SitesBLAST
Comparing N515DRAFT_0922 FitnessBrowser__Dyella79:N515DRAFT_0922 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 20 (the maximum) hits to proteins with known functional sites (download)
6eonA Galactanase bt0290 (see paper)
37% identity, 93% coverage: 43:620/623 of query aligns to 3:581/754 of 6eonA
Sites not aligning to the query:
4e8cA Crystal structure of streptococcal beta-galactosidase in complex with galactose (see paper)
34% identity, 92% coverage: 42:616/623 of query aligns to 2:576/594 of 4e8cA
3wf2A Crystal structure of human beta-galactosidase in complex with nbt-dgj
33% identity, 90% coverage: 46:607/623 of query aligns to 9:579/605 of 3wf2A
- binding (2R,3S,4R,5S)-N-butyl-3,4,5-trihydroxy-2-(hydroxymethyl)piperidine-1-carbothioamide: Y55 (= Y92), A100 (= A138), E101 (= E139), N159 (= N198), E160 (= E199), E240 (= E271), L246 (= L277), N293 (= N322), Y305 (= Y339), Y457 (= Y492)
3wf1A Crystal structure of human beta-galactosidase in complex with 6s-nbi- gj
33% identity, 90% coverage: 46:607/623 of query aligns to 9:579/605 of 3wf1A
- binding (3E,5S,6R,7S,8S,8aS)-3-(butylimino)hexahydro[1,3]thiazolo[3,4-a]pyridine-5,6,7,8-tetrol: Y55 (= Y92), C99 (= C137), A100 (= A138), E101 (= E139), E160 (= E199), E240 (= E271), Y242 (= Y273), W245 (= W276), Y278 (= Y307), Y305 (= Y339)
3wf0A Crystal structure of human beta-galactosidase in complex with 6s-nbi- dgj
33% identity, 90% coverage: 46:607/623 of query aligns to 9:579/605 of 3wf0A
- binding (3Z,6S,7R,8S,8aS)-3-(butylimino)hexahydro[1,3]thiazolo[3,4-a]pyridine-6,7,8-triol: Y55 (= Y92), C99 (= C137), A100 (= A138), E101 (= E139), N159 (= N198), E160 (= E199), E240 (= E271), W245 (= W276), L246 (= L277), Y457 (= Y492)
3wezA Crystal structure of human beta-galactosidase in complex with noev
33% identity, 90% coverage: 46:607/623 of query aligns to 9:579/605 of 3wezA
- binding (1S,2S,3S,6R)-4-(hydroxymethyl)-6-(octylamino)cyclohex-4-ene-1,2,3-triol: Y55 (= Y92), C99 (= C137), A100 (= A138), E101 (= E139), E160 (= E199), E240 (= E271), Y242 (= Y273), L246 (= L277), N293 (= N322), Y305 (= Y339), Y457 (= Y492)
3thdA Crystal structure of human beta-galactosidase in complex with 1- deoxygalactonojirimycin (see paper)
33% identity, 90% coverage: 46:607/623 of query aligns to 9:579/605 of 3thdA
- binding (2R,3S,4R,5S)-2-(hydroxymethyl)piperidine-3,4,5-triol: Y55 (= Y92), C99 (= C137), A100 (= A138), E101 (= E139), N159 (= N198), E160 (= E199), E240 (= E271), Y305 (= Y339)
- binding sulfate ion: S294 (≠ A323), P295 (≠ K329), Y296 (≠ F330), R323 (= R357), Q327 (≠ G361), R429 (= R455), N430 (≠ V456)
3thcA Crystal structure of human beta-galactosidase in complex with galactose (see paper)
33% identity, 90% coverage: 46:607/623 of query aligns to 9:579/605 of 3thcA
- binding beta-D-galactopyranose: Y55 (= Y92), C99 (= C137), A100 (= A138), E101 (= E139), E160 (= E199), E240 (= E271), Y242 (= Y273), Y278 (= Y307), Y305 (= Y339)
- binding sulfate ion: S294 (≠ A323), P295 (≠ K329), Y296 (≠ F330), R323 (= R357), Q327 (≠ G361), R429 (= R455), N430 (≠ V456)
P16278 Beta-galactosidase; Acid beta-galactosidase; Lactase; Elastin receptor 1; EC 3.2.1.23 from Homo sapiens (Human) (see 33 papers)
32% identity, 90% coverage: 46:607/623 of query aligns to 37:621/677 of P16278
- R49 (≠ Q58) to C: in GM1G1 and GM1G2; decrease in galactosidase activity; dbSNP:rs72555358
- I51 (≠ R60) to T: in GM1G3; no effect on catalytic activity; decreased protein stability; dbSNP:rs72555390
