SitesBLAST
Comparing WP_011318250.1 NCBI__GCF_000204075.1:WP_011318250.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 11 hits to proteins with known functional sites (download)
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)
34% identity, 95% coverage: 12:483/495 of query aligns to 192:711/751 of P32356
- T260 (≠ E80) mutation to A: Abolishes activity; when associated with A-20; A-21; A-58; A-60; A-83; A-135; A-149 and A-475.
- WD 309:310 (= WD 107:108) binding substrate
- N346 (= N144) binding substrate
- RSQ 355:357 (= RSQ 153:155) binding substrate
- E424 (= E215) binding substrate
- R473 (= R269) binding substrate
- S475 (= S271) 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 (= G272) binding substrate
- D478 (= D274) mutation to A: Abolishes catalytic activity.
- E674 (= E452) mutation to A: Abolishes catalytic activity.
- R686 (≠ S464) mutation to A: Decreases catalytic activity.
- E690 (≠ C468) mutation to A: Severely decreases catalytic activity.
- Y691 (≠ F469) 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 Ca(2+)
- 116 binding Ca(2+)
- 118 binding Ca(2+)
- 120 binding Ca(2+); Q→A: Decreases catalytic activity.
- 125 binding Ca(2+)
- 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.
5n6nC Crystal structure of the 14-3-3:neutral trehalase nth1 complex (see paper)
34% identity, 95% coverage: 12:483/495 of query aligns to 150:658/698 of 5n6nC
- binding beta-D-fructofuranose: K216 (≠ E78), I217 (≠ V79), F261 (= F101), N297 (≠ Q137), H298 (= H138), G300 (= G140), K351 (≠ E184), D425 (= D274), Q570 (= Q402)
- binding alpha-D-glucopyranose: D188 (= D50), P257 (= P97), W267 (= W107), D268 (= D108), H298 (= H138), G423 (= G272), D425 (= D274), Q487 (≠ R329), A529 (≠ S371), T530 (≠ S372), K531 (≠ P373), W571 (= W403), W655 (= W480)
Sites not aligning to the query:
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)
35% identity, 81% coverage: 84:483/495 of query aligns to 266:689/735 of O42893
Sites not aligning to the query:
- 6 S→A: Abolishes activation during osmotic stress and thermal stress. Increases cellular trehalose level during osmotic stress but not thermal stress. Does not affect binding to tps1.
- 41 S→A: Decreases activation during osmotic stress and thermal stress. Increases cellular trehalose level during osmotic stress but not thermal stress. Does not affect binding to tps1.
- 47 modified: Phosphothreonine
- 49 modified: Phosphoserine
- 50 modified: Phosphothreonine
- 51 modified: Phosphoserine; S→A: Abolishes activation during osmotic stress and thermal stress. Increases cellular trehalose level during osmotic stress but not thermal stress. Does not affect binding to tps1.
- 71 mutation S->A,D: Abolishes activation and increases cellular trehalose level during osmotic stress and thermal stress. Does not affect binding to tps1.
- 97 D→L: Abolishes calcium binding. Abolishes activation and increases cellular trehalose level during osmotic stress and thermal stress.
- 100 R→L: Decreases calcium binding. Decreases activation and increases cellular trehalose level during osmotic stress and thermal stress. Does not affect binding to tps1.
- 108 D→L: Abolishes calcium binding. Abolishes activation and increases cellular trehalose level during osmotic stress and thermal stress. Does not affect binding to tps1.
2jjbA Family 37 trehalase from escherichia coli in complex with casuarine-6- o-alpha-glucopyranose (see paper)
34% identity, 81% coverage: 87:489/495 of query aligns to 99:487/504 of 2jjbA
- binding casuarine: F113 (= F101), W119 (= W107), D120 (= D108), G270 (= G272), D272 (= D274), W407 (= W403), F476 (= F478), W478 (= W480)
- binding alpha-D-glucopyranose: R112 (= R100), Y117 (= Y105), N156 (= N144), Y162 (≠ M150), R165 (= R153), R237 (≠ A213), E239 (= E215), D272 (= D274)
2jf4A Family 37 trehalase from escherichia coli in complex with validoxylamine (see paper)
