SitesBLAST
Comparing WP_020176885.1 NCBI__GCF_000385335.1:WP_020176885.1 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)
3mmtA Crystal structure of fructose bisphosphate aldolase from bartonella henselae, bound to fructose bisphosphate (see paper)
54% identity, 99% coverage: 4:338/340 of query aligns to 5:341/341 of 3mmtA
- active site: D25 (= D24), K138 (= K136), E180 (= E177), E182 (= E179), K225 (= K219), S294 (= S291)
- binding 1,6-fructose diphosphate (linear form): A23 (= A22), D25 (= D24), S27 (= S26), T30 (= T29), K99 (= K97), K138 (= K136), E180 (= E177), K225 (= K219), S266 (= S261), G267 (= G262), G296 (≠ S293), R297 (= R294)
Q9SJQ9 Fructose-bisphosphate aldolase 6, cytosolic; AtFBA6; Cytosolic aldolase 2; cAld2; EC 4.1.2.13 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
53% identity, 93% coverage: 18:333/340 of query aligns to 24:337/358 of Q9SJQ9
- C68 (≠ S62) 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: 18:333/340 of query aligns to 19:332/334 of 6rngB
Q8I8I2 Fructose-bisphosphate aldolase 1; TgALD; TgALD1; TgAldolase; EC 4.1.2.13 from Toxoplasma gondii (see 2 papers)
51% identity, 97% coverage: 4:333/340 of query aligns to 14:343/363 of Q8I8I2
- D34 (= D24) binding dihydroxyacetone phosphate; mutation to A: Abolishes enzymatic activity. Reduces ACT1 binding. Slightly reduces MIC2 binding.
- E35 (= E25) mutation to A: Reduces enzymatic activity. Enhances MIC2 binding.
- S36 (= S26) binding D-glyceraldehyde 3-phosphate
- T39 (= T29) binding D-glyceraldehyde 3-phosphate
- K42 (= K32) mutation to A: Does not affect enzymatic activity. Reduces ACT1 binding. Reduces MIC2 binding. Abolishes enzymatic activity and reduces MIC2 binding; when associated with A-43.; mutation to E: Does not affect enzymatic activity. Reduces MIC2 binding. Reduces enzymatic activity, ACT1 binding and MIC2 binding; when associated with G-43.
- R43 (= R33) mutation to A: Does not affect enzymatic activity. Reduces ACT1 binding. Reduces MIC2 binding. Abolishes enzymatic activity and reduces MIC2 binding; when associated with A-42.; mutation to D: Abolishes enzymatic activity. Reduces MIC2 binding.
- K107 (= K97) binding D-glyceraldehyde 3-phosphate; mutation to A: Abolishes enzymatic activity. Reduces MIC2 binding.
- K146 (= K136) binding dihydroxyacetone phosphate; mutation to A: Abolishes enzymatic activity. Reduces MIC2 binding.
- R148 (= R138) mutation to A: Abolishes enzymatic activity. Reduces ACT1 binding. Reduces MIC2 binding.
- E189 (= E177) binding D-glyceraldehyde 3-phosphate
- K231 (= K219) active site, Schiff-base intermediate with dihydroxyacetone phosphate; binding dihydroxyacetone phosphate; mutation to A: Abolishes enzymatic activity. Reduces MIC2 binding.
- S273 (= S261) binding dihydroxyacetone phosphate
- G274 (= G262) binding dihydroxyacetone phosphate
- G303 (≠ S293) binding dihydroxyacetone phosphate
- R304 (= R294) binding dihydroxyacetone phosphate; mutation to A: Abolishes enzymatic activity. Reduces MIC2 binding.
- Q307 (= Q297) mutation to F: Abolishes enzymatic activity. Reduces MIC2 binding.; mutation to G: Does not affect enzymatic activity. Does not affect MIC2 binding.
