SitesBLAST
Comparing WP_037573293.1 NCBI__GCF_000744815.1:WP_037573293.1 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)
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)
40% identity, 97% coverage: 1:273/282 of query aligns to 1:272/285 of P13243
- T212 (≠ S213) modified: Phosphothreonine
- T234 (= T235) modified: Phosphothreonine
3q94A The crystal structure of fructose 1,6-bisphosphate aldolase from bacillus anthracis str. 'Ames ancestor'
39% identity, 97% coverage: 1:273/282 of query aligns to 1:272/285 of 3q94A
- active site: D85 (= D84), H86 (= H85), E145 (≠ P144), H181 (= H182), H209 (= H210), N231 (= N232)
- binding zinc ion: H86 (= H85), E114 (≠ A113), H163 (≠ A164), H181 (= H182), H209 (= H210), E235 (≠ A236), E239 (≠ A240)
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)
37% identity, 99% coverage: 1:280/282 of query aligns to 1:278/286 of P0AB74
- D82 (= D84) active site, Proton donor
- H83 (= H85) binding Zn(2+)
- H180 (= H182) binding Zn(2+)
- H208 (= H210) binding Zn(2+)
1gvfB Structure of tagatose-1,6-bisphosphate aldolase (see paper)
37% identity, 99% coverage: 2:280/282 of query aligns to 1:269/275 of 1gvfB
- active site: D81 (= D84), H82 (= H85), H171 (= H182), H199 (= H210), N221 (= N232)
- binding phosphoglycolohydroxamic acid: D81 (= D84), H82 (= H85), H171 (= H182), G172 (≠ A183), H199 (= H210), G200 (= G211), S202 (= S213), N221 (= N232), V222 (= V233), A223 (≠ G234), T224 (= T235)
- binding zinc ion: H82 (= H85), H171 (= H182), H199 (= H210)
4to8A Methicillin-resistant staphylococcus aureus class iib fructose 1,6- bisphosphate aldolase (see paper)
36% identity, 96% coverage: 3:274/282 of query aligns to 2:265/279 of 4to8A
1rv8B Class ii fructose-1,6-bisphosphate aldolase from thermus aquaticus in complex with cobalt (see paper)
35% identity, 97% coverage: 3:275/282 of query aligns to 2:294/305 of 1rv8B
- active site: D80 (= D84), H81 (= H85), E140 (≠ P144), H178 (= H182), H208 (= H210), N251 (= N232)
- binding cobalt (ii) ion: H81 (= H85), E132 (= E136), H178 (= H182), H208 (= H210)
- binding sulfate ion: R116 (= R120), H123 (= H127), S211 (= S213), D253 (≠ G234), T254 (= T235)
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, 97% coverage: 1:273/282 of query aligns to 1:263/280 of 8q59A
- binding (3~{S},4~{S})-2,3,4-tris(oxidanyl)-5-oxidanylidene-6-phosphonooxy-hexane-1-sulfonic acid: G50 (≠ S50), Q51 (≠ E51), K52 (≠ N52), D82 (= D84), H83 (= H85), H172 (= H182), G173 (≠ A183), H200 (= H210), G201 (= G211), S203 (= S213), N222 (= N232), D224 (≠ G234), T225 (= T235)
- binding zinc ion: H83 (= H85), H172 (= H182), H200 (= H210)
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)
34% identity, 97% coverage: 1:273/282 of query aligns to 1:294/323 of A8B2U2
- S50 (= S50) binding beta-D-fructose 1,6-bisphosphate
- D83 (= D84) active site, Proton donor; mutation to A: Severe loss of catalytic activity.
- H84 (= H85) binding Zn(2+)
- H178 (= H182) binding beta-D-fructose 1,6-bisphosphate; binding Zn(2+)
- G179 (≠ A183) binding beta-D-fructose 1,6-bisphosphate
- K182 (≠ E186) binding beta-D-fructose 1,6-bisphosphate
- H210 (= H210) binding Zn(2+)
- G211 (= G211) binding beta-D-fructose 1,6-bisphosphate
- S213 (= S213) binding beta-D-fructose 1,6-bisphosphate
- N253 (= N232) binding beta-D-fructose 1,6-bisphosphate
- D255 (≠ G234) binding beta-D-fructose 1,6-bisphosphate; 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 (≠ T235) binding beta-D-fructose 1,6-bisphosphate
- R259 (≠ N238) binding beta-D-fructose 1,6-bisphosphate; 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 (= D257) 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.
