SitesBLAST
Comparing CA265_RS02480 FitnessBrowser__Pedo557:CA265_RS02480 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)
44% identity, 93% coverage: 27:605/620 of query aligns to 2:585/754 of 6eonA
Sites not aligning to the query:
3wf2A Crystal structure of human beta-galactosidase in complex with nbt-dgj
38% identity, 92% coverage: 33:604/620 of query aligns to 11:602/605 of 3wf2A
- binding (2R,3S,4R,5S)-N-butyl-3,4,5-trihydroxy-2-(hydroxymethyl)piperidine-1-carbothioamide: Y55 (= Y77), A100 (= A122), E101 (= E123), N159 (= N181), E160 (= E182), E240 (= E257), L246 (≠ F263), N293 (= N310), Y305 (= Y326), Y457 (≠ F473)
3wf1A Crystal structure of human beta-galactosidase in complex with 6s-nbi- gj
38% identity, 92% coverage: 33:604/620 of query aligns to 11:602/605 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 (= Y77), C99 (= C121), A100 (= A122), E101 (= E123), E160 (= E182), E240 (= E257), Y242 (= Y259), W245 (= W262), Y278 (= Y295), Y305 (= Y326)
3wf0A Crystal structure of human beta-galactosidase in complex with 6s-nbi- dgj
38% identity, 92% coverage: 33:604/620 of query aligns to 11:602/605 of 3wf0A
- binding (3Z,6S,7R,8S,8aS)-3-(butylimino)hexahydro[1,3]thiazolo[3,4-a]pyridine-6,7,8-triol: Y55 (= Y77), C99 (= C121), A100 (= A122), E101 (= E123), N159 (= N181), E160 (= E182), E240 (= E257), W245 (= W262), L246 (≠ F263), Y457 (≠ F473)
3wezA Crystal structure of human beta-galactosidase in complex with noev
38% identity, 92% coverage: 33:604/620 of query aligns to 11:602/605 of 3wezA
- binding (1S,2S,3S,6R)-4-(hydroxymethyl)-6-(octylamino)cyclohex-4-ene-1,2,3-triol: Y55 (= Y77), C99 (= C121), A100 (= A122), E101 (= E123), E160 (= E182), E240 (= E257), Y242 (= Y259), L246 (≠ F263), N293 (= N310), Y305 (= Y326), Y457 (≠ F473)
3thdA Crystal structure of human beta-galactosidase in complex with 1- deoxygalactonojirimycin (see paper)
38% identity, 92% coverage: 33:604/620 of query aligns to 11:602/605 of 3thdA
- binding (2R,3S,4R,5S)-2-(hydroxymethyl)piperidine-3,4,5-triol: Y55 (= Y77), C99 (= C121), A100 (= A122), E101 (= E123), N159 (= N181), E160 (= E182), E240 (= E257), Y305 (= Y326)
- binding sulfate ion: S294 (≠ T315), P295 (= P316), Y296 (= Y317), R323 (= R344), Q327 (= Q348), R429 (= R443), N430 (≠ R444)
3thcA Crystal structure of human beta-galactosidase in complex with galactose (see paper)
38% identity, 92% coverage: 33:604/620 of query aligns to 11:602/605 of 3thcA
- binding beta-D-galactopyranose: Y55 (= Y77), C99 (= C121), A100 (= A122), E101 (= E123), E160 (= E182), E240 (= E257), Y242 (= Y259), Y278 (= Y295), Y305 (= Y326)
- binding sulfate ion: S294 (≠ T315), P295 (= P316), Y296 (= Y317), R323 (= R344), Q327 (= Q348), R429 (= R443), N430 (≠ R444)
4e8cA Crystal structure of streptococcal beta-galactosidase in complex with galactose (see paper)
39% identity, 94% coverage: 28:607/620 of query aligns to 3:589/594 of 4e8cA
P16278 Beta-galactosidase; Acid beta-galactosidase; Lactase; Elastin receptor 1; EC 3.2.1.23 from Homo sapiens (Human) (see 33 papers)
38% identity, 92% coverage: 33:604/620 of query aligns to 39:644/677 of P16278
- R49 (≠ Q43) to C: in GM1G1 and GM1G2; decrease in galactosidase activity; dbSNP:rs72555358
- I51 (= I45) to T: in GM1G3; no effect on catalytic activity; decreased protein stability; dbSNP:rs72555390
- R59 (= R53) 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 (= R62) 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 (= T76) to M: in GM1G3; mild phenotype; dbSNP:rs72555393
