SitesBLAST
Comparing CCNA_02369 FitnessBrowser__Caulo:CCNA_02369 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)
4e2oA Crystal structure of alpha-amylase from geobacillus thermoleovorans, gta, complexed with acarbose (see paper)
30% identity, 85% coverage: 38:553/604 of query aligns to 1:394/445 of 4e2oA
- active site: D104 (= D166), R180 (= R301), D182 (= D303), E211 (= E337), H278 (= H407), D279 (= D408)
- binding 6-amino-4-hydroxymethyl-cyclohex-4-ene-1,2,3-triol: Y69 (= Y131), H109 (= H171), D182 (= D303), E211 (= E337), H278 (= H407), D279 (= D408)
- binding beta-D-glucopyranose: W135 (≠ G213), Y147 (= Y226), R185 (= R306), W213 (≠ F339)
- binding calcium ion: N108 (= N170), E142 (≠ K220), D151 (= D266), H186 (= H307)
- binding alpha-D-quinovopyranose: T183 (= T304), H186 (= H307), E211 (= E337)
- binding alpha-D-glucopyranose: W70 (= W132), L149 (= L264), D327 (= D461), R331 (= R481)
P21543 Beta/alpha-amylase; EC 3.2.1.2; EC 3.2.1.1 from Paenibacillus polymyxa (Bacillus polymyxa) (see paper)
28% identity, 84% coverage: 44:552/604 of query aligns to 747:1146/1196 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.
7d9bA Crystal structure of alpha-glucosidase (see paper)
26% identity, 93% coverage: 43:603/604 of query aligns to 141:588/588 of 7d9bA
7dchA Alpha-glucosidase from weissella cibaria bbk-1 bound with acarbose (see paper)
25% identity, 93% coverage: 43:603/604 of query aligns to 141:588/588 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 (= H129), Y215 (= Y131), E295 (≠ D215), M311 (≠ V230), D483 (= D461), R487 (≠ S465)
- binding calcium ion: N154 (= N56), D156 (= D58), N159 (= N61), D160 (= D62), G180 (= G85), D182 (= D87)
- binding alpha-D-glucopyranose: Y215 (= Y131), H255 (= H171), F305 (≠ W224), F305 (≠ W224), D344 (= D303), V345 (≠ T304), Q373 (≠ E337), Q373 (≠ E337), H438 (= H407), D439 (= D408)
7d9cA Alpha-glucosidase from weissella cibaria bbk-1 bound with maltose (see paper)
25% identity, 93% coverage: 43:603/604 of query aligns to 141:588/588 of 7d9cA
- binding beta-D-glucopyranose: Y215 (= Y131), H255 (= H171), F305 (≠ W224), D344 (= D303), V345 (≠ T304), Q373 (≠ E337), H438 (= H407), D439 (= D408)
- binding calcium ion: N154 (= N56), D156 (= D58), N159 (= N61), D160 (= D62), G180 (= G85), D182 (= D87)
- binding alpha-D-glucopyranose: H213 (= H129), H213 (= H129), Y215 (= Y131), Y215 (= Y131), Y215 (= Y131), H255 (= H171), E295 (≠ D215), E295 (≠ D215), F305 (≠ W224), M311 (≠ V230), M311 (≠ V230), D344 (= D303), Q373 (≠ E337), H438 (= H407), D439 (= D408), D483 (= D461), D483 (= D461), R487 (≠ S465), R487 (≠ S465)
6wniA Crystal structure of clda, the first cyclomaltodextrin glucanotransferase with a three-domain abc distribution
28% identity, 88% coverage: 41:570/604 of query aligns to 2:453/494 of 6wniA
- active site: D126 (= D166), R219 (= R301), D221 (= D303), E250 (= E337), H321 (= H407), D322 (= D408)
- binding calcium ion: N17 (= N56), D19 (= D58), N22 (= N61), D23 (= D62), G44 (= G85), D46 (= D87), D72 (≠ V113), N73 (= N114), N75 (≠ Q118), E100 (≠ D140), E101 (≠ P141), N130 (= N170), Q182 (vs. gap), D191 (≠ T269), H225 (= H307)
9cgtA Structure of cyclodextrin glycosyltransferase complexed with a thio- maltopentaose (see paper)
27% identity, 82% coverage: 33:525/604 of query aligns to 2:412/684 of 9cgtA
