SitesBLAST
Comparing N515DRAFT_3389 FitnessBrowser__Dyella79:N515DRAFT_3389 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)
Q60053 Neopullulanase 1; Alpha-amylase I; TVA I; EC 3.2.1.135 from Thermoactinomyces vulgaris (see paper)
70% identity, 98% coverage: 12:673/673 of query aligns to 2:666/666 of Q60053
- A31 (≠ S38) binding
- D33 (= D40) binding
- N35 (= N42) binding
- D71 (= D78) binding
- D125 (= D132) binding
- N174 (= N181) binding
- D176 (= D183) binding
- N179 (= N186) binding
- D180 (= D187) binding
- G216 (= G223) binding
- D218 (= D225) binding
- D305 (= D312) binding
- N309 (≠ W316) binding
- F310 (≠ W317) binding
- S312 (≠ T319) binding
- E317 (= E324) binding
1uh3A Thermoactinomyces vulgaris r-47 alpha-amylase/acarbose complex (see paper)
72% identity, 95% coverage: 37:673/673 of query aligns to 1:637/637 of 1uh3A
- active site: D262 (= D298), R354 (= R390), D356 (= D392), E396 (= E432), H471 (= H507), D472 (= D508)
- binding 6-amino-4-hydroxymethyl-cyclohex-4-ene-1,2,3-triol: N3 (= N39), I43 (≠ L79), T44 (= T80), Y223 (= Y259), H267 (= H303), F310 (= F346), D356 (= D392), E396 (= E432), H471 (= H507), D472 (= D508)
- binding calcium ion: A2 (≠ S38), D4 (= D40), N6 (= N42), D42 (= D78), D96 (= D132), N145 (= N181), D147 (= D183), N150 (= N186), D151 (= D187), G187 (= G223), D189 (= D225), D276 (= D312), N279 (= N315), F281 (≠ W317), S283 (≠ T319), E288 (= E324)
- binding alpha-D-glucopyranose: K40 (= K76), W51 (≠ Y87), W51 (≠ Y87), F58 (= F94), F58 (= F94), W65 (= W101), N68 (= N104), Y89 (= Y125), Y89 (= Y125), A115 (≠ S151), D116 (≠ G152), D117 (= D153), D117 (= D153), Y119 (= Y155), H221 (= H257), Y223 (= Y259), W485 (= W521), D516 (= D552), R520 (= R556), S587 (= S623), V588 (≠ T624), V588 (≠ T624), S589 (≠ A625), G629 (= G665)
- binding 4,6-dideoxy-alpha-D-xylo-hexopyranose: G41 (= G77), W65 (= W101), D75 (= D111), Y360 (= Y396), E396 (= E432), D418 (= D454), W448 (= W484), D472 (= D508)
- binding (1S,2S,3R,6R)-6-amino-4-(hydroxymethyl)cyclohex-4-ene-1,2,3-triol: N400 (= N436), N455 (= N491)
2d0fA Crystal structure of thermoactinomyces vulgaris r-47 alpha-amylase 1 (tvai) mutant d356n complexed with p2, a pullulan model oligosaccharide (see paper)
72% identity, 95% coverage: 37:673/673 of query aligns to 1:637/637 of 2d0fA
- active site: D262 (= D298), R354 (= R390), N356 (≠ D392), E396 (= E432), H471 (= H507), D472 (= D508)
- binding beta-D-glucopyranose: W65 (= W101), N68 (= N104), Y223 (= Y259), H267 (= H303), F310 (= F346), N356 (≠ D392), E396 (= E432), D472 (= D508)
- binding calcium ion: A2 (≠ S38), D4 (= D40), N6 (= N42), D42 (= D78), D96 (= D132), N145 (= N181), D147 (= D183), N150 (= N186), D151 (= D187), G187 (= G223), D189 (= D225), D276 (= D312), N279 (= N315), F281 (≠ W317), S283 (≠ T319), E288 (= E324)
- binding alpha-D-glucopyranose: G41 (= G77), W65 (= W101), D75 (= D111), D180 (≠ S216), S182 (≠ N218), S182 (≠ N218), H221 (= H257), H221 (= H257), Y223 (= Y259), S315 (≠ T351), D516 (= D552), R520 (= R556)
P38939 Amylopullulanase; Alpha-amylase/pullulanase; EC 3.2.1.1; EC 3.2.1.41 from Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium thermohydrosulfuricum) (see paper)
34% identity, 94% coverage: 40:671/673 of query aligns to 245:917/1481 of P38939
- D628 (= D392) mutation D->N,E: Loss of function.