- Y83 (= Y77) 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 (≠ S117) to R: in GM1G1; decrease in galactosidase activity; dbSNP:rs28934274
- E129 (= E123) binding ; to Q: in dbSNP:rs886042079
- M132 (≠ F126) to T: in GM1G1; 4.3% of wild-type galactosidase activity; dbSNP:rs1553612189
- G134 (= G128) to R: in GM1G2; uncertain significance
- R148 (= R142) to C: in GM1G3 and GM1G2; dbSNP:rs192732174
- S149 (= S143) to F: in MPS4B; 2.0% of wild-type galactosidase activity; dbSNP:rs778700089
- D151 (= D145) to Y: in GM1G1; complete lack of protein; loss of galactosidase activity
- L155 (= L149) to R: in GM1G2 and GM1G3; 6.7% of wild-type galactosidase activity; dbSNP:rs376710410
- L162 (≠ I156) to S: in GM1G1; loss of galactosidase activity
- L173 (≠ Q167) to P: in GM1G1; loss of galactosidase activity; dbSNP:rs397515617
- Q184 (= Q178) to R: in GM1G1; loss of galactosidase activity
- N187 (= N181) binding
- G190 (= G184) to D: in GM1G1; 3.4% of wild-type galactosidase activity; dbSNP:rs756575833
- C195 (≠ S188) modified: Disulfide link with 230
- D198 (≠ E191) to Y: in MPS4B; 17.4% of wild-type galactosidase activity
- R201 (≠ S194) 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 (≠ N220) modified: Disulfide link with 195
- L236 (= L226) to P: in GM1G1; decrease in galactosidase activity
- T239 (≠ A229) to M: in GM1G1; loss of galactosidase activity; severe mutation; causes a rapid degradation of the protein precursor; dbSNP:rs746766232
- N247 (≠ E237) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- Q255 (≠ D245) to H: in GM1G1; 2.4% of wild-type galactosidase activity; dbSNP:rs1553610553
- G262 (= G251) to E: in GM1G2; decrease in galactosidase activity; dbSNP:rs377174858
- Y270 (= Y259) to D: in GM1G3; originally classified as Morquio syndrome; dbSNP:rs376663785
- W273 (= W262) to L: in MPS4B; decreased galactosidase activity; dbSNP:rs72555362
- H281 (= H270) to Y: in GM1G1 and GM1G3; dbSNP:rs745386663
- L297 (= L286) to F: in GM1G3; decrease in galactosidase activity
- F314 (≠ R303) to L: in GM1G2; decrease in galactosidase activity
- N318 (= N307) to H: in GM1G1; uncertain significance
- T329 (≠ S322) to I: in GM1G1; 5.0% of wild-type galactosidase activity
- Y331 (= Y324) to C: in GM1G1; uncertain significance
- D332 (= D325) to E: in GM1G1; 2.3% of wild-type galactosidase activity; to N: in GM1G1; decrease in galactosidase activity; dbSNP:rs781658798
- Y333 (= Y326) binding ; to H: in GM1G2; 3.0% of wild-type galactosidase activity; the mutant protein is localized in the lysosomal-endosomal compartment
- L337 (= L330) to P: in GM1G1 and GM1G2; loss of galactosidase activity; dbSNP:rs752177002
- P397 (≠ L384) to A: in MPS4B; 24.0% of wild-type galactosidase activity
- Q408 (≠ E398) to P: in MPS4B; 1.1% of wild-type galactosidase activity; dbSNP:rs72555369
- G414 (= G404) to V: in GM1G2; decrease in galactosidase activity
- T420 (= T410) to K: in GM1G3; decrease in galactosidase activity; to P: in GM1G1; loss of galactosidase activity; dbSNP:rs200181401
- S434 (≠ E424) to L: in GM1-gangliosidosis; unclassified clinical type; dbSNP:rs267599773
- L436 (vs. gap) to F: seems to have a modulating action in the expression of the severity of other mutations; dbSNP:rs34421970
- G438 (vs. gap) to E: in GM1G3 and MPS4B; mild form; 5.7% of wild-type galactosidase activity; dbSNP:rs72555367
- D441 (= D427) to N: in GM1G1; loss of galactosidase activity; dbSNP:rs780724173
