| Basic Information | |
|---|---|
| Species | Volvox carteri |
| Cazyme ID | Vocar20014198m |
| Family | GH32 |
| Protein Properties | Length: 1568 Molecular Weight: 163010 Isoelectric Point: 4.6686 |
| Chromosome | Chromosome/Scaffold: 6 Start: 2293198 End: 2303002 |
| Description | Glycosyl hydrolases family 32 protein |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH32 | 179 | 401 | 0 |
| HVMPVSGWGSDPNGPIFYKGRYHLFYQARPGTCQWHWGVGWDHVVSYDLAHWDRLPPAIFPTPGGPDADGCFSGSIAVEPRTGVPVCFYTGARLRTNREV PLPHPPPSHDMGLPHFEAQCCAVCDPDDELLVKWRKVPMPLMELPHTGQLTAWRDPWFVEQGDGRGREWTMLIGSGLKDGGGTALVYRTQDITRGWRFVG DLCSWPNPKMGVVWECPFLVQLQ | |||
| Full Sequence |
|---|
| Protein Sequence Length: 1568 Download |
| MELRSRCVRE YTHVTGRQEN PNEPVADTPF MSAIEGKAAA AATAANNRTS VELAAALRAP 60 EPADADAVGV DAAIITIICT AGPGNLQSTS GLAGAAAAAC KPAALSHLLP TCTPHTNLQQ 120 DLDADHNPVP ADSLKLPSSS RNGGGGGQGS CGGDHSTPPY CFPSPSHDRD QESLKPMFHV 180 MPVSGWGSDP NGPIFYKGRY HLFYQARPGT CQWHWGVGWD HVVSYDLAHW DRLPPAIFPT 240 PGGPDADGCF SGSIAVEPRT GVPVCFYTGA RLRTNREVPL PHPPPSHDMG LPHFEAQCCA 300 VCDPDDELLV KWRKVPMPLM ELPHTGQLTA WRDPWFVEQG DGRGREWTML IGSGLKDGGG 360 TALVYRTQDI TRGWRFVGDL CSWPNPKMGV VWECPFLVQL QPLPLCAHVL PTTDLAGLME 420 AEGEEGEGEE EAGEGEGEER EGEEEAGEGE GEEREHMVEM EPMATAVAAA GKAEVEEDGL 480 AEVVEDIIEA KAFGPKAAAA AKAEEAAMAP TPPTLRTNDA LKNSGEVEEV AEDGFQAAVR 540 AEVGSVMQTM AVIVYEEAEV ALAQTGTGAE AVEEGEPSGV IAGRESSSGA SDTSMVHGSR 600 LECTASGSSS LRSRSRSGDS GNGGAVGDSE TASEWQRQAV SSSIGGGGGD KGGYAAEVPT 660 SLVEAVRQTL AAEPVVQLAA MPQPVRSVDI AAAEPVMIKM SVSRTGCADV AAVAELVDAL 720 LQAVTQEQQS TACTATKAAA VESSSAIAAA HAAATEFDFV TAVAPAAAVR HGADVIDFSV 780 IAAAPWTAPA DLGSDASTAI ASITVRRAVS LLPSPVLENG ASSHAADAGD ASGGGHVDPR 840 APSVPAAAAA ATADEEIAAA APGQAPIVRS CCLTSSTLTA SATVPAAAAA DRAVLQDLHF 900 MVTQVMEARR ARAGAAAAAA AEEEDAALRG DSGGTMGSVT ASGGKLSYSP GVMGHSAVPE 960 PDTEVEPLPA PVTMRYHKAQ PLRPLTATVA ALSAGCGTSV ATDLRCSAAA PDALDSPQML 1020 AATPANSATE LDSPASAPAF SYAAAVAAAA AATATAATAS IVETKPTVEL KPKAVRPNAD 1080 AASSDFRIGD GAMHVQLPLL NAGGSGGVAS GGTSPVPTLA RAADVASTTR HAFASSVPQH 1140 RRWLFGNAPD ACHISGDLVG TRPIYWIGEY DSTAAKYDIA NAVGAAPLDI GNCLYAPACF 1200 QDAQAYNFLS GSTTCICTTT TSTSCCLLAE VGTLLPSLPP AQHEQGRHIL WGYMKELRRV 1260 PPAPALCDKY SYAGCVSLPR ALYLRGDKLF QLPLPELTAL RSDVAVHFSR VSLTHGSPWR 1320 LMGLRGLHLD LEMAISPGTA HRTVVLLRSW RPRGRGAAAL VYDWTSRRLY VVFEAMHPSR 1380 QALWRGEHPP AGASTASAMT PPPSSSASVA TTQPQQQGPH LHQHHHHSFP PDLPSELIRA 1440 DPDLELSSDT SLEGPLSDEE EMVEEDTAGG GDLDLPPGSP LRLRVFLDAS CLEVFTGSGQ 1500 VLTTRVYRGH APHVKPQQPQ PHQQHADPGI EVWSVGGSCS LDDLHAYEMD TAWLREGDAP 1560 LDGFVRK* 1620 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00251 | Glyco_hydro_32N | 2.0e-5 | 1165 | 1293 | 131 | + 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. | ||
| cd08996 | GH32_B_Fructosidase | 7.0e-8 | 1137 | 1296 | 161 | + 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-45 | 179 | 401 | 229 | + Glycosyl hydrolases family 32. | ||
| pfam00251 | Glyco_hydro_32N | 5.0e-47 | 179 | 410 | 241 | + 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. | ||
| cd08996 | GH32_B_Fructosidase | 2.0e-48 | 185 | 400 | 219 | + 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 | 181 | 410 | 1 | 230 | glycoside-hydrolase-like protein [Chlamydomonas reinhardtii] |
| RefSeq | XP_001690911.1 | 0.00002 | 1144 | 1284 | 620 | 706 | glycoside-hydrolase-like protein [Chlamydomonas reinhardtii] |
| RefSeq | XP_001690911.1 | 0.000002 | 1470 | 1509 | 922 | 963 | glycoside-hydrolase-like protein [Chlamydomonas reinhardtii] |
| RefSeq | XP_001691098.1 | 0 | 175 | 409 | 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 | 4e-26 | 174 | 427 | 2 | 224 | A Chain A, The Three-Dimensional Structure Of Beta-Fructosidase (Invertase) From Thermotoga Maritima |
| PDB | 1uyp_E | 4e-26 | 174 | 427 | 2 | 224 | A Chain A, The Three-Dimensional Structure Of Beta-Fructosidase (Invertase) From Thermotoga Maritima |
| PDB | 1uyp_D | 4e-26 | 174 | 427 | 2 | 224 | A Chain A, The Three-Dimensional Structure Of Beta-Fructosidase (Invertase) From Thermotoga Maritima |
| PDB | 1uyp_C | 4e-26 | 174 | 427 | 2 | 224 | A Chain A, The Three-Dimensional Structure Of Beta-Fructosidase (Invertase) From Thermotoga Maritima |
| PDB | 1uyp_B | 4e-26 | 174 | 427 | 2 | 224 | 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 | 211 | 175 | 380 | 0 |
| BG844411 | 212 | 167 | 373 | 0 |
| BI724909 | 166 | 175 | 337 | 5.99994e-41 |
| GW237518 | 158 | 171 | 323 | 2e-40 |
| BI723643 | 145 | 175 | 318 | 7e-37 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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