y
Basic Information | |
---|---|
Species | Physcomitrella patens |
Cazyme ID | Pp1s213_129V6.1 |
Family | GH16 |
Protein Properties | Length: 301 Molecular Weight: 33398 Isoelectric Point: 9.6158 |
Chromosome | Chromosome/Scaffold: 213 Start: 679953 End: 681862 |
Description | xyloglucan endotransglucosylase/hydrolase 9 |
View CDS |
External Links |
---|
NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
GH16 | 43 | 215 | 4.1e-24 |
WTKNVKYTNDGRGVQLVLDPLSASGAASKTSYLFGGFGAWIKLPPRNSAGTVTTFYMLSTGPKYCEFDFEFLGNETGQPFLLHTNIHVNGVGGREQQIYL GFDPSETFHYYNFQWNKDVLVLYVDNTPVRMFKNLEGIVPNFKYPNSQAMGIYMSIWDGSTWATQGGRIPINW |
Full Sequence |
---|
Protein Sequence Length: 301 Download |
MGPRRAPSRS CIAIALLCLS IFVGGGHAQS RPGRGLAASF NPWTKNVKYT NDGRGVQLVL 60 DPLSASGAAS KTSYLFGGFG AWIKLPPRNS AGTVTTFYML STGPKYCEFD FEFLGNETGQ 120 PFLLHTNIHV NGVGGREQQI YLGFDPSETF HYYNFQWNKD VLVLYVDNTP VRMFKNLEGI 180 VPNFKYPNSQ AMGIYMSIWD GSTWATQGGR IPINWSAAPF VATYQNFRLN GCAVHNVLDQ 240 NSLRLCQGSK YASPGAYAQT VGMARVRQMR WVRANRVVYN YCDDRKRYPI APAECAHNTL 300 * 360 |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd02175 | GH16_lichenase | 2.0e-20 | 40 | 205 | 182 | + lichenase, member of glycosyl hydrolase family 16. Lichenase, also known as 1,3-1,4-beta-glucanase, is a member of glycosyl hydrolase family 16, that specifically cleaves 1,4-beta-D-glucosidic bonds in mixed-linked beta glucans that also contain 1,3-beta-D-glucosidic linkages. Natural substrates of beta-glucanase are beta-glucans from grain endosperm cell walls or lichenan from the Islandic moss, Cetraria islandica. This protein is found not only in bacteria but also in anaerobic fungi. This domain includes two seven-stranded antiparallel beta-sheets that are adjacent to one another forming a compact, jellyroll beta-sandwich structure. | ||
cd00413 | Glyco_hydrolase_16 | 6.0e-21 | 29 | 212 | 199 | + glycosyl hydrolase family 16. The O-Glycosyl hydrolases are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A glycosyl hydrolase classification system based on sequence similarity has led to the definition of more than 95 different families inlcuding glycosyl hydrolase family 16. Family 16 includes lichenase, xyloglucan endotransglycosylase (XET), beta-agarase, kappa-carrageenase, endo-beta-1,3-glucanase, endo-beta-1,3-1,4-glucanase, and endo-beta-galactosidase, all of which have a conserved jelly roll fold with a deep active site channel harboring the catalytic residues. | ||
pfam00722 | Glyco_hydro_16 | 9.0e-57 | 43 | 216 | 176 | + Glycosyl hydrolases family 16. | ||
PLN03161 | PLN03161 | 8.0e-76 | 52 | 295 | 247 | + Probable xyloglucan endotransglucosylase/hydrolase protein; Provisional | ||
cd02176 | GH16_XET | 3.0e-145 | 27 | 295 | 270 | + Xyloglucan endotransglycosylase, member of glycosyl hydrolase family 16. Xyloglucan endotransglycosylases (XETs) cleave and religate xyloglucan polymers in plant cell walls via a transglycosylation mechanism. Xyloglucan is a soluble hemicellulose with a backbone of beta-1,4-linked glucose units, partially substituted with alpha-1,6-linked xylopyranose branches. It binds noncovalently to cellulose, cross-linking the adjacent cellulose microfibrils, giving it a key structural role as a matrix polymer. Therefore, XET plays an important role in all plant processes that require cell wall remodeling. |
Gene Ontology | |
---|---|
GO Term | Description |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005618 | cell wall |
GO:0005975 | carbohydrate metabolic process |
GO:0006073 | cellular glucan metabolic process |
GO:0016762 | xyloglucan:xyloglucosyl transferase activity |
Annotations - NR Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | XP_001770193.1 | 0 | 66 | 300 | 2 | 234 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001772866.1 | 0 | 55 | 300 | 49 | 295 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001777007.1 | 0 | 1 | 300 | 1 | 300 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001781669.1 | 0 | 66 | 300 | 1 | 234 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001784557.1 | 0 | 11 | 300 | 9 | 297 | predicted protein [Physcomitrella patens subsp. patens] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 1un1_B | 0 | 46 | 298 | 29 | 275 | A Chain A, Crystal Structure Of The Toxoplasma Gondii Cyclophilin, 49.m03261 |
PDB | 1un1_A | 0 | 46 | 298 | 29 | 275 | A Chain A, Crystal Structure Of The Toxoplasma Gondii Cyclophilin, 49.m03261 |
PDB | 1umz_B | 0 | 46 | 298 | 29 | 275 | A Chain A, Xyloglucan Endotransglycosylase In Complex With The Xyloglucan Nonasaccharide Xllg. |
PDB | 1umz_A | 0 | 46 | 298 | 29 | 275 | A Chain A, Xyloglucan Endotransglycosylase In Complex With The Xyloglucan Nonasaccharide Xllg. |
PDB | 2uwb_B | 3.00018e-42 | 52 | 295 | 36 | 267 | A Chain A, Crystal Structure Of The Nasturtium Seedling Mutant Xyloglucanase Isoform Nxg1-Delta-Yniig |
Signal Peptide | |||||
---|---|---|---|---|---|
Cleavage Site | |||||
28 |
EST Download unfiltered results here | ||||
---|---|---|---|---|
Hit | Length | Start | End | EValue |
BY950833 | 216 | 1 | 213 | 0 |
CN202713 | 247 | 12 | 258 | 0 |
BY945550 | 164 | 1 | 164 | 0 |
FC341472 | 261 | 40 | 300 | 0 |
BJ952635 | 192 | 110 | 301 | 0 |
Orthologous Group | |||||
---|---|---|---|---|---|
Species | ID | ||||
Physcomitrella patens | Pp1s81_246V6.1 | Pp1s122_57V6.1 | Pp1s309_36V6.1 | Pp1s410_28V6.1 | Pp1s486_17V6.1 |
Pp1s486_14V6.1 | Pp1s141_131V6.1 |
Sequence Alignments (This image is cropped. Click for full image.) |
---|
![]() |