34% identity, 81% coverage: 87:489/495 of query aligns to 92:482/500 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: F106 (= F101), Y110 (= Y105), W112 (= W107), D113 (= D108), N149 (= N144), R158 (= R153), R230 (≠ A213), E232 (= E215), G263 (= G272), D265 (= D274), W400 (= W403), E464 (≠ G470), Y465 (= Y471), F471 (= F478), W473 (= W480)
2wynA Structure of family 37 trehalase from escherichia coli in complex with a casuarine-6-o-a-d-glucoside analogue (see paper)
34% identity, 81% coverage: 87:489/495 of query aligns to 99:489/506 of 2wynA
- binding alpha-D-glucopyranose: Y117 (= Y105), N156 (= N144), Y162 (≠ M150), R165 (= R153), R237 (≠ A213), E239 (= E215)
- binding (1r,2r,3r,6r,7r,7ar)-3,7-bis(hydroxymethyl)hexahydro-1h-pyrrolizine-1,2,6-triol: F113 (= F101), W119 (= W107), D120 (= D108), G270 (= G272), D272 (= D274), W407 (= W403), Y472 (= Y471), F478 (= F478), W480 (= W480)
2jg0A Family 37 trehalase from escherichia coli in complex with 1- thiatrehazolin (see paper)
34% identity, 81% coverage: 87:489/495 of query aligns to 99:489/507 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 (= R100), F113 (= F101), Y117 (= Y105), W119 (= W107), D120 (= D108), N156 (= N144), Y162 (≠ M150), R165 (= R153), R237 (≠ A213), E239 (= E215), A267 (≠ R269), G270 (= G272), D272 (= D274), W407 (= W403), E471 (≠ G470), Y472 (= Y471), F478 (= F478), W480 (= W480)
5z66A Structure of periplasmic trehalase from diamondback moth gut bacteria complexed with validoxylamine (see paper)
34% identity, 82% coverage: 86:489/495 of query aligns to 105:495/512 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 (= P97), F120 (= F101), Y124 (= Y105), W126 (= W107), D127 (= D108), N163 (= N144), Y169 (≠ M150), Q174 (= Q155), R243 (≠ G225), E245 (≠ S227), G276 (= G272), D278 (= D274), W413 (= W403), E477 (≠ G470), Y478 (= Y471), F484 (= F478), W486 (= W480)
Q9SU50 Trehalase; Alpha,alpha-trehalase; Alpha,alpha-trehalose glucohydrolase; Trehalase 1; AtTRE1; EC 3.2.1.28 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
29% identity, 85% coverage: 68:489/495 of query aligns to 192:613/626 of Q9SU50
- R224 (= R100) binding alpha,alpha-trehalose
- D232 (= D108) binding alpha,alpha-trehalose
- N268 (= N144) binding alpha,alpha-trehalose
- R277 (= R153) binding alpha,alpha-trehalose
- Q279 (= Q155) binding alpha,alpha-trehalose
- R344 (≠ A213) binding alpha,alpha-trehalose
- E346 (= E215) binding alpha,alpha-trehalose
- E580 (= E452) binding alpha,alpha-trehalose
- E595 (≠ I467) binding alpha,alpha-trehalose
Sites not aligning to the query:
- 1:61 modified: Variant sequence, Missing (in isoform 2)
- 71 S→A: Abolishes trehalase activity; when associated with A-126.
- 128 T→A: Abolishes trehalase activity; when associated with A-71.
7eawA Trehalase of arabidopsis thaliana acid mutant -d380a trehalose complex
29% identity, 85% coverage: 68:489/495 of query aligns to 118:539/560 of 7eawA
- binding alpha-D-glucopyranose: R150 (= R100), F151 (= F101), F151 (= F101), Y155 (= Y105), W157 (= W107), D158 (= D108), N194 (= N144), Y200 (≠ M150), Q205 (= Q155), R270 (≠ A213), E272 (= E215), A301 (≠ R269), E506 (= E452), E521 (≠ Y471), Y522 (≠ S472), Y522 (≠ S472)
Q9W2M2 Trehalase; Alpha,alpha-trehalase; Alpha,alpha-trehalose glucohydrolase; EC 3.2.1.28 from Drosophila melanogaster (Fruit fly) (see paper)
29% identity, 84% coverage: 73:490/495 of query aligns to 165:575/596 of Q9W2M2
- N451 (≠ S372) modified: carbohydrate, N-linked (GlcNAc...) asparagine
Query Sequence
>WP_011318250.1 NCBI__GCF_000204075.1:WP_011318250.1
MTKNTVRTYIKQTWKTLTRSHQHLLESAQDTKLEHQPNTPWIIYISPQEDCNTVKSVLER
SLSTKEMQQIEIRTLPSEVEAIQEHGLLYLPGPYVVPGGRFNEMYGWDSYFILLGLLQDE
EWELAQSQVDQLLYQVQHYGTILNANRTYMLTRSQPPVLSMMVLALFQHTQDQAWLKSTL
PLLEQFYYYWVVPPHLNSATGLSRYYALGEGAAPEVLFSELDEAGRSHYERVKEYYKTFE
IDDYDVSLFYDSEKDELTDLFYKGDRSMRESGFDITNRFGPFSVDIVHYAPVCLNSLLYQ
MEQDLTQIHKILDNPELAEQWSDRANIRRERINQYLWDEEKGIYLDYHFYSGKRRHYEFA
TTFYPLWTGLSSPEQAQRIVENLSLFTAPGGIFTSTRVTGNQWDAPFGWAPLTLIAVQGL
YRYGYRKEGDDIAHKFLTMAIQEFTKYGFFVEKYDVERCSAQVSDEICFGYSSNEIGFGW
TNGVILELLANLDDS
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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