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Basic Information | |
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Species | Glycine max |
Cazyme ID | Glyma17g34570.1 |
Family | GH32 |
Protein Properties | Length: 563 Molecular Weight: 64421.1 Isoelectric Point: 4.8659 |
Chromosome | Chromosome/Scaffold: 17 Start: 38567619 End: 38570943 |
Description | beta-fructofuranosidase 5 |
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 | 31 | 351 | 0 |
HFQPPQNWMNDPNAPMYYKGVYHFFYQHNPYAPTFGEKMVWAHSVSYDLINWIHLNHAIEPSDSYDINSCWSGSATILPGEEEQPVILYTGIDNNKYQVQ NMAMPKDLSDPFLREWVKHPQNPAMTPPSGVEVNNFRDPSTAWQGKDGKWRVVIGAQNGDEGKTILYQSEDFVNWRVELNPFFATDNTGVCECPDFFPVS INSTNGVDASVQSQSVRHVLKISYLRRHQDYYFLGKYVYDEGNFVPDVKFTGTSSDLRLDYGKFYASKSFFDHAKNRRILWGWVNECDTRQNDIEKGWAG LQCIPRQVWLDESGKQLMQWP |
Full Sequence |
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Protein Sequence Length: 563 Download |
MEINGEGASP HSINSIKFKV PEKQPYRTWY HFQPPQNWMN DPNAPMYYKG VYHFFYQHNP 60 YAPTFGEKMV WAHSVSYDLI NWIHLNHAIE PSDSYDINSC WSGSATILPG EEEQPVILYT 120 GIDNNKYQVQ NMAMPKDLSD PFLREWVKHP QNPAMTPPSG VEVNNFRDPS TAWQGKDGKW 180 RVVIGAQNGD EGKTILYQSE DFVNWRVELN PFFATDNTGV CECPDFFPVS INSTNGVDAS 240 VQSQSVRHVL KISYLRRHQD YYFLGKYVYD EGNFVPDVKF TGTSSDLRLD YGKFYASKSF 300 FDHAKNRRIL WGWVNECDTR QNDIEKGWAG LQCIPRQVWL DESGKQLMQW PIEEIEKLRD 360 KQISILGEKL VGGSIIEVSG ITASQADVEV LFELPELENV EWLDESEVDP HLLCSEEYAT 420 RSGTIGPFGL LALASEDQTE HTAVFFRIYR ASNRYICFMC SDQSRSSLRQ DLDKTTYGTI 480 FDIDPNVKTI SLRSLIDRSI IESFGEKGRI CITSRVYPSM SIDKNAHLYV FNNGSQSVVI 540 SELNAWSMKQ AEFGQEESIN KQ* 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR01322 | scrB_fam | 9.0e-54 | 22 | 359 | 355 | + sucrose-6-phosphate hydrolase. [Energy metabolism, Biosynthesis and degradation of polysaccharides]. | ||
COG1621 | SacC | 2.0e-68 | 22 | 378 | 366 | + Beta-fructosidases (levanase/invertase) [Carbohydrate transport and metabolism] | ||
cd08996 | GH32_B_Fructosidase | 1.0e-89 | 37 | 354 | 330 | + 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 | 6.0e-137 | 31 | 351 | 329 | + 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-151 | 31 | 485 | 465 | + 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 |
PDB | 1ST8 | 0 | 23 | 559 | 4 | 539 | A Chain A, Crystal Structure Of Fructan 1-Exohydrolase Iia From Cichorium Intybus |
EMBL | CAD49079.1 | 0 | 14 | 560 | 33 | 575 | fructan 1-exohydrolase [Campanula rapunculoides] |
RefSeq | XP_002278918.1 | 0 | 21 | 553 | 36 | 559 | PREDICTED: hypothetical protein isoform 3 [Vitis vinifera] |
RefSeq | XP_002309496.1 | 0 | 24 | 553 | 35 | 559 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002309497.1 | 0 | 1 | 558 | 25 | 571 | predicted protein [Populus trichocarpa] |
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 | 2aey_A | 0 | 23 | 559 | 4 | 539 | A Chain A, Structure Of Mouse Golgi Alpha-1,2-Mannosidase Ia Reveals The Molecular Basis For Substrate Specificity Among Class I Enzymes (Family 47 Glycosidases) |
PDB | 2ade_A | 0 | 23 | 559 | 4 | 539 | A Chain A, Structure Of Mouse Golgi Alpha-1,2-Mannosidase Ia Reveals The Molecular Basis For Substrate Specificity Among Class I Enzymes (Family 47 Glycosidases) |
PDB | 2add_A | 0 | 23 | 559 | 4 | 539 | A Chain A, Structure Of Mouse Golgi Alpha-1,2-Mannosidase Ia Reveals The Molecular Basis For Substrate Specificity Among Class I Enzymes (Family 47 Glycosidases) |
PDB | 1st8_A | 0 | 23 | 559 | 4 | 539 | A Chain A, Crystal Structure Of Fructan 1-Exohydrolase Iia From Cichorium Intybus |
PDB | 2aez_A | 0 | 23 | 559 | 4 | 539 | A Chain A, Crystal Structure Of Fructan 1-Exohydrolase Iia (E201q) From Cichorium Intybus In Complex With 1-Kestose |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
fructan degradation | RXN-1841 | EC-3.2.1.80 | fructan β-fructosidase |
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 |
CT842376 | 533 | 27 | 550 | 0 |
FE693031 | 280 | 271 | 550 | 0 |
FE709664 | 229 | 164 | 392 | 0 |
BG645655 | 264 | 9 | 271 | 0 |
BE659875 | 234 | 328 | 561 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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