- R59 (= R68) to C: in GM1G1; loss of galactosidase activity; severe mutation; dbSNP:rs756878418; to H: in GM1G1; with cardiac involvement in some patients; loss of galactosidase activity; severe mutation; dbSNP:rs72555392
- R68 (= R77) to Q: in GM1G2; 7.4% of wild-type galactosidase activity; dbSNP:rs572237881; to W: in GM1G2 and GM1G1; loss of galactosidase activity; dbSNP:rs72555370
- T82 (≠ I91) to M: in GM1G3; mild phenotype; dbSNP:rs72555393
- Y83 (= Y92) binding ; to C: in MPS4B; decrease in galactosidase activity; dbSNP:rs1553612220; to H: in MPS4B; 2-5% of wild-type galactosidase activity; dbSNP:rs72555364
- G123 (= G133) to R: in GM1G1; decrease in galactosidase activity; dbSNP:rs28934274
- E129 (= E139) binding ; to Q: in dbSNP:rs886042079
- M132 (≠ F142) to T: in GM1G1; 4.3% of wild-type galactosidase activity; dbSNP:rs1553612189
- G134 (= G144) to R: in GM1G2; uncertain significance
- R148 (= R158) to C: in GM1G3 and GM1G2; dbSNP:rs192732174
- S149 (≠ K160) to F: in MPS4B; 2.0% of wild-type galactosidase activity; dbSNP:rs778700089
- D151 (= D162) to Y: in GM1G1; complete lack of protein; loss of galactosidase activity
- L155 (≠ M166) to R: in GM1G2 and GM1G3; 6.7% of wild-type galactosidase activity; dbSNP:rs376710410
- L162 (≠ M173) to S: in GM1G1; loss of galactosidase activity
- L173 (≠ M184) to P: in GM1G1; loss of galactosidase activity; dbSNP:rs397515617
- Q184 (= Q195) to R: in GM1G1; loss of galactosidase activity
- N187 (= N198) binding
- G190 (≠ A201) to D: in GM1G1; 3.4% of wild-type galactosidase activity; dbSNP:rs756575833
- C195 (≠ G205) modified: Disulfide link with 230
- D198 (≠ A208) to Y: in MPS4B; 17.4% of wild-type galactosidase activity
- R201 (≠ E211) to C: in GM1G1 and GM1G2; no effect on intrinsic catalytic activity; decreased protein stability; 8.4% of wild-type galactosidase activity; activity severely reduced in transfection with variant F-436; dbSNP:rs72555360; to H: in GM1G1 and GM1G2; also in a patient with a slowly progressive GM1-gangliosidosis form; 36.2% of wild-type galactosidase activity; dbSNP:rs189115557
- C230 (≠ G244) modified: Disulfide link with 195
- L236 (= L249) to P: in GM1G1; decrease in galactosidase activity
- T239 (≠ D252) to M: in GM1G1; loss of galactosidase activity; severe mutation; causes a rapid degradation of the protein precursor; dbSNP:rs746766232
- N247 (≠ A260) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- Q255 (vs. gap) to H: in GM1G1; 2.4% of wild-type galactosidase activity; dbSNP:rs1553610553
- G262 (vs. gap) to E: in GM1G2; decrease in galactosidase activity; dbSNP:rs377174858
- Y270 (= Y273) to D: in GM1G3; originally classified as Morquio syndrome; dbSNP:rs376663785
- W273 (= W276) to L: in MPS4B; decreased galactosidase activity; dbSNP:rs72555362
- H281 (vs. gap) to Y: in GM1G1 and GM1G3; dbSNP:rs745386663
- L297 (≠ M298) to F: in GM1G3; decrease in galactosidase activity
- F314 (= F315) to L: in GM1G2; decrease in galactosidase activity
- N318 (≠ A319) to H: in GM1G1; uncertain significance
- T329 (= T335) to I: in GM1G1; 5.0% of wild-type galactosidase activity
- Y331 (= Y337) to C: in GM1G1; uncertain significance
- D332 (= D338) to E: in GM1G1; 2.3% of wild-type galactosidase activity; to N: in GM1G1; decrease in galactosidase activity; dbSNP:rs781658798
- Y333 (= Y339) binding ; to H: in GM1G2; 3.0% of wild-type galactosidase activity; the mutant protein is localized in the lysosomal-endosomal compartment
