SitesBLAST
Comparing Pf6N2E2_4966 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_4966 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 15 hits to proteins with known functional sites (download)
7fdzA Levansucrase from brenneria sp. Enid 312 with sucrose (see paper)
80% identity, 97% coverage: 12:424/424 of query aligns to 6:416/417 of 7fdzA
- binding beta-D-fructofuranose: W46 (= W52), N47 (≠ D53), H98 (= H104), W132 (= W138), A133 (= A139), R203 (= R209), D204 (= D210), E288 (= E294), S354 (= S360)
- binding alpha-D-glucopyranose: H98 (= H104), W132 (= W138), Q286 (= Q292), E288 (= E294), H306 (= H312)
7osoA The crystal structure of erwinia tasmaniensis levansucrase in complex with (s)-1,2,4-butanentriol (see paper)
71% identity, 97% coverage: 13:424/424 of query aligns to 3:412/412 of 7osoA
- binding (2~{S})-butane-1,2,4-triol: W42 (= W52), D43 (= D53), L66 (= L76), H94 (= H104), W128 (= W138), E284 (= E294)
- binding zinc ion: D49 (= D59), D51 (= D61), D53 (≠ N63), D137 (= D147), E138 (≠ R148), H302 (= H312), D314 (= D324)
4d47A X-ray structure of the levansucrase from erwinia amylovora (see paper)
71% identity, 97% coverage: 13:423/424 of query aligns to 3:411/411 of 4d47A
- active site: D43 (= D53), A129 (= A139), D200 (= D210), E284 (= E294)
- binding beta-D-fructofuranose: W42 (= W52), D43 (= D53), H94 (= H104), W128 (= W138), R199 (= R209), D200 (= D210), E284 (= E294)
- binding alpha-D-glucopyranose: H94 (= H104), H302 (= H312)
P0DJA3 Levansucrase; Beta-D-fructofuranosyl transferase; Sucrose 6-fructosyl transferase; EC 2.4.1.10 from Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) (see paper)
51% identity, 96% coverage: 14:420/424 of query aligns to 9:404/423 of P0DJA3
- W80 (= W100) mutation to R: Exhibits kinetic parameters and transfructosylation activity that are almost the same as those of the wild-type enzyme, but is unable to catalyze the synthesis of highly polymerized fructans.
- E117 (= E137) mutation to Q: Does not affect sucrose hydrolase activity. Exhibits greater transfructosylating activity.
- D194 (= D210) mutation D->A,E,H,Q,S: Abolishes sucrose hydrolysis.; mutation to N: Abolishes sucrose hydrolysis. 3-fold increase in KM for sucrose. Transfructosylating activity is not affected.
- E211 (= E227) mutation to Q: Retains 28% of the sucrose hydrolase activity, but transfructosylating activity is greatly reduced.
- V223 (= V239) mutation to A: 8-fold increase in KM for sucrose. Shows higher activity toward stachyose.
- D275 (= D291) mutation to N: No change in activity.
- E278 (= E294) mutation to D: 30-fold decrease in kcat for sucrose hydrolysis. KM for sucrose and transfructosylating activity are only slightly affected.; mutation to H: 210-fold decrease in kcat for sucrose hydrolysis. 3-fold increase in KM for sucrose.
- H296 (= H312) mutation H->K,R: Decreases both transfructosylating and hydrolyzing activities.
- D302 (= D318) mutation to N: No change in activity.
- D308 (= D324) mutation to N: No change in activity.
8i2rA Beijerinckia indica beta-fructosyltransferase variant h395r/f473y in complex with fructose (see paper)
39% identity, 95% coverage: 18:419/424 of query aligns to 22:475/477 of 8i2rA
Sites not aligning to the query:
Q43998 Levansucrase; Beta-D-fructofuranosyl transferase; Sucrose 6-fructosyl transferase; EC 2.4.1.10 from Gluconacetobacter diazotrophicus (Acetobacter diazotrophicus) (see 2 papers)
39% identity, 92% coverage: 18:406/424 of query aligns to 88:524/584 of Q43998
- D135 (= D53) mutation to N: 2300-fold decrease in kcat for sucrose hydrolysis.
- C339 (≠ V239) modified: Disulfide link with 395; mutation to S: 60-fold decrease in kcat for sucrose hydrolysis.
- C395 (≠ G288) modified: Disulfide link with 339; mutation to S: 60-fold decrease in kcat for sucrose hydrolysis.