- E657 (= E432) mutation E->Q,D: Loss of function.
- D734 (= D508) mutation D->Q,E: Loss of function.
3a6oA Crystal structure of thermoactinomyces vulgaris r-47 alpha- amylase 2/acarbose complex (see paper)
32% identity, 91% coverage: 62:671/673 of query aligns to 17:581/585 of 3a6oA
- active site: D239 (= D298), R323 (= R390), D325 (= D392), E354 (= E432), H420 (= H507), D421 (= D508)
- binding acarbose derived pentasaccharide: H164 (≠ N218), H202 (= H257), Y204 (= Y259), H244 (= H303), F286 (vs. gap), M293 (= M352), R323 (= R390), D325 (= D392), V326 (≠ A393), E354 (= E432), W356 (= W434), H420 (= H507), D421 (= D508), D465 (= D552), R469 (= R556)
- binding calcium ion: N143 (= N181), D145 (= D183), N148 (= N186), D149 (= D187), G169 (= G223), D171 (= D225)
Q08751 Neopullulanase 2; Alpha-amylase II; TVA II; EC 3.2.1.135 from Thermoactinomyces vulgaris (see paper)
32% identity, 91% coverage: 62:671/673 of query aligns to 17:581/585 of Q08751
- N143 (= N181) binding
- D145 (= D183) binding
- N148 (= N186) binding
- D149 (= D187) binding
- G169 (= G223) binding
- D171 (= D225) binding
P38940 Neopullulanase; EC 3.2.1.135 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
32% identity, 90% coverage: 65:671/673 of query aligns to 20:582/588 of P38940
- N147 (= N181) binding
- N149 (≠ D183) binding
- S153 (≠ D187) binding
- G172 (= G223) binding
- D174 (= D225) binding
1j0iA Crystal structure of neopullulanase complex with panose (see paper)
32% identity, 90% coverage: 65:671/673 of query aligns to 20:582/588 of 1j0iA
- active site: D242 (= D298), R326 (= R390), D328 (= D392), E357 (= E432), H423 (= H507), D424 (= D508)
- binding alpha-D-glucopyranose: Y207 (= Y259), Y207 (= Y259), H247 (= H303), F289 (= F346), M295 (= M352), D328 (= D392), E357 (= E432), H423 (= H507), D424 (= D508), D468 (= D552), R472 (= R556)
1j0hA Crystal structure of bacillus stearothermophilus neopullulanase (see paper)
32% identity, 90% coverage: 65:671/673 of query aligns to 20:582/588 of 1j0hA
- active site: D242 (= D298), R326 (= R390), D328 (= D392), E357 (= E432), H423 (= H507), D424 (= D508)
- binding calcium ion: N147 (= N181), N149 (≠ D183), P150 (≠ T184), S153 (≠ D187), G172 (= G223), D174 (= D225)
1gviB Thermus maltogenic amylase in complex with beta-cd (see paper)
31% identity, 90% coverage: 65:671/673 of query aligns to 20:582/588 of 1gviB
- active site: D242 (= D298), R326 (= R390), D328 (= D392), L357 (≠ E432), H423 (= H507), D424 (= D508)
- binding alpha-D-glucopyranose: Y45 (= Y87), W47 (≠ S89), H205 (= H257), Y207 (= Y259), H247 (= H303), F289 (= F346), F289 (= F346), D328 (= D392), W359 (= W434), Y377 (= Y453), H423 (= H507), D424 (= D508), D424 (= D508), R472 (= R556)
1g1yA Crystal structure of alpha-amylase ii (tvaii) from thermoactinomyces vulgaris r-47 and beta-cyclodextrin complex (see paper)
32% identity, 91% coverage: 62:671/673 of query aligns to 17:581/585 of 1g1yA
- active site: D239 (= D298), R323 (= R390), D325 (= D392), A354 (≠ E432), H420 (= H507), D421 (= D508)
- binding alpha-D-glucopyranose: H202 (= H257), Y204 (= Y259), F286 (vs. gap), F286 (vs. gap), M293 (= M352), M293 (= M352), V326 (≠ A393), W356 (= W434), D421 (= D508), D465 (= D552), R469 (= R556)
Q59226 Cyclomaltodextrinase; CDase; CDase I-5; Cyclomaltodextrin hydrolase, decycling; EC 3.2.1.135; EC 3.2.1.54 from Bacillus sp. (see paper)
33% identity, 84% coverage: 67:630/673 of query aligns to 22:543/558 of Q59226
- V380 (= V460) mutation to T: Decreased activity with beta-cyclodextrin as substrate, but an increase in starch hydrolyzing activity compared to the wild type. No effect in pullulan hydrolyzing activity.