- Y444 (≠ L430) to C: in MPS4B; loss of galactosidase activity
- N464 (= N451) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- R482 (= R470) to C: in MPS4B; loss of galactosidase activity; dbSNP:rs72555365; to H: in MPS4B and GM1G1; severe decrease in galactosidase activity; dbSNP:rs72555391
- N484 (= N472) 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 (= K482) to N: in GM1G2; decrease in galactosidase activity; dbSNP:rs1172435886
- G494 (= G483) to S: in MPS4B; loss of galactosidase activity
- N498 (≠ Y487) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- T500 (≠ S489) to A: in MPS4B; mild form; 2.1% of wild-type galactosidase activity; dbSNP:rs72555368
- W509 (= W498) to C: in MPS4B; also in a patient with a slowly progressive form of GM1-gangliosidosis; loss of galactosidase activity; dbSNP:rs72555363
- L514 (≠ F505) to P: in GM1G1; decrease in galactosidase activity
- R521 (≠ K512) 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 (vs. gap) to G: results in near-normal activity corresponding to 60%-100% of the wild-type depending on the expression system; dbSNP:rs73826339
- G554 (= G528) to E: in GM1-gangliosidosis; unclassified clinical type
- N555 (≠ T529) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- G579 (= G548) to D: in GM1G1 and GM1G2; loss of galactosidase activity; severe mutation; dbSNP:rs746350513
- R590 (≠ K559) to C: in GM1G1; loss of galactosidase activity; dbSNP:rs794727165
- Y591 (= Y560) 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 (≠ I563) to W: reduction of galactosidase activity; dbSNP:rs201807974
- P597 (= P565) to L: in GM1G2; decrease in galactosidase activity; to S: in GM1G1; 2.1% of wild-type galactosidase activity
- T600 (= T568) to I: in GM1G2; decrease in galactosidase activity
- C626 (vs. gap) modified: Disulfide link with 634
- C634 (≠ N594) modified: Disulfide link with 626
Sites not aligning to the query:
- 10 P → L: in dbSNP:rs7637099
3w5fA Crystal structure of tomato beta-galactosidase 4
33% identity, 49% coverage: 32:334/620 of query aligns to 10:301/701 of 3w5fA
6ik5A Crystal structure of tomato beta-galactosidase (tbg) 4 in complex with galactose (see paper)
33% identity, 49% coverage: 32:334/620 of query aligns to 8:299/705 of 6ik5A
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)
35% identity, 24% coverage: 35:182/620 of query aligns to 13:181/778 of O58247
- D180 (≠ N181) mutation to N: Loss of activity.
- E181 (= E182) 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
44% identity, 16% coverage: 35:136/620 of query aligns to 11:116/786 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)
44% identity, 16% coverage: 35:136/620 of query aligns to 11:116/786 of Q76HN4
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 178 D→N: Loss of activity.
- 178:179 binding
- 179 E→Q: Retains less than 3% of wild-type activity.
- 306 binding ; E→Q: Retains 40% of wild-type activity.
- 347 binding ; E→Q: Loss of activity.
- 379 binding
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)
28% identity, 49% coverage: 32:337/620 of query aligns to 50:375/1007 of A2QAN3
- Y96 (= Y77) binding
- NAE 140:142 (≠ CAE 121:123) binding
- N156 (≠ K137) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- N199 (= N181) binding
- C205 (≠ G187) modified: Disulfide link with 206
- C206 (≠ S188) modified: Disulfide link with 205
- C266 (vs. gap) modified: Disulfide link with 315
- E298 (= E257) active site, Nucleophile; mutation to Q: Loss of hydrolytic activity.
