SitesBLAST
Comparing Ac3H11_658 FitnessBrowser__acidovorax_3H11:Ac3H11_658 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)
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)
46% identity, 97% coverage: 1:339/349 of query aligns to 6:322/323 of A8B2U2
- S50 (= S45) binding
- D83 (= D78) active site, Proton donor; mutation to A: Severe loss of catalytic activity.
- H84 (= H79) binding
- H178 (= H193) binding ; binding
- G179 (= G194) binding
- K182 (= K197) binding
- H210 (= H227) binding
- G211 (= G228) binding
- S213 (= S230) binding
- N253 (= N270) binding
- D255 (= D272) 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 (≠ T273) binding
- R259 (= R276) 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 (= D295) 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 (= R297) binding
3gayA Structure of giardia fructose-1,6-biphosphate aldolase in complex with tagatose-1,6-biphosphate (see paper)
46% identity, 97% coverage: 1:339/349 of query aligns to 5:318/319 of 3gayA
- binding 1,6-di-O-phosphono-D-tagatose: N23 (= N19), S49 (= S45), D82 (= D78), H174 (= H193), G175 (= G194), K178 (= K197), H206 (= H227), G207 (= G228), S209 (= S230), N249 (= N270), D251 (= D272), S252 (≠ T273), R255 (= R276)
- binding zinc ion: H83 (= H79), H174 (= H193), H206 (= H227)
3ohiA Structure of giardia fructose-1,6-biphosphate aldolase in complex with 3-hydroxy-2-pyridone (see paper)
46% identity, 97% coverage: 1:339/349 of query aligns to 5:318/319 of 3ohiA
- binding ({3-hydroxy-2-oxo-4-[2-(phosphonooxy)ethyl]pyridin-1(2H)-yl}methyl)phosphonic acid: S49 (= S45), D82 (= D78), H83 (= H79), H174 (= H193), G175 (= G194), K178 (= K197), G207 (= G228), S209 (= S230), N249 (= N270), D251 (= D272), S252 (≠ T273), R255 (= R276)
- binding zinc ion: H83 (= H79), H174 (= H193), H206 (= H227)
3gb6A Structure of giardia fructose-1,6-biphosphate aldolase d83a mutant in complex with fructose-1,6-bisphosphate (see paper)
46% identity, 97% coverage: 1:339/349 of query aligns to 5:317/318 of 3gb6A
- binding 1,6-di-O-phosphono-D-fructose: N23 (= N19), S49 (= S45), H173 (= H193), G174 (= G194), K177 (= K197), H205 (= H227), G206 (= G228), S208 (= S230), N248 (= N270), D250 (= D272), S251 (≠ T273), R254 (= R276)
2isvB Structure of giardia fructose-1,6-biphosphate aldolase in complex with phosphoglycolohydroxamate (see paper)
44% identity, 97% coverage: 1:339/349 of query aligns to 5:307/307 of 2isvB
- binding phosphoglycolohydroxamic acid: D82 (= D78), H168 (= H193), G169 (= G194), K172 (= K197), H195 (= H227), G196 (= G228), S198 (= S230), N238 (= N270), D240 (= D272), S241 (≠ T273)
- binding zinc ion: H83 (= H79), H168 (= H193), H195 (= H227)
2isvA Structure of giardia fructose-1,6-biphosphate aldolase in complex with phosphoglycolohydroxamate (see paper)
43% identity, 97% coverage: 1:339/349 of query aligns to 5:298/298 of 2isvA
1rv8B Class ii fructose-1,6-bisphosphate aldolase from thermus aquaticus in complex with cobalt (see paper)
45% identity, 92% coverage: 3:323/349 of query aligns to 7:304/305 of 1rv8B
- active site: D80 (= D78), H81 (= H79), E140 (= E152), H178 (= H193), H208 (= H227), N251 (= N270)
