| Basic Information | |
|---|---|
| Species | Chlamydomonas reinhardtii |
| Cazyme ID | Cre12.g488050.t1.2 |
| Family | GH32 |
| Protein Properties | Length: 1102 Molecular Weight: 113110 Isoelectric Point: 7.1384 |
| Chromosome | Chromosome/Scaffold: 12 Start: 1407979 End: 1413874 |
| Description | cell wall invertase 4 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH32 | 10 | 229 | 0 |
| HVMPPQGWINDPNGPLFYKGYYHMFYQYVETGCQWSWGLMWGHAVSRDLVTWEHLPPAIVPSFGGFDGDGCFSGCATLDENGVPTILYTGVRLRSSEVCG PLPPPECDLGTACIETQCIAYADPADPKLTYWTKEEVPFLALPPPNMQLTAWRDPFVIGQPGQDGQDCWTIMIGAGVRDRGGTALVYRSPTLRGGSWTYA GELCRGAGDTGVIWECPVMM | |||
| Full Sequence |
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| Protein Sequence Length: 1102 Download |
| MAAEPRPRFH VMPPQGWIND PNGPLFYKGY YHMFYQYVET GCQWSWGLMW GHAVSRDLVT 60 WEHLPPAIVP SFGGFDGDGC FSGCATLDEN GVPTILYTGV RLRSSEVCGP LPPPECDLGT 120 ACIETQCIAY ADPADPKLTY WTKEEVPFLA LPPPNMQLTA WRDPFVIGQP GQDGQDCWTI 180 MIGAGVRDRG GTALVYRSPT LRGGSWTYAG ELCRGAGDTG VIWECPVMMH PPPLPAVTRL 240 LASPAAPPMP KPMSSPPFIC AIGGGGGGNM GSAPKQEGLE AAEDRGTEQP AIVLSPTAAV 300 ISPPRPPPHE LQQGKVAGSP AAPHAHIQLP VVLPSSPRPP MVRHLADAAG AAGATNAVAA 360 AAATAAAAAS AVGPYGGGTT SASLGLVAAV MSPRRPYPMV SVPAATGPAS SPLRSPARWK 420 LPSTLTPLPL PPSPPPPLVP QSPGSVLRHM TSPGGRYAGG YPSAVSPSAA FGALGSSAAA 480 TINGARLRAT TPPASPRIAR LPLLPTAPSP RPAAGPAAAA AAAPCTDGAA ASMSEGKRSA 540 SGMVMALLGA PAAATSPAKP ATPAPASPAT VIPDPGPPLI TAKLQLPKQQ TVTAQEAQQH 600 QQQHLDAAPP PGRLAARQLR RQQLLQAHGS FFCVCPDDCN SMSVYYLGAF RPAAGAFDLG 660 SALGPFRLDL GDIFYAPNTL ADPQGRSLLW GWLQEKPRKV GEYDYAGCLS LPRLLYLEVN 720 EEALDQEEEE AASVATGATM DGLPLTPGVG GAGQQQSGRR RGPAVHLVQR PPPELAKLRV 780 PGRQWCSDGL LLEAGATTPV CLPASAASHL ELELCMAPLP QPLMPQPTTP ATPSGAAGGA 840 AAAAAAMFGH SRQHGGPSAP AAAAGVVPCP QGTCGGGGSR CSGVLLHSWR GGVEGGAALL 900 YHWDSGVLEV VFEALDPHTL TFSLAAPGAR RVGGPLLRPP APGQPLSLRV FLDYSCLEVF 960 TGDGEVLTAR VYRGVPPAPP PAPRGSSGRG SSSGGGSAAT TRRVSPLGTP RRQQQQAAVL 1020 QALQLKGLAL PASPSAAAGM LPDPFNHEQG HHGPHHHLLA HDAYASGGAA AAGVELVSFG 1080 CATEFESVAA YEVGEIWVDC A* 1140 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| smart00640 | Glyco_32 | 3.0e-7 | 634 | 814 | 189 | + Glycosyl hydrolases family 32. | ||
| cd08996 | GH32_B_Fructosidase | 4.0e-12 | 636 | 717 | 84 | + 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. | ||
| smart00640 | Glyco_32 | 1.0e-51 | 10 | 228 | 222 | + Glycosyl hydrolases family 32. | ||
| cd08996 | GH32_B_Fructosidase | 1.0e-56 | 16 | 239 | 225 | + 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. | ||
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| RefSeq | XP_001690911.1 | 0 | 12 | 1101 | 1 | 1090 | glycoside-hydrolase-like protein [Chlamydomonas reinhardtii] |
| RefSeq | XP_001691098.1 | 0 | 4 | 236 | 17 | 252 | predicted protein [Chlamydomonas reinhardtii] |
| RefSeq | YP_002570662.1 | 9e-36 | 3 | 226 | 32 | 231 | Glycosyl hydrolase family 32 domain protein [Chloroflexus sp. Y-400-fl] |
| RefSeq | YP_002753177.1 | 2e-36 | 1 | 226 | 41 | 260 | glycosyl hydrolase family, 32 [Acidobacterium capsulatum ATCC 51196] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2aey_A | 1e-29 | 6 | 243 | 8 | 219 | A Chain A, The Three-Dimensional Structure Of Beta-Fructosidase (Invertase) From Thermotoga Maritima |
| PDB | 2ade_A | 1e-29 | 6 | 243 | 8 | 219 | A Chain A, The Three-Dimensional Structure Of Beta-Fructosidase (Invertase) From Thermotoga Maritima |
| PDB | 2add_A | 1e-29 | 6 | 243 | 8 | 219 | A Chain A, The Three-Dimensional Structure Of Beta-Fructosidase (Invertase) From Thermotoga Maritima |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| sucrose degradation III | RXN-1461 | EC-3.2.1.26 | β-fructofuranosidase |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| BI723642 | 210 | 4 | 212 | 0 |
| BG844411 | 202 | 4 | 204 | 0 |
| BI724909 | 165 | 4 | 167 | 0 |
| BI723643 | 146 | 4 | 148 | 0 |
| BG847761 | 139 | 4 | 141 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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