SitesBLAST
Comparing SMc03983 FitnessBrowser__Smeli:SMc03983 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)
70% identity, 99% coverage: 1:338/341 of query aligns to 3:341/341 of 3mmtA
- active site: D25 (= D23), K138 (= K136), E180 (= E177), E182 (= E179), K225 (= K222), S294 (= S291)
- binding 1,6-fructose diphosphate (linear form): A23 (= A21), D25 (= D23), S27 (= S25), T30 (= T28), K99 (= K97), K138 (= K136), E180 (= E177), K225 (= K222), S266 (= S263), G267 (= G264), G296 (= G293), R297 (= R294)
P07764 Fructose-bisphosphate aldolase; EC 4.1.2.13 from Drosophila melanogaster (Fruit fly) (see 2 papers)
52% identity, 98% coverage: 1:333/341 of query aligns to 12:342/361 of P07764
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylthreonine
4aldA Human muscle fructose 1,6-bisphosphate aldolase complexed with fructose 1,6-bisphosphate (see paper)
53% identity, 97% coverage: 3:334/341 of query aligns to 13:343/363 of 4aldA
- active site: D33 (= D23), K146 (= K136), E187 (= E177), E189 (= E179), K229 (= K222), S300 (= S291)
- binding 1,6-fructose diphosphate (linear form): E34 (= E24), S35 (= S25), S38 (≠ T28), K107 (= K97), K146 (= K136), R148 (= R138), E187 (= E177), L270 (= L262), S271 (= S263), G272 (= G264), R303 (= R294)
Sites not aligning to the query:
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)
53% identity, 97% coverage: 3:334/341 of query aligns to 14:344/364 of P04075
- K99 (≠ R88) modified: N6-(2-hydroxyisobutyryl)lysine
- K111 (≠ T100) modified: N6-malonyllysine; alternate
- D129 (= D118) to G: in GSD12; thermolabile; dbSNP:rs121909533
- K147 (= K136) modified: N6-(2-hydroxyisobutyryl)lysine
- E207 (= E199) to K: in GSD12; reduces thermal stability; 3-fold decrease in catalytic efficiency mostly due to reduced substrate affinity; dbSNP:rs121909534
- K312 (≠ N302) modified: N6-malonyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 347 G → S: in GSD12; likely benign; does not affect thermal stability; 4-fold decrease in catalytic efficiency due to reduced enzyme activity; dbSNP:rs138824667
2ot0A Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with a c-terminal peptide of wiskott-aldrich syndrome protein (see paper)
52% identity, 99% coverage: 3:338/341 of query aligns to 13:347/356 of 2ot0A
- active site: D33 (= D23), K146 (= K136), E187 (= E177), E189 (= E179), K229 (= K222), S300 (= S291)
- binding : E34 (= E24), S38 (≠ T28), R42 (= R32), K146 (= K136), R148 (= R138), R303 (= R294), Q306 (= Q297)
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)
53% identity, 97% coverage: 3:334/341 of query aligns to 13:343/363 of 1zalA
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)
53% identity, 97% coverage: 3:334/341 of query aligns to 13:343/363 of 1zajA
- active site: D33 (= D23), K146 (= K136), E187 (= E177), E189 (= E179), K229 (= K222), S300 (= S291)
- binding d-mannitol-1,6-diphosphate: D33 (= D23), S35 (= S25), S38 (≠ T28), K107 (= K97), K146 (= K136), E187 (= E177), K229 (= K222), S271 (= S263), G272 (= G264), Y301 (= Y292), G302 (= G293), R303 (= R294)
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)
53% identity, 97% coverage: 3:334/341 of query aligns to 10:340/346 of 5tlzA
- active site: D30 (= D23), K143 (= K136), E184 (= E177), E186 (= E179), K226 (= K222), S297 (= S291)
- binding naphthalene-2,6-diyl bis[dihydrogen (phosphate)]: D30 (= D23), S32 (= S25), S35 (≠ T28), K104 (= K97), S268 (= S263), G269 (= G264), G299 (= G293), R300 (= R294)
Sites not aligning to the query:
P00883 Fructose-bisphosphate aldolase A; Muscle-type aldolase; EC 4.1.2.13 from Oryctolagus cuniculus (Rabbit) (see 5 papers)
53% identity, 97% coverage: 3:334/341 of query aligns to 14:344/364 of P00883
- E35 (= E24) mutation to A: Reduces activity 14-fold.
