| Basic Information | |
|---|---|
| Species | Arabidopsis lyrata |
| Cazyme ID | 877397 |
| Family | GH35 |
| Protein Properties | Length: 687 Molecular Weight: 77135.5 Isoelectric Point: 6.0848 |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
 | |||
| Family | Start | End | Evalue |
| GH35 | 69 | 393 | 0 |
| FWKDGNHFQIIGGDLHYFRVLPEYWEDRLLRAKALGLNTIQVYVPWNLHEPKPGKMVFEGIGDLVSFLKLCDKLDFMVMLRAGPYICGEWDLGGFPAWLL SVKPRLQLRTSDPAYLKLVERWWGVLLPKIFPLIYSNGGPVIMVQIENEYGSYGNDKAYLRKLVSMARGHLGDDIIVYTTDGGTKETLEKGTVPVDDVYS AVDFTTGDDPWPIFELQKKFNAPGSSPPLSSEFYTGWLTHWGEKIAKTDAEFTATSLEKILSRNGSAVLYMVHGGTNFGFYNGANTGSEESDYKPDLTSY DYDAPIKESGDIDNPKFRALQRVIK | |||
| Full Sequence |
|---|
| Protein Sequence Length: 687 Download |
| MAMTSRRSWP STGRQTRHQL AFVLLLVLVA VGIYVPVLAL PSLSLPPEIP GDEKMIMMSR 60 KFYIKDDSFW KDGNHFQIIG GDLHYFRVLP EYWEDRLLRA KALGLNTIQV YVPWNLHEPK 120 PGKMVFEGIG DLVSFLKLCD KLDFMVMLRA GPYICGEWDL GGFPAWLLSV KPRLQLRTSD 180 PAYLKLVERW WGVLLPKIFP LIYSNGGPVI MVQIENEYGS YGNDKAYLRK LVSMARGHLG 240 DDIIVYTTDG GTKETLEKGT VPVDDVYSAV DFTTGDDPWP IFELQKKFNA PGSSPPLSSE 300 FYTGWLTHWG EKIAKTDAEF TATSLEKILS RNGSAVLYMV HGGTNFGFYN GANTGSEESD 360 YKPDLTSYDY DAPIKESGDI DNPKFRALQR VIKKYNVASH SIIPSNKQRK AYGPIKMQMT 420 TSLIDLVSMA DPADVIISAN PISMESAGQM FGFVLYESSY IAKKSGNILR IPKVHDRAQV 480 FVSCLSQDVG VLRYIGTTER WNNQPVSLPT IECTTNTSLF ILVENMGRVN YGPYIFDEKG 540 ILSSVYLDGQ ILHGWKMIPI PFHNLNQVPN ISFEMQHTKK RNVVGQKEPA LFAGEFSINT 600 TEEIEDTYLS FNGWGKGVAF INEFNIGRYW PSVGPQCNLY VPAPLLKPGK NTLVIFELES 660 PHLELLLESV DQEDFVCGSY DSKVSQ* |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam02449 | Glyco_hydro_42 | 2.0e-7 | 82 | 219 | 155 | + Beta-galactosidase. This group of beta-galactosidase enzymes belong to the glycosyl hydrolase 42 family. The enzyme catalyzes the hydrolysis of terminal, non-reducing terminal beta-D-galactosidase residues. | ||
| COG1874 | LacA | 3.0e-34 | 67 | 656 | 636 | + Beta-galactosidase [Carbohydrate transport and metabolism] | ||
| PLN03059 | PLN03059 | 1.0e-45 | 68 | 405 | 351 | + beta-galactosidase; Provisional | ||
| pfam01301 | Glyco_hydro_35 | 5.0e-159 | 68 | 395 | 328 | + Glycosyl hydrolases family 35. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
| GO:0005975 | carbohydrate metabolic process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAD55646.1 | 0 | 1 | 649 | 1 | 587 | AC008017_19 Similar to acid beta-galactosidase [Arabidopsis thaliana] |
| EMBL | CBI35958.1 | 0 | 57 | 684 | 70 | 707 | unnamed protein product [Vitis vinifera] |
| RefSeq | NP_001031273.1 | 0 | 87 | 686 | 26 | 634 | BGAL17 (beta-galactosidase 17); beta-galactosidase/ catalytic/ cation binding [Arabidopsis thaliana] |
| RefSeq | NP_565051.1 | 0 | 1 | 686 | 1 | 696 | BGAL17 (beta-galactosidase 17); beta-galactosidase/ catalytic/ cation binding [Arabidopsis thaliana] |
| RefSeq | XP_002327549.1 | 0 | 60 | 686 | 1 | 642 | predicted protein [Populus trichocarpa] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3thd_D | 0 | 67 | 659 | 16 | 599 | A Chain A, Structure Of The Thermostable Pectate Lyase Pl 47 |
| PDB | 3thd_C | 0 | 67 | 659 | 16 | 599 | A Chain A, Structure Of The Thermostable Pectate Lyase Pl 47 |
| PDB | 3thd_B | 0 | 67 | 659 | 16 | 599 | A Chain A, Structure Of The Thermostable Pectate Lyase Pl 47 |
| PDB | 3thd_A | 0 | 67 | 659 | 16 | 599 | A Chain A, Structure Of The Thermostable Pectate Lyase Pl 47 |
| PDB | 3thc_D | 0 | 67 | 659 | 16 | 599 | A Chain A, Crystal Structure Of Human Beta-Galactosidase In Complex With Galactose |
