SitesBLAST
Comparing WP_035135982.1 NCBI__GCF_000769915.1:WP_035135982.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 13 hits to proteins with known functional sites (download)
1h54B Maltose phosphorylase from lactobacillus brevis (see paper)
48% identity, 97% coverage: 11:754/769 of query aligns to 10:743/754 of 1h54B
Q8L163 Kojibiose phosphorylase; KP; KPase; EC 2.4.1.230 from Thermoanaerobacter brockii (Thermoanaerobium brockii) (see paper)
29% identity, 98% coverage: 6:762/769 of query aligns to 14:775/775 of Q8L163
- R33 (≠ S25) mutation to Q: Retains 30% of kojibiose phosphorylase activity.
- R48 (= R40) mutation to Q: Retains 60% of kojibiose phosphorylase activity.
- K114 (≠ E119) mutation to Q: Retains 85% of kojibiose phosphorylase activity.
- R137 (= R142) mutation to Q: Retains 60% of kojibiose phosphorylase activity.
- D177 (≠ A182) mutation to N: No change in kojibiose phosphorylase activity.
- D271 (≠ N270) mutation to N: Retains 70% of kojibiose phosphorylase activity.
- E284 (≠ V283) mutation to Q: No change in kojibiose phosphorylase activity.
- D340 (= D339) mutation to N: Retains 90% of kojibiose phosphorylase activity.
- D362 (= D361) mutation to N: Loss of kojibiose phosphorylase activity.
- K403 (≠ T403) mutation to Q: Retains 74% of kojibiose phosphorylase activity.
- D459 (= D449) mutation to N: Strong decrease in kojibiose phosphorylase activity. Increases KM for kojibiose, beta-G1P and glucose but minimally affects the value for phosphate.
- R476 (= R466) mutation to Q: Retains 50% of kojibiose phosphorylase activity.
- K614 (= K603) mutation to N: Loss of kojibiose phosphorylase activity.
- E642 (= E631) mutation to Q: Loss of kojibiose phosphorylase activity.
- K749 (≠ S737) mutation to Q: Retains 78% of kojibiose phosphorylase activity.
3wiqA Crystal structure of kojibiose phosphorylase complexed with kojibiose (see paper)
29% identity, 95% coverage: 18:746/769 of query aligns to 10:751/751 of 3wiqA
- active site: E483 (= E491)
- binding beta-D-glucopyranose: Y337 (= Y354), W391 (≠ M411), E392 (≠ V412), T417 (vs. gap), E483 (= E491), K596 (= K603)
- binding alpha-D-glucopyranose: Y337 (= Y354), F342 (≠ Y359), W343 (= W360), D344 (= D361), E483 (= E491), K596 (= K603), Q597 (= Q604)
- binding sulfate ion: Y337 (= Y354), S632 (= S639), H675 (= H682)
3wirA Crystal structure of kojibiose phosphorylase complexed with glucose (see paper)
29% identity, 95% coverage: 18:750/769 of query aligns to 10:755/756 of 3wirA
- active site: E483 (= E491)
- binding beta-D-glucopyranose: Y337 (= Y354), Y337 (= Y354), F342 (≠ Y359), W343 (= W360), D344 (= D361), W391 (≠ M411), E392 (≠ V412), P402 (≠ N421), T417 (vs. gap), E483 (= E491), E483 (= E491), K596 (= K603), Q597 (= Q604)
- binding phosphate ion: Y337 (= Y354), S631 (= S638), S632 (= S639)
D6XZ22 1,2-alpha-glucosylglycerol phosphorylase; 2-O-alpha-glucosylglycerol phosphorylase; GGP; EC 2.4.1.332 from Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10) (see 2 papers)
27% identity, 98% coverage: 11:765/769 of query aligns to 14:756/761 of D6XZ22
- Y327 (= Y354) mutation to F: Abolishes both phosphorylase and hydrolase activities.
- YQ 327:328 (≠ YG 354:355) binding glycerol
- WD 333:334 (= WD 360:361) binding substrate
- W381 (vs. gap) mutation to F: Impaired phosphorylase activity without affecting the hydrolase activity.
- E475 (= E491) mutation E->A,Q: Loss of function.
- Y572 (vs. gap) mutation to F: Impairs both phosphorylase and hydrolase activities.
- K587 (= K603) mutation to A: Abolishes both phosphorylase and hydrolase activities.
