| Basic Information | |
|---|---|
| Species | Malus domestica |
| Cazyme ID | MDP0000561738 |
| Family | GH32 |
| Protein Properties | Length: 704 Molecular Weight: 78696 Isoelectric Point: 10.1113 |
| Chromosome | Chromosome/Scaffold: 009168711 Start: 11396 End: 17464 |
| Description | Glycosyl hydrolases family 32 protein |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH32 | 194 | 501 | 0 |
| AGPLIYKGIYHLFYQYNPKGVVWGNIVWAHSTSTDLVNWTPHDAAIFPSQPSDINGCWSGSATILPSGKPVILYTGINPQNQQVQNLAFPKNLSDPFLRE WVKVPQNPLMAPTQANHINASSFRDPTTAWLGPDKRWRVIIGSKQNQRGLAILYRSKDFLHWVKAKHPLHSAKKTGMWECPDFFPVSIHGQNGLDSSENG PAVKHVLKASLDNTKHEYYTIGTYNIDKDIYIPDKGSVESDSGLRYDYGKFYASKTFFDSSKNRRILWGWINESSSVEGDIKKGWSGLQAIPRTLWLAKS GKQLVQWP | |||
| Full Sequence |
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| Protein Sequence Length: 704 Download |
| MKQSTNTSPF TALAVRTSAI KPWPVKRTAP HSPPRGHHHK HQPPYLISSQ ISTRSRSPHL 60 GRPPSSRQWN NFARRSPVNH DSRAKSPDSQ PELREGGTSR SDLGQRFNYR TRSSTEHRTP 120 PFEALLEIGH AVLRLEASHH VYRSLQTSEL TSSHQDTEPY RTGYHFQPPK NWINGFSALS 180 NFKSTKALSI TLAAGPLIYK GIYHLFYQYN PKGVVWGNIV WAHSTSTDLV NWTPHDAAIF 240 PSQPSDINGC WSGSATILPS GKPVILYTGI NPQNQQVQNL AFPKNLSDPF LREWVKVPQN 300 PLMAPTQANH INASSFRDPT TAWLGPDKRW RVIIGSKQNQ RGLAILYRSK DFLHWVKAKH 360 PLHSAKKTGM WECPDFFPVS IHGQNGLDSS ENGPAVKHVL KASLDNTKHE YYTIGTYNID 420 KDIYIPDKGS VESDSGLRYD YGKFYASKTF FDSSKNRRIL WGWINESSSV EGDIKKGWSG 480 LQAIPRTLWL AKSGKQLVQW PVQEIEKLRG KTVKLPSTVL KGGSVREVVG VTAAQADVEI 540 TFGISDFKKA EVLDPSWTDP QLLCGQKSAT VKGSLGPFGL YVLASKDLKE YTAVFYRIFK 600 ANNKYVVLLC SDQSRSSLNK DNDKTTYGAF VKVDPLREKL SLRNLIDHSI VESFGGEGKA 660 CITARVYPTL AIDDDAHLYA FNYGTEDVKI TGSAWSLKTA KIN* 720 |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd08772 | GH43_62_32_68 | 3.0e-49 | 196 | 489 | 308 | + Glycosyl hydrolase families: GH43, GH62, GH32, GH68. Members of the glycosyl hydrolase families 32, 43, 62 and 68 (GH32, GH43, GH62, GH68) all possess 5-bladed beta-propeller domains and comprise clans F and J, as classified by the carbohydrate-active enzymes database (CAZY). Clan F consists of families GH43 and GH62. GH43 includes beta-xylosidases, beta-xylanases, alpha-L-arabinases, and alpha-L-arabinofuranosidases, using aryl-glycosides as substrates, while family GH62 contains alpha-L-arabinofuranosidases (EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose sidechains from xylans. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Clan J consists of families GH32 and GH68. GH32 comprises sucrose-6-phosphate hydrolases, invertases, inulinases, levanases, eukaryotic fructosyltransferases, and bacterial fructanotransferases while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), all of which use sucrose as their preferential donor substrate. Members of this clan are retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) that 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. Structures of all families in the two clans manifest a funnel-shaped active site that comprises two subsites with a single route for access by ligands. | ||
| COG1621 | SacC | 3.0e-62 | 146 | 669 | 540 | + Beta-fructosidases (levanase/invertase) [Carbohydrate transport and metabolism] | ||
| cd08996 | GH32_B_Fructosidase | 3.0e-88 | 195 | 504 | 322 | + 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 | 1.0e-146 | 165 | 501 | 345 | + 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-180 | 165 | 658 | 504 | + 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 | AAD10960.1 | 0 | 131 | 703 | 18 | 577 | cell wall invertase precursor [Fragaria x ananassa] |
| GenBank | AAT09980.1 | 0 | 128 | 703 | 17 | 576 | cell wall apoplastic invertase [Vitis vinifera] |
| EMBL | CAD91338.1 | 0 | 137 | 703 | 20 | 564 | beta-fructofuranosidase [Glycine max] |
| EMBL | CBI35961.1 | 0 | 129 | 703 | 18 | 574 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002279788.1 | 0 | 129 | 703 | 18 | 575 | PREDICTED: hypothetical protein [Vitis vinifera] |
| 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 | 2qqw_A | 0 | 158 | 703 | 2 | 537 | A Chain A, Crystal Structure Of A Cell-Wall Invertase (D23a) From Arabidopsis Thaliana In Complex With Sucrose |
| PDB | 2xqr_K | 0 | 158 | 703 | 2 | 537 | B Chain B, Crystal Structure Of Plant Cell Wall Invertase In Complex With A Specific Protein Inhibitor |
| PDB | 2xqr_I | 0 | 158 | 703 | 2 | 537 | B Chain B, Crystal Structure Of Plant Cell Wall Invertase In Complex With A Specific Protein Inhibitor |
| PDB | 2xqr_G | 0 | 158 | 703 | 2 | 537 | B Chain B, Crystal Structure Of Plant Cell Wall Invertase In Complex With A Specific Protein Inhibitor |
| PDB | 2xqr_E | 0 | 158 | 703 | 2 | 537 | B Chain B, Crystal Structure Of Plant Cell Wall Invertase In Complex With A Specific Protein Inhibitor |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| CT842376 | 578 | 138 | 703 | 0 |
| DY273985 | 347 | 197 | 542 | 0 |
| FC881182 | 304 | 197 | 500 | 0 |
| EB152734 | 230 | 421 | 650 | 0 |
| DY666802 | 292 | 126 | 416 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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