SitesBLAST
Comparing Ga0059261_1581 FitnessBrowser__Korea:Ga0059261_1581 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)
P21543 Beta/alpha-amylase; EC 3.2.1.2; EC 3.2.1.1 from Paenibacillus polymyxa (Bacillus polymyxa) (see paper)
28% identity, 94% coverage: 23:589/604 of query aligns to 737:1186/1196 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.
6wniA Crystal structure of clda, the first cyclomaltodextrin glucanotransferase with a three-domain abc distribution
29% identity, 88% coverage: 30:563/604 of query aligns to 1:447/494 of 6wniA
- active site: D126 (= D156), R219 (= R297), D221 (= D299), E250 (= E333), H321 (= H404), D322 (= D405)
- binding calcium ion: N17 (= N46), D19 (= D48), N22 (= N51), D23 (= D52), G44 (= G75), D46 (= D77), D72 (≠ K103), N73 (= N104), N75 (vs. gap), E100 (≠ D130), E101 (≠ P131), N130 (= N160), Q182 (≠ G261), D191 (= D268), H225 (= H303)
6saoA Structural and functional characterisation of three novel fungal amylases with enhanced stability and ph tolerance (see paper)
25% identity, 94% coverage: 21:589/604 of query aligns to 1:427/438 of 6saoA
- binding 4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-alpha-D-glucopyranose: Y74 (= Y121), W75 (= W122), H114 (= H161), A154 (≠ N240), D190 (= D299), T191 (= T300), H194 (= H303), E214 (= E333), F216 (≠ A335), Q279 (≠ H404), D280 (= D405), D323 (= D459)
- binding beta-D-glucopyranose: F216 (≠ A335), D217 (≠ E337), G218 (= G338), Y240 (≠ A362)
- binding calcium ion: N113 (= N160), E149 (≠ V235), D159 (= D268), H194 (= H303)
- binding alpha-D-glucopyranose: H72 (= H119), Y74 (= Y121), W75 (= W122), K193 (≠ R302), F216 (≠ A335), D323 (= D459), R327 (= R463)
P43379 Cyclomaltodextrin glucanotransferase; Cyclodextrin-glycosyltransferase; CGTase; EC 2.4.1.19 from Niallia circulans (Bacillus circulans) (see 3 papers)
28% identity, 86% coverage: 3:522/604 of query aligns to 10:439/713 of P43379
- C70 (≠ T62) modified: Disulfide link with 77
- C77 (≠ H74) modified: Disulfide link with 70
- D256 (= D299) mutation to N: Reduces activity 23000-fold. Reduces activity 520000-fold; when associated with N-355.
- E284 (= E333) mutation to Q: Reduces activity 4100-fold.
- D355 (= D405) mutation to N: Reduces activity 56000-fold. Reduces activity 520000-fold; when associated with N-256.
Sites not aligning to the query:
9cgtA Structure of cyclodextrin glycosyltransferase complexed with a thio- maltopentaose (see paper)
26% identity, 83% coverage: 24:522/604 of query aligns to 5:412/684 of 9cgtA
- active site: D135 (= D156), R227 (= R297), D229 (= D299), A257 (≠ F328), H327 (= H404), D328 (= D405)
- binding 4-thio-alpha-D-glucopyranose: K47 (≠ D66), Y89 (≠ G110), W101 (= W122), D196 (≠ G265), H327 (= H404), D328 (= D405)
- binding calcium ion: D27 (≠ N46), N29 (≠ D48), N32 (= N51), N33 (≠ D52), G51 (= G75), D53 (= D77), N139 (= N160), I190 (≠ T259), D199 (= D268), H233 (= H303)
- binding alpha-D-glucopyranose: Y100 (= Y121), W101 (= W122), R375 (= R463)
- binding 1-thio-alpha-D-glucopyranose: H233 (= H303), F259 (≠ I330), D328 (= D405)
8cgtA Structure of cyclodextrin glycosyltransferase complexed with a thio- maltohexaose (see paper)
26% identity, 83% coverage: 24:522/604 of query aligns to 5:412/684 of 8cgtA
- active site: D135 (= D156), R227 (= R297), D229 (= D299), A257 (≠ F328), H327 (= H404), D328 (= D405)
- binding 4-thio-alpha-D-glucopyranose: K47 (≠ D66), Y89 (≠ G110), N94 (≠ T115), W101 (= W122), D196 (≠ G265), L197 (= L266), D328 (= D405)
