SitesBLAST
Comparing BWI76_RS06250 FitnessBrowser__Koxy:BWI76_RS06250 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)
32% identity, 95% coverage: 10:586/605 of query aligns to 52:634/666 of Q60053
- D71 (= D29) binding
- D125 (≠ W85) binding
- N174 (≠ R135) binding
- D176 (≠ Q137) binding
- N179 (≠ E140) binding
- D180 (≠ A141) binding
- G216 (= G176) binding
- D218 (= D178) binding
- D305 (= D260) binding
- N309 (≠ R264) binding
- F310 (vs. gap) binding
- S312 (= S266) binding
- E317 (≠ H271) binding
Sites not aligning to the query:
- 31 binding
- 33 binding
- 35 binding
1uh3A Thermoactinomyces vulgaris r-47 alpha-amylase/acarbose complex (see paper)
32% identity, 95% coverage: 10:586/605 of query aligns to 23:605/637 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: I43 (≠ D30), T44 (≠ L31), Y223 (= Y211), H267 (= H251), F310 (≠ W292), D356 (= D336), E396 (= E373), H471 (= H447), D472 (= D448)
- binding calcium ion: D42 (= D29), D96 (≠ W85), N145 (≠ R135), D147 (≠ Q137), N150 (≠ E140), D151 (≠ A141), G187 (= G176), D189 (= D178), D276 (= D260), N279 (≠ Q263), F281 (vs. gap), S283 (= S266), E288 (≠ H271)
- binding alpha-D-glucopyranose: K40 (≠ S27), W51 (≠ R38), W51 (≠ R38), F58 (≠ E45), F58 (≠ E45), W65 (≠ R52), N68 (≠ Q55), Y89 (≠ R78), Y89 (≠ R78), A115 (= A109), D116 (≠ V110), D117 (= D111), D117 (= D111), Y119 (vs. gap), 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: G41 (= G28), W65 (≠ R52), D75 (≠ V62), 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:
2d0fA Crystal structure of thermoactinomyces vulgaris r-47 alpha-amylase 1 (tvai) mutant d356n complexed with p2, a pullulan model oligosaccharide (see paper)
32% identity, 95% coverage: 10:586/605 of query aligns to 23:605/637 of 2d0fA
- active site: D262 (= D246), R354 (= R334), N356 (≠ D336), E396 (= E373), H471 (= H447), D472 (= D448)
- binding beta-D-glucopyranose: W65 (≠ R52), N68 (≠ Q55), Y223 (= Y211), H267 (= H251), F310 (≠ W292), N356 (≠ D336), E396 (= E373), D472 (= D448)
- binding calcium ion: D42 (= D29), D96 (≠ W85), N145 (≠ R135), D147 (≠ Q137), N150 (≠ E140), D151 (≠ A141), G187 (= G176), D189 (= D178), D276 (= D260), N279 (≠ Q263), F281 (vs. gap), S283 (= S266), E288 (≠ H271)
- binding alpha-D-glucopyranose: G41 (= G28), W65 (≠ R52), D75 (≠ V62), 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)
34% identity, 80% coverage: 76:562/605 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 (≠ K415) 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.
1j0iA Crystal structure of neopullulanase complex with panose (see paper)
32% identity, 80% coverage: 76:561/605 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 (≠ Y295), M295 (≠ L301), D328 (= D336), E357 (= E373), H423 (= H447), D424 (= D448), D468 (= D492), R472 (= R496)
1j0hA Crystal structure of bacillus stearothermophilus neopullulanase (see paper)
32% identity, 80% coverage: 76:561/605 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 (≠ Q137), P150 (≠ S138), S153 (≠ A141), G172 (= G176), D174 (= D178)
P38940 Neopullulanase; EC 3.2.1.135 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
32% identity, 80% coverage: 76:561/605 of query aligns to 81:539/588 of P38940
- N147 (≠ R135) binding
- N149 (≠ Q137) binding
- S153 (≠ A141) binding
- G172 (= G176) binding
- D174 (= D178) binding
1gviB Thermus maltogenic amylase in complex with beta-cd (see paper)
33% identity, 81% coverage: 76:565/605 of query aligns to 81:544/588 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 (≠ W292), F289 (≠ W292), D328 (= D336), W359 (≠ F375), Y377 (= Y393), H423 (= H447), D424 (= D448), D424 (= D448), R472 (= R496)
Sites not aligning to the query:
3a6oA Crystal structure of thermoactinomyces vulgaris r-47 alpha- amylase 2/acarbose complex (see paper)
34% identity, 75% coverage: 115:568/605 of query aligns to 123:544/585 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 (≠ Q137), N148 (≠ E140), D149 (= D162), G169 (= G176), D171 (= D178)
Q08751 Neopullulanase 2; Alpha-amylase II; TVA II; EC 3.2.1.135 from Thermoactinomyces vulgaris (see paper)
34% identity, 75% coverage: 115:568/605 of query aligns to 123:544/585 of Q08751
- N143 (≠ R135) binding
- D145 (≠ Q137) binding
- N148 (≠ E140) binding
- D149 (= D162) binding
- G169 (= G176) binding
- D171 (= 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)
30% identity, 89% coverage: 35:573/605 of query aligns to 275:883/1481 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.