5tklA Crystal structure of fbp aldolase from toxoplasma gondii, condensation intermediate (see paper)
50% identity, 98% coverage: 4:336/340 of query aligns to 14:346/350 of 5tklA
- active site: D34 (= D24), K146 (= K136), E189 (= E177), E191 (= E179), K231 (= K219), S301 (= S291)
- binding glyceraldehyde-3-phosphate: S36 (= S26), T39 (= T29), K107 (= K97), K146 (= K136), R148 (= R138), E189 (= E177), K231 (= K219)
- binding 1,6-di-O-phosphono-D-fructose: A32 (= A22), D34 (= D24), S36 (= S26), T39 (= T29), K107 (= K97), K146 (= K136), R148 (= R138), E189 (= E177), K231 (= K219), S273 (= S261), G274 (= G262), G303 (≠ S293), R304 (= R294)
Sites not aligning to the query:
Q9ZU52 Fructose-bisphosphate aldolase 3, chloroplastic; AtFBA3; Protein PIGMENT DEFECTIVE 345; EC 4.1.2.13 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
48% identity, 99% coverage: 5:339/340 of query aligns to 47:377/391 of Q9ZU52
Sites not aligning to the query:
- 387 modified: N6,N6,N6-trimethyllysine
4tr9A Ternary co-crystal structure of fructose-bisphosphate aldolase from plasmodium falciparum in complex with trap and a small molecule inhibitor (see paper)
48% identity, 97% coverage: 4:333/340 of query aligns to 15:344/347 of 4tr9A
- active site: D35 (= D24), K147 (= K136), E190 (= E177), E192 (= E179), K232 (= K219), S302 (= S291)
- binding N'-[(E)-(2,4-dichlorophenyl)methylidene]-3,4-dihydroxybenzohydrazide: D35 (= D24), K147 (= K136), R149 (= R138)
- binding : E36 (= E25), R44 (= R33), E192 (= E179), F253 (≠ D240), V256 (= V243), R257 (≠ E244), R260 (≠ L247), S274 (= S261), G275 (= G262), L292 (≠ R279), G293 (≠ F280), P294 (≠ K281), G304 (≠ S293), R305 (= R294)
2ephD Crystal structure of fructose-bisphosphate aldolase from plasmodium falciparum in complex with trap-tail determined at 2.7 angstrom resolution (see paper)
48% identity, 97% coverage: 4:333/340 of query aligns to 17:346/351 of 2ephD
- active site: D37 (= D24), K149 (= K136), E192 (= E177), E194 (= E179), K234 (= K219), S304 (= S291)
- binding : E38 (= E25), R46 (= R33), K149 (= K136), R151 (= R138), R307 (= R294), Q310 (= Q297), A311 (≠ Q298)
P14223 Fructose-bisphosphate aldolase; PfAldo; 41 kDa antigen; EC 4.1.2.13 from Plasmodium falciparum (see paper)
48% identity, 96% coverage: 4:328/340 of query aligns to 20:344/369 of P14223
- D40 (= D24) mutation to G: Reduces binding to TRAP.
- E41 (= E25) mutation to G: Abolishes binding to TRAP.
- R49 (= R33) 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 (= R294) mutation to S: Severe reduction in the binding to TRAP.
- Q313 (= Q297) mutation to S: Severe reduction in the binding to TRAP.
- A314 (≠ Q298) mutation to G: Reduces binding to TRAP.
- L317 (= L301) mutation to D: Abolishes binding to TRAP.
2ot0A Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with a c-terminal peptide of wiskott-aldrich syndrome protein (see paper)
47% identity, 99% coverage: 3:338/340 of query aligns to 12:347/356 of 2ot0A
- active site: D33 (= D24), K146 (= K136), E187 (= E177), E189 (= E179), K229 (= K219), S300 (= S291)
- binding : E34 (= E25), S38 (≠ T29), R42 (= R33), K146 (= K136), R148 (= R138), R303 (= R294), Q306 (= Q297)
Sites not aligning to the query:
4aldA Human muscle fructose 1,6-bisphosphate aldolase complexed with fructose 1,6-bisphosphate (see paper)
48% identity, 97% coverage: 3:333/340 of query aligns to 12:342/363 of 4aldA
- active site: D33 (= D24), K146 (= K136), E187 (= E177), E189 (= E179), K229 (= K219), S300 (= S291)
- binding 1,6-fructose diphosphate (linear form): E34 (= E25), S35 (= S26), S38 (≠ T29), K107 (= K97), K146 (= K136), R148 (= R138), E187 (= E177), L270 (= L260), S271 (= S261), G272 (= G262), R303 (= R294)
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)
48% identity, 97% coverage: 3:333/340 of query aligns to 12:342/350 of 5tlhA
- active site: D33 (= D24), K146 (= K136), E187 (= E177), E189 (= E179), K229 (= K219), S300 (= S291)
- binding methylenediphosphonic acid: S38 (≠ T29), K107 (= K97), K146 (= K136), R148 (= R138)
- binding [(6-hydroxynaphthalen-2-yl)methylene]bis(phosphonic acid): E34 (= E25), R42 (= R33), S45 (≠ K36), 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)
48% identity, 97% coverage: 3:333/340 of query aligns to 13:343/364 of P04075
- K99 (≠ T88) modified: N6-(2-hydroxyisobutyryl)lysine
- K111 (≠ M100) modified: N6-malonyllysine; alternate
- D129 (= D118) to G: in GSD12; thermolabile; dbSNP:rs121909533
- K147 (= K136) modified: N6-(2-hydroxyisobutyryl)lysine
- E207 (= E196) to K: in GSD12; reduces thermal stability; 3-fold decrease in catalytic efficiency mostly due to reduced substrate affinity; dbSNP:rs121909534
- K312 (≠ D302) 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
P00883 Fructose-bisphosphate aldolase A; Muscle-type aldolase; EC 4.1.2.13 from Oryctolagus cuniculus (Rabbit) (see 5 papers)
48% identity, 97% coverage: 3:333/340 of query aligns to 13:343/364 of P00883
- E35 (= E25) mutation to A: Reduces activity 14-fold.