- binding calcium ion: D27 (≠ N46), N29 (≠ D48), N32 (= N51), N33 (≠ D52), G51 (= G75), D53 (= D77), N139 (= N160), I190 (≠ T259), D199 (= D268), H233 (= H303)
- binding alpha-D-glucopyranose: Y100 (= Y121), W101 (= W122), H233 (= H303), F259 (≠ I330), D328 (= D405), D371 (= D459), R375 (= R463)
1cgtA Structure of cyclodextrin glycosyltransferase refined at 2.0 angstroms resolution (see paper)
26% identity, 83% coverage: 24:522/604 of query aligns to 5:412/684 of 1cgtA
- active site: D135 (= D156), R227 (= R297), D229 (= D299), E257 (≠ F328), H327 (= H404), D328 (= D405)
- binding calcium ion: D27 (≠ N46), N29 (≠ D48), N32 (= N51), N33 (≠ D52), G51 (= G75), D53 (= D77), N139 (= N160), I190 (≠ T259), D199 (= D268), H233 (= H303)
6cgtA Hoxa complex of cyclodextrin glycosyltransferase mutant (see paper)
26% identity, 83% coverage: 24:522/604 of query aligns to 5:412/684 of 6cgtA
- active site: D135 (= D156), R227 (= R297), D229 (= D299), E257 (≠ F328), H327 (= H404), D328 (= D405)
- binding calcium ion: D27 (≠ N46), N29 (≠ D48), N32 (= N51), N33 (≠ D52), G51 (= G75), D53 (= D77), N139 (= N160), I190 (≠ T259), D199 (= D268), H233 (= H303)
- binding 4-amino-4,6-dideoxy-beta-D-glucopyranose: Y89 (≠ G110), Y195 (≠ V264), A230 (≠ T300), H233 (= H303), E257 (≠ F328), D328 (= D405), D371 (= D459)
- binding alpha-D-glucopyranose: W101 (= W122), K232 (≠ R302), F259 (≠ I330), D371 (= D459), R375 (= R463)
- binding oxiranpseudoglucose: Y100 (= Y121), H140 (= H161), D229 (= D299), E257 (≠ F328), H327 (= H404), D328 (= D405)
1ukqA Crystal structure of cyclodextrin glucanotransferase complexed with a pseudo-maltotetraose derived from acarbose (see paper)
28% identity, 81% coverage: 32:522/604 of query aligns to 13:412/686 of 1ukqA
- active site: D135 (= D156), R227 (= R297), D229 (= D299), E257 (= E333), H327 (= H404), D328 (= D405)
- binding 6-amino-4-hydroxymethyl-cyclohex-4-ene-1,2,3-triol: Y100 (= Y121), H140 (= H161), D229 (= D299), E257 (= E333), H327 (= H404), D328 (= D405)
- binding beta-D-glucopyranose: F259 (≠ A335), D328 (= D405)
- binding calcium ion: D27 (≠ N46), N29 (≠ D48), N32 (= N51), N33 (≠ D52), G51 (= G75), D53 (= D77), N139 (= N160), I190 (≠ T259), D199 (= D268), H233 (= H303)
- binding alpha-D-quinovopyranose: E257 (= E333), F259 (≠ A335)
- binding alpha-D-glucopyranose: Y100 (= Y121), W101 (= W122), D371 (= D459), R375 (= R463)
1i75A Crystal structure of cyclodextrin glucanotransferase from alkalophilic bacillus sp.#1011 complexed with 1-deoxynojirimycin (see paper)
28% identity, 81% coverage: 32:522/604 of query aligns to 13:412/686 of 1i75A
- active site: D135 (= D156), R227 (= R297), D229 (= D299), E257 (= E333), H327 (= H404), D328 (= D405)
- binding calcium ion: D27 (≠ N46), N29 (≠ D48), N32 (= N51), N33 (≠ D52), G51 (= G75), D53 (= D77), N139 (= N160), I190 (≠ T259), D199 (= D268), H233 (= H303)
- binding 1-deoxynojirimycin: Y100 (= Y121), L194 (≠ F263), D229 (= D299)
Sites not aligning to the query:
1cygA Cyclodextrin glucanotransferase (E.C.2.4.1.19) (cgtase)
28% identity, 86% coverage: 33:553/604 of query aligns to 11:435/680 of 1cygA
- active site: D131 (= D156), R223 (= R297), D225 (= D299), E253 (≠ I330), H323 (= H404), D324 (= D405)
- binding calcium ion: D24 (≠ N46), N26 (≠ D48), T27 (≠ P49), N29 (= N51), N30 (≠ D52), G48 (= G75), D50 (= D77), N135 (= N160), I186 (≠ T259), D195 (= D268), H229 (= H303)
