SitesBLAST
Comparing 14541 FitnessBrowser__Keio:14541 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
34% identity, 91% coverage: 42:591/604 of query aligns to 84:640/666 of Q60053
- D125 (≠ W85) binding
- N174 (≠ R135) binding
- D176 (≠ L137) binding
- N179 (≠ E140) binding
- D180 (≠ A141) binding
- G216 (= G176) binding
- D218 (= D178) binding
- D305 (= D260) binding
- N309 (≠ R264) binding
- F310 (vs. gap) binding
- S312 (≠ T266) binding
- E317 (≠ H271) binding
Sites not aligning to the query:
- 31 binding
- 33 binding
- 35 binding
- 71 binding
1uh3A Thermoactinomyces vulgaris r-47 alpha-amylase/acarbose complex (see paper)
34% identity, 91% coverage: 42:593/604 of query aligns to 55:613/637 of 1uh3A
- active site: D262 (= D246), R354 (= R334), D356 (= D336), E396 (= E373), H471 (= H447), D472 (= D448)
- binding 6-amino-4-hydroxymethyl-cyclohex-4-ene-1,2,3-triol: Y223 (= Y211), H267 (= H251), F310 (≠ W292), D356 (= D336), E396 (= E373), H471 (= H447), D472 (= D448)
- binding calcium ion: D96 (≠ W85), N145 (≠ R135), D147 (≠ L137), N150 (≠ E140), D151 (≠ A141), G187 (= G176), D189 (= D178), D276 (= D260), N279 (= N263), F281 (vs. gap), S283 (≠ T266), E288 (≠ H271)
- binding alpha-D-glucopyranose: F58 (≠ E45), F58 (≠ E45), W65 (≠ K52), N68 (≠ S55), Y89 (≠ R78), Y89 (≠ R78), A115 (≠ L105), D116 (≠ E106), D117 (≠ Q107), D117 (≠ Q107), Y119 (≠ A109), H221 (= H209), Y223 (= Y211), W485 (≠ A461), D516 (= D492), R520 (= R496), S587 (≠ E561), V588 (≠ A562), V588 (≠ A562), S589 (≠ C563)
- binding 4,6-dideoxy-alpha-D-xylo-hexopyranose: W65 (≠ K52), D75 (≠ T62), Y360 (≠ M340), E396 (= E373), D418 (≠ R394), W448 (= W424), D472 (= D448)
- binding (1S,2S,3R,6R)-6-amino-4-(hydroxymethyl)cyclohex-4-ene-1,2,3-triol: N400 (≠ D377), N455 (≠ G431)
Sites not aligning to the query:
- binding 6-amino-4-hydroxymethyl-cyclohex-4-ene-1,2,3-triol: 3, 43, 44
- binding calcium ion: 2, 4, 6, 42
- binding alpha-D-glucopyranose: 40, 51, 51, 629
- binding 4,6-dideoxy-alpha-D-xylo-hexopyranose: 41
2d0fA Crystal structure of thermoactinomyces vulgaris r-47 alpha-amylase 1 (tvai) mutant d356n complexed with p2, a pullulan model oligosaccharide (see paper)
34% identity, 91% coverage: 42:593/604 of query aligns to 55:613/637 of 2d0fA
- active site: D262 (= D246), R354 (= R334), N356 (≠ D336), E396 (= E373), H471 (= H447), D472 (= D448)
- binding beta-D-glucopyranose: W65 (≠ K52), N68 (≠ S55), Y223 (= Y211), H267 (= H251), F310 (≠ W292), N356 (≠ D336), E396 (= E373), D472 (= D448)
- binding calcium ion: D96 (≠ W85), N145 (≠ R135), D147 (≠ L137), N150 (≠ E140), D151 (≠ A141), G187 (= G176), D189 (= D178), D276 (= D260), N279 (= N263), F281 (vs. gap), S283 (≠ T266), E288 (≠ H271)
- binding alpha-D-glucopyranose: W65 (≠ K52), D75 (≠ T62), D180 (vs. gap), S182 (≠ G171), S182 (≠ G171), H221 (= H209), H221 (= H209), Y223 (= Y211), S315 (= S297), D516 (= D492), R520 (= R496)
Sites not aligning to the query:
Q59226 Cyclomaltodextrinase; CDase; CDase I-5; Cyclomaltodextrin hydrolase, decycling; EC 3.2.1.135; EC 3.2.1.54 from Bacillus sp. (see paper)
36% identity, 81% coverage: 76:562/604 of query aligns to 78:537/558 of Q59226
- V380 (≠ L400) 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 (≠ Q415) 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.