- binding cobalt (ii) ion: H81 (= H79), E132 (= E137), H178 (= H193), H208 (= H227)
- binding sulfate ion: R116 (= R121), H123 (= H128), S211 (= S230), D253 (= D272), T254 (= T273)
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)
42% identity, 89% coverage: 3:314/349 of query aligns to 7:297/307 of 3n9sA
- active site: C69 (≠ V65), E70 (= E66), G136 (= G139), H180 (= H193), A226 (≠ Y243), N253 (= N270)
- binding calcium ion: D104 (= D100), S106 (= S102), E134 (= E137)
- binding 4-{hydroxy[(phosphonooxy)acetyl]amino}butyl dihydrogen phosphate: N23 (= N19), S49 (= S45), D82 (= D78), H83 (= H79), H180 (= H193), G181 (= G194), K184 (= K197), H210 (= H227), G211 (= G228), S213 (= S230), N253 (= N270), D255 (= D272), T256 (= T273)
- binding zinc ion: H83 (= H79), H180 (= H193), H210 (= H227)
3c52A Class ii fructose-1,6-bisphosphate aldolase from helicobacter pylori in complex with phosphoglycolohydroxamic acid, a competitive inhibitor (see paper)
40% identity, 89% coverage: 3:314/349 of query aligns to 7:286/296 of 3c52A
- active site: C69 (≠ V65), E70 (= E66), G136 (= G139), H169 (= H193), A215 (≠ Y243), N242 (= N270)
- binding calcium ion: D104 (= D100), S106 (= S102), E134 (= E137)
- binding phosphoglycolohydroxamic acid: D82 (= D78), H83 (= H79), H169 (= H193), K173 (= K197), H199 (= H227), G200 (= G228), S202 (= S230), N242 (= N270), D244 (= D272), T245 (= T273)
- binding zinc ion: H83 (= H79), H169 (= H193), H199 (= H227)
3n9rA Class ii fructose-1,6-bisphosphate aldolase from helicobacter pylori in complex with n-(4-hydroxybutyl)-phosphoglycolohydroxamic acid, a competitive inhibitor (see paper)
40% identity, 89% coverage: 3:314/349 of query aligns to 7:287/297 of 3n9rA
- active site: C69 (≠ V65), E70 (= E66), G136 (= G139), H170 (= H193), A216 (≠ Y243), N243 (= N270)
- binding 2-[hydroxy(4-hydroxybutyl)amino]-2-oxoethyl dihydrogen phosphate: H83 (= H79), H170 (= H193), G171 (= G194), K174 (= K197), H200 (= H227), G201 (= G228), S203 (= S230), N243 (= N270), D245 (= D272), T246 (= T273)
- binding zinc ion: H83 (= H79), H170 (= H193), H200 (= H227)
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)
40% identity, 89% coverage: 3:314/349 of query aligns to 7:287/297 of 3c56A
- active site: C69 (≠ V65), E70 (= E66), G136 (= G139), H170 (= H193), A216 (≠ Y243), N243 (= N270)
- binding 3-{hydroxy[(phosphonooxy)acetyl]amino}propyl dihydrogen phosphate: N23 (= N19), S49 (= S45), D82 (= D78), H170 (= H193), K174 (= K197), G201 (= G228), S203 (= S230), N243 (= N270), D245 (= D272), T246 (= T273), R249 (= R276)
- binding zinc ion: H83 (= H79), H170 (= H193), H200 (= H227)
5ucpA Class ii fructose-1,6-bisphosphate aldolase e142a variant of helicobacter pylori with fbp and cleavage products (see paper)
40% identity, 89% coverage: 3:314/349 of query aligns to 7:282/292 of 5ucpA
- binding 1,6-di-O-phosphono-D-fructose: S49 (= S45), D82 (= D78), H83 (= H79), H165 (= H193), K169 (= K197), G196 (= G228), S198 (= S230), N238 (= N270), D240 (= D272), T241 (= T273), R244 (= R276)
- binding zinc ion: H83 (= H79), H83 (= H79), H83 (= H79), E134 (= E137), H165 (= H193), H165 (= H193), H165 (= H193), H195 (= H227), H195 (= H227)