Sites not aligning to the query:
- 31 modified: Pyrrolidone carboxylic acid
3vssA Microbacterium saccharophilum k-1 beta-fructofuranosidase catalytic domain complexed with fructose (see paper)
40% identity, 93% coverage: 18:413/424 of query aligns to 26:472/494 of 3vssA
- binding beta-D-fructofuranose: D74 (= D53), G90 (= G69), W91 (= W70), E130 (vs. gap), W161 (= W138), S162 (≠ A139), R243 (= R209), D244 (= D210), H253 (≠ D219), E256 (≠ K221), E336 (= E294), Y419 (= Y359), S420 (= S360)
Sites not aligning to the query:
7bj4A Inulosucrase from halalkalicoccus jeotgali bound to kestose (see paper)
38% identity, 94% coverage: 18:416/424 of query aligns to 5:396/406 of 7bj4A
- binding beta-D-fructofuranose: D39 (= D53), L62 (= L76), H74 (= H104), W107 (= W138), A108 (= A139), R188 (= R209), R188 (= R209), E258 (≠ Q292), E260 (= E294), E260 (= E294), H278 (= H312)
- binding alpha-D-glucopyranose: H74 (= H104), N343 (≠ H361), L352 (≠ T370)
P05655 Levansucrase; Beta-D-fructofuranosyl transferase; Fructosyltransferase; FTF; Sucrose 6-fructosyl transferase; EC 2.4.1.10 from Bacillus subtilis (strain 168) (see 4 papers)
27% identity, 85% coverage: 51:409/424 of query aligns to 84:461/473 of P05655
- W85 (= W52) binding sucrose
- D86 (= D53) binding sucrose; mutation to A: Lack of levan synthesis.
- D117 (= D89) mutation to A: 2-fold decrease in catalytic efficiency. Synthesizes a bimodal levan molecular weight distribution.
- S164 (≠ A139) binding sucrose; mutation to A: Drastic decrease in catalytic efficiency. Slight increase in affinity for sucrose. Increases transfructosylation activity. Uses acceptors such as glucose and short levans with an average molecular weight of 7.6 kDa more efficiently than wild-type enzyme, leading to the enhanced synthesis of medium and high molecular weight polymer.; mutation to K: Loss of activity.
- F182 (≠ V158) mutation to A: 3.7-fold decrease in catalytic efficiency. 1.6-fold increase in KM for sucrose. Synthesizes only high molecular weight levans.; mutation to W: 2.1-fold decrease in catalytic efficiency. Synthesizes a bimodal levan molecular weight distribution.; mutation to Y: 1.7-fold decrease in catalytic efficiency. Synthesizes a bimodal levan molecular weight distribution.
- Y187 (vs. gap) mutation to A: Slight decrease in catalytic efficiency. Synthesizes a bimodal levan molecular weight distribution.
- Y237 (≠ W206) mutation to A: Slight decrease in catalytic efficiency. Synthesizes only high molecular weight levans.
- D241 (= D210) binding Ca(2+)
- N242 (≠ P211) mutation to A: 14.6-fold decrease in catalytic efficiency. 2.2-fold increase in KM for sucrose. Levans are barely formed.
- H243 (≠ W212) mutation to L: Decrease in catalytic efficiency.
- R246 (= R215) binding sucrose
- D247 (= D216) binding sucrose; mutation to A: Lack of levan synthesis.
- Q272 (vs. gap) binding Ca(2+)
- L308 (≠ V268) binding Ca(2+)
- N310 (≠ R270) binding Ca(2+)
- D339 (= D291) binding Ca(2+)
- E340 (≠ Q292) binding sucrose
- I341 (≠ T293) mutation to V: Increases transfructosylation activity.
- E342 (= E294) mutation to A: Lack of levan synthesis.
- A344 (≠ P296) mutation to P: Increases transfructosylation activity.
- R360 (≠ H312) binding sucrose; mutation to K: Decrease in catalytic efficiency. Reduces affinity for sucrose. Synthesizes mainly oligosaccharides, but can still catalyze the synthesis of low amounts of levan.; mutation to S: Drastic decrease in catalytic efficiency. Reduces affinity for sucrose. Synthesizes only oligosaccharides.
- G361 (vs. gap) mutation to F: Drastic decrease in catalytic efficiency. Reduces affinity for sucrose. Synthesizes mainly oligosaccharides, but can still catalyze the synthesis of low amounts of levan.
- K363 (≠ F314) mutation to A: 2.9-fold decrease in catalytic efficiency. Synthesizes only high molecular weight levans.
- F414 (≠ Y362) mutation to W: Increases transfructosylation activity.
- Y429 (≠ P377) mutation to N: Drastic decrease in catalytic efficiency. Reduces affinity for sucrose. Synthesizes only oligosaccharides.
- R433 (≠ T381) mutation to A: Drastic decrease in catalytic efficiency. Reduces affinity for sucrose. Synthesizes only oligosaccharides.