1g1yA Crystal structure of alpha-amylase ii (tvaii) from thermoactinomyces vulgaris r-47 and beta-cyclodextrin complex (see paper)
34% identity, 75% coverage: 115:568/605 of query aligns to 123:544/585 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)
7d9bA Crystal structure of alpha-glucosidase (see paper)
31% identity, 83% coverage: 74:573/605 of query aligns to 81:565/588 of 7d9bA
7dchA Alpha-glucosidase from weissella cibaria bbk-1 bound with acarbose (see paper)
30% identity, 83% coverage: 74:573/605 of query aligns to 81:565/588 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 (vs. gap), M311 (≠ L298), D483 (= D492), R487 (= R496)
- binding calcium ion: N154 (≠ R135), D156 (≠ Q137), N159 (≠ G153), D160 (≠ H154), G180 (= G176), D182 (= D178)
- binding alpha-D-glucopyranose: Y215 (= Y211), H255 (= H251), F305 (≠ L293), F305 (≠ L293), 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)
30% identity, 83% coverage: 74:573/605 of query aligns to 81:565/588 of 7d9cA
- binding beta-D-glucopyranose: Y215 (= Y211), H255 (= H251), F305 (≠ L293), D344 (= D336), V345 (= V337), Q373 (≠ E373), H438 (= H447), D439 (= D448)
- binding calcium ion: N154 (≠ R135), D156 (≠ Q137), N159 (≠ G153), D160 (≠ H154), G180 (= G176), D182 (= D178)
- binding alpha-D-glucopyranose: H213 (= H209), H213 (= H209), Y215 (= Y211), Y215 (= Y211), Y215 (= Y211), H255 (= H251), E295 (vs. gap), E295 (vs. gap), F305 (≠ L293), M311 (≠ L298), M311 (≠ L298), D344 (= D336), Q373 (≠ E373), H438 (= H447), D439 (= D448), D483 (= D492), D483 (= D492), R487 (= R496), R487 (= R496)
2z1kA Crystal structure of ttha1563 from thermus thermophilus hb8
35% identity, 71% coverage: 119:546/605 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)
5ot1A The type iii pullulan hydrolase from thermococcus kodakarensis (see paper)
31% identity, 73% coverage: 118:556/605 of query aligns to 102:535/572 of 5ot1A
- active site: D234 (= D246), R317 (= R334), D319 (= D336), E350 (= E373), H416 (= H447), D417 (= D448)
- binding calcium ion: N119 (≠ R135), N121 (≠ S136), N124 (≠ R139), D125 (≠ E140), G164 (= G176), D166 (= D178)
6a0kA Cyclic alpha-maltosyl-(1-->6)-maltose hydrolase from arthrobacter globiformis, complex with panose (see paper)
31% identity, 76% coverage: 115:573/605 of query aligns to 2:422/450 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 (≠ L298), S164 (≠ P299), 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: 117:573/605 of query aligns to 1:419/440 of 5zxgA
5a2bA Crystal structure of anoxybacillus alpha-amylase provides insights into a new glycosyl hydrolase subclass (see paper)
27% identity, 66% coverage: 172:572/605 of query aligns to 34:410/452 of 5a2bA
- active site: D110 (= D246), R186 (= R334), D188 (= D336), E217 (= E373), H284 (= H447), D285 (= D448)
- binding calcium ion: G38 (= G176), D40 (= D178), N67 (≠ A205), E84 (≠ D220), N114 (= N250), E148 (≠ A289), D157 (≠ K300), H192 (= H353)
- binding alpha-D-glucopyranose: H73 (= H209), Y75 (= Y211), Y75 (= Y211), W76 (≠ D212), H115 (= H251), D188 (= D336), T189 (≠ V337), E217 (= E373), H284 (= H447), D285 (= D448), D333 (= D492), R337 (= R496)
Sites not aligning to the query:
Query Sequence
>BWI76_RS06250 FitnessBrowser__Koxy:BWI76_RS06250
MLKAWHLPVAPFIKEQQERLMITLWLSGDDLPPRVTLRAEEDNEELSLPMHRLRQAPHPG
VVAWRGEINLVNGQPRRRYSFKLLWADRQLWFTPQGFNRFPPARLEQFAVDLPDSGPQWV
ADQVFYQIFPDRFARSQSREAEQDATYYHHAAGHDIVRKAWDEPLTAEAGGSTFYGGDLD
GISEKLPYLKQLGVTALYLNPVFVAPSVHKYDTEDYRRVDPQFGGDAALLRLRHNTQKEG
MRLILDGVFNHSGDSHAWFDRHQRGSGGACHNADSPWRDWYNFSPEGVAHDWLGYASLPK
LDYRSSTLIDEIYGGEDSVVRHWLKAPWSMDGWRLDVVHMLGEGGGARNNLRHIAGITQA
AKLERPDAFVFGEHFGDARQWLQADVEDSAMNYRGFTFPLWGFLANTDISYDPQKIDAQT
CMAWMDNYRAGLSHQQQLRMFNQLDSHDTARFKSLLGKDVARLPLAVVWLFSWPGVPCIY
YGDEVGVDGNNDPFCRKPFPWDPALQDGDLLDLYKRMSKLRKAHQALRYGGCQVIYAEDN
VVVFVRVYKQQRVLVAINRGEACEVVIEDSPLLDVNGWQLKEGAGALHDGVLTLPAISAS
VWFSR
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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