5uckA Class ii fructose-1,6-bisphosphate aldolase of helicobacter pylori with cleavage products (see paper)
40% identity, 89% coverage: 3:314/349 of query aligns to 7:281/291 of 5uckA
- binding glyceraldehyde-3-phosphate: S49 (= S45), D82 (= D78), H83 (= H79), H164 (= H193), D239 (= D272), R243 (= R276)
- binding zinc ion: H83 (= H79), H83 (= H79), E134 (= E137), H164 (= H193), H194 (= H227), H194 (= H227)
5ud4A Class ii fructose-1,6-bisphosphate aldolase h180q variant of helicobacter pylori with tbp (see paper)
40% identity, 89% coverage: 3:314/349 of query aligns to 7:283/293 of 5ud4A
- binding 1,6-di-O-phosphono-D-tagatose: S49 (= S45), D82 (= D78), Q166 (≠ H193), G167 (= G194), K170 (= K197), G197 (= G228), S199 (= S230), N239 (= N270), D241 (= D272), T242 (= T273), R245 (= R276)
- binding zinc ion: H83 (= H79), H83 (= H79), E134 (= E137), H196 (= H227), H196 (= H227)
5ud0A Class ii fructose-1,6-bisphosphate aldolase e149a variant of helicobacter pylori with cleavage products (see paper)
39% identity, 90% coverage: 2:314/349 of query aligns to 6:272/282 of 5ud0A
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)
36% identity, 93% coverage: 1:323/349 of query aligns to 6:284/285 of P13243
- T212 (≠ S230) modified: Phosphothreonine
- T234 (= T273) modified: Phosphothreonine
3q94A The crystal structure of fructose 1,6-bisphosphate aldolase from bacillus anthracis str. 'Ames ancestor'
35% identity, 93% coverage: 1:323/349 of query aligns to 6:284/285 of 3q94A
- active site: D85 (= D78), H86 (= H79), E145 (= E152), H181 (= H193), H209 (= H227), N231 (= N270)
- binding zinc ion: H86 (= H79), E114 (= E114), H163 (≠ V175), H181 (= H193), H209 (= H227), E235 (≠ D274), E239 (≠ A278)
4to8A Methicillin-resistant staphylococcus aureus class iib fructose 1,6- bisphosphate aldolase (see paper)
36% identity, 93% coverage: 1:323/349 of query aligns to 5:276/279 of 4to8A
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)
34% identity, 90% coverage: 2:314/349 of query aligns to 7:274/286 of P0AB74
- D82 (= D78) active site, Proton donor
- H83 (= H79) binding
- H180 (= H193) binding
- H208 (= H227) binding
1gvfB Structure of tagatose-1,6-bisphosphate aldolase (see paper)
33% identity, 90% coverage: 2:314/349 of query aligns to 6:265/275 of 1gvfB
- active site: D81 (= D78), H82 (= H79), H171 (= H193), H199 (= H227), N221 (= N270)
- binding phosphoglycolohydroxamic acid: D81 (= D78), H82 (= H79), H171 (= H193), G172 (= G194), H199 (= H227), G200 (= G228), S202 (= S230), N221 (= N270), V222 (≠ I271), A223 (≠ D272), T224 (= T273)
- binding zinc ion: H82 (= H79), H171 (= H193), H199 (= H227)
Query Sequence
>Ac3H11_658 FitnessBrowser__acidovorax_3H11:Ac3H11_658
MRELLDHAAANSYGIPAFNVNNLEQVQAVMAAADEVGAPVILQASAGARKYAGEPFIKHL
IQAAVEAFPHIPLVMHQDHGTSPKVCAGAIDLGFGSVMMDGSLMEDGKTPSSFEYNVEVT
RKVVDMAHKVGVTVEGELGCLGNLETGEAGEEDGIGADVKLDHSQMLTDPEEAAVFVKAT
QLDALAIAIGTSHGAYKFSRKPTGDILAISRVKEIHKRIPNTHLVMHGSSSVPAELLAII
NQYGGKMKETYGVPVEEIQEAIKHGVRKINIDTDIRLAMTGAVRKFLAENPDKFDAREWL
KPAREAAKQVCKARYLEFGCEGQGAKIKGHSLQVVAAQYASGALAQVVN
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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