- active site: D135 (= D166), R227 (= R301), D229 (= D303), A257 (≠ N331), H327 (= H407), D328 (= D408)
- binding 4-thio-alpha-D-glucopyranose: K47 (≠ D76), Y89 (≠ P120), W101 (= W132), D196 (≠ T269), H327 (= H407), D328 (= D408)
- binding calcium ion: D27 (≠ N56), N29 (≠ D58), N32 (= N61), N33 (≠ D62), G51 (= G85), D53 (= D87), N139 (= N170), I190 (≠ L263), D199 (≠ G272), H233 (= H307)
- binding alpha-D-glucopyranose: Y100 (= Y131), W101 (= W132), R375 (= R481)
- binding 1-thio-alpha-D-glucopyranose: H233 (= H307), F259 (≠ H333), D328 (= D408)
8cgtA Structure of cyclodextrin glycosyltransferase complexed with a thio- maltohexaose (see paper)
27% identity, 82% coverage: 33:525/604 of query aligns to 2:412/684 of 8cgtA
- active site: D135 (= D166), R227 (= R301), D229 (= D303), A257 (≠ N331), H327 (= H407), D328 (= D408)
- binding 4-thio-alpha-D-glucopyranose: K47 (≠ D76), Y89 (≠ P120), N94 (≠ S125), W101 (= W132), D196 (≠ T269), L197 (= L270), D328 (= D408)
- binding calcium ion: D27 (≠ N56), N29 (≠ D58), N32 (= N61), N33 (≠ D62), G51 (= G85), D53 (= D87), N139 (= N170), I190 (≠ L263), D199 (≠ G272), H233 (= H307)
- binding alpha-D-glucopyranose: Y100 (= Y131), W101 (= W132), H233 (= H307), F259 (≠ H333), D328 (= D408), D371 (= D461), R375 (= R481)
6cgtA Hoxa complex of cyclodextrin glycosyltransferase mutant (see paper)
29% identity, 82% coverage: 33:525/604 of query aligns to 2:412/684 of 6cgtA
- active site: D135 (= D166), R227 (= R301), D229 (= D303), E257 (= E337), H327 (= H407), D328 (= D408)
- binding calcium ion: D27 (≠ N56), N29 (≠ D58), N32 (= N61), N33 (≠ D62), G51 (= G85), D53 (= D87), N139 (= N170), I190 (≠ Y248), D199 (= D266), H233 (= H307)
- binding 4-amino-4,6-dideoxy-beta-D-glucopyranose: Y89 (≠ P120), Y195 (≠ G253), A230 (≠ T304), H233 (= H307), E257 (= E337), D328 (= D408), D371 (= D461)
- binding alpha-D-glucopyranose: W101 (= W132), K232 (≠ R306), F259 (= F339), D371 (= D461), R375 (= R481)
- binding oxiranpseudoglucose: Y100 (= Y131), H140 (= H171), D229 (= D303), E257 (= E337), H327 (= H407), D328 (= D408)
5cgtA Maltotriose complex of preconditioned cyclodextrin glycosyltransferase mutant (see paper)
28% identity, 82% coverage: 33:525/604 of query aligns to 2:412/684 of 5cgtA
- active site: D135 (= D166), R227 (= R301), A229 (≠ D303), E257 (= E337), H327 (= H407), D328 (= D408)
- binding beta-D-glucopyranose: Y100 (= Y131), H140 (= H171), A229 (≠ D303), E257 (= E337), H327 (= H407), D328 (= D408)
- binding calcium ion: D27 (≠ N56), N29 (≠ D58), N32 (= N61), N33 (≠ D62), G51 (= G85), D53 (= D87), N139 (= N170), I190 (≠ L263), D199 (≠ G272), H233 (= H307)
- binding alpha-D-glucopyranose: Y100 (= Y131), W101 (= W132), Y195 (≠ A268), H233 (= H307), E257 (= E337), D371 (= D461), R375 (= R481)
Sites not aligning to the query:
P43379 Cyclomaltodextrin glucanotransferase; Cyclodextrin-glycosyltransferase; CGTase; EC 2.4.1.19 from Niallia circulans (Bacillus circulans) (see 3 papers)
27% identity, 86% coverage: 9:525/604 of query aligns to 2:439/713 of P43379
- C70 (≠ A72) modified: Disulfide link with 77
- C77 (≠ H84) modified: Disulfide link with 70
- D256 (= D303) mutation to N: Reduces activity 23000-fold. Reduces activity 520000-fold; when associated with N-355.
