| Basic Information | |
|---|---|
| Species | Thellungiella halophila |
| Cazyme ID | Thhalv10020395m |
| Family | GH32 |
| Protein Properties | Length: 568 Molecular Weight: 63931.5 Isoelectric Point: 9.3864 |
| Chromosome | Chromosome/Scaffold: 13 Start: 4855619 End: 4857751 |
| Description | cell wall invertase 5 |
| View CDS | |
| External Links |
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| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| GH32 | 46 | 364 | 0 |
| HFQPPKNWMNGPMIYKGIYHLFYQWYPNGVVTDFNKIVWGHATSTDLINWTPHSPAIKPSRPSDINGCWSGSVTILPNGKPVILYTGNDRNNHQVQNLAR PKNLSDPYLRHWTKSPANPLVTPNAVNHINSTAFRDPTTAWLGRNGRWRVITGSQEGRRGLALLHTSRDFTSWKQSTKPLHYNDGTGMWECPDFFPVARF NPQGLDTSSFGESIKHVLKVSLSETSHDYYTIGTYDRMRDVYVPDDGFVQDGTAPRYDYGKFYASKTFYDSVYRRRILWGWVNESSPVKDNVDKGWAGLQ AIPRKVWLDESGKRLMLWP | |||
| Full Sequence |
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| Protein Sequence Length: 568 Download |
| MTNIVWCNIA IFLLASLFLT DNALVLEALH HAPNRIKDQP YRTGYHFQPP KNWMNGPMIY 60 KGIYHLFYQW YPNGVVTDFN KIVWGHATST DLINWTPHSP AIKPSRPSDI NGCWSGSVTI 120 LPNGKPVILY TGNDRNNHQV QNLARPKNLS DPYLRHWTKS PANPLVTPNA VNHINSTAFR 180 DPTTAWLGRN GRWRVITGSQ EGRRGLALLH TSRDFTSWKQ STKPLHYNDG TGMWECPDFF 240 PVARFNPQGL DTSSFGESIK HVLKVSLSET SHDYYTIGTY DRMRDVYVPD DGFVQDGTAP 300 RYDYGKFYAS KTFYDSVYRR RILWGWVNES SPVKDNVDKG WAGLQAIPRK VWLDESGKRL 360 MLWPVKEIER LRAKQVKLEN KVLEGGGSVL DVHGVTASQA DVEVFFKVTG LEEADVIEPG 420 WTDPQLICSQ NKTASSGLGP FGLMVLASKN LEEYTSVYLR IFKARQNSKD HVVVMCSDQS 480 RSSLEKGNDK TPFGAFLDIS PYQPISLRTL IDNSIVESFV GKGKTCITSR VYPKLAIGKN 540 AHLFAFNNGS QNVDVLSLSA WSMKSSL* |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| TIGR01322 | scrB_fam | 1.0e-49 | 33 | 534 | 530 | + sucrose-6-phosphate hydrolase. [Energy metabolism, Biosynthesis and degradation of polysaccharides]. | ||
| COG1621 | SacC | 2.0e-63 | 38 | 533 | 516 | + Beta-fructosidases (levanase/invertase) [Carbohydrate transport and metabolism] | ||
| cd08996 | GH32_B_Fructosidase | 2.0e-86 | 52 | 367 | 332 | + 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-133 | 46 | 364 | 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 | 2.0e-168 | 46 | 523 | 491 | + Glycosyl hydrolases family 32. | ||
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2QQU | 0 | 38 | 566 | 1 | 534 | A Chain A, Crystal Structure Of A Cell-Wall Invertase (D239a) From Arabidopsis Thaliana In Complex With Sucrose |
| DDBJ | BAB01930.1 | 0 | 1 | 566 | 1 | 578 | beta-fructofuranosidase (EC 3.2.1.26) [Arabidopsis thaliana] |
| RefSeq | NP_187994.1 | 0 | 1 | 567 | 1 | 569 | AtcwINV5 (Arabidopsis thaliana cell wall invertase 5); hydrolase, hydrolyzing O-glycosyl compounds |
| RefSeq | NP_566464.1 | 0 | 1 | 566 | 1 | 581 | ATBFRUCT1; beta-fructofuranosidase/ hydrolase, hydrolyzing O-glycosyl compounds [Arabidopsis thaliana] |
| Swiss-Prot | Q9LIB9 | 0 | 1 | 567 | 1 | 572 | INV5_ARATH RecName: Full=Beta-fructofuranosidase, insoluble isoenzyme CWINV5; AltName: Full=Cell wall invertase 5; Short=AtcwINV5; AltName: Full=Sucrose hydrolase 5; AltName: Full=Cell wall beta-fructosidase 5; Flags: Precursor |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2qqu_A | 0 | 38 | 566 | 1 | 534 | A Chain A, Crystal Structure Of A Cell-Wall Invertase (D239a) From Arabidopsis Thaliana In Complex With Sucrose |
| PDB | 2qqw_A | 0 | 38 | 566 | 1 | 534 | A Chain A, Crystal Structure Of A Cell-Wall Invertase (D23a) From Arabidopsis Thaliana In Complex With Sucrose |
| PDB | 2xqr_K | 0 | 38 | 566 | 1 | 534 | B Chain B, Crystal Structure Of Plant Cell Wall Invertase In Complex With A Specific Protein Inhibitor |
| PDB | 2xqr_I | 0 | 38 | 566 | 1 | 534 | B Chain B, Crystal Structure Of Plant Cell Wall Invertase In Complex With A Specific Protein Inhibitor |
| PDB | 2xqr_G | 0 | 38 | 566 | 1 | 534 | B Chain B, Crystal Structure Of Plant Cell Wall Invertase In Complex With A Specific Protein Inhibitor |
