SitesBLAST
Comparing 3607858 Dshi_1266 ketose-bisphosphate aldolase (RefSeq) 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)
P13243 Probable fructose-bisphosphate aldolase; FBP aldolase; FBPA; Fructose-1,6-bisphosphate aldolase; EC 4.1.2.13 from Bacillus subtilis (strain 168) (see paper)
38% identity, 91% coverage: 1:255/280 of query aligns to 1:261/285 of P13243
- T212 (≠ S205) modified: Phosphothreonine
- T234 (= T228) modified: Phosphothreonine
3q94A The crystal structure of fructose 1,6-bisphosphate aldolase from bacillus anthracis str. 'Ames ancestor'
38% identity, 89% coverage: 1:250/280 of query aligns to 1:256/285 of 3q94A
- active site: D85 (= D82), H86 (= H83), E145 (= E142), H181 (= H174), H209 (= H202), N231 (= N225)
- binding zinc ion: H86 (= H83), E114 (= E111), H163 (≠ R156), H181 (= H174), H209 (= H202), E235 (= E229), E239 (≠ A233)
5ud0A Class ii fructose-1,6-bisphosphate aldolase e149a variant of helicobacter pylori with cleavage products (see paper)
33% identity, 97% coverage: 7:277/280 of query aligns to 6:272/282 of 5ud0A
8q59A Crystal structure of metal-dependent class ii sulfofructose phosphate aldolase from yersinia aldovae in complex with sulfofructose phosphate (yasqia-zn-sfp) (see paper)
37% identity, 89% coverage: 1:249/280 of query aligns to 1:246/280 of 8q59A
- binding (3~{S},4~{S})-2,3,4-tris(oxidanyl)-5-oxidanylidene-6-phosphonooxy-hexane-1-sulfonic acid: G50 (= G50), Q51 (≠ P51), K52 (≠ S52), D82 (= D82), H83 (= H83), H172 (= H174), G173 (≠ L175), H200 (= H202), G201 (= G203), S203 (= S205), N222 (= N225), D224 (≠ G227), T225 (= T228)
- binding zinc ion: H83 (= H83), H172 (= H174), H200 (= H202)
8q5aA Crystal structure of metal-dependent class ii sulfofructosephosphate aldolase from hafnia paralvei hpsqia-zn in complex with dihydroxyacetone phosphate (dhap) (see paper)
39% identity, 86% coverage: 9:249/280 of query aligns to 9:246/276 of 8q5aA
3n9sA Class ii fructose-1,6-bisphosphate aldolase from helicobacter pylori in complex with n-(4-hydroxybutyl)- glycolohydroxamic acid bis- phosphate, a competitive inhibitor (see paper)
33% identity, 97% coverage: 7:277/280 of query aligns to 6:297/307 of 3n9sA
- active site: C69 (≠ A70), E70 (= E71), G136 (= G136), H180 (= H174), A226 (vs. gap), N253 (= N225)
- binding calcium ion: D104 (= D104), S106 (= S106), E134 (= E134)
- binding 4-{hydroxy[(phosphonooxy)acetyl]amino}butyl dihydrogen phosphate: N23 (≠ V24), S49 (≠ G50), D82 (= D82), H83 (= H83), H180 (= H174), G181 (vs. gap), K184 (≠ Q176), H210 (= H202), G211 (= G203), S213 (= S205), N253 (= N225), D255 (≠ G227), T256 (= T228)
- binding zinc ion: H83 (= H83), H180 (= H174), H210 (= H202)
4to8A Methicillin-resistant staphylococcus aureus class iib fructose 1,6- bisphosphate aldolase (see paper)
36% identity, 89% coverage: 3:250/280 of query aligns to 2:248/279 of 4to8A
5ucpA Class ii fructose-1,6-bisphosphate aldolase e142a variant of helicobacter pylori with fbp and cleavage products (see paper)
33% identity, 97% coverage: 7:277/280 of query aligns to 6:282/292 of 5ucpA
- binding 1,6-di-O-phosphono-D-fructose: S49 (≠ G50), D82 (= D82), H83 (= H83), H165 (= H174), K169 (≠ Q176), G196 (= G203), S198 (= S205), N238 (= N225), D240 (≠ G227), T241 (= T228), R244 (= R231)
- binding zinc ion: H83 (= H83), H83 (= H83), H83 (= H83), E134 (= E134), H165 (= H174), H165 (= H174), H165 (= H174), H195 (= H202), H195 (= H202)
5uckA Class ii fructose-1,6-bisphosphate aldolase of helicobacter pylori with cleavage products (see paper)
33% identity, 97% coverage: 7:277/280 of query aligns to 6:281/291 of 5uckA
- binding glyceraldehyde-3-phosphate: S49 (≠ G50), D82 (= D82), H83 (= H83), H164 (= H174), D239 (≠ G227), R243 (= R231)
- binding zinc ion: H83 (= H83), H83 (= H83), E134 (= E134), H164 (= H174), H194 (= H202), H194 (= H202)
