SitesBLAST
Comparing WP_027722924.1 NCBI__GCF_000425265.1:WP_027722924.1 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)
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)
52% identity, 100% coverage: 1:307/307 of query aligns to 1:307/323 of A8B2U2
- S50 (= S50) binding beta-D-fructose 1,6-bisphosphate
- D83 (= D82) active site, Proton donor; mutation to A: Severe loss of catalytic activity.
- H84 (= H83) binding Zn(2+)
- H178 (= H178) binding beta-D-fructose 1,6-bisphosphate; binding Zn(2+)
- G179 (= G179) binding beta-D-fructose 1,6-bisphosphate
- K182 (= K182) binding beta-D-fructose 1,6-bisphosphate
- H210 (= H209) binding Zn(2+)
- G211 (= G210) binding beta-D-fructose 1,6-bisphosphate
- S213 (= S212) binding beta-D-fructose 1,6-bisphosphate
- N253 (= N252) binding beta-D-fructose 1,6-bisphosphate
- D255 (= D254) 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 (≠ T255) binding beta-D-fructose 1,6-bisphosphate
- R259 (= R258) 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 (= D277) 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 (= R279) 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)
51% identity, 100% coverage: 2:307/307 of query aligns to 1:303/319 of 3gayA
- binding 1,6-di-O-phosphono-D-tagatose: N23 (= N24), S49 (= S50), D82 (= D82), H174 (= H178), G175 (= G179), K178 (= K182), H206 (= H209), G207 (= G210), S209 (= S212), N249 (= N252), D251 (= D254), S252 (≠ T255), R255 (= R258)
- binding zinc ion: H83 (= H83), H174 (= H178), H206 (= H209)
3ohiA Structure of giardia fructose-1,6-biphosphate aldolase in complex with 3-hydroxy-2-pyridone (see paper)
50% identity, 100% coverage: 2:307/307 of query aligns to 1:303/319 of 3ohiA
- binding ({3-hydroxy-2-oxo-4-[2-(phosphonooxy)ethyl]pyridin-1(2H)-yl}methyl)phosphonic acid: S49 (= S50), D82 (= D82), H83 (= H83), H174 (= H178), G175 (= G179), K178 (= K182), G207 (= G210), S209 (= S212), N249 (= N252), D251 (= D254), S252 (≠ T255), R255 (= R258)
- binding zinc ion: H83 (= H83), H174 (= H178), H206 (= H209)
1rv8B Class ii fructose-1,6-bisphosphate aldolase from thermus aquaticus in complex with cobalt (see paper)
50% identity, 99% coverage: 3:307/307 of query aligns to 2:305/305 of 1rv8B
- active site: D80 (= D82), H81 (= H83), E140 (= E142), H178 (= H178), H208 (= H209), N251 (= N252)
- binding cobalt (ii) ion: H81 (= H83), E132 (= E134), H178 (= H178), H208 (= H209)
- binding sulfate ion: R116 (≠ Q118), H123 (= H125), S211 (= S212), D253 (= D254), T254 (= T255)
3gb6A Structure of giardia fructose-1,6-biphosphate aldolase d83a mutant in complex with fructose-1,6-bisphosphate (see paper)
50% identity, 100% coverage: 2:307/307 of query aligns to 1:302/318 of 3gb6A
- binding 1,6-di-O-phosphono-D-fructose: N23 (= N24), S49 (= S50), H173 (= H178), G174 (= G179), K177 (= K182), H205 (= H209), G206 (= G210), S208 (= S212), N248 (= N252), D250 (= D254), S251 (≠ T255), R254 (= R258)
2isvB Structure of giardia fructose-1,6-biphosphate aldolase in complex with phosphoglycolohydroxamate (see paper)
49% identity, 100% coverage: 2:307/307 of query aligns to 1:292/307 of 2isvB
- binding phosphoglycolohydroxamic acid: D82 (= D82), H168 (= H178), G169 (= G179), K172 (= K182), H195 (= H209), G196 (= G210), S198 (= S212), N238 (= N252), D240 (= D254), S241 (≠ T255)