- E284 (= E337) mutation to Q: Reduces activity 4100-fold.
- D355 (= D408) mutation to N: Reduces activity 56000-fold. Reduces activity 520000-fold; when associated with N-256.
Sites not aligning to the query:
3a6oA Crystal structure of thermoactinomyces vulgaris r-47 alpha- amylase 2/acarbose complex (see paper)
27% identity, 92% coverage: 42:597/604 of query aligns to 129:580/585 of 3a6oA
- active site: D239 (= D166), R323 (= R301), D325 (= D303), E354 (= E337), H420 (= H407), D421 (= D408)
- binding acarbose derived pentasaccharide: H164 (≠ R79), H202 (= H129), Y204 (= Y131), H244 (= H171), F286 (= F257), M293 (≠ L270), R323 (= R301), D325 (= D303), V326 (≠ T304), E354 (= E337), W356 (≠ F339), H420 (= H407), D421 (= D408), D465 (= D461), R469 (= R466)
- binding calcium ion: N143 (= N56), D145 (= D58), N148 (= N61), D149 (= D62), G169 (= G85), D171 (= D87)
Q08751 Neopullulanase 2; Alpha-amylase II; TVA II; EC 3.2.1.135 from Thermoactinomyces vulgaris (see paper)
27% identity, 92% coverage: 42:597/604 of query aligns to 129:580/585 of Q08751
- N143 (= N56) binding
- D145 (= D58) binding
- N148 (= N61) binding
- D149 (= D62) binding
- G169 (= G85) binding
- D171 (= D87) binding
P25718 Periplasmic alpha-amylase; 1,4-alpha-D-glucan glucanohydrolase; EC 3.2.1.1 from Escherichia coli (strain K12) (see 2 papers)
27% identity, 84% coverage: 42:549/604 of query aligns to 187:672/676 of P25718
- C537 (≠ R379) modified: Disulfide link with 121
Sites not aligning to the query:
- 1:17 signal peptide
- 57 modified: Disulfide link with 75
- 75 modified: Disulfide link with 57
- 121 modified: Disulfide link with 537
8im8A Crystal structure of periplasmic alpha-amylase (mals) from e.Coli (see paper)
27% identity, 84% coverage: 45:549/604 of query aligns to 71:553/557 of 8im8A
1qhoA Five-domain alpha-amylase from bacillus stearothermophilus, maltose/acarbose complex (see paper)
26% identity, 80% coverage: 44:525/604 of query aligns to 9:413/686 of 1qhoA
- active site: D127 (= D166), R226 (= R301), D228 (= D303), E256 (= E337), H328 (= H407), D329 (= D408)
- binding 4-amino-4,6-dideoxy-alpha-D-glucopyranose: A229 (≠ T304), H232 (= H307), E256 (= E337), D329 (= D408)
- binding beta-D-glucopyranose: Y258 (≠ F339), G259 (≠ D340), D261 (= D342)
- binding calcium ion: D21 (≠ N56), D23 (= D58), N26 (= N61), N27 (≠ D62), G48 (= G85), D50 (= D87), D76 (≠ V113), N77 (= N114), D79 (≠ Q118), E101 (≠ D140), E102 (≠ P141), N131 (= N170), Q184 (≠ A241), D198 (= D266), H232 (= H307)
- binding alpha-D-glucopyranose: Y92 (= Y131), Y92 (= Y131), W93 (= W132), H132 (= H171), T189 (vs. gap), D190 (= D245), D190 (= D245), P191 (= P246), D228 (= D303), K231 (≠ R306), E256 (= E337), Y258 (≠ F339), H328 (= H407), D329 (= D408), D372 (= D461), D372 (= D461), R376 (≠ K488), Q412 (≠ T524), R413 (= R525)
Sites not aligning to the query:
1g1yA Crystal structure of alpha-amylase ii (tvaii) from thermoactinomyces vulgaris r-47 and beta-cyclodextrin complex (see paper)
27% identity, 92% coverage: 42:597/604 of query aligns to 129:580/585 of 1g1yA
