Basic Information | |
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Species | Brachypodium distachyon |
Cazyme ID | Bradi2g39450.1 |
Family | GH35 |
Protein Properties | Length: 567 Molecular Weight: 61339.8 Isoelectric Point: 7.4279 |
Chromosome | Chromosome/Scaffold: 2 Start: 39508137 End: 39510726 |
Description | beta-galactosidase 15 |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH35 | 31 | 175 | 0 |
LVIDGERRIIVSGSIHYPRSTPEMWPELIRKAKEGGLDAIETYVFWNGHEPRKRQVLNITTSRASTTYAILRIGPYICGEWNYGGLPAWLRDISGMQFRM HNDPFEKKMETFTSLIVAKLKEAKLFAGQGGPIILSQFEDRDVNV |
Full Sequence |
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Protein Sequence Length: 567 Download |
MDRILPLLLL AAAAVVLGAG GTEISHNNRA LVIDGERRII VSGSIHYPRS TPEMWPELIR 60 KAKEGGLDAI ETYVFWNGHE PRKRQVLNIT TSRASTTYAI LRIGPYICGE WNYGGLPAWL 120 RDISGMQFRM HNDPFEKKME TFTSLIVAKL KEAKLFAGQG GPIILSQFED RDVNVTLDDG 180 ATHVIVPAWS VSILPGCKAV AYNTARIKTQ TSVMAKKPHQ LPETTTAAGQ QQPMWSWMPE 240 NLAPFMTDEK GSFRKNELLE QITTSADESD YLWYRTSFEH KGEASYKLHV NTTGHELYAF 300 VNGKLVGKHH SPNGGFVFQL ETPVKLHSGK NYISLLSATI GLKNYGALFE MMPAGIVGGP 360 VKLIKTTSNT TAMDLSNSSW SYKSGLAGEY RSIHLDGDDT RQQWQSLNGT IPVHRPFTWY 420 KATFSAPAGS EPVVADLLGL GKGVAWVNGH NLGRYWPSYE AGGDPSAAAF KTVGVGAACV 480 EGVQVGDDVA LACGGHGRTI SSVDVASVGV TRGRCGGAYE GGCESEKALE ALKKACVGKE 540 SCTVRHTEEF LVAAGVSGEL TVQVTC* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam02140 | Gal_Lectin | 1.0e-7 | 491 | 566 | 83 | + Galactose binding lectin domain. | ||
COG1874 | LacA | 2.0e-11 | 24 | 121 | 107 | + Beta-galactosidase [Carbohydrate transport and metabolism] | ||
PLN03059 | PLN03059 | 2.0e-55 | 24 | 193 | 179 | + beta-galactosidase; Provisional | ||
PLN03059 | PLN03059 | 1.0e-59 | 170 | 566 | 475 | + beta-galactosidase; Provisional | ||
pfam01301 | Glyco_hydro_35 | 1.0e-62 | 30 | 169 | 149 | + Glycosyl hydrolases family 35. |
Gene Ontology | |
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GO Term | Description |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005529 | Interacting selectively and non-covalently with any carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates." [CHEBI:16646, GOC:mah] |
GO:0005975 | carbohydrate metabolic process |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | ACN27651.1 | 0 | 5 | 175 | 4 | 183 | unknown [Zea mays] |
GenBank | ACN27651.1 | 0 | 155 | 566 | 365 | 821 | unknown [Zea mays] |
GenBank | EEE50782.1 | 0 | 163 | 566 | 381 | 828 | hypothetical protein OsJ_31141 [Oryza sativa Japonica Group] |
RefSeq | NP_001043252.1 | 0 | 20 | 175 | 27 | 191 | Os01g0533400 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_001043252.1 | 0 | 163 | 566 | 381 | 827 | Os01g0533400 [Oryza sativa (japonica cultivar-group)] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3thd_D | 9e-20 | 23 | 171 | 10 | 165 | A Chain A, Structure Of The Catalytic Domain Of Human Bile Salt Activated Lipase |
PDB | 3thd_D | 0.001 | 333 | 458 | 450 | 571 | A Chain A, Structure Of The Catalytic Domain Of Human Bile Salt Activated Lipase |
PDB | 3thd_C | 9e-20 | 23 | 171 | 10 | 165 | A Chain A, Structure Of The Catalytic Domain Of Human Bile Salt Activated Lipase |
PDB | 3thd_C | 0.001 | 333 | 458 | 450 | 571 | A Chain A, Structure Of The Catalytic Domain Of Human Bile Salt Activated Lipase |
PDB | 3thd_B | 9e-20 | 23 | 171 | 10 | 165 | A Chain A, Structure Of The Catalytic Domain Of Human Bile Salt Activated Lipase |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
lactose degradation III | BETAGALACTOSID-RXN | EC-3.2.1.23 | β-galactosidase |