3n9rA Class ii fructose-1,6-bisphosphate aldolase from helicobacter pylori in complex with n-(4-hydroxybutyl)-phosphoglycolohydroxamic acid, a competitive inhibitor (see paper)
33% identity, 97% coverage: 7:277/280 of query aligns to 6:287/297 of 3n9rA
- active site: C69 (≠ A70), E70 (= E71), G136 (= G136), H170 (= H174), A216 (vs. gap), N243 (= N225)
- binding 2-[hydroxy(4-hydroxybutyl)amino]-2-oxoethyl dihydrogen phosphate: H83 (= H83), H170 (= H174), G171 (vs. gap), K174 (≠ Q176), H200 (= H202), G201 (= G203), S203 (= S205), N243 (= N225), D245 (≠ G227), T246 (= T228)
- binding zinc ion: H83 (= H83), H170 (= H174), H200 (= H202)
3c56A Class ii fructose-1,6-bisphosphate aldolase from helicobacter pylori in complex with n-(3-hydroxypropyl)-glycolohydroxamic acid bisphosphate, a competitive inhibitor (see paper)
33% identity, 97% coverage: 7:277/280 of query aligns to 6:287/297 of 3c56A
- active site: C69 (≠ A70), E70 (= E71), G136 (= G136), H170 (= H174), A216 (vs. gap), N243 (= N225)
- binding 3-{hydroxy[(phosphonooxy)acetyl]amino}propyl dihydrogen phosphate: N23 (≠ V24), S49 (≠ G50), D82 (= D82), H170 (= H174), K174 (≠ Q176), G201 (= G203), S203 (= S205), N243 (= N225), D245 (≠ G227), T246 (= T228), R249 (= R231)
- binding zinc ion: H83 (= H83), H170 (= H174), H200 (= H202)
3c52A Class ii fructose-1,6-bisphosphate aldolase from helicobacter pylori in complex with phosphoglycolohydroxamic acid, a competitive inhibitor (see paper)
33% identity, 97% coverage: 7:277/280 of query aligns to 6:286/296 of 3c52A
- active site: C69 (≠ A70), E70 (= E71), G136 (= G136), H169 (= H174), A215 (vs. gap), N242 (= N225)
- binding calcium ion: D104 (= D104), S106 (= S106), E134 (= E134)
- binding phosphoglycolohydroxamic acid: D82 (= D82), H83 (= H83), H169 (= H174), K173 (≠ Q176), H199 (= H202), G200 (= G203), S202 (= S205), N242 (= N225), D244 (≠ G227), T245 (= T228)
- binding zinc ion: H83 (= H83), H169 (= H174), H199 (= H202)
5ud4A Class ii fructose-1,6-bisphosphate aldolase h180q variant of helicobacter pylori with tbp (see paper)
32% identity, 97% coverage: 7:277/280 of query aligns to 6:283/293 of 5ud4A
- binding 1,6-di-O-phosphono-D-tagatose: S49 (≠ G50), D82 (= D82), Q166 (≠ H174), G167 (vs. gap), K170 (≠ Q176), G197 (= G203), S199 (= S205), N239 (= N225), D241 (≠ G227), T242 (= T228), R245 (= R231)
- binding zinc ion: H83 (= H83), H83 (= H83), E134 (= E134), H196 (= H202), H196 (= H202)
1rv8B Class ii fructose-1,6-bisphosphate aldolase from thermus aquaticus in complex with cobalt (see paper)
36% identity, 89% coverage: 3:250/280 of query aligns to 2:276/305 of 1rv8B
- active site: D80 (= D82), H81 (= H83), E140 (vs. gap), H178 (= H174), H208 (= H202), N251 (= N225)
- binding cobalt (ii) ion: H81 (= H83), E132 (= E134), H178 (= H174), H208 (= H202)
- binding sulfate ion: R116 (≠ A118), H123 (= H125), S211 (= S205), D253 (≠ G227), T254 (= T228)
3gayA Structure of giardia fructose-1,6-biphosphate aldolase in complex with tagatose-1,6-biphosphate (see paper)
30% identity, 89% coverage: 3:250/280 of query aligns to 2:274/319 of 3gayA
- binding 1,6-di-O-phosphono-D-tagatose: N23 (≠ V24), S49 (≠ G50), D82 (= D82), H174 (= H174), G175 (vs. gap), K178 (vs. gap), H206 (= H202), G207 (= G203), S209 (= S205), N249 (= N225), D251 (≠ G227), S252 (≠ T228), R255 (= R231)
- binding zinc ion: H83 (= H83), H174 (= H174), H206 (= H202)
A8B2U2 Fructose-bisphosphate aldolase; Glfba; glFBPA; Fructose-1,6-bisphosphate aldolase; EC 4.1.2.13 from Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia) (see 4 papers)
30% identity, 89% coverage: 1:250/280 of query aligns to 1:278/323 of A8B2U2
- S50 (≠ G50) binding
- D83 (= D82) active site, Proton donor; mutation to A: Severe loss of catalytic activity.