- I388 (≠ S475) mutation to E: Decreased activity with starch as substrate, but an increase in beta-cyclodextrin hydrolyzing activity compared to the wild type. No effect in pullulan hydrolyzing activity.
7d9bA Crystal structure of alpha-glucosidase (see paper)
28% identity, 88% coverage: 63:654/673 of query aligns to 18:582/588 of 7d9bA
7dchA Alpha-glucosidase from weissella cibaria bbk-1 bound with acarbose (see paper)
27% identity, 88% coverage: 63:654/673 of query aligns to 18:582/588 of 7dchA
- binding 4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-alpha-D-glucopyranose: H213 (= H257), Y215 (= Y259), E295 (≠ S345), M311 (≠ G361), D483 (= D552), R487 (= R556)
- binding calcium ion: N154 (= N181), D156 (= D183), N159 (= N186), D160 (= D187), G180 (= G223), D182 (= D225)
- binding alpha-D-glucopyranose: Y215 (= Y259), H255 (= H303), F305 (≠ L355), F305 (≠ L355), D344 (= D392), V345 (≠ A393), Q373 (≠ E432), Q373 (≠ E432), H438 (= H507), D439 (= D508)
7d9cA Alpha-glucosidase from weissella cibaria bbk-1 bound with maltose (see paper)
27% identity, 88% coverage: 63:654/673 of query aligns to 18:582/588 of 7d9cA
- binding beta-D-glucopyranose: Y215 (= Y259), H255 (= H303), F305 (≠ L355), D344 (= D392), V345 (≠ A393), Q373 (≠ E432), H438 (= H507), D439 (= D508)
- binding calcium ion: N154 (= N181), D156 (= D183), N159 (= N186), D160 (= D187), G180 (= G223), D182 (= D225)
- binding alpha-D-glucopyranose: H213 (= H257), H213 (= H257), Y215 (= Y259), Y215 (= Y259), Y215 (= Y259), H255 (= H303), E295 (≠ S345), E295 (≠ S345), F305 (≠ L355), M311 (≠ G361), M311 (≠ G361), D344 (= D392), Q373 (≠ E432), H438 (= H507), D439 (= D508), D483 (= D552), D483 (= D552), R487 (= R556), R487 (= R556)
6a0kA Cyclic alpha-maltosyl-(1-->6)-maltose hydrolase from arthrobacter globiformis, complex with panose (see paper)
30% identity, 70% coverage: 163:631/673 of query aligns to 4:420/450 of 6a0kA
- active site: D116 (= D298), R199 (= R390), D201 (= D392), E230 (= E432), H296 (= H507), D297 (= D508)
- binding beta-D-glucopyranose: Y204 (≠ Q395), E231 (≠ F433), W232 (= W434)
- binding alpha-D-glucopyranose: H79 (= H257), Y81 (= Y259), Y81 (= Y259), H121 (= H303), C163 (≠ M352), S164 (≠ P353), R199 (= R390), D201 (= D392), Y204 (≠ Q395), F205 (≠ Y396), E230 (= E432), W232 (= W434), H296 (= H507), D297 (= D508), D341 (= D552), R345 (= R556)