- Y304 (≠ F263) 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 (≠ P274) modified: Disulfide link with 266
- Y355 (= Y317) 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 (≠ P319) 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 (= Y326) 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)
28% identity, 49% coverage: 32:337/620 of query aligns to 10:335/968 of 5ifpA
Sites not aligning to the query:
5iftA Structure of e298q-beta-galactosidase from aspergillus niger in complex with 3-b-galactopyranosyl glucose (see paper)
28% identity, 49% coverage: 32:337/620 of query aligns to 10:335/968 of 5iftA
- binding beta-D-galactopyranose: Y56 (= Y77), N100 (≠ C121), A101 (= A122), E102 (= E123), E160 (= E182), Q258 (≠ E257), Y264 (≠ F263), Y302 (= Y295), Y324 (= Y326)
- binding alpha-D-glucopyranose: E160 (= E182), F224 (vs. gap)
- binding alpha-D-mannopyranose: W267 (= W266), G268 (= G267), E282 (≠ K281), R285 (≠ S284)
Sites not aligning to the query:
4iugA Crystal structure of beta-galactosidase from aspergillus oryzae in complex with galactose (see paper)
28% identity, 49% coverage: 32:337/620 of query aligns to 11:327/957 of 4iugA
- binding beta-D-mannopyranose: R71 (≠ D91)
- binding beta-D-galactopyranose: Y57 (= Y77), N101 (≠ C121), A102 (= A122), E103 (= E123), E161 (= E182), D210 (= D234), Y212 (vs. gap), E250 (= E257), F256 (= F263), Y294 (= Y295), Y316 (= Y326)
- binding alpha-D-mannopyranose: A219 (vs. gap), G260 (= G267), G261 (≠ A268), P262 (= P269), Y268 (≠ A275), N272 (≠ T279), H273 (≠ G280), E274 (≠ K281), R277 (≠ S284)
Sites not aligning to the query:
Q2UCU3 Beta-galactosidase A; Acidic beta-galactosidase; Ao-beta-gal; Lactase A; EC 3.2.1.23 from Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) (see paper)
28% identity, 49% coverage: 32:337/620 of query aligns to 50:375/1005 of Q2UCU3
- Y96 (= Y77) binding
- NAE 140:142 (≠ CAE 121:123) binding
- N199 (= N181) binding
- D258 (= D234) binding
- C266 (vs. gap) modified: Disulfide link with 315
- C315 (≠ P274) modified: Disulfide link with 266
- Y364 (= Y326) binding
- N373 (= N335) modified: carbohydrate, N-linked (GlcNAc...) asparagine
Sites not aligning to the query:
- 402 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 622 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 760 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 777 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 914 modified: carbohydrate, N-linked (GlcNAc...) asparagine
Q700S9 Beta-galactosidase A; Lactase A; EC 3.2.1.23 from Penicillium sp. (see paper)
27% identity, 49% coverage: 32:337/620 of query aligns to 50:376/1011 of Q700S9
- Y96 (= Y77) binding
- NAE 140:142 (≠ CAE 121:123) binding
- N199 (= N181) binding
- C205 (≠ G187) modified: Disulfide link with 206
- C206 (≠ S188) modified: Disulfide link with 205
- C267 (≠ L233) modified: Disulfide link with 316
- C316 (≠ P274) modified: Disulfide link with 267
- Y365 (= Y326) binding
- N374 (= N335) 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
Query Sequence
>CA265_RS02480 FitnessBrowser__Pedo557:CA265_RS02480
MYLFNTIRAVILALLFTIPVFAQETHTFALGDDAFLLDGKPFQMISGEIHYPRIPREAWR
SRMKMAKAMGLNTIGTYVFWNLHEPQKGIFDFKGNNDVAEFVRIAKEEGLWVILRPSPYV
CAEWEFGGYPYWLENEKGLVVRSKDPLYLKEYEKYIMEVGKQLAPLQVNHGGNILMVQIE
NEYGSYGSDKEYLSINQKLFIKAGFDGLLYTCDPAPDLTNGYLPGLLPAVNGLDNPEKVK
KLIADHHNGKGPYYIAEWYPAWFDWWGAPHHTVPAARFTGKLDSVLAAGISINMYMFHGG
TTRGFMNGANFKDETPYEPQISSYDYDAPLDEAGNATAKFHAFRSIIQKHLPAGTTLPPV
PNPKPAIRIPTIKLGLTASLTGNLSKGTYHDSPLTFEELLQDYGFVLYRTTLTGGIKGTL
KIKELRDYALIMVNGKQIATLDRRLNQDSLNISLPQGKVVLDILVENLGRINFGKYLLQN
RKGITGYVSFNNRKIKGWTMYRFPFNDLSKIKYQSTVKAGNTPVIKKGTFNLTAIGDTYL
DMRKWGKGMVWVNGHNLGKYWSIGPQETLYLPAEWLRKGVNSIEVLELLRPNQNEITGID
HPLLDGIDHSVPDHLPRKID
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