| Basic Information | |
|---|---|
| Species | Volvox carteri |
| Cazyme ID | Vocar20013968m |
| Family | GH32 |
| Protein Properties | Length: 1374 Molecular Weight: 141597 Isoelectric Point: 4.8463 |
| Chromosome | Chromosome/Scaffold: 6 Start: 2240435 End: 2249445 |
| Description | beta-fructofuranosidase 5 |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH32 | 105 | 343 | 0 |
| HVMPVSGWGSDPNGPIFYKGRYHLFYQARPGTCQWYWGMCWDHVVSYDLAHWERLPMALVPTPGGIDADGCFSGSIQVEPQSGIPVCFYTAARLRTNREV ALPHPPPSHDMGLKHIETQCCAICDPGMSVCDAAWGEEAACGHDELLVKWRKVPMPLMELPHTGQLTAWRDPWFVEQGDGRGREWTMLIGSGLKDGGGTA LVYRTQDITRGWRFVGHLCSWPDPGTGICWECPFLVQLQ | |||
| Full Sequence |
|---|
| Protein Sequence Length: 1374 Download |
| MSYAADLLGR RGGEGVWHHQ AVGDPCKEVQ QRYERCLFAN SEKGSDNAMT SASIGSSIAA 60 GAAAIPTTAS LAVLVDLGNH AAGMATGAAP PQPTAAADSL KPMFHVMPVS GWGSDPNGPI 120 FYKGRYHLFY QARPGTCQWY WGMCWDHVVS YDLAHWERLP MALVPTPGGI DADGCFSGSI 180 QVEPQSGIPV CFYTAARLRT NREVALPHPP PSHDMGLKHI ETQCCAICDP GMSVCDAAWG 240 EEAACGHDEL LVKWRKVPMP LMELPHTGQL TAWRDPWFVE QGDGRGREWT MLIGSGLKDG 300 GGTALVYRTQ DITRGWRFVG HLCSWPDPGT GICWECPFLV QLQPLPLCAH VLPTTDLAAL 360 MEAEGDGEGE DVVEQTAEEA KMIAGGGYDR SKELDDANGG YDTYGDYQRD DNEGRRVGSV 420 ASAEGVEAVA GPMPGPRLLV SSSSASALTA DSGRVLAVGL VDTLLHVVTS AAGPAVTSGG 480 AGGNAFADGL GPASLLPSIG TLAPRAASAD GNGGGGIDIS ITAAAAAPSG DGAAGAADVS 540 TVTITVTRAA GHTGETEGVS GAAAVVATAA STAAAAAAVA GVNGVGSITT ATATVQDGGE 600 GAKSASAVIQ FTVAPMTAAS SLDAVVPAAA VPRRSVSSLD AARTTQPPQP SSVPAAVPAA 660 TADEGIAAAA PGQAPIVRSC CLTSSTLTAS ATVPAAAAAD RAVLQDLHTM VTQVMEARRA 720 RARADAEAAA AAAAAAEEDA SLRGDSGGAV GSETTSGGKL SYSPGVMGHS AVPEPDTEVE 780 PLPAPVTMRY HKAQPLLPAG VPYSAAVVAA SCLPLHGDVD SASGHAHAPS LLPDRRWFFC 840 CAPDACTYSI IYWIGEYDST TAKYDMKGAE AGGRPRKLDL GNVLYAPTCF KDPQGRHILW 900 GYMKELRNVP APPCLCNKYS YAGCVSLPRA LYLRGDKLFQ LPLPELTALR SDVAVHFSRV 960 SLTHGSPWRL MGLRGLHLDL EMAISPGTAH RTVVLLRSWR PRGRGAAALV YDWTSRRLYV 1020 VFEAMHPSRQ ALWCGEHPPA GASTASAMTP PTPMAMQPPH EPWREGAKSS SSPPSAEAAV 1080 PGGGGGRGGN TSISTSTTTN SNSKGGNDGS SSDEAATLGG ATYGWPSVET GLLPAEMAPD 1140 VSSSEDVGSS SGGDGCFVGD SAGGATTMSL LPRRSGSSSS SGHLQAEAAA GVGGVGPSRP 1200 DGGLASARIA AAAAAAGGVG GGSEGGGNAD GPELDELDEE ENEHFDVIRD PDFIPDPDMN 1260 PLVEDWIRMK RDEAGGDLDL PPGSPLRLRV FLDASCLEVF TGSGQVLTTR VYRGHAPHVK 1320 QPDHHRQPPD QQQHADPGIE VWSVGGSCSL DDLHAYEMDT AWLREGDAPR QDT* 1380 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| smart00640 | Glyco_32 | 1.0e-11 | 814 | 1011 | 213 | + Glycosyl hydrolases family 32. | ||
| cd08996 | GH32_B_Fructosidase | 3.0e-14 | 829 | 945 | 126 | + 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 | 6.0e-42 | 105 | 343 | 244 | + Glycosyl hydrolases family 32. | ||
| cd08996 | GH32_B_Fructosidase | 9.0e-43 | 111 | 342 | 232 | + 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 | 107 | 352 | 1 | 230 | glycoside-hydrolase-like protein [Chlamydomonas reinhardtii] |
| RefSeq | XP_001690911.1 | 0.00000000000001 | 838 | 933 | 620 | 706 | glycoside-hydrolase-like protein [Chlamydomonas reinhardtii] |
| RefSeq | XP_001690911.1 | 0.000002 | 1273 | 1314 | 920 | 963 | glycoside-hydrolase-like protein [Chlamydomonas reinhardtii] |
| RefSeq | XP_001691098.1 | 0 | 101 | 351 | 19 | 254 | predicted protein [Chlamydomonas reinhardtii] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1uyp_F | 1e-27 | 100 | 342 | 2 | 197 | A Chain A, The Three-Dimensional Structure Of Beta-Fructosidase (Invertase) From Thermotoga Maritima |
| PDB | 1uyp_E | 1e-27 | 100 | 342 | 2 | 197 | A Chain A, The Three-Dimensional Structure Of Beta-Fructosidase (Invertase) From Thermotoga Maritima |
| PDB | 1uyp_D | 1e-27 | 100 | 342 | 2 | 197 | A Chain A, The Three-Dimensional Structure Of Beta-Fructosidase (Invertase) From Thermotoga Maritima |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| BI723642 | 227 | 101 | 322 | 0 |
| BG844411 | 220 | 101 | 315 | 0 |
| GW237518 | 168 | 98 | 265 | 4e-39 |
| BI724909 | 183 | 101 | 280 | 2e-37 |
| GW237519 | 203 | 147 | 346 | 2e-36 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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