- R280 (= R259) binding beta-D-fructose 1,6-bisphosphate
3gayA Structure of giardia fructose-1,6-biphosphate aldolase in complex with tagatose-1,6-biphosphate (see paper)
33% identity, 96% coverage: 3:273/282 of query aligns to 2:290/319 of 3gayA
- binding 1,6-di-O-phosphono-D-tagatose: N23 (= N24), S49 (= S50), D82 (= D84), H174 (= H182), G175 (≠ A183), K178 (≠ E186), H206 (= H210), G207 (= G211), S209 (= S213), N249 (= N232), D251 (≠ G234), S252 (≠ T235), R255 (≠ N238)
- binding zinc ion: H83 (= H85), H174 (= H182), H206 (= H210)
3ohiA Structure of giardia fructose-1,6-biphosphate aldolase in complex with 3-hydroxy-2-pyridone (see paper)
33% identity, 96% coverage: 3:273/282 of query aligns to 2:290/319 of 3ohiA
- binding ({3-hydroxy-2-oxo-4-[2-(phosphonooxy)ethyl]pyridin-1(2H)-yl}methyl)phosphonic acid: S49 (= S50), D82 (= D84), H83 (= H85), H174 (= H182), G175 (≠ A183), K178 (≠ E186), G207 (= G211), S209 (= S213), N249 (= N232), D251 (≠ G234), S252 (≠ T235), R255 (≠ N238)
- binding zinc ion: H83 (= H85), H174 (= H182), H206 (= H210)
3gb6A Structure of giardia fructose-1,6-biphosphate aldolase d83a mutant in complex with fructose-1,6-bisphosphate (see paper)
33% identity, 96% coverage: 3:273/282 of query aligns to 2:289/318 of 3gb6A
- binding 1,6-di-O-phosphono-D-fructose: N23 (= N24), S49 (= S50), H173 (= H182), G174 (≠ A183), K177 (≠ E186), H205 (= H210), G206 (= G211), S208 (= S213), N248 (= N232), D250 (≠ G234), S251 (≠ T235), R254 (≠ N238)
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)
32% identity, 98% coverage: 3:278/282 of query aligns to 2:302/307 of 3n9sA
- active site: C69 (= C75), E70 (≠ D76), G136 (= G138), H180 (= H182), A226 (vs. gap), N253 (= N232)
- binding calcium ion: D104 (= D106), S106 (≠ G108), E134 (= E136)
- binding 4-{hydroxy[(phosphonooxy)acetyl]amino}butyl dihydrogen phosphate: N23 (= N24), S49 (= S50), D82 (= D84), H83 (= H85), H180 (= H182), G181 (≠ A183), K184 (≠ E186), H210 (= H210), G211 (= G211), S213 (= S213), N253 (= N232), D255 (≠ G234), T256 (= T235)
- binding zinc ion: H83 (= H85), H180 (= H182), H210 (= H210)
8q5aA Crystal structure of metal-dependent class ii sulfofructosephosphate aldolase from hafnia paralvei hpsqia-zn in complex with dihydroxyacetone phosphate (dhap) (see paper)
33% identity, 97% coverage: 1:273/282 of query aligns to 1:263/276 of 8q5aA
2isvA Structure of giardia fructose-1,6-biphosphate aldolase in complex with phosphoglycolohydroxamate (see paper)
32% identity, 96% coverage: 3:273/282 of query aligns to 2:270/298 of 2isvA
2isvB Structure of giardia fructose-1,6-biphosphate aldolase in complex with phosphoglycolohydroxamate (see paper)
32% identity, 96% coverage: 3:273/282 of query aligns to 2:279/307 of 2isvB
- binding phosphoglycolohydroxamic acid: D82 (= D84), H168 (= H182), G169 (vs. gap), K172 (≠ T185), H195 (= H210), G196 (= G211), S198 (= S213), N238 (= N232), D240 (≠ G234), S241 (≠ T235)
- binding zinc ion: H83 (= H85), H168 (= H182), H195 (= H210)
3n9rA Class ii fructose-1,6-bisphosphate aldolase from helicobacter pylori in complex with n-(4-hydroxybutyl)-phosphoglycolohydroxamic acid, a competitive inhibitor (see paper)
32% identity, 98% coverage: 3:278/282 of query aligns to 2:292/297 of 3n9rA