SitesBLAST
Comparing Synpcc7942_1791 FitnessBrowser__SynE:Synpcc7942_1791 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 13 hits to proteins with known functional sites (download)
7cdyA Crystal structure of glucose dehydrogenase
41% identity, 85% coverage: 58:405/411 of query aligns to 3:346/346 of 7cdyA
P75804 Aldose sugar dehydrogenase YliI; Asd; Soluble aldose sugar dehydrogenase YliI; EC 1.1.5.- from Escherichia coli (strain K12) (see paper)
40% identity, 85% coverage: 55:402/411 of query aligns to 24:367/371 of P75804
- Q82 (= Q113) binding
- E240 (= E278) binding
- Y250 (= Y288) binding
- Y261 (= Y299) binding
2g8sA Crystal structure of the soluble aldose sugar dehydrogenase (asd) from escherichia coli in the apo-form (see paper)
39% identity, 85% coverage: 55:402/411 of query aligns to 2:345/348 of 2g8sA
7cgzA Glucose dehydrogenase
40% identity, 85% coverage: 58:405/411 of query aligns to 3:321/321 of 7cgzA
2ismB Crystal structure of the putative oxidoreductase (glucose dehydrogenase) (ttha0570) from thermus theromophilus hb8
35% identity, 83% coverage: 56:398/411 of query aligns to 2:319/333 of 2ismB
3a9hA Crystal structure of pqq-dependent sugar dehydrogenase holo-form (see paper)
32% identity, 83% coverage: 56:398/411 of query aligns to 4:320/338 of 3a9hA
- active site: H120 (= H175), D139 (= D194), R182 (= R252), T224 (= T294), K226 (≠ S296), G228 (≠ T309)
- binding calcium ion: E208 (= E278), Y218 (= Y288)
- binding alpha-D-glucopyranose: G228 (≠ T309), R229 (≠ Q310), F232 (≠ M313), V233 (≠ I314), D234 (= D315)
- binding pyrroloquinoline quinone: E57 (≠ Q113), H120 (= H175), N183 (= N253), Q185 (= Q255), H201 (= H271), V204 (≠ R274), T243 (≠ A323), L269 (= L349), R270 (≠ V350), R298 (= R376), R300 (= R378), R320 (≠ K398)
3a9gA Crystal structure of pqq-dependent sugar dehydrogenase apo-form (see paper)
32% identity, 83% coverage: 56:398/411 of query aligns to 4:320/338 of 3a9gA
- active site: H120 (= H175), D139 (= D194), R182 (= R252), T224 (= T294), K226 (≠ S296), G228 (≠ T309)
- binding calcium ion: E208 (= E278), Y218 (= Y288)
- binding alpha-D-glucopyranose: R144 (≠ P199), D148 (≠ M213), G228 (≠ T309), R229 (≠ Q310), F232 (≠ M313), V233 (≠ I314), D234 (= D315)
1cq1A Soluble quinoprotein glucose dehydrogenase from acinetobacter calcoaceticus in complex with pqqh2 and glucose (see paper)
29% identity, 81% coverage: 61:393/411 of query aligns to 22:418/444 of 1cq1A
- active site: H138 (= H175), D157 (= D194), R222 (= R252), A263 (vs. gap), Y265 (vs. gap), D267 (vs. gap), E303 (≠ S296)
- binding beta-D-glucopyranose: D137 (≠ Q174), H138 (= H175), Q162 (≠ E201), Y337 (≠ H317)
- binding calcium ion: G241 (= G272), P242 (≠ S273), E247 (= E278), Y257 (= Y288), A263 (vs. gap), Y265 (vs. gap), D267 (vs. gap), E303 (≠ S296)
- binding pyrroloquinoline quinone: Q76 (= Q113), H138 (= H175), R222 (= R252), N223 (= N253), Q240 (≠ H271), Y337 (≠ H317), T342 (≠ A323), A344 (= A325), L370 (= L349), K371 (≠ V350), R400 (= R376), R402 (= R378)
1c9uA Crystal structure of the soluble quinoprotein glucose dehydrogenase in complex with pqq (see paper)
29% identity, 81% coverage: 61:393/411 of query aligns to 22:418/444 of 1c9uA
- active site: H138 (= H175), D157 (= D194), R222 (= R252), A263 (vs. gap), Y265 (vs. gap), D267 (vs. gap), E303 (≠ S296)
- binding calcium ion: R222 (= R252), G241 (= G272), P242 (≠ S273), E247 (= E278), Y257 (= Y288), A263 (vs. gap), Y265 (vs. gap), D267 (vs. gap), E303 (≠ S296)