- L337 (≠ I343) to P: in GM1G1 and GM1G2; loss of galactosidase activity; dbSNP:rs752177002
- P397 (= P406) to A: in MPS4B; 24.0% of wild-type galactosidase activity
- Q408 (vs. gap) to P: in MPS4B; 1.1% of wild-type galactosidase activity; dbSNP:rs72555369
- G414 (= G418) to V: in GM1G2; decrease in galactosidase activity
- T420 (≠ A424) to K: in GM1G3; decrease in galactosidase activity; to P: in GM1G1; loss of galactosidase activity; dbSNP:rs200181401
- S434 (vs. gap) to L: in GM1-gangliosidosis; unclassified clinical type; dbSNP:rs267599773
- L436 (≠ I434) to F: seems to have a modulating action in the expression of the severity of other mutations; dbSNP:rs34421970
- G438 (= G436) to E: in GM1G3 and MPS4B; mild form; 5.7% of wild-type galactosidase activity; dbSNP:rs72555367
- D441 (= D439) to N: in GM1G1; loss of galactosidase activity; dbSNP:rs780724173
- Y444 (≠ T442) to C: in MPS4B; loss of galactosidase activity
- N464 (≠ S462) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- R482 (≠ H489) to C: in MPS4B; loss of galactosidase activity; dbSNP:rs72555365; to H: in MPS4B and GM1G1; severe decrease in galactosidase activity; dbSNP:rs72555391
- N484 (≠ G491) to K: in MPS4B; mild form; fibroblasts from MPS4B compound heterozygotes for K-484 and A-500 have 1.9% of wild-type galactosidase activity; dbSNP:rs968221254
- K493 (= K500) to N: in GM1G2; decrease in galactosidase activity; dbSNP:rs1172435886
- G494 (= G501) to S: in MPS4B; loss of galactosidase activity
- N498 (≠ A505) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- T500 (≠ R507) to A: in MPS4B; mild form; 2.1% of wild-type galactosidase activity; dbSNP:rs72555368
- W509 (= W516) to C: in MPS4B; also in a patient with a slowly progressive form of GM1-gangliosidosis; loss of galactosidase activity; dbSNP:rs72555363
- L514 (= L523) to P: in GM1G1; decrease in galactosidase activity
- R521 (vs. gap) to C: in GM1G3; likely benign; galactosidase activity is reduced in homozygous patient fibroblasts to 30% of control values; has 25% of wild-type galactosidase activity when expressed in a heterologous system; dbSNP:rs4302331
- S532 (≠ L534) to G: results in near-normal activity corresponding to 60%-100% of the wild-type depending on the expression system; dbSNP:rs73826339
- G554 (= G547) to E: in GM1-gangliosidosis; unclassified clinical type
- N555 (≠ T548) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- G579 (= G567) to D: in GM1G1 and GM1G2; loss of galactosidase activity; severe mutation; dbSNP:rs746350513
- R590 (= R578) to C: in GM1G1; loss of galactosidase activity; dbSNP:rs794727165
- Y591 (= Y579) to C: in GM1G1; with cardiac involvement in some patients; loss of galactosidase activity; severe mutation; causes a rapid degradation of the protein precursor; dbSNP:rs72555371; to N: in GM1G1; with cardiac involvement in some patients; loss of galactosidase activity; severe mutation; causes a rapid degradation of the protein precursor; dbSNP:rs72555373
- R595 (vs. gap) to W: reduction of galactosidase activity; dbSNP:rs201807974
- P597 (= P584) to L: in GM1G2; decrease in galactosidase activity; to S: in GM1G1; 2.1% of wild-type galactosidase activity
- T600 (≠ R587) to I: in GM1G2; decrease in galactosidase activity
Sites not aligning to the query:
- 10 P → L: in dbSNP:rs7637099
- 626 modified: Disulfide link with 634
- 634 modified: Disulfide link with 626
3w5fA Crystal structure of tomato beta-galactosidase 4