- R43 (= R33) binding beta-D-fructose 1,6-bisphosphate; 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 (= K219) active site, Schiff-base intermediate with dihydroxyacetone-P; mutation to M: Loss of activity.
- SGG 272:274 (= SGG 261:263) binding beta-D-fructose 1,6-bisphosphate
- S301 (= S291) binding beta-D-fructose 1,6-bisphosphate
- R304 (= R294) binding beta-D-fructose 1,6-bisphosphate; 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)
48% identity, 97% coverage: 3:333/340 of query aligns to 9:339/346 of 5tlzA
- active site: D30 (= D24), K143 (= K136), E184 (= E177), E186 (= E179), K226 (= K219), S297 (= S291)
- binding naphthalene-2,6-diyl bis[dihydrogen (phosphate)]: D30 (= D24), S32 (= S26), S35 (≠ T29), K104 (= K97), S268 (= S261), G269 (= G262), G299 (≠ S293), R300 (= R294)
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)
48% identity, 97% coverage: 3:333/340 of query aligns to 12:342/349 of 5tlwA
- active site: D33 (= D24), K146 (= K136), E187 (= E177), E189 (= E179), K229 (= K219), S300 (= S291)
- binding {[4-(phosphonooxy)phenyl]methylene}bis(phosphonic acid): S35 (= S26), S38 (≠ T29), 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)
48% identity, 97% coverage: 3:333/340 of query aligns to 12:342/349 of 5tleA
- active site: D33 (= D24), K146 (= K136), E187 (= E177), E189 (= E179), K229 (= K219), S300 (= S291)
- binding {[6-(phosphonooxy)naphthalen-2-yl]methylene}bis(phosphonic acid): D33 (= D24), S35 (= S26), S38 (≠ T29), K107 (= K97), K229 (= K219), L270 (= L260), G272 (= G262), G302 (≠ S293), 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)
48% identity, 97% coverage: 3:333/340 of query aligns to 12:342/349 of 3tu9A
- active site: D33 (= D24), K146 (= K136), E187 (= E177), E189 (= E179), K229 (= K219), S300 (= S291)
- binding 2-O-methyl-1,6-di-O-phosphono-D-mannitol: A31 (= A22), D33 (= D24), E34 (= E25), S35 (= S26), S38 (≠ T29), K107 (= K97), K146 (= K136), E187 (= E177), K229 (= K219), S271 (= S261), G272 (= G262), Y301 (= Y292), G302 (≠ S293), 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)
48% identity, 97% coverage: 3:333/340 of query aligns to 12:342/349 of 2ot1A
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)
48% identity, 97% coverage: 3:333/340 of query aligns to 12:342/363 of 1zalA
Sites not aligning to the query:
Query Sequence
>WP_020176885.1 NCBI__GCF_000385335.1:WP_020176885.1
MTRQKLIDTARALLANYKGLLAMDESTETCNKRFAKAGIPQTEEARRAYRELIVTTPGLA
DSINGAILYDETIHQKTKDGTPFVKVLTDAGIIPGIKVDMGAKDLALFPGEKVTEGLDGL
RTRLKAYVEMGARFAKWRAVITIGDGIPTLGCIEANAHALARYAALCQEADVVPIIEPEV
LMDGTHSLEACRAATEEVLHHVFEALHAQRVMLEGMILKPNMVLPGLASPKQESVDEVAD
ATVETFLRTVPAAVPGIAFLSGGQSGELASARLNAMNVRFKSRLPWVLTFSYSRAIQQPA
LDIWRGEEANVAAAQQALYHRAALNRAARCGDYNAAMEKP
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