1uksA Crystal structure of f183l/f259l mutant cyclodextrin glucanotransferase complexed with a pseudo-maltotetraose derived from acarbose (see paper)
28% identity, 81% coverage: 32:522/604 of query aligns to 13:412/686 of 1uksA
- active site: D135 (= D156), R227 (= R297), D229 (= D299), E257 (= E333), H327 (= H404), D328 (= D405)
- binding 6-amino-4-hydroxymethyl-cyclohex-4-ene-1,2,3-triol: W101 (= W122), Y195 (≠ V264), L197 (= L266)
- binding calcium ion: D27 (≠ N46), N29 (≠ D48), N32 (= N51), N33 (≠ D52), G51 (= G75), D53 (= D77), N139 (= N160), I190 (≠ T259), D199 (= D268), H233 (= H303)
- binding beta-D-galactopyranose: A230 (≠ T300), K232 (≠ R302), H233 (= H303), E257 (= E333), L259 (≠ A335)
- binding alpha-D-glucopyranose: N94 (≠ T115), D196 (≠ G265)
- binding 4,6-dideoxy-alpha-D-xylo-hexopyranose: D229 (= D299), H327 (= H404), D328 (= D405)
5cgtA Maltotriose complex of preconditioned cyclodextrin glycosyltransferase mutant (see paper)
26% identity, 83% coverage: 24:522/604 of query aligns to 5:412/684 of 5cgtA
- active site: D135 (= D156), R227 (= R297), A229 (≠ D299), E257 (≠ F328), H327 (= H404), D328 (= D405)
- binding beta-D-glucopyranose: Y100 (= Y121), H140 (= H161), A229 (≠ D299), E257 (≠ F328), H327 (= H404), D328 (= D405)
- binding calcium ion: D27 (≠ N46), N29 (≠ D48), N32 (= N51), N33 (≠ D52), G51 (= G75), D53 (= D77), N139 (= N160), I190 (≠ T259), D199 (= D268), H233 (= H303)
- binding alpha-D-glucopyranose: Y100 (= Y121), W101 (= W122), Y195 (≠ V264), H233 (= H303), E257 (≠ F328), D371 (= D459), R375 (= R463)
Sites not aligning to the query:
1cguA Catalytic center of cyclodextrin glycosyltransferase derived from x- ray structure analysis combined with site-directed mutagenesis (see paper)
26% identity, 83% coverage: 24:522/604 of query aligns to 5:412/684 of 1cguA
- active site: D135 (= D156), R227 (= R297), A229 (≠ D299), E257 (≠ F328), H327 (= H404), D328 (= D405)
- binding calcium ion: D27 (≠ N46), N29 (≠ D48), N32 (= N51), N33 (≠ D52), G51 (= G75), D53 (= D77), N139 (= N160), I190 (≠ T259), D199 (= D268), H233 (= H303)
- binding alpha-D-glucopyranose: Y100 (= Y121), Y100 (= Y121), W101 (= W122), H140 (= H161), E257 (≠ F328), H327 (= H404), D328 (= D405), D371 (= D459), R375 (= R463)
1dedA Crystal structure of alkalophilic asparagine 233-replaced cyclodextrin glucanotransferase complexed with an inhibitor, acarbose, at 2.0 a resolution (see paper)
28% identity, 81% coverage: 32:522/604 of query aligns to 13:412/686 of 1dedA
- active site: D135 (= D156), R227 (= R297), D229 (= D299), E257 (= E333), H327 (= H404), D328 (= D405)
- binding 4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-alpha-D-glucopyranose: H98 (= H119), Y100 (= Y121), W101 (= W122), L197 (= L266), D229 (= D299), H327 (= H404), D328 (= D405), D371 (= D459), R375 (= R463)
- binding calcium ion: D27 (≠ N46), N29 (≠ D48), N32 (= N51), N33 (≠ D52), G51 (= G75), D53 (= D77), N139 (= N160), I190 (≠ T259), D199 (= D268), N233 (≠ H303)
- binding alpha-D-glucopyranose: L194 (≠ F263), Y195 (≠ V264), N233 (≠ H303), E257 (= E333)
Sites not aligning to the query:
- binding 4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-alpha-D-glucopyranose: 662, 663, 664, 686
- binding beta-D-glucopyranose: 616, 651, 662, 667
1d7fA Crystal structure of asparagine 233-replaced cyclodextrin glucanotransferase from alkalophilic bacillus sp. 1011 determined at 1.9 a resolution (see paper)
