SitesBLAST
Comparing WP_011426723.1 NCBI__GCF_000092045.1:WP_011426723.1 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)
3mmtA Crystal structure of fructose bisphosphate aldolase from bartonella henselae, bound to fructose bisphosphate (see paper)
69% identity, 99% coverage: 1:337/340 of query aligns to 3:341/341 of 3mmtA
- active site: D25 (= D23), K138 (= K136), E180 (= E177), E182 (= E179), K225 (= K222), S294 (= S290)
- 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 (= G292), R297 (= R293)
P07764 Fructose-bisphosphate aldolase; EC 4.1.2.13 from Drosophila melanogaster (Fruit fly) (see 2 papers)
53% identity, 98% coverage: 1:332/340 of query aligns to 12:342/361 of P07764
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylthreonine
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, 94% coverage: 16:335/340 of query aligns to 23:340/358 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
54% identity, 94% coverage: 16:333/340 of query aligns to 18:333/334 of 6rngB
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: 3:332/340 of query aligns to 14:343/364 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 (= K301) 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
4aldA Human muscle fructose 1,6-bisphosphate aldolase complexed with fructose 1,6-bisphosphate (see paper)
53% identity, 97% coverage: 3:332/340 of query aligns to 13:342/363 of 4aldA
- active site: D33 (= D23), K146 (= K136), E187 (= E177), E189 (= E179), K229 (= K222), S300 (= S290)
- 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 (= R293)
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)
53% identity, 97% coverage: 3:332/340 of query aligns to 13:342/356 of 2ot0A
- active site: D33 (= D23), K146 (= K136), E187 (= E177), E189 (= E179), K229 (= K222), S300 (= S290)
- binding : E34 (= E24), S38 (≠ T28), R42 (= R32), K146 (= K136), R148 (= R138), R303 (= R293), Q306 (= Q296)
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: 3:332/340 of query aligns to 14:343/364 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 (= R293) 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
5tlzA Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with the inhibitor naphthalene 2,6-bisphosphate (see paper)
53% identity, 97% coverage: 3:332/340 of query aligns to 10:339/346 of 5tlzA
- active site: D30 (= D23), K143 (= K136), E184 (= E177), E186 (= E179), K226 (= K222), S297 (= S290)
- binding naphthalene-2,6-diyl bis[dihydrogen (phosphate)]: D30 (= D23), S32 (= S25), S35 (≠ T28), K104 (= K97), S268 (= S263), G269 (= G264), G299 (= G292), R300 (= R293)
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: 3:332/340 of query aligns to 13:342/363 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: 3:332/340 of query aligns to 13:342/363 of 1zajA
- active site: D33 (= D23), K146 (= K136), E187 (= E177), E189 (= E179), K229 (= K222), S300 (= S290)
- 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 (= Y291), G302 (= G292), R303 (= R293)
Sites not aligning to the query:
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: 3:332/340 of query aligns to 13:342/349 of 5tlwA
- active site: D33 (= D23), K146 (= K136), E187 (= E177), E189 (= E179), K229 (= K222), S300 (= S290)
- binding {[4-(phosphonooxy)phenyl]methylene}bis(phosphonic acid): S35 (= S25), S38 (≠ T28), K107 (= K97), K146 (= K136), R148 (= R138), R303 (= R293)
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: 3:332/340 of query aligns to 13:342/349 of 5tleA
- active site: D33 (= D23), K146 (= K136), E187 (= E177), E189 (= E179), K229 (= K222), S300 (= S290)