- binding zinc ion: H83 (= H83), H168 (= H178), H195 (= H209)
2isvA Structure of giardia fructose-1,6-biphosphate aldolase in complex with phosphoglycolohydroxamate (see paper)
48% identity, 100% coverage: 2:307/307 of query aligns to 1:283/298 of 2isvA
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)
44% identity, 99% coverage: 3:306/307 of query aligns to 2:306/307 of 3n9sA
- active site: C69 (≠ L70), E70 (≠ L71), G136 (= G136), H180 (= H178), A226 (≠ F225), N253 (= N252)
- binding calcium ion: D104 (= D104), S106 (= S106), E134 (= E134)
- binding 4-{hydroxy[(phosphonooxy)acetyl]amino}butyl dihydrogen phosphate: N23 (= N24), S49 (= S50), D82 (= D82), H83 (= H83), H180 (= H178), G181 (= G179), K184 (= K182), H210 (= H209), G211 (= G210), S213 (= S212), N253 (= N252), D255 (= D254), T256 (= T255)
- binding zinc ion: H83 (= H83), H180 (= H178), H210 (= H209)
4to8A Methicillin-resistant staphylococcus aureus class iib fructose 1,6- bisphosphate aldolase (see paper)
46% identity, 100% coverage: 2:307/307 of query aligns to 1:277/279 of 4to8A
3c52A Class ii fructose-1,6-bisphosphate aldolase from helicobacter pylori in complex with phosphoglycolohydroxamic acid, a competitive inhibitor (see paper)
44% identity, 99% coverage: 3:306/307 of query aligns to 2:295/296 of 3c52A
- active site: C69 (≠ L70), E70 (≠ L71), G136 (= G136), H169 (= H178), A215 (≠ F225), N242 (= N252)
- binding calcium ion: D104 (= D104), S106 (= S106), E134 (= E134)
- binding phosphoglycolohydroxamic acid: D82 (= D82), H83 (= H83), H169 (= H178), K173 (= K182), H199 (= H209), G200 (= G210), S202 (= S212), N242 (= N252), D244 (= D254), T245 (= T255)
- binding zinc ion: H83 (= H83), H169 (= H178), H199 (= H209)
3n9rA Class ii fructose-1,6-bisphosphate aldolase from helicobacter pylori in complex with n-(4-hydroxybutyl)-phosphoglycolohydroxamic acid, a competitive inhibitor (see paper)
44% identity, 99% coverage: 3:306/307 of query aligns to 2:296/297 of 3n9rA
- active site: C69 (≠ L70), E70 (≠ L71), G136 (= G136), H170 (= H178), A216 (≠ F225), N243 (= N252)
- binding 2-[hydroxy(4-hydroxybutyl)amino]-2-oxoethyl dihydrogen phosphate: H83 (= H83), H170 (= H178), G171 (= G179), K174 (= K182), H200 (= H209), G201 (= G210), S203 (= S212), N243 (= N252), D245 (= D254), T246 (= T255)
- binding zinc ion: H83 (= H83), H170 (= H178), H200 (= H209)
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)
44% identity, 99% coverage: 3:306/307 of query aligns to 2:296/297 of 3c56A
- active site: C69 (≠ L70), E70 (≠ L71), G136 (= G136), H170 (= H178), A216 (≠ F225), N243 (= N252)
- binding 3-{hydroxy[(phosphonooxy)acetyl]amino}propyl dihydrogen phosphate: N23 (= N24), S49 (= S50), D82 (= D82), H170 (= H178), K174 (= K182), G201 (= G210), S203 (= S212), N243 (= N252), D245 (= D254), T246 (= T255), R249 (= R258)
- binding zinc ion: H83 (= H83), H170 (= H178), H200 (= H209)
5uckA Class ii fructose-1,6-bisphosphate aldolase of helicobacter pylori with cleavage products (see paper)
43% identity, 99% coverage: 3:306/307 of query aligns to 2:290/291 of 5uckA
- binding glyceraldehyde-3-phosphate: S49 (= S50), D82 (= D82), H83 (= H83), H164 (= H178), D239 (= D254), R243 (= R258)