- H84 (= H83) binding
- H178 (= H174) binding ; binding
- G179 (vs. gap) binding
- K182 (vs. gap) binding
- H210 (= H202) binding
- G211 (= G203) binding
- S213 (= S205) binding
- N253 (= N225) binding
- D255 (≠ G227) binding ; mutation to A: 9.4-fold reduction in substrate affinity and 50-fold reduction in catalytic affinity. Has some activity towards tagatose-1,6-bisphosphate.
- S256 (≠ T228) binding
- R259 (= R231) binding ; mutation to A: 1.8-fold reduction in substrate affinity and 2.8-fold reduction in catalytic efficiency. 6-fold reduction in substrate affinity and 24-fold reduction in catalytic efficiency; when associated with A-278.
- D278 (= D250) mutation to A: 159-fold reduction in substrate affinity and 2770-fold reduction in catalytic efficiency. 6-fold reduction in substrate affinity and 24-fold reduction in catalytic efficiency; when associated with A-259.
Sites not aligning to the query:
3ohiA Structure of giardia fructose-1,6-biphosphate aldolase in complex with 3-hydroxy-2-pyridone (see paper)
29% identity, 89% coverage: 3:250/280 of query aligns to 2:274/319 of 3ohiA
- binding ({3-hydroxy-2-oxo-4-[2-(phosphonooxy)ethyl]pyridin-1(2H)-yl}methyl)phosphonic acid: S49 (≠ G50), D82 (= D82), H83 (= H83), H174 (= H174), G175 (vs. gap), K178 (vs. gap), G207 (= G203), S209 (= S205), N249 (= N225), D251 (≠ G227), S252 (≠ T228), R255 (= R231)
- binding zinc ion: H83 (= H83), H174 (= H174), H206 (= H202)
P0AB74 D-tagatose-1,6-bisphosphate aldolase subunit KbaY; TBPA; TagBP aldolase; D-tagatose-bisphosphate aldolase class II; Ketose 1,6-bisphosphate aldolase class II; Tagatose-bisphosphate aldolase; EC 4.1.2.40 from Escherichia coli (strain K12) (see paper)
33% identity, 91% coverage: 1:256/280 of query aligns to 1:261/286 of P0AB74
- D82 (= D82) active site, Proton donor
- H83 (= H83) binding
- H180 (= H174) binding
- H208 (= H202) binding
3gb6A Structure of giardia fructose-1,6-biphosphate aldolase d83a mutant in complex with fructose-1,6-bisphosphate (see paper)
29% identity, 89% coverage: 3:250/280 of query aligns to 2:273/318 of 3gb6A
- binding 1,6-di-O-phosphono-D-fructose: N23 (≠ V24), S49 (≠ G50), H173 (= H174), G174 (vs. gap), K177 (vs. gap), H205 (= H202), G206 (= G203), S208 (= S205), N248 (= N225), D250 (≠ G227), S251 (≠ T228), R254 (= R231)
1gvfB Structure of tagatose-1,6-bisphosphate aldolase (see paper)
32% identity, 91% coverage: 2:256/280 of query aligns to 1:252/275 of 1gvfB
- active site: D81 (= D82), H82 (= H83), H171 (= H174), H199 (= H202), N221 (= N225)
- binding phosphoglycolohydroxamic acid: D81 (= D82), H82 (= H83), H171 (= H174), G172 (≠ L175), H199 (= H202), G200 (= G203), S202 (= S205), N221 (= N225), V222 (≠ I226), A223 (≠ G227), T224 (= T228)
- binding zinc ion: H82 (= H83), H171 (= H174), H199 (= H202)
Query Sequence
>3607858 Dshi_1266 ketose-bisphosphate aldolase (RefSeq)
MTLATLSEVLQPALEGGYAVGGLVCLGWEEMRAYTRAAEAEGVPLILQAGPSCRAHTPLP
VLGAMFRHLAERASVPVVAHLDHGYSFAECQEALDSGFTSLMFDGSRLPLEENIAQTARI
VDLAHKAGISCEGEIGFVGYAEGDASQGTDPEEAARFARETGVDAMAISVGNVHLQQNRE
GGLDEGRIAEIAARTEVPLVIHGGSGVPLAQRTRLARGSTICKFNIGTELRMAFGAALRE
AVTSDPDRFDRVQILREVEAPVEAAARLALRALAPEREVA
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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