| Basic Information | |
|---|---|
| Species | Manihot esculenta |
| Cazyme ID | cassava4.1_034059m |
| Family | GH32 |
| Protein Properties | Length: 577 Molecular Weight: 64553.1 Isoelectric Point: 7.0188 |
| Chromosome | Chromosome/Scaffold: 05875 Start: 522938 End: 525387 |
| Description | Glycosyl hydrolases family 32 protein |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH32 | 53 | 371 | 0 |
| HFQPSKNWMNGPMIYKGIYHLFYQYNPKGAVWMWGSIVWAHSTSTDLVNWTPQSVAIYPSQPSDSNGTWSGSATIFPDGTPAMLFTGVNTLGQQVQNLAM PKNTCDPYLLEWVKSPSNPVMAPTRENHINASSFRDPTTAWLCADGRWKVVIGSKINRKGVAYLYTSEDFVHWIEAQNLFHSAEDTGMWECVDFFPVSVN SSVGVDLQMLRSNIKYVFKASLDDTKHDYYTVGEYDHVKNVYTPDEGSVDGDSGLRYDYGKFYASKTFFDSARNRRILWGWVNESSSVTADIKKGWSGIQ AIPRTIWLDKSGKQLVQWP | |||
| Full Sequence |
|---|
| Protein Sequence Length: 577 Download |
| MAIICSLRLL LLFALLFGHG VFELEASHQI YHTLQNLDDF DAKTTQPYRT AYHFQPSKNW 60 MNGPMIYKGI YHLFYQYNPK GAVWMWGSIV WAHSTSTDLV NWTPQSVAIY PSQPSDSNGT 120 WSGSATIFPD GTPAMLFTGV NTLGQQVQNL AMPKNTCDPY LLEWVKSPSN PVMAPTRENH 180 INASSFRDPT TAWLCADGRW KVVIGSKINR KGVAYLYTSE DFVHWIEAQN LFHSAEDTGM 240 WECVDFFPVS VNSSVGVDLQ MLRSNIKYVF KASLDDTKHD YYTVGEYDHV KNVYTPDEGS 300 VDGDSGLRYD YGKFYASKTF FDSARNRRIL WGWVNESSSV TADIKKGWSG IQAIPRTIWL 360 DKSGKQLVQW PIQEIEKLRT NAVRLPGKIL KKGSVLEVPG VTAAQADVEI TFNVSDFSTG 420 EVLDPSWTNP QLLCCQKGAS VKGSLGPFGL LVLASESLQE YTAVFFRIFK GKNKYVVLMC 480 SDQSRSSLNP DNDKTTYGAF VDVDPVHEQL SLRSLIDHSV VESFGGQGKS CMTARVYPTF 540 TVKEDAPAHL YVFNNGSESV TITRLSAWSM KKAKIN* 600 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| TIGR01322 | scrB_fam | 9.0e-48 | 47 | 538 | 515 | + sucrose-6-phosphate hydrolase. [Energy metabolism, Biosynthesis and degradation of polysaccharides]. | ||
| COG1621 | SacC | 3.0e-64 | 44 | 539 | 514 | + Beta-fructosidases (levanase/invertase) [Carbohydrate transport and metabolism] | ||
| cd08996 | GH32_B_Fructosidase | 9.0e-82 | 59 | 374 | 331 | + 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 | 2.0e-132 | 53 | 371 | 330 | + 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 | 8.0e-171 | 53 | 528 | 489 | + Glycosyl hydrolases family 32. | ||
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAT09980.1 | 0 | 1 | 576 | 1 | 576 | cell wall apoplastic invertase [Vitis vinifera] |
| EMBL | CBI35961.1 | 0 | 18 | 576 | 18 | 574 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002279788.1 | 0 | 18 | 576 | 18 | 575 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002521396.1 | 0 | 1 | 576 | 3 | 576 | Beta-fructofuranosidase, cell wall isozyme precursor, putative [Ricinus communis] |
| RefSeq | XP_002521398.1 | 0 | 61 | 576 | 1 | 514 | Beta-fructofuranosidase, cell wall isozyme precursor, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2qqw_A | 0 | 45 | 576 | 1 | 537 | A Chain A, Crystal Structure Of A Cell-Wall Invertase (D23a) From Arabidopsis Thaliana In Complex With Sucrose |
| PDB | 2xqr_K | 0 | 45 | 576 | 1 | 537 | B Chain B, Crystal Structure Of Plant Cell Wall Invertase In Complex With A Specific Protein Inhibitor |
| PDB | 2xqr_I | 0 | 45 | 576 | 1 | 537 | B Chain B, Crystal Structure Of Plant Cell Wall Invertase In Complex With A Specific Protein Inhibitor |
| PDB | 2xqr_G | 0 | 45 | 576 | 1 | 537 | B Chain B, Crystal Structure Of Plant Cell Wall Invertase In Complex With A Specific Protein Inhibitor |
| PDB | 2xqr_E | 0 | 45 | 576 | 1 | 537 | B Chain B, Crystal Structure Of Plant Cell Wall Invertase In Complex With A Specific Protein Inhibitor |
| Metabolic Pathways | |||
|---|---|---|---|
| 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 |