- R43 (= R32) binding ; mutation to A: Reduces activity 14-fold.
- K147 (= K136) mutation to A: Loss of activity.
- E188 (= E177) active site, Proton acceptor; mutation to A: Reduces activity over 100-fold.; mutation to Q: Reduces activity over 1000-fold.
- E190 (= E179) mutation to Q: Reduces activity 20-fold.
- K230 (= K222) active site, Schiff-base intermediate with dihydroxyacetone-P; mutation to M: Loss of activity.
- SGG 272:274 (= SGG 263:265) binding
- R304 (= R294) binding ; mutation to A: Reduces activity 400-fold.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 361 modified: Deamidated asparagine; in form beta
5tlwA Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with the inhibitor 1-phosphate-benzene 4-bisphosphonate (see paper)
53% identity, 97% coverage: 3:334/341 of query aligns to 13:343/349 of 5tlwA
- active site: D33 (= D23), K146 (= K136), E187 (= E177), E189 (= E179), K229 (= K222), S300 (= S291)
- binding {[4-(phosphonooxy)phenyl]methylene}bis(phosphonic acid): S35 (= S25), S38 (≠ T28), K107 (= K97), K146 (= K136), R148 (= R138), R303 (= R294)
Sites not aligning to the query:
5tleA Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with the inhibitor 2-phosphate-naphthalene 6-bisphosphonate (see paper)
53% identity, 97% coverage: 3:334/341 of query aligns to 13:343/349 of 5tleA
- active site: D33 (= D23), K146 (= K136), E187 (= E177), E189 (= E179), K229 (= K222), S300 (= S291)
- binding {[6-(phosphonooxy)naphthalen-2-yl]methylene}bis(phosphonic acid): D33 (= D23), S35 (= S25), S38 (≠ T28), K107 (= K97), K229 (= K222), L270 (= L262), G272 (= G264), G302 (= G293), R303 (= R294)
Sites not aligning to the query:
3tu9A Crystal structure of rabbit muscle aldolase bound with 5-o-methyl mannitol 1,6-phosphate (see paper)
53% identity, 97% coverage: 3:334/341 of query aligns to 13:343/349 of 3tu9A
- active site: D33 (= D23), K146 (= K136), E187 (= E177), E189 (= E179), K229 (= K222), S300 (= S291)
- binding 2-O-methyl-1,6-di-O-phosphono-D-mannitol: A31 (= A21), D33 (= D23), E34 (= E24), S35 (= S25), S38 (≠ T28), K107 (= K97), K146 (= K136), E187 (= E177), K229 (= K222), S271 (= S263), G272 (= G264), Y301 (= Y292), G302 (= G293), R303 (= R294)
Sites not aligning to the query:
2ot1A Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with naphthol as-e phosphate, a competitive inhibitor (see paper)
53% identity, 97% coverage: 3:334/341 of query aligns to 13:343/349 of 2ot1A
Sites not aligning to the query:
5tlhA Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with the inhibitor 2-naphthol 6-bisphosphonate (see paper)
53% identity, 97% coverage: 3:334/341 of query aligns to 13:343/350 of 5tlhA
- active site: D33 (= D23), K146 (= K136), E187 (= E177), E189 (= E179), K229 (= K222), S300 (= S291)
- binding methylenediphosphonic acid: S38 (≠ T28), K107 (= K97), K146 (= K136), R148 (= R138)
- binding [(6-hydroxynaphthalen-2-yl)methylene]bis(phosphonic acid): E34 (= E24), R42 (= R32), S45 (= S35), R303 (= R294)
Sites not aligning to the query:
Q9SJQ9 Fructose-bisphosphate aldolase 6, cytosolic; AtFBA6; Cytosolic aldolase 2; cAld2; EC 4.1.2.13 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
51% identity, 99% coverage: 1:336/341 of query aligns to 1:340/358 of Q9SJQ9
- C68 (≠ Y62) modified: S-glutathionyl cysteine; transient
- C173 (= C167) modified: S-glutathionyl cysteine; transient; alternate; modified: S-nitrosocysteine; transient; alternate
6rngB Dipeptide gly-pro binds to a glycolytic enzyme fructose bisphosphate aldolase
53% identity, 93% coverage: 16:333/341 of query aligns to 18:332/334 of 6rngB
1fdjA Fructose 1,6-bisphosphate aldolase from rabbit liver
49% identity, 97% coverage: 3:333/341 of query aligns to 13:342/363 of 1fdjA
P05062 Fructose-bisphosphate aldolase B; Liver-type aldolase; EC 4.1.2.13 from Homo sapiens (Human) (see 14 papers)
49% identity, 97% coverage: 3:333/341 of query aligns to 14:343/364 of P05062
- R43 (= R32) mutation to A: Loss of enzymatic activity. Retains the ability to interact with G6PD.