33% identity, 48% coverage: 48:347/623 of query aligns to 11:301/701 of 3w5fA
6ik5A Crystal structure of tomato beta-galactosidase (tbg) 4 in complex with galactose (see paper)
33% identity, 48% coverage: 48:347/623 of query aligns to 9:299/705 of 6ik5A
Q700S9 Beta-galactosidase A; Lactase A; EC 3.2.1.23 from Penicillium sp. (see paper)
28% identity, 55% coverage: 18:362/623 of query aligns to 21:388/1011 of Q700S9
- Y96 (= Y92) binding
- NAE 140:142 (≠ CAE 137:139) binding
- N199 (= N198) binding
- C205 (vs. gap) modified: Disulfide link with 206
- C206 (vs. gap) modified: Disulfide link with 205
- C267 (≠ G251) modified: Disulfide link with 316
- C316 (vs. gap) modified: Disulfide link with 267
- Y365 (= Y339) binding
- N374 (≠ E348) modified: carbohydrate, N-linked (GlcNAc...) asparagine
Sites not aligning to the query:
- 456 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 625 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 707 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 763 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 780 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 917 modified: carbohydrate, N-linked (GlcNAc...) asparagine
1xc6A Native structure of beta-galactosidase from penicillium sp. In complex with galactose (see paper)
29% identity, 51% coverage: 47:362/623 of query aligns to 10:348/971 of 1xc6A
- binding beta-D-galactopyranose: Y56 (= Y92), N100 (≠ C137), A101 (= A138), E102 (= E139), E160 (= E199), Y221 (vs. gap), E259 (≠ Q259), Y303 (= Y307), Y325 (= Y339)
- binding alpha-D-mannopyranose: E283 (≠ W280), R286 (≠ Q283), E338 (≠ D352)
Sites not aligning to the query:
1tg7A Native structure of beta-galactosidase from penicillium sp. (see paper)
29% identity, 51% coverage: 47:362/623 of query aligns to 10:348/971 of 1tg7A
Sites not aligning to the query:
5iftA Structure of e298q-beta-galactosidase from aspergillus niger in complex with 3-b-galactopyranosyl glucose (see paper)
27% identity, 53% coverage: 48:375/623 of query aligns to 11:360/968 of 5iftA
- binding beta-D-galactopyranose: Y56 (= Y92), N100 (≠ C137), A101 (= A138), E102 (= E139), E160 (= E199), Q258 (= Q259), Y264 (≠ M265), Y302 (= Y307), Y324 (= Y339)
- binding alpha-D-glucopyranose: E160 (= E199), F224 (≠ L249)
- binding alpha-D-mannopyranose: W267 (= W268), G268 (≠ V269), E282 (= E284), R285 (= R287), E337 (≠ D352)
Sites not aligning to the query:
A2QAN3 Beta-galactosidase A; An-beta-gal; Lactase A; EC 3.2.1.23 from Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513) (see paper)
27% identity, 53% coverage: 48:375/623 of query aligns to 51:400/1007 of A2QAN3
- Y96 (= Y92) binding
- NAE 140:142 (≠ CAE 137:139) binding
- N156 (≠ D154) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- N199 (= N198) binding
- C205 (≠ G204) modified: Disulfide link with 206
- C206 (≠ G205) modified: Disulfide link with 205
- C266 (vs. gap) modified: Disulfide link with 315
- E298 (≠ Q259) active site, Nucleophile; mutation to Q: Loss of hydrolytic activity.
- Y304 (≠ M265) mutation to A: Nearly complete loss of hydrolytic activity against lactose compared to wild-type due to decreased substrate affinity.; mutation to F: Over 33% increase of hydrolytic activity against lactose compared to wild-type. No effect on hydrolytic activity compared to wild-type; when associated with H-355 and G-357. 58% reduction in hydrolytic activity compared to wild-type; when associated with H-355, G-357 and F-806.
