SitesBLAST
Comparing 15319 FitnessBrowser__Keio:15319 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 12 hits to proteins with known functional sites (download)
2jjbA Family 37 trehalase from escherichia coli in complex with casuarine-6- o-alpha-glucopyranose (see paper)
98% identity, 91% coverage: 35:546/565 of query aligns to 1:504/504 of 2jjbA
- binding casuarine: F113 (= F153), Y117 (= Y157), W119 (= W159), D120 (= D160), Q167 (= Q207), G270 (= G310), D272 (= D312), W407 (= W447), Y470 (= Y512), F476 (= F518), W478 (= W520)
- binding alpha-D-glucopyranose: R112 (= R152), F113 (= F153), Y117 (= Y157), N156 (= N196), Y162 (= Y202), R165 (= R205), R237 (= R277), E239 (= E279), S240 (= S280), A267 (= A307), D272 (= D312), Y470 (= Y512)
2jg0A Family 37 trehalase from escherichia coli in complex with 1- thiatrehazolin (see paper)
99% identity, 90% coverage: 37:547/565 of query aligns to 1:507/507 of 2jg0A
- binding N-[(3aS,4R,5S,6S,6aS)-4,5,6-trihydroxy-4-(hydroxymethyl)-4,5,6,6a-tetrahydro-3aH-cyclopenta[d][1,3]thiazol-2-yl]-alpha- D-glucopyranosylamine: R112 (= R152), F113 (= F153), Y117 (= Y157), W119 (= W159), D120 (= D160), N156 (= N196), Y162 (= Y202), R165 (= R205), Q167 (= Q207), R237 (= R277), E239 (= E279), S240 (= S280), A267 (= A307), G270 (= G310), D272 (= D312), W407 (= W447), W413 (= W453), E471 (= E511), Y472 (= Y512), F478 (= F518), W480 (= W520)
2wynA Structure of family 37 trehalase from escherichia coli in complex with a casuarine-6-o-a-d-glucoside analogue (see paper)
99% identity, 91% coverage: 35:546/565 of query aligns to 1:506/506 of 2wynA
- binding alpha-D-glucopyranose: R112 (= R152), F113 (= F153), Y117 (= Y157), N156 (= N196), Y162 (= Y202), R165 (= R205), R237 (= R277), E239 (= E279), A267 (= A307), D272 (= D312), Y472 (= Y512)
- binding (1r,2r,3r,6r,7r,7ar)-3,7-bis(hydroxymethyl)hexahydro-1h-pyrrolizine-1,2,6-triol: P109 (= P149), F113 (= F153), Y117 (= Y157), W119 (= W159), D120 (= D160), Q167 (= Q207), G270 (= G310), D272 (= D312), Q406 (= Q446), W407 (= W447), Y472 (= Y512), F478 (= F518), W480 (= W520)
2jf4A Family 37 trehalase from escherichia coli in complex with validoxylamine (see paper)
98% identity, 90% coverage: 37:547/565 of query aligns to 1:500/500 of 2jf4A
- binding (1s,2s,3r,6s)-4-(hydroxymethyl)-6-{[(1s,2s,3s,4r,5r)-2,3,4-trihydroxy-5-(hydroxymethyl)cyclohexyl]amino}cyclohex-4-ene-1,2,3-triol: P102 (= P149), R105 (= R152), F106 (= F153), Y110 (= Y157), W112 (= W159), D113 (= D160), N149 (= N196), Y155 (= Y202), R158 (= R205), Q160 (= Q207), R230 (= R277), E232 (= E279), S233 (= S280), A260 (= A307), G263 (= G310), D265 (= D312), Q399 (= Q446), W400 (= W447), E464 (= E511), Y465 (= Y512), F471 (= F518), W473 (= W520)
5z66A Structure of periplasmic trehalase from diamondback moth gut bacteria complexed with validoxylamine (see paper)
82% identity, 89% coverage: 40:543/565 of query aligns to 6:509/512 of 5z66A
- binding (1s,2s,3r,6s)-4-(hydroxymethyl)-6-{[(1s,2s,3s,4r,5r)-2,3,4-trihydroxy-5-(hydroxymethyl)cyclohexyl]amino}cyclohex-4-ene-1,2,3-triol: P116 (= P149), R119 (= R152), F120 (= F153), Y124 (= Y157), W126 (= W159), D127 (= D160), N163 (= N196), Y169 (= Y202), R172 (= R205), Q174 (= Q207), R243 (= R277), E245 (= E279), S246 (= S280), A273 (= A307), G276 (= G310), D278 (= D312), Q412 (= Q446), W413 (= W447), E477 (= E511), Y478 (= Y512), F484 (= F518), W486 (= W520)
Q9W2M2 Trehalase; Alpha,alpha-trehalase; Alpha,alpha-trehalose glucohydrolase; EC 3.2.1.28 from Drosophila melanogaster (Fruit fly) (see paper)
34% identity, 86% coverage: 45:529/565 of query aligns to 59:574/596 of Q9W2M2
- N451 (≠ A415) modified: carbohydrate, N-linked (GlcNAc...) asparagine
7eawA Trehalase of arabidopsis thaliana acid mutant -d380a trehalose complex