- R46 (≠ S35) to W: in HFI; reduced enzymatic activity; dbSNP:rs41281039; mutation to A: Decreases enzymatic activity. Retains the ability to interact with G6PD.
- I74 (= I63) to T: in HFI; affects proper folding; dbSNP:rs781023784
- K108 (= K97) mutation to A: Decreases enzymatic activity. Retains the ability to interact with G6PD.
- C135 (≠ L124) to R: in HFI; America; partial activity
- K147 (= K136) mutation to A: Loss of enzymatic activity. Impairs the interaction with G6PD.
- W148 (= W137) to R: in one subject with fructose intolerance; rare variant; America; dbSNP:rs118204430
- R149 (= R138) mutation to A: Loss of enzymatic activity. Impairs the interaction with G6PD.
- A150 (≠ G139) to P: in HFI; frequent mutation; dbSNP:rs1800546
- A175 (= A164) to D: in HFI; frequent mutation; dbSNP:rs76917243
- V222 (= V214) to F: in HFI; affects proper folding; dbSNP:rs1554702442
- L229 (= L221) to P: in HFI; affects proper folding; dbSNP:rs1554702433
- K230 (= K222) mutation to A: Loss of enzymatic activity. Impairs the interaction with G6PD.
- L257 (= L248) to P: in HFI; Italy; dbSNP:rs764701775
- R304 (= R294) to Q: in HFI; 100-fold decrease in catalytic efficiency for substrates F1,6BP and F1P; dbSNP:rs145078268; to W: in HFI; Turkey; 4800-fold decrease in catalytic efficiency for F1,6BP and inactive with F1P; dbSNP:rs555935217; mutation to A: Decreases enzymatic activity. Impairs the interaction with G6PD.
- N335 (≠ C325) to K: in HFI; frequent mutation; dbSNP:rs78340951
- A338 (= A328) to V: in HFI; Turkey and South Europe; dbSNP:rs77718928
- Y343 (≠ W333) to H: in HFI; almost no effect on enzymatic activity at 30 degrees Celsius, but reduced activity at higher temperatures; dbSNP:rs369586696
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
Q91Y97 Fructose-bisphosphate aldolase B; Aldolase 2; Liver-type aldolase; EC 4.1.2.13 from Mus musculus (Mouse)
49% identity, 97% coverage: 3:333/341 of query aligns to 14:343/364 of Q91Y97
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
5tklA Crystal structure of fbp aldolase from toxoplasma gondii, condensation intermediate (see paper)
50% identity, 98% coverage: 1:333/341 of query aligns to 12:343/350 of 5tklA
- active site: D34 (= D23), K146 (= K136), E189 (= E177), E191 (= E179), K231 (= K222), S301 (= S291)
- binding glyceraldehyde-3-phosphate: S36 (= S25), T39 (= T28), K107 (= K97), K146 (= K136), R148 (= R138), E189 (= E177), K231 (= K222)
- binding 1,6-di-O-phosphono-D-fructose: A32 (= A21), D34 (= D23), S36 (= S25), T39 (= T28), K107 (= K97), K146 (= K136), R148 (= R138), E189 (= E177), K231 (= K222), S273 (= S263), G274 (= G264), G303 (= G293), R304 (= R294)
Sites not aligning to the query:
Query Sequence
>SMc03983 FitnessBrowser__Smeli:SMc03983
MSERLEDIAVAMVANGRGLLAADESTATIKKRFDSIGLESTETSRRDYREMLLRSDDAMR
EYISGVILYEETLFQKAADGTPLADVIRNAGSIPGIKVDTGAKPMAHFPNETITEGLDGL
AARLARYHEAGARFAKWRGVIAISDALPTWGAIRANAHALARYAALCQEAKIVPIVEPEV
LMDGAPGDHSIERSEEVTEWVLRTVFEELGELRVRLEGMILKPSMVIDGKKARKASVDEV
AERTIKVLKRTVPAAVPGIAFLSGGQSTEEATAHLSAMNAAHDLPWKLTFSYGRALQQEA
LNAWGGKSENVAAGQRAFAHRAKMCSLAAKGSWTKDFEKAA
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