- C315 (≠ L277) modified: Disulfide link with 266
- Y355 (≠ G320) mutation to H: No effect on hydrolytic activity compared to wild-type; when associated with F-304 and G-357. 58% reduction in hydrolytic activity compared to wild-type; when associated with F-304, G-357 and F-806.
- N357 (= N322) mutation to G: No effect on hydrolytic activity compared to wild-type; when associated with F-304 and H-355. 58% reduction in hydrolytic activity compared to wild-type; when associated with F-304, H-355 and F-806.
- Y364 (= Y339) binding
Sites not aligning to the query:
- 402 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 478 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 522 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 622 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 739 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 760 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 777 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 806 W→F: 43% loss of hydrolytic activity against lactose compared to wild-type. 58% reduction in hydrolytic activity compared to wild-type; when associated with F-304, H-355 and G-357.; W→S: 90% loss of hydrolytic activity against lactose compared to wild-type.
- 914 modified: carbohydrate, N-linked (GlcNAc...) asparagine
5ifpA Structure of beta-galactosidase from aspergillus niger (see paper)
27% identity, 53% coverage: 48:375/623 of query aligns to 11:360/968 of 5ifpA
Sites not aligning to the query:
O58247 Exo-beta-D-glucosaminidase; GlcNase; EC 3.2.1.- from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) (see paper)
32% identity, 24% coverage: 48:199/623 of query aligns to 11:181/778 of O58247
- D180 (≠ N198) mutation to N: Loss of activity.
- E181 (= E199) mutation to Q: Retains 10% of wild-type activity.
Sites not aligning to the query:
- 308 E→Q: Retains 15% of wild-type activity.
- 349 E→Q: Loss of activity.
5gsmA Glycoside hydrolase b with product
34% identity, 25% coverage: 46:199/623 of query aligns to 8:179/786 of 5gsmA
Sites not aligning to the query:
Q76HN4 Exo-beta-D-glucosaminidase; GlcNase; EC 3.2.1.- from Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)) (see 2 papers)
34% identity, 25% coverage: 46:199/623 of query aligns to 8:179/786 of Q76HN4
- Y53 (= Y92) binding
- GE 102:103 (≠ AE 138:139) binding
- D178 (≠ N198) mutation to N: Loss of activity.
- DE 178:179 (≠ NE 198:199) binding
- E179 (= E199) mutation to Q: Retains less than 3% of wild-type activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 306 binding ; E→Q: Retains 40% of wild-type activity.
- 347 binding ; E→Q: Loss of activity.
- 379 binding
Query Sequence
>N515DRAFT_0922 FitnessBrowser__Dyella79:N515DRAFT_0922
MRRREFLRLSALAPLGAMSLRLDAVTVPSLQAEPVPDGRPHRFALGKRAFLLDGREFQLR
SGEMHPIRVPAEYWTQRIRMVKAMGLNTVAIYLMWNALEKEPGVFDFESGNRDFVRFIKL
CQQEGMWVYLRPGPYVCAEWDFGGLPPYLLREPDMRVRHKDDARYMKAVTRYMDAIAPRI
APLMAERGGPILMVQVENEYASFGGDLAYLEQIQAMWRERGIHGPFSISDGLATIQKQQT
YLPGTALGLDGDTDFAAAQAIAGEMPVWVGEGYPGWLTHWGDQEFQRGDYAATLKKLMAE
GRSFNLYVAHGGTNFGFGAGANADADYGKFEPTITSYDYGAPIDERGEATADYRQFREII
GEHLSRPLSEVPAAPPAMRFAKIELKPYASLWDNLTPAPKSVEDGPVANELLLAQDHGMV
LYRAMSLKGGRLSIEGVRDYATVFGAGRYLGYISRVRKPGLSEATEVEVPAPHAQDGEAI
EILVDSFGHVGYGQAMADRKGIVGAIRLNGELQRRWSVHGFPLDAAYLAGLRPLAQAPER
PAVFFKGTLTLEKTADTYLGMDAWDKGYVWVNGHLLGRYWRIGPQQRLFCPASWLKAGKN
EVLVFDMHRTEGAAIEGFERLHG
Or try a new SitesBLAST search
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