5zxgA Cyclic alpha-maltosyl-(1-->6)-maltose hydrolase from arthrobacter globiformis, ligand-free form (see paper)
30% identity, 70% coverage: 163:631/673 of query aligns to 1:417/440 of 5zxgA
2z1kA Crystal structure of ttha1563 from thermus thermophilus hb8
30% identity, 74% coverage: 165:663/673 of query aligns to 2:462/474 of 2z1kA
- active site: D115 (= D298), R199 (= R390), D201 (= D392), E231 (= E432), H313 (= H507), D314 (= D508)
- binding alpha-D-glucopyranose: H78 (= H257), Y80 (= Y259), H81 (≠ D260), H120 (= H303), W163 (≠ F346), W163 (≠ F346), W164 (≠ Y347), W164 (≠ Y347), L169 (≠ M352), D201 (= D392), V202 (≠ A393), N204 (≠ Q395), E205 (≠ Y396), E205 (≠ Y396), E231 (= E432), E231 (= E432), W233 (= W434), T274 (vs. gap), G275 (vs. gap), H313 (= H507), D314 (= D508), R362 (= R556)
5ot1A The type iii pullulan hydrolase from thermococcus kodakarensis (see paper)
29% identity, 71% coverage: 113:592/673 of query aligns to 56:511/572 of 5ot1A
- active site: D234 (= D298), R317 (= R390), D319 (= D392), E350 (= E432), H416 (= H507), D417 (= D508)
- binding calcium ion: N119 (= N181), N121 (≠ D183), N124 (= N186), D125 (= D187), G164 (= G223), D166 (= D225)
P21543 Beta/alpha-amylase; EC 3.2.1.2; EC 3.2.1.1 from Paenibacillus polymyxa (Bacillus polymyxa) (see paper)
27% identity, 81% coverage: 122:663/673 of query aligns to 691:1186/1196 of P21543
Sites not aligning to the query:
- 118 modified: Disulfide link with 126; C→S: 5-fold decrease in activity.
- 126 modified: Disulfide link with 118; C→V: 20-fold decrease in activity.
- 358 C→S: 60-fold decrease in activity.
Query Sequence
>N515DRAFT_3389 FitnessBrowser__Dyella79:N515DRAFT_3389
MNRSTEAMHRSMRAVRGVALTALACALLALPWAAQAASNDNNVEWNGLFHDQGPLFVDHP
EPTSAQTVTLTFRSFKGDLTSANIKYYDSADGAFHWVAMHWASNDPTGTFDYWQGTVPAS
SSEKYYRFQLNDGSASAWYNAAGTSSSEPSSGDFYLIPGFKTPDWMKNGVIYQIFPDRFY
NGDTSNDVQTGQYSYGGQSTQKVAWGGSVFATGSGSNNLVFFGGDLAGVDQKLGYIKQTL
GANIVYLNPVFTSPTNHKYDTEDYYHVDPAFGSNTTLQTLIADVHASTNGPKGYVMLDGV
FNHTGDTSQWFDRYNWWSTQGAYESTSSTWYGYYTFQQWPGTYSSFYGYSTMPKLDYGAS
GSAVRNQIYGSTSSVVKTWLSSPYGIDGWRLDAPQYIDAGGNNGSDAINHQIMAELRTAV
KAVNANAEILGEFWGNANPWTGNGKEWDSALNYDGFTQPVSEWITGYDYSGNAASIPASQ
FDSWLHGTRANYPGNVQQTMANFLSSHDIQRFAQRAGGDIWKTYLALIFQMTYVGTPTIY
YGDEYGMQGGNDPDNRRTFDWTQGSTTNAAVALTQKLIAIRNQYAALRTGSFMSLLTDDS
NKLYAYGRFDASHRVAVALNNDSTAHSVTVPVWQLSMANGSAVTDLLSGNTYTVSGGNVV
VSVNGHYGAILAQ
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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