- KQ 587:588 (= KQ 603:604) binding substrate
4ktrA Crystal structure of 2-o-alpha-glucosylglycerol phosphorylase in complex with isofagomine and glycerol (see paper)
27% identity, 98% coverage: 11:765/769 of query aligns to 14:756/762 of 4ktrA
4ktpB Crystal structure of 2-o-alpha-glucosylglycerol phosphorylase in complex with glucose (see paper)
27% identity, 98% coverage: 11:765/769 of query aligns to 14:756/761 of 4ktpB
4ktpA Crystal structure of 2-o-alpha-glucosylglycerol phosphorylase in complex with glucose (see paper)
27% identity, 98% coverage: 11:765/769 of query aligns to 14:756/767 of 4ktpA
8iucA Crystal structure of gh65 alpha-1,2-glucosidase from flavobacterium johnsoniae in complex with isomaltose (see paper)
23% identity, 82% coverage: 87:718/769 of query aligns to 63:641/659 of 8iucA
Sites not aligning to the query:
7fe4A Crystal structure of gh65 alpha-1,2-glucosidase from flavobacterium johnsoniae in complex with glucose (see paper)
23% identity, 82% coverage: 87:718/769 of query aligns to 63:641/659 of 7fe4A
- binding beta-D-glucopyranose: E253 (≠ K290), R257 (≠ A294), P307 (= P346), Y315 (= Y354), F320 (≠ Y359), W321 (= W360), D322 (= D361), W369 (≠ M411), E370 (≠ V412), P380 (≠ C419), A383 (≠ E422), N444 (≠ G485), E450 (= E491), E450 (= E491), W451 (≠ Y492), D456 (≠ N497), K516 (= K603), K516 (= K603), Q517 (= Q604), D551 (≠ S638), M555 (≠ L640)
Sites not aligning to the query:
A5FBJ5 Kojibiose hydrolase; Alpha-1,2-D-glucoside glucohydrolase; Alpha-1,2-glucosidase; FjGH65A; Kojibiase; EC 3.2.1.216 from Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / BCRC 14874 / CCUG 350202 / NBRC 14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae) (see paper)
23% identity, 82% coverage: 87:718/769 of query aligns to 85:663/681 of A5FBJ5
- W343 (= W360) binding beta-D-glucose
- D344 (= D361) binding beta-D-glucose
- W391 (≠ M411) binding beta-D-glucose
- E392 (≠ V412) binding beta-D-glucose
- T407 (≠ E424) binding beta-D-glucose
- E472 (= E491) binding beta-D-glucose; mutation to Q: Loss of activity with kojibiose as substrate.
- W473 (≠ Y492) binding beta-D-glucose
- K538 (= K603) binding beta-D-glucose; binding beta-D-glucose; binding beta-D-glucose
- Q539 (= Q604) binding beta-D-glucose
- D573 (≠ S638) binding beta-D-glucose
- E616 (= E676) mutation to Q: Loss of activity with kojibiose as substrate.
Sites not aligning to the query:
- 74 binding beta-D-glucose
Q32M88 Protein-glucosylgalactosylhydroxylysine glucosidase; Acid trehalase-like protein 1; EC 3.2.1.107 from Homo sapiens (Human) (see paper)
29% identity, 37% coverage: 294:580/769 of query aligns to 226:502/737 of Q32M88
- D301 (= D361) mutation D->E,N: Abolishes catalytic activity.
- D429 (≠ N490) mutation to E: Abolishes catalytic activity.; mutation to N: Significantly impairs catalytic activity.
- E430 (= E491) mutation E->D,Q: Abolishes catalytic activity.
Sites not aligning to the query:
- 574 mutation E->D,Q: Abolishes catalytic activity.
P48016 Periplasmic acid trehalase ATH1; Alpha,alpha-trehalase; Alpha,alpha-trehalose glucohydrolase; EC 3.2.1.28 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
24% identity, 40% coverage: 277:587/769 of query aligns to 427:722/1211 of P48016
Sites not aligning to the query:
- 1:100 mutation Missing: Abolishes cell surface localization. Abolishes acid trehalase activity.
- 2 K→R: Abolishes its ubiquitination; when associated with R-27 and R-37. Normal protein targeting to vacuolar lumen; when associated with R-27 and R-37.
- 27 K→R: Abolishes its ubiquitination; when associated with R-27 and R-37. Normal protein targeting to vacuolar lumen; when associated with R-2 and R-37.
- 37 K→R: Abolishes its ubiquitination; when associated with R-27 and R-37. Normal protein targeting to vacuolar lumen; when associated with R-2 and R-27.
- 47:69 mutation Missing: Abnormal protein expression.
- 49:68 NSILLLMMLFLLAIFVTALY→VAILLLMMLFLLAIFVVALF: Protein mislocalized to the vacuolar membrane in a small proportion of cells.
Query Sequence
>WP_035135982.1 NCBI__GCF_000769915.1:WP_035135982.1
MNQDYIVPDNWSIIEEGFEADRVKSSESLFSIGNGAMGQRANFEEHYSGPTFQGSYIAGV
YYPDKTKVGWWKNGYPEYFAKVLNAPNWIGIEVQVNGEALDLNTCKEIKNYKRELNMKEG
WYNRSFTAVLQNGTEVAVNVRRFLSLVSDELGVIKYEVTPVNQSAQIVYKPYVDAGVKNE
DANWEEKFWEPLDVQHSGNDAFVTARTFKTHFTAATYMHNSLLLNGTEEVVVAEDIVATN
DKVQFSYSLDAKQGETAAIVKFGGYTVSLNHEEGALIDAAKNVIANAVSKGYDALLEEQK
QAWAGIWEMADITIDGDVKAQQGIRFNIFQLNQTYLGKDPRLNIGPKGFTGEKYGGSTYW
DTEAYCIPFYMATKDQQVARNLLTYRHNQLGKAIENAQKLGFTNGAALYPMVTMNGEECH
NEWEITFEEIHRNGAIAFAIYNYYRFTGDYSYIPEKGLEVLIGIARFWYQRATFSTAKNK
YVILGVTGPNEYENNVNNNWYTNYIAQWCINYAIENITKVKDEFTADHSRIMGLTNLTAE
EIQQWQKVADNMYFPYSEEHGVFLQQDGFLDKEMVRVSDLDRSQRPINQKWSWDRILRSP
YIKQADVLQGFYFFEDHFTREDLEKHFDFYEPFTVHESSLSPCVHSIQAAGLNRMEQAYT
FYLRTSRLDLDDYNKEVKEGLHITSMAGTWMSIVEGFGGMRVKNGNLHFEPRIPEQWEGY
SFKINFRNQIVKISVHSGETRFDLEGDKELTVFVHGKEVKVEPNKAVTI
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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