- binding pyrroloquinoline quinone: Q76 (= Q113), H138 (= H175), R222 (= R252), N223 (= N253), Q240 (≠ H271), Y337 (≠ H317), W340 (= W320), T342 (≠ A323), L370 (= L349), K371 (≠ V350), R400 (= R376), R402 (= R378)
1cruA Soluble quinoprotein glucose dehydrogenase from acinetobacter calcoaceticus in complex with pqq and methylhydrazine (see paper)
29% identity, 81% coverage: 61:393/411 of query aligns to 22:422/448 of 1cruA
- active site: H142 (= H175), D161 (= D194), R226 (= R252), A267 (vs. gap), Y269 (vs. gap), D271 (vs. gap), E307 (≠ S296)
- binding calcium ion: G245 (= G272), P246 (≠ S273), E251 (= E278), Y261 (= Y288), A267 (vs. gap), Y269 (vs. gap), D271 (vs. gap), E307 (≠ S296)
- binding methylhydrazine: Y341 (≠ H317), W344 (= W320)
- binding pyrroloquinoline quinone: Q76 (= Q113), H142 (= H175), R226 (= R252), N227 (= N253), Q244 (≠ H271), Y341 (≠ H317), T346 (≠ A323), A348 (= A325), L374 (= L349), K375 (≠ V350), R404 (= R376), R406 (= R378)
P13650 Quinoprotein glucose dehydrogenase B; Glucose dehydrogenase B [pyrroloquinoline-quinone]; Soluble glucose dehydrogenase; s-GDH; EC 1.1.5.2 from Acinetobacter calcoaceticus (see paper)
28% identity, 81% coverage: 61:393/411 of query aligns to 46:448/478 of P13650
- Q100 (= Q113) binding
- D167 (≠ Q174) binding
- Q192 (≠ E201) binding
- R252 (= R252) binding
- G271 (= G272) binding
- P272 (≠ S273) binding
- E277 (= E278) binding
- Y287 (= Y288) binding
- A293 (vs. gap) binding
- Y295 (vs. gap) binding
- D297 (vs. gap) binding
- E333 (≠ S296) binding
- Y367 (≠ H317) binding
- T372 (≠ A323) binding
- K401 (≠ V350) binding
5minB Apo form of the soluble pqq-dependent glucose dehydrogenase from acinetobacter calcoaceticus
28% identity, 81% coverage: 61:393/411 of query aligns to 22:424/453 of 5minB
- active site: H144 (= H175), D163 (= D194), R228 (= R252), A269 (vs. gap), Y271 (vs. gap), D273 (vs. gap), E309 (≠ S296)
- binding calcium ion: E253 (= E278), Y263 (= Y288), A269 (vs. gap), Y271 (vs. gap), D273 (vs. gap), E309 (≠ S296)
3dasA Structure of the pqq-bound form of aldose sugar dehydrogenase (adh) from streptomyces coelicolor
30% identity, 82% coverage: 61:398/411 of query aligns to 14:318/334 of 3dasA
- active site: H127 (= H175), E146 (≠ D194), R189 (= R252), E230 (≠ T294), K232 (≠ S296), G234 (≠ T309)
- binding alpha-L-arabinopyranose: K199 (= K262), D248 (≠ P322), R268 (≠ V350), G269 (= G351), E270 (≠ R352), K278 (≠ S360), G279 (≠ P361)
- binding calcium ion: G208 (= G272), Q209 (≠ S273), E214 (= E278), Y224 (= Y288)
- binding pyrroloquinoline quinone: E66 (≠ Q113), H127 (= H175), R189 (= R252), N190 (= N253), Q192 (= Q255), F207 (≠ H271), S251 (≠ A325), R268 (≠ V350), R296 (= R376), R298 (= R378), R318 (≠ K398)
Query Sequence
>Synpcc7942_1791 FitnessBrowser__SynE:Synpcc7942_1791
MTFSTAATALIGLAIATGCASCSSASLPPTASAPVKTAAKPTALLVPESVPELTTVEVTP
LVEGLEHPWSLAWLPNGDLLITERPGRLRLVRQGKLEPTAIAGLPADLFAQGQGGLLDIA
VDPQFEQNRWVYFSYAAGTEAVNRVQVARGKLNGLRLENVEVIFTVRPDKSSAQHFGSRL
AWLPDRTLLIAIGDGGNPPVELNGRLIRHQAQMPESGLGKIHRINRDGSIPADNPFRNQP
KAQASLWSLGHRNIQGLAVDPKTGTVWSTEHGSRGGDELNQIKAGENYGWPEVTFSQEYW
GAEITPLRTQAGMIDPHLVWTPAIAPSGITVYRGTKVPDWQGKIFAGGLVGRDIRVIQLS
PEGQATNVSRIPIGARVRDVRQGPSGDLYVLTDESSGKLIRVRSTTASTQS
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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