- 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 (= G292), R303 (= R293)
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: 3:332/340 of query aligns to 13:342/349 of 3tu9A
- active site: D33 (= D23), K146 (= K136), E187 (= E177), E189 (= E179), K229 (= K222), S300 (= S290)
- 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 (= Y291), G302 (= G292), R303 (= R293)
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: 3:332/340 of query aligns to 13:342/349 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: 3:332/340 of query aligns to 13:342/350 of 5tlhA
- active site: D33 (= D23), K146 (= K136), E187 (= E177), E189 (= E179), K229 (= K222), S300 (= S290)
- 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 (≠ T35), R303 (= R293)
Sites not aligning to the query:
5tklA Crystal structure of fbp aldolase from toxoplasma gondii, condensation intermediate (see paper)
53% identity, 98% coverage: 1:332/340 of query aligns to 12:343/350 of 5tklA
- active site: D34 (= D23), K146 (= K136), E189 (= E177), E191 (= E179), K231 (= K222), S301 (= S290)
- 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 (= G292), R304 (= R293)
Sites not aligning to the query:
2ephD Crystal structure of fructose-bisphosphate aldolase from plasmodium falciparum in complex with trap-tail determined at 2.7 angstrom resolution (see paper)
51% identity, 98% coverage: 1:333/340 of query aligns to 15:347/351 of 2ephD
- active site: D37 (= D23), K149 (= K136), E192 (= E177), E194 (= E179), K234 (= K222), S304 (= S290)
- binding : E38 (= E24), R46 (= R32), K149 (= K136), R151 (= R138), R307 (= R293), Q310 (= Q296), A311 (≠ D297)
4tr9A Ternary co-crystal structure of fructose-bisphosphate aldolase from plasmodium falciparum in complex with trap and a small molecule inhibitor (see paper)
51% identity, 98% coverage: 1:333/340 of query aligns to 13:345/347 of 4tr9A
- active site: D35 (= D23), K147 (= K136), E190 (= E177), E192 (= E179), K232 (= K222), S302 (= S290)
- binding N'-[(E)-(2,4-dichlorophenyl)methylidene]-3,4-dihydroxybenzohydrazide: D35 (= D23), K147 (= K136), R149 (= R138)
- binding : E36 (= E24), R44 (= R32), E192 (= E179), F253 (≠ E242), V256 (= V245), R257 (≠ Q246), R260 (≠ K249), S274 (= S263), G275 (= G264), L292 (≠ F281), G293 (vs. gap), P294 (≠ D282), G304 (= G292), R305 (= R293)
P14223 Fructose-bisphosphate aldolase; PfAldo; 41 kDa antigen; EC 4.1.2.13 from Plasmodium falciparum (see paper)
51% identity, 96% coverage: 1:327/340 of query aligns to 18:344/369 of P14223
- D40 (= D23) mutation to G: Reduces binding to TRAP.
- E41 (= E24) mutation to G: Abolishes binding to TRAP.
- R49 (= R32) mutation R->D,G: Abolishes binding to TRAP.
- K152 (= K136) mutation to D: Severe reduction in the binding to TRAP.
- R154 (= R138) mutation to G: Abolishes binding to TRAP.
- R310 (= R293) mutation to S: Severe reduction in the binding to TRAP.
- Q313 (= Q296) mutation to S: Severe reduction in the binding to TRAP.
- A314 (≠ D297) mutation to G: Reduces binding to TRAP.
- L317 (= L300) mutation to D: Abolishes binding to TRAP.
Query Sequence
>WP_011426723.1 NCBI__GCF_000092045.1:WP_011426723.1
MSERLEDIAVQMVAGGRGLLAADESTSTIKKRFDTINLESTETSRRDYREMLFRSDEAMK
KYISGVILFEETLYQKAADGTPFVDIIRAAGSIPGIKVDTGAKPMAKFPGETITEGLDGL
GERLAKYYEAGARFAKWRGVIAISSSLPTRGSVRANAQALARYAALCQEAKIVPIVEPEC
LMDGKPGDHNIDRCAEVTESTLQIVFEELAEARVSLEGMILKPNMVIDGKNARKASVAEV
AERTVQVLKRTVPSAVPGIAFLSGGQTTEEATAHLSAINGFDLPWLVTFSYGRALQDSAL
KAWNGKPENVAAGQREFTHRAEMNSLAAKGSWKKDLEQAA
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