28% identity, 81% coverage: 32:522/604 of query aligns to 13:412/686 of 1d7fA
- active site: D135 (= D156), R227 (= R297), D229 (= D299), E257 (= E333), H327 (= H404), D328 (= D405)
- binding calcium ion: D27 (≠ N46), N29 (≠ D48), N32 (= N51), N33 (≠ D52), G51 (= G75), D53 (= D77), N139 (= N160), I190 (≠ T259), D199 (= D268), N233 (≠ H303)
P25718 Periplasmic alpha-amylase; 1,4-alpha-D-glucan glucanohydrolase; EC 3.2.1.1 from Escherichia coli (strain K12) (see 2 papers)
28% identity, 85% coverage: 10:521/604 of query aligns to 170:650/676 of P25718
- C537 (≠ M376) 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)
28% identity, 85% coverage: 10:521/604 of query aligns to 51:531/557 of 8im8A
1dtuA Bacillus circulans strain 251 cyclodextrin glycosyltransferase: a mutant y89d/s146p complexed to an hexasaccharide inhibitor (see paper)
28% identity, 81% coverage: 32:522/604 of query aligns to 13:412/686 of 1dtuA
- active site: D135 (= D156), R227 (= R297), D229 (= D299), E257 (= E333), H327 (= H404), D328 (= D405)
- binding 1-amino-2,3-dihydroxy-5-hydroxymethyl cyclohex-5-ene: Y100 (= Y121), H140 (= H161), D229 (= D299), E257 (= E333), H327 (= H404), D328 (= D405)
- binding calcium ion: D27 (≠ N46), N29 (≠ D48), N32 (= N51), N33 (≠ D52), G51 (= G75), D53 (= D77), N139 (= N160), I190 (≠ T259), D199 (= D268), H233 (= H303)
- binding alpha-D-quinovopyranose: A230 (≠ T300), H233 (= H303), E257 (= E333), D328 (= D405)
- binding alpha-D-glucopyranose: Y100 (= Y121), W101 (= W122), K232 (≠ R302), F259 (≠ A335), D371 (= D459), R375 (= R463), E411 (≠ T521), R412 (= R522)
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
2cxgA Cyclodextrin glycosyltransferase complexed to the inhibitor acarbose (see paper)
28% identity, 81% coverage: 32:522/604 of query aligns to 13:412/686 of 2cxgA
- active site: D135 (= D156), R227 (= R297), D229 (= D299), E257 (= E333), H327 (= H404), D328 (= D405)
- binding 6-amino-4-hydroxymethyl-cyclohex-4-ene-1,2,3-triol: Y100 (= Y121), H140 (= H161), D229 (= D299), E257 (= E333), H327 (= H404), D328 (= D405)
- binding calcium ion: D27 (≠ N46), N29 (≠ D48), N32 (= N51), N33 (≠ D52), G51 (= G75), D53 (= D77), N139 (= N160), I190 (≠ T259), D199 (= D268), H233 (= H303)
- binding alpha-D-quinovopyranose: A230 (≠ T300), H233 (= H303), E257 (= E333), D328 (= D405)
- binding alpha-D-glucopyranose: Y100 (= Y121), W101 (= W122), L197 (= L266), K232 (≠ R302), F259 (≠ A335), D371 (= D459), R375 (= R463), E411 (≠ T521), R412 (= R522)
Sites not aligning to the query:
- binding alpha-D-glucopyranose: 413, 414, 446, 598, 599, 600, 600, 601, 602, 603, 616, 627, 633, 636, 651, 662, 667
Query Sequence
>Ga0059261_1581 FitnessBrowser__Korea:Ga0059261_1581
MRSLAFALTLLAGTVASAQTAAPAELRARAAETEVLYFLLPDRFENGDPSNDRGGLRGDR
LTTGFDPAHKGFFHGGDLKGLIRRLDYIQSLGASAIWLGPIYKNKPVQGGPGQETAGYHG
YWITDFTRVDPHFGTNDEMKAFVDAAHARGIKVYLDIITNHTADVIQYRECPKSACDYRS
RADYPYQRKGGVKGAAINPGFAGDGVQTPENFAKLSDPNYAYTTVVPEAERTVKVPAWLN
DPIHYHNRGNTTFRNESSTMGDFVGLDDLMTESPRVLQGFIDIYGAWIDQFGIDGFRIDT
ARHVNPEFWQGFSKAMIERAKARGIPNFHIFGEVANEGDVGDLALHTRVHQLPSVLDFGF
RAAVQHTVAGEKGPDMLAAMFDRDALYEGGAEAALRLPTFISNHDHGRFSTDVRKAFPKA
SDDEVLARVKLAHAMLLLLRGVPTIYSGDEQGFVSDGNDQDAREDMFPSKVAIYNDNRLL
GTDKTTADSNFDTGHPLYMEISKLSAIRKATPALSRGRQVTRAYDEKPGLFAVSRFDPAS
GAEVLVAFNTSAAPITRQVEVGVSSTAFAPLVGQCAASASAPGSVTVTLPAFGYVACVAA
GGAK
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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