3a6oA Crystal structure of thermoactinomyces vulgaris r-47 alpha- amylase 2/acarbose complex (see paper)
35% identity, 75% coverage: 117:567/604 of query aligns to 125:543/585 of 3a6oA
- active site: D239 (= D246), R323 (= R334), D325 (= D336), E354 (= E373), H420 (= H447), D421 (= D448)
- binding acarbose derived pentasaccharide: H164 (≠ G171), H202 (= H209), Y204 (= Y211), H244 (= H251), F286 (≠ Y295), M293 (≠ L298), R323 (= R334), D325 (= D336), V326 (= V337), E354 (= E373), W356 (≠ F375), H420 (= H447), D421 (= D448), D465 (= D492), R469 (= R496)
- binding calcium ion: N143 (≠ R135), D145 (≠ L137), N148 (≠ H149), D149 (≠ H150), G169 (= G176), D171 (= D178)
Q08751 Neopullulanase 2; Alpha-amylase II; TVA II; EC 3.2.1.135 from Thermoactinomyces vulgaris (see paper)
35% identity, 75% coverage: 117:567/604 of query aligns to 125:543/585 of Q08751
- N143 (≠ R135) binding
- D145 (≠ L137) binding
- N148 (≠ H149) binding
- D149 (≠ H150) binding
- G169 (= G176) binding
- D171 (= D178) binding
1g1yA Crystal structure of alpha-amylase ii (tvaii) from thermoactinomyces vulgaris r-47 and beta-cyclodextrin complex (see paper)
35% identity, 75% coverage: 117:567/604 of query aligns to 125:543/585 of 1g1yA
- active site: D239 (= D246), R323 (= R334), D325 (= D336), A354 (≠ E373), H420 (= H447), D421 (= D448)
- binding alpha-D-glucopyranose: H202 (= H209), Y204 (= Y211), F286 (≠ Y295), F286 (≠ Y295), M293 (≠ L298), M293 (≠ L298), V326 (= V337), W356 (≠ F375), D421 (= D448), D465 (= D492), R469 (= R496)
1gviB Thermus maltogenic amylase in complex with beta-cd (see paper)
33% identity, 82% coverage: 76:568/604 of query aligns to 81:547/588 of 1gviB
- active site: D242 (= D246), R326 (= R334), D328 (= D336), L357 (≠ E373), H423 (= H447), D424 (= D448)
- binding alpha-D-glucopyranose: H205 (= H209), Y207 (= Y211), H247 (= H251), F289 (≠ E306), F289 (≠ E306), D328 (= D336), W359 (≠ F375), Y377 (= Y393), H423 (= H447), D424 (= D448), D424 (= D448), R472 (= R496)
Sites not aligning to the query:
1j0iA Crystal structure of neopullulanase complex with panose (see paper)
33% identity, 80% coverage: 76:561/604 of query aligns to 81:539/588 of 1j0iA
- active site: D242 (= D246), R326 (= R334), D328 (= D336), E357 (= E373), H423 (= H447), D424 (= D448)
- binding alpha-D-glucopyranose: Y207 (= Y211), Y207 (= Y211), H247 (= H251), F289 (≠ L293), M295 (≠ L298), D328 (= D336), E357 (= E373), H423 (= H447), D424 (= D448), D468 (= D492), R472 (= R496)
1j0hA Crystal structure of bacillus stearothermophilus neopullulanase (see paper)
33% identity, 80% coverage: 76:561/604 of query aligns to 81:539/588 of 1j0hA
- active site: D242 (= D246), R326 (= R334), D328 (= D336), E357 (= E373), H423 (= H447), D424 (= D448)
- binding calcium ion: N147 (≠ R135), N149 (≠ L137), P150 (= P138), S153 (≠ A141), G172 (= G176), D174 (= D178)
P38940 Neopullulanase; EC 3.2.1.135 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
33% identity, 80% coverage: 76:561/604 of query aligns to 81:539/588 of P38940
- N147 (≠ R135) binding
- N149 (≠ L137) binding
- S153 (≠ A141) binding
- G172 (= G176) binding
- D174 (= D178) binding
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)
31% identity, 87% coverage: 48:573/604 of query aligns to 304:883/1481 of P38939
- D628 (= D336) mutation D->N,E: Loss of function.