3om2A Crystal structure of b. Megaterium levansucrase mutant d257a (see paper)
28% identity, 92% coverage: 20:409/424 of query aligns to 26:438/448 of 3om2A
1pt2A Crystal structure of levansucrase (e342a) complexed with sucrose (see paper)
27% identity, 85% coverage: 51:409/424 of query aligns to 51:428/440 of 1pt2A
- active site: D53 (= D53), S131 (≠ A139), D214 (= D216), A309 (≠ E294)
- binding calcium ion: D208 (= D210), Q239 (vs. gap), L275 (≠ V268), N277 (≠ R270), D306 (= D291)
- binding beta-D-fructofuranose: D53 (= D53), L76 (= L76), W130 (= W138), S131 (≠ A139), R213 (= R215), D214 (= D216), Y378 (= Y359)
- binding alpha-D-glucopyranose: W130 (= W138), R213 (= R215), E307 (≠ Q292), R327 (≠ H312)
3byjA Crystal structure of b. Subtilis levansucrase mutant d86a
27% identity, 85% coverage: 51:409/424 of query aligns to 51:428/440 of 3byjA
Q74K42 Inulosucrase; IS; EC 2.4.1.9 from Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533) (see paper)
24% identity, 77% coverage: 48:373/424 of query aligns to 267:620/797 of Q74K42
- W271 (= W52) binding substrate
- D272 (= D53) mutation to N: Loss of catalytic activity.
- N301 (≠ D99) mutation to A: 25% of wild-type activity.; mutation to S: 40% of wild-type activity.
- NVN 301:303 (≠ DWN 99:101) mutation Missing: 1.5% of wild-type activity.
- N305 (≠ R103) mutation to A: 29% of wild-type activity.; mutation to S: 50% of wild-type activity.
- N317 (= N119) binding Ca(2+)
- S340 (≠ A139) binding substrate
- D419 (vs. gap) binding Ca(2+)
- RD 424:425 (= RD 209:210) binding substrate
- Q450 (vs. gap) binding Ca(2+)
- W487 (≠ F259) binding Ca(2+)
- N489 (≠ T261) binding Ca(2+)
- D521 (= D291) binding Ca(2+)
- EIE 522:524 (≠ QTE 292:294) binding substrate
- R542 (≠ H312) binding substrate
Sites not aligning to the query:
- 660 binding Ca(2+)
- 662 binding Ca(2+)
- 667 binding Ca(2+)
2yfrA Crystal structure of inulosucrase from lactobacillus johnsonii ncc533 (see paper)
24% identity, 77% coverage: 48:373/424 of query aligns to 92:445/533 of 2yfrA
Sites not aligning to the query:
2yfsA Crystal structure of inulosucrase from lactobacillus johnsonii ncc533 in complex with sucrose (see paper)
24% identity, 77% coverage: 48:373/424 of query aligns to 92:445/533 of 2yfsA
- active site: N97 (≠ D53), S165 (≠ A139), D250 (= D210), E349 (= E294)
- binding calcium ion: N142 (= N119), D244 (vs. gap), Q275 (vs. gap), W312 (≠ F259), N314 (≠ T261), D346 (= D291)
- binding beta-D-fructofuranose: W96 (= W52), N97 (≠ D53), M121 (≠ L76), N126 (≠ D99), V127 (≠ W100), S165 (≠ A139), D250 (= D210), E349 (= E294)
- binding alpha-D-glucopyranose: E347 (≠ Q292), E349 (= E294), R367 (≠ H312)
Sites not aligning to the query:
Query Sequence
>Pf6N2E2_4966 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_4966
MKTTTEKFGVTPHQPSLWTRADALKVRADDPTTTQPLVSADFPVLNNDVFIWDTMPLRDL
DGNVTSVDGWSVIFTLTADRHPNDPAYLDEDGNYDILRDWNDRHGRAKMYYWFSRTGKNW
EFGGRVMAEGVSPTAREWAGTPILLNDRGEVDLYYTAVTPGATIVKVRGRVVTTEHGVSM
VGFEKVKPLFEADGKMYQTEAQNAFWGFRDPWPFRDPKDGKLYMLFEGNVAGERGSHKVG
EAEIGDVPPGYEDVGNSRFQTACVGIAVARDADGDDWEMLPPLLTAVGVNDQTERPHFVF
QDGKYYLFTISHTFTYADGVTGPDGVYGFVADSLFGPYVPLNGSGLVLGNPSSQPFQTYS
HYVMPNGLVTSFIDSVPTDETGTQIRVGGTEAPTVGMKIKGQQTFVVAEYDYGYIPPMLD
VTLK
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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