Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s66_29V6.1 |
Family | GH32 |
Protein Properties | Length: 641 Molecular Weight: 71820.8 Isoelectric Point: 6.0382 |
Chromosome | Chromosome/Scaffold: 66 Start: 139232 End: 141611 |
Description | Glycosyl hydrolases family 32 protein |
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 |
GH32 | 115 | 433 | 0 |
HFQPEKNWMNDPNGPMYYKGYYHFFYQYNPNAPVWGDIVWGHAVSTDLIHWLYLDIALVPDQWYDIQGVWSGSITMREDGVPIILYTGSSHASEQTQNIA YPEDPSDPLLRKWVKDPENPILRHPDGIDIRDFRDPTTAWKDVDGHWLMTVGAKRHNMGVALLYKSKDLKHWELQENFLHGVANTGMWECIDFYPVSVLG YRGLDSYSAAPSVKYVLKASLDDDRHDYYALGSYNVKSKSFHADDPSRDTGIGLRYDYGKFYASKSFYDAAQQRRILWGWANESDSEAADYAKGWSSVQA IPRTIRYDSKTMRNLIQEP |
Full Sequence |
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Protein Sequence Length: 641 Download |
MTRNPLLDAL VSEPSMDLES NGVSSEQSDA LSASTSRPAL SKMWMCVVLF TAACCIAMLA 60 HPTAVTTYLS EVSTGTKLHH GELRRVTHAP ISSTSGNGTI LPREVASYLH RTSFHFQPEK 120 NWMNDPNGPM YYKGYYHFFY QYNPNAPVWG DIVWGHAVST DLIHWLYLDI ALVPDQWYDI 180 QGVWSGSITM REDGVPIILY TGSSHASEQT QNIAYPEDPS DPLLRKWVKD PENPILRHPD 240 GIDIRDFRDP TTAWKDVDGH WLMTVGAKRH NMGVALLYKS KDLKHWELQE NFLHGVANTG 300 MWECIDFYPV SVLGYRGLDS YSAAPSVKYV LKASLDDDRH DYYALGSYNV KSKSFHADDP 360 SRDTGIGLRY DYGKFYASKS FYDAAQQRRI LWGWANESDS EAADYAKGWS SVQAIPRTIR 420 YDSKTMRNLI QEPVEELKEL RGPRVSQKSV RLAPGSVVEV HGAIGGQLDI EVVIEYPNVT 480 KLSQNGALID DGDHFDCSQG GAAHRGTFGP FGLLVLADES LNERTAVFFY ISYSKEGKWR 540 TRLCSDQTKS SMLPDVDTTI YGSFVEVLPS EDFLSLRVLV DRSIVESFGQ GGRMTITSRV 600 YPTMATDTAS HLYLFNNATT AITVRSIDVW QMRSVAMHAI * |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR01322 | scrB_fam | 2.0e-51 | 110 | 602 | 523 | + sucrose-6-phosphate hydrolase. [Energy metabolism, Biosynthesis and degradation of polysaccharides]. | ||
COG1621 | SacC | 1.0e-68 | 110 | 634 | 544 | + Beta-fructosidases (levanase/invertase) [Carbohydrate transport and metabolism] | ||
cd08996 | GH32_B_Fructosidase | 1.0e-90 | 121 | 436 | 328 | + 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 | 3.0e-133 | 115 | 433 | 327 | + 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 | 2.0e-166 | 115 | 592 | 488 | + Glycosyl hydrolases family 32. |
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 | ACT21538.1 | 0 | 110 | 634 | 45 | 565 | acid invertase [Vigna radiata] |
Swiss-Prot | P29001 | 0 | 110 | 635 | 115 | 636 | INVA_PHAAU RecName: Full=Acid beta-fructofuranosidase; AltName: Full=Acid sucrose hydrolase; AltName: Full=Acid invertase; Short=AI; AltName: Full=Vacuolar invertase; Contains: RecName: Full=Acid beta-fructofuranosidase 30 kDa subunit; Contains: RecName: Full=Acid beta-fructofuranosidase 38 kDa subunit; Flags: Precursor |
RefSeq | XP_001764172.1 | 0 | 104 | 640 | 28 | 564 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001784437.1 | 0 | 130 | 637 | 1 | 513 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002532576.1 | 0 | 110 | 634 | 119 | 639 | Acid beta-fructofuranosidase precursor, putative [Ricinus communis] |
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 | 3ugh_B | 0 | 110 | 638 | 18 | 542 | D Chain D, 3.1 Angstrom Cryoem Structure Of Cytoplasmic Polyhedrosis Virus |
PDB | 3ugh_A | 0 | 110 | 638 | 18 | 542 | D Chain D, 3.1 Angstrom Cryoem Structure Of Cytoplasmic Polyhedrosis Virus |
PDB | 3ugg_B | 0 | 110 | 638 | 18 | 542 | D Chain D, 3.1 Angstrom Cryoem Structure Of Cytoplasmic Polyhedrosis Virus |
PDB | 3ugg_A | 0 | 110 | 638 | 18 | 542 | D Chain D, 3.1 Angstrom Cryoem Structure Of Cytoplasmic Polyhedrosis Virus |
PDB | 3ugf_B | 0 | 110 | 638 | 18 | 542 | A Chain A, Crystal Structure Of A 6-Sst6-Sft From Pachysandra Terminalis |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
sucrose degradation III | RXN-1461 | EC-3.2.1.26 | β-fructofuranosidase |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
FC330584 | 266 | 202 | 467 | 0 |
DC940328 | 235 | 381 | 615 | 0 |
CT842376 | 547 | 101 | 639 | 0 |
DY919082 | 291 | 143 | 433 | 0 |
FC906419 | 292 | 124 | 415 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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