- active site: D239 (= D166), R323 (= R301), D325 (= D303), A354 (≠ E337), H420 (= H407), D421 (= D408)
- binding alpha-D-glucopyranose: H202 (= H129), Y204 (= Y131), F286 (= F257), F286 (= F257), M293 (≠ L270), M293 (≠ L270), V326 (≠ T304), W356 (≠ F339), D421 (= D408), D465 (= D461), R469 (= R466)
P19531 Maltogenic alpha-amylase; Glucan 1,4-alpha-maltohydrolase; EC 3.2.1.133 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
26% identity, 80% coverage: 44:525/604 of query aligns to 42:446/719 of P19531
- D54 (≠ N56) binding
- D56 (= D58) binding
- N59 (= N61) binding
- N60 (≠ D62) binding
- G81 (= G85) binding
- D83 (= D87) binding
- D109 (≠ V113) binding
- N110 (= N114) binding
- D112 (≠ Q118) binding
- E134 (≠ D140) binding
- E135 (≠ P141) binding
- N164 (= N170) binding
- Q217 (≠ A241) binding
- D231 (= D266) binding
- H265 (= H307) binding
Sites not aligning to the query:
6aijA Cyclodextrin glycosyltransferase from paenibacillus macerans mutant n603d
27% identity, 86% coverage: 32:550/604 of query aligns to 1:436/687 of 6aijA
- active site: R227 (= R301), D229 (= D303), E258 (= E337), H328 (= H407), D329 (= D408)
- binding calcium ion: D27 (≠ N56), D29 (= D58), N32 (= N61), N33 (≠ D62), G51 (= G85), D53 (= D87), N139 (= N170), I190 (≠ L263), D199 (≠ G272), H233 (= H307), D264 (≠ V343), E292 (≠ D369), E299 (≠ D378)
1dtuA Bacillus circulans strain 251 cyclodextrin glycosyltransferase: a mutant y89d/s146p complexed to an hexasaccharide inhibitor (see paper)
27% identity, 82% coverage: 32:525/604 of query aligns to 1:412/686 of 1dtuA
- active site: D135 (= D166), R227 (= R301), D229 (= D303), E257 (= E337), H327 (= H407), D328 (= D408)
- binding 1-amino-2,3-dihydroxy-5-hydroxymethyl cyclohex-5-ene: Y100 (= Y131), H140 (= H171), D229 (= D303), E257 (= E337), H327 (= H407), D328 (= D408)
- binding calcium ion: D27 (≠ N56), N29 (≠ D58), N32 (= N61), N33 (≠ D62), G51 (= G85), D53 (= D87), N139 (= N170), I190 (≠ L263), D199 (≠ G272), H233 (= H307)
- binding alpha-D-quinovopyranose: A230 (≠ T304), H233 (= H307), E257 (= E337), D328 (= D408)
- binding alpha-D-glucopyranose: Y100 (= Y131), W101 (= W132), K232 (≠ R306), F259 (= F339), D371 (= D461), R375 (= R481), E411 (≠ T524), R412 (= R525)
Sites not aligning to the query:
- binding alpha-D-glucopyranose: 413, 414, 446, 598, 599, 600, 600, 601, 602, 603, 616, 627, 633, 651, 662, 667
Query Sequence
>CCNA_02369 FitnessBrowser__Caulo:CCNA_02369
MSALTPWRRTLLAMTAVSALGMDAMTTAAAAAPDPYLQRKPQDEVIYFVLPDRFENGDAT
NDHGGPALGALADGFDPARAGFYHGGDLKGVTRRLDYIQGLGATAVWLAPIFVNRAVQGP
PGQESAAHHGYWITDFTDVDPHLGTKADFKALVDAAHARGMKVYMDIVLNHTADVIQYKE
CPDNRCAYRGVSDYPYVRRGGVDGAPINDGFDGKDFSKLKRPDWAYTPYVPPGQERAKTP
AWLNDPIYYHNRGDSTFAGESSLLGDFATLDGVFTEHPRVVEGFIEVYGRWIDDFGIDGY
RIDTARHVNPEFWQAFVPAMLARAKAKGIENFHIFGEVFDADVATLARHVKVDKLPTVLD
FAFQAAVTDVALGRAGPDRLASVFAGDVVYEGGEATARQLPTFLGNHDMGRIGHFVLKAH
PKIGDDALLARITLANAIMLTARGVPTIYYGDEQGFTGDGDYADSREDMFPSQVASYNDN
RLVGSSAKGPRTAFQTDSVLYRRIAALAKLRGMTPALREGRQVTRIAEGKPGLLAFSRLM
AGTEVLAVFNTSDKPIKARVPVEMGSAAWKSLHGACISSAVAPGSYAVELAPFDYMICVS
EGRS
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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