36% identity, 79% coverage: 86:530/565 of query aligns to 78:540/560 of 7eawA
- binding alpha-D-glucopyranose: P147 (= P149), R150 (= R152), F151 (= F153), F151 (= F153), Y155 (= Y157), Y155 (= Y157), W157 (= W159), D158 (= D160), N194 (= N196), Y200 (= Y202), R203 (= R205), Q205 (= Q207), R270 (= R277), E272 (= E279), S273 (= S280), A301 (= A307), Q453 (= Q446), W460 (= W453), E506 (= E496), E521 (= E511), Y522 (= Y512), Y522 (= Y512), F528 (= F518), W530 (= W520)
5n6nC Crystal structure of the 14-3-3:neutral trehalase nth1 complex (see paper)
30% identity, 67% coverage: 145:523/565 of query aligns to 253:658/698 of 5n6nC
- binding beta-D-fructofuranose: F261 (= F153), Y265 (= Y157), N297 (≠ D189), H298 (≠ T190), Y299 (= Y191), G300 (= G192), K351 (≠ Q253), D425 (≠ L324), G527 (≠ N412), Q570 (= Q446), S590 (≠ N466), Y591 (= Y467)
- binding alpha-D-glucopyranose: P257 (= P149), Y265 (= Y157), W267 (= W159), D268 (= D160), N297 (≠ D189), H298 (≠ T190), Q315 (= Q207), G423 (≠ Q322), D425 (≠ L324), Q487 (= Q372), G527 (≠ N412), A529 (= A414), T530 (≠ A415), K531 (= K416), W571 (= W447), W655 (= W520)
Sites not aligning to the query:
P32356 Cytosolic neutral trehalase; Alpha,alpha-trehalase; Alpha,alpha-trehalose glucohydrolase; EC 3.2.1.28 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
30% identity, 67% coverage: 145:523/565 of query aligns to 295:711/751 of P32356
- WD 309:310 (= WD 159:160) binding
- N346 (= N196) binding
- RSQ 355:357 (= RSQ 205:207) binding
- E424 (= E279) binding
- R473 (≠ A307) binding
- S475 (= S309) mutation to A: Abolishes activity; when associated with A-20; A-21; A-58; A-60; A-83; A-135; A-149 and A-260.
- G476 (= G310) binding
- D478 (= D312) mutation to A: Abolishes catalytic activity.
- E674 (= E496) mutation to A: Abolishes catalytic activity.
- R686 (vs. gap) mutation to A: Decreases catalytic activity.
- E690 (vs. gap) mutation to A: Severely decreases catalytic activity.
- Y691 (vs. gap) mutation to A: Abolishes catalytic activity.
Sites not aligning to the query:
- 20 modified: Phosphoserine; by PKA; S→A: Abolishes activity; when associated with A-21; A-58; A-60; A-83; A-135; A-149; A-260 and A-475. Abolishes activation by BMH1 and BMH2; when associated with A-21; A-60 and A-83.
- 21 modified: Phosphoserine; by PKA; S→A: Abolishes activity; when associated with A-20; A-58; A-60; A-83; A-135; A-149; A-260 and A-475. Abolishes activation by BMH1 and BMH2; when associated with A-20; A-60 and A-83.
- 55 BMH1 binding
- 58 T→A: Abolishes activity; when associated with A-20; A-21; A-60; A-83; A-135; A-149; A-260 and A-475.
- 60 modified: Phosphoserine; by PKA; S→A: Abolishes activity; when associated with A-20; A-21; A-58; A-83; A-135; A-149; A-260 and A-475. Abolishes activation by BMH1 and BMH2; when associated with A-20; A-21 and A-83.
- 83 modified: Phosphoserine; by PKA; S→A: Abolishes activity; when associated with A-20; A-21; A-58; A-60; A-135; A-149; A-260 and A-475. Abolishes activation by BMH1 and BMH2; when associated with A-20; A-21 and A-60.
- 114 binding
- 116 binding
- 118 binding
- 120 binding ; Q→A: Decreases catalytic activity.
- 125 binding
- 135 T→A: Abolishes activity; when associated with A-20; A-21; A-58; A-60; A-83; A-149; A-260 and A-475.
- 149 T→A: Abolishes activity; when associated with A-20; A-21; A-58; A-60; A-83; A-135; A-260 and A-475.
- 260 T→A: Abolishes activity; when associated with A-20; A-21; A-58; A-60; A-83; A-135; A-149 and A-475.
O42893 Cytosolic neutral trehalase; Alpha,alpha-trehalase; Alpha,alpha-trehalose glucohydrolase; Neutral trehalase; EC 3.2.1.28 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 3 papers)
28% identity, 67% coverage: 145:523/565 of query aligns to 276:689/735 of O42893