- E657 (= E373) mutation E->Q,D: Loss of function.
- D734 (= D448) mutation D->Q,E: Loss of function.
7d9bA Crystal structure of alpha-glucosidase (see paper)
29% identity, 94% coverage: 13:581/604 of query aligns to 27:574/588 of 7d9bA
7dchA Alpha-glucosidase from weissella cibaria bbk-1 bound with acarbose (see paper)
29% identity, 94% coverage: 13:581/604 of query aligns to 27:574/588 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 (= H209), Y215 (= Y211), E295 (≠ S282), M311 (≠ L298), D483 (= D492), R487 (= R496)
- binding calcium ion: N154 (≠ R135), D156 (≠ H150), N159 (≠ G153), D160 (≠ Q154), G180 (= G176), D182 (= D178)
- binding alpha-D-glucopyranose: Y215 (= Y211), H255 (= H251), F305 (≠ W292), F305 (≠ W292), D344 (= D336), V345 (= V337), Q373 (≠ E373), Q373 (≠ E373), H438 (= H447), D439 (= D448)
7d9cA Alpha-glucosidase from weissella cibaria bbk-1 bound with maltose (see paper)
29% identity, 94% coverage: 13:581/604 of query aligns to 27:574/588 of 7d9cA
- binding beta-D-glucopyranose: Y215 (= Y211), H255 (= H251), F305 (≠ W292), D344 (= D336), V345 (= V337), Q373 (≠ E373), H438 (= H447), D439 (= D448)
- binding calcium ion: N154 (≠ R135), D156 (≠ H150), N159 (≠ G153), D160 (≠ Q154), G180 (= G176), D182 (= D178)
- binding alpha-D-glucopyranose: H213 (= H209), H213 (= H209), Y215 (= Y211), Y215 (= Y211), Y215 (= Y211), H255 (= H251), E295 (≠ S282), E295 (≠ S282), F305 (≠ W292), M311 (≠ L298), M311 (≠ L298), D344 (= D336), Q373 (≠ E373), H438 (= H447), D439 (= D448), D483 (= D492), D483 (= D492), R487 (= R496), R487 (= R496)
5ot1A The type iii pullulan hydrolase from thermococcus kodakarensis (see paper)
30% identity, 75% coverage: 118:568/604 of query aligns to 102:547/572 of 5ot1A
- active site: D234 (= D246), R317 (= R334), D319 (= D336), E350 (= E373), H416 (= H447), D417 (= D448)
- binding calcium ion: N119 (≠ R135), N121 (≠ L137), N124 (≠ E140), D125 (vs. gap), G164 (= G176), D166 (= D178)
6a0kA Cyclic alpha-maltosyl-(1-->6)-maltose hydrolase from arthrobacter globiformis, complex with panose (see paper)
31% identity, 76% coverage: 117:573/604 of query aligns to 4:422/450 of 6a0kA
- active site: D116 (= D246), R199 (= R334), D201 (= D336), E230 (= E373), H296 (= H447), D297 (= D448)
- binding beta-D-glucopyranose: Y204 (≠ H339), E231 (≠ H374), W232 (≠ F375)
- binding alpha-D-glucopyranose: H79 (= H209), Y81 (= Y211), Y81 (= Y211), H121 (= H251), C163 (≠ E306), S164 (= S307), R199 (= R334), D201 (= D336), Y204 (≠ H339), F205 (≠ M340), E230 (= E373), W232 (≠ F375), H296 (= H447), D297 (= D448), D341 (= D492), R345 (= R496)