- binding zinc ion: H83 (= H83), H83 (= H83), E134 (= E134), H164 (= H178), H194 (= H209), H194 (= H209)
5ucpA Class ii fructose-1,6-bisphosphate aldolase e142a variant of helicobacter pylori with fbp and cleavage products (see paper)
43% identity, 99% coverage: 3:306/307 of query aligns to 2:291/292 of 5ucpA
- binding 1,6-di-O-phosphono-D-fructose: S49 (= S50), D82 (= D82), H83 (= H83), H165 (= H178), K169 (= K182), G196 (= G210), S198 (= S212), N238 (= N252), D240 (= D254), T241 (= T255), R244 (= R258)
- binding zinc ion: H83 (= H83), H83 (= H83), H83 (= H83), E134 (= E134), H165 (= H178), H165 (= H178), H165 (= H178), H195 (= H209), H195 (= H209)
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)
43% identity, 100% coverage: 1:307/307 of query aligns to 1:285/285 of P13243
- T212 (≠ S212) modified: Phosphothreonine
- T234 (= T255) modified: Phosphothreonine
5ud4A Class ii fructose-1,6-bisphosphate aldolase h180q variant of helicobacter pylori with tbp (see paper)
43% identity, 99% coverage: 3:306/307 of query aligns to 2:292/293 of 5ud4A
- binding 1,6-di-O-phosphono-D-tagatose: S49 (= S50), D82 (= D82), Q166 (≠ H178), G167 (= G179), K170 (= K182), G197 (= G210), S199 (= S212), N239 (= N252), D241 (= D254), T242 (= T255), R245 (= R258)
- binding zinc ion: H83 (= H83), H83 (= H83), E134 (= E134), H196 (= H209), H196 (= H209)
3q94A The crystal structure of fructose 1,6-bisphosphate aldolase from bacillus anthracis str. 'Ames ancestor'
42% identity, 100% coverage: 1:307/307 of query aligns to 1:285/285 of 3q94A
- active site: D85 (= D82), H86 (= H83), E145 (= E142), H181 (= H178), H209 (= H209), N231 (= N252)
- binding zinc ion: H86 (= H83), E114 (≠ D111), H163 (≠ E160), H181 (= H178), H209 (= H209), E235 (≠ D256), E239 (≠ A260)
5ud0A Class ii fructose-1,6-bisphosphate aldolase e149a variant of helicobacter pylori with cleavage products (see paper)
41% identity, 99% coverage: 3:306/307 of query aligns to 2:281/282 of 5ud0A
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)
39% identity, 100% coverage: 1:306/307 of query aligns to 1:283/286 of P0AB74
- D82 (= D82) active site, Proton donor
- H83 (= H83) binding Zn(2+)
- H180 (= H178) binding Zn(2+)
- H208 (= H209) binding Zn(2+)
1gvfB Structure of tagatose-1,6-bisphosphate aldolase (see paper)
38% identity, 99% coverage: 3:306/307 of query aligns to 2:274/275 of 1gvfB
- active site: D81 (= D82), H82 (= H83), H171 (= H178), H199 (= H209), N221 (= N252)
- binding phosphoglycolohydroxamic acid: D81 (= D82), H82 (= H83), H171 (= H178), G172 (= G179), H199 (= H209), G200 (= G210), S202 (= S212), N221 (= N252), V222 (≠ I253), A223 (≠ D254), T224 (= T255)
- binding zinc ion: H82 (= H83), H171 (= H178), H199 (= H209)
Query Sequence
>WP_027722924.1 NCBI__GCF_000425265.1:WP_027722924.1
MPLVSPKEMFEGAYDGGYAIGAFNVNNMEIIQGIMEAGSEENAPLILQVSAGARKYAGQG
YIMKLMEAALLETDLPVVLHLDHGANFEICKEVIDGGFTSVMIDGSHLPFDENIALTQQV
VAYAHDKGVWVEAELGRLAGVEEDVVSDEHIYTDPDQAVEFVERTGCDSLAIAIGTSHGA
YKFKGEAKLDFDRLDKIASLIPKFPIVLHGASSVVQEYVVMANNFGADIGGAKGVPEDLL
RKAASKAVCKINIDTDIRLAMTAVIRKFLVENPAAFDPRGYLGESRKAVKEMVRHKITKV
LGCSNKA
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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