| Basic Information | |
|---|---|
| Species | Physcomitrella patens |
| Cazyme ID | Pp1s51_338V6.1 |
| Family | GH32 |
| Protein Properties | Length: 569 Molecular Weight: 64056 Isoelectric Point: 8.8828 |
| Chromosome | Chromosome/Scaffold: 51 Start: 1996006 End: 1999198 |
| Description | Glycosyl hydrolases family 32 protein |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
 | |||
| Family | Start | End | Evalue |
| GH32 | 42 | 357 | 0 |
| RGITSSRKGPVYYKGYYHLFYQYNPFAAIPGNIEWHHVVSKDLIRWKFLGATLKRDQWYDANGCFSGSITILDDGTPVILYTGNSFENKQVQARADPEDP SDPLLRKWVKAPYNPIAPIPPGYNSSQFRDPTEAWRLSDGMWRMLVGANAGEGGLIGTALLYKSTDFQTWNFSNRLHENPTTGMWECPDLFPVRIKGRKG LNASAVGKGVLHVLKVSLDLNKHDYYSVGNYLTETDTYKPLIAEIDTGIGLRYDYGKYYASKTFFDPIRQRRIVYGWTNESTSTMDDVAKGWAGLQSIPR IVYLDQRANTSLIQWP | |||
| Full Sequence |
|---|
| Protein Sequence Length: 569 Download |
| MEVYRCKPAA ATVVLLLLCL TWTTTLLPLR STTKDWAYLT ERGITSSRKG PVYYKGYYHL 60 FYQYNPFAAI PGNIEWHHVV SKDLIRWKFL GATLKRDQWY DANGCFSGSI TILDDGTPVI 120 LYTGNSFENK QVQARADPED PSDPLLRKWV KAPYNPIAPI PPGYNSSQFR DPTEAWRLSD 180 GMWRMLVGAN AGEGGLIGTA LLYKSTDFQT WNFSNRLHEN PTTGMWECPD LFPVRIKGRK 240 GLNASAVGKG VLHVLKVSLD LNKHDYYSVG NYLTETDTYK PLIAEIDTGI GLRYDYGKYY 300 ASKTFFDPIR QRRIVYGWTN ESTSTMDDVA KGWAGLQSIP RIVYLDQRAN TSLIQWPIEE 360 VQTLRRKKIT VKDVNLEGGE VARLMDVSGV QLDIEVAFKI PDVKQGSTPT ELIAESGPSI 420 CSQKGASMRG MYGPFGLLVL ASNDLTEQTA VYFYFVFTKK DGWKTLVCSD QSRSTVSMNL 480 TPDKTTYGSY VRVYDDEKLL KLRLLVDHSV VETFAQGGRT VITTRVYPKF AQSKNARVFL 540 FNNGSETVNV DSATVWNMAT VRFVDFGQ* |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
 | ||||||||
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| TIGR01322 | scrB_fam | 8.0e-53 | 50 | 529 | 501 | + sucrose-6-phosphate hydrolase. [Energy metabolism, Biosynthesis and degradation of polysaccharides]. | ||
| COG1621 | SacC | 2.0e-65 | 50 | 528 | 490 | + Beta-fructosidases (levanase/invertase) [Carbohydrate transport and metabolism] | ||
| cd08996 | GH32_B_Fructosidase | 7.0e-88 | 50 | 360 | 317 | + Glycosyl hydrolase family 32, beta-fructosidases. Glycosyl hydrolase family GH32 cleaves sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). This family also contains other fructofuranosidases such as inulinase (EC 3.2.1.7), exo-inulinase (EC 3.2.1.80), levanase (EC 3.2.1.65), and transfructosidases such sucrose:sucrose 1-fructosyltransferase (EC 2.4.1.99), fructan:fructan 1-fructosyltransferase (EC 2.4.1.100), sucrose:fructan 6-fructosyltransferase (EC 2.4.1.10), fructan:fructan 6G-fructosyltransferase (EC 2.4.1.243) and levan fructosyltransferases (EC 2.4.1.-). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. | ||
| pfam00251 | Glyco_hydro_32N | 2.0e-114 | 50 | 357 | 316 | + Glycosyl hydrolases family 32 N-terminal domain. This domain corresponds to the N-terminal domain of glycosyl hydrolase family 32 which forms a five bladed beta propeller structure. | ||
| smart00640 | Glyco_32 | 3.0e-151 | 50 | 518 | 478 | + Glycosyl hydrolases family 32. | ||
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| RefSeq | XP_001755639.1 | 0 | 52 | 566 | 57 | 570 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_001761961.1 | 0 | 50 | 568 | 20 | 538 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_001764172.1 | 0 | 5 | 561 | 2 | 559 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_001774490.1 | 0 | 28 | 561 | 10 | 580 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_001783601.1 | 0 | 49 | 566 | 25 | 541 | 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 | 3ugh_B | 0 | 41 | 566 | 27 | 544 | A Chain A, Crystal Structure Analysis Of A 14 Repeat C-Terminal Fragment Of Toxin Tcda In Clostridium Difficile |
| PDB | 3ugh_A | 0 | 41 | 566 | 27 | 544 | A Chain A, Crystal Structure Analysis Of A 14 Repeat C-Terminal Fragment Of Toxin Tcda In Clostridium Difficile |
| PDB | 3ugg_B | 0 | 41 | 566 | 27 | 544 | A Chain A, Crystal Structure Analysis Of A 14 Repeat C-Terminal Fragment Of Toxin Tcda In Clostridium Difficile |
| PDB | 3ugg_A | 0 | 41 | 566 | 27 | 544 | A Chain A, Crystal Structure Analysis Of A 14 Repeat C-Terminal Fragment Of Toxin Tcda In Clostridium Difficile |
| PDB | 3ugf_B | 0 | 41 | 566 | 27 | 544 | A Chain A, Crystal Structure Of A 6-Sst6-Sft From Pachysandra Terminalis |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| sucrose degradation III | RXN-1461 | EC-3.2.1.26 | β-fructofuranosidase |