5zxgA Cyclic alpha-maltosyl-(1-->6)-maltose hydrolase from arthrobacter globiformis, ligand-free form (see paper)
31% identity, 76% coverage: 117:573/604 of query aligns to 1:419/440 of 5zxgA
2z1kA Crystal structure of ttha1563 from thermus thermophilus hb8
34% identity, 71% coverage: 119:546/604 of query aligns to 2:412/474 of 2z1kA
- active site: D115 (= D246), R199 (= R334), D201 (= D336), E231 (= E373), H313 (= H447), D314 (= D448)
- binding alpha-D-glucopyranose: H78 (= H209), Y80 (= Y211), H81 (≠ D212), H120 (= H251), W163 (= W292), W163 (= W292), W164 (≠ L293), W164 (≠ L293), L169 (= L298), D201 (= D336), V202 (= V337), N204 (≠ H339), E205 (≠ M340), E205 (≠ M340), E231 (= E373), E231 (= E373), W233 (≠ F375), T274 (= T420), G275 (≠ C421), H313 (= H447), D314 (= D448), R362 (= R496)
4e2oA Crystal structure of alpha-amylase from geobacillus thermoleovorans, gta, complexed with acarbose (see paper)
29% identity, 65% coverage: 174:566/604 of query aligns to 30:398/445 of 4e2oA
- active site: D104 (= D246), R180 (= R334), D182 (= D336), E211 (= E373), H278 (= H447), D279 (= D448)
- binding 6-amino-4-hydroxymethyl-cyclohex-4-ene-1,2,3-triol: Y69 (= Y211), H109 (= H251), D182 (= D336), E211 (= E373), H278 (= H447), D279 (= D448)
- binding beta-D-glucopyranose: W135 (= W280), Y147 (≠ A296), R185 (≠ H339), W213 (≠ F375)
- binding calcium ion: N108 (= N250), E142 (≠ D291), D151 (≠ K300), H186 (≠ M340)
- binding alpha-D-quinovopyranose: T183 (≠ V337), H186 (≠ M340), E211 (= E373)
- binding alpha-D-glucopyranose: W70 (≠ D212), L149 (= L298), D327 (= D492), R331 (= R496)
Query Sequence
>14541 FitnessBrowser__Keio:14541
MLNAWHLPVPPFVKQSKDQLLITLWLTGEDPPQRIMLRTEHDNEEMSVPMHKQRSQPQPG
VTAWRAAIDLSSGQPRRRYSFKLLWHDRQRWFTPQGFSRMPPARLEQFAVDVPDIGPQWA
ADQIFYQIFPDRFARSLPREAEQDHVYYHHAAGQEIILRDWDEPVTAQAGGSTFYGGDLD
GISEKLPYLKKLGVTALYLNPVFKAPSVHKYDTEDYRHVDPQFGGDGALLRLRHNTQQLG
MRLVLDGVFNHSGDSHAWFDRHNRGTGGACHNPESPWRDWYSFSDDGTALDWLGYASLPK
LDYQSESLVNEIYRGEDSIVRHWLKAPWNMDGWRLDVVHMLGEAGGARNNMQHVAGITEA
AKETQPEAYIVGEHFGDARQWLQADVEDAAMNYRGFTFPLWGFLANTDISYDPQQIDAQT
CMAWMDNYRAGLSHQQQLRMFNQLDSHDTARFKTLLGRDIARLPLAVVWLFTWPGVPCIY
YGDEVGLDGKNDPFCRKPFPWQVEKQDTALFALYQRMIALRKKSQALRHGGCQVLYAEDN
VVVFVRVLNQQRVLVAINRGEACEVVLPASPFLNAVQWQCKEGHGQLTDGILALPAISAT
VWMN
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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