihydrogen (phosphate)]: A28 (= A23), D30 (= D25), E31 (= E26), S32 (= S27), S35 (≠ T30), K104 (= K98), K143 (= K137), R145 (= R139), S268 (= S261), G269 (= G262), G299 (= G291), R300 (= R292)
Sites not aligning to the query:
1zalA Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with partially disordered tagatose-1,6-bisphosphate, a weak competitive inhibitor (see paper)
51% identity, 97% coverage: 2:331/340 of query aligns to 10:342/363 of 1zalA
- active site: D33 (= D25), K146 (= K137), E187 (= E178), E189 (= E180), K229 (= K220), S300 (= S289)
- binding phosphate ion: D33 (= D25), E34 (= E26), S35 (= S27), S38 (≠ T30), K107 (= K98), K229 (= K220), L270 (= L260), S271 (= S261), G272 (= G262), S300 (= S289), Y301 (= Y290), G302 (= G291), R303 (= R292)
Sites not aligning to the query:
1zajA Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with mannitol-1,6-bisphosphate, a competitive inhibitor (see paper)
51% identity, 97% coverage: 2:331/340 of query aligns to 10:342/363 of 1zajA
- active site: D33 (= D25), K146 (= K137), E187 (= E178), E189 (= E180), K229 (= K220), S300 (= S289)
- binding d-mannitol-1,6-diphosphate: A31 (= A23), D33 (= D25), E34 (= E26), S35 (= S27), S38 (≠ T30), K107 (= K98), K146 (= K137), R148 (= R139), E187 (= E178), K229 (= K220), L270 (= L260), S271 (= S261), G272 (= G262), S300 (= S289), Y301 (= Y290