Basic Information | |
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Species | Capsella rubella |
Cazyme ID | Carubv10008754m |
Family | GH32 |
Protein Properties | Length: 554 Molecular Weight: 62307.8 Isoelectric Point: 4.6253 |
Chromosome | Chromosome/Scaffold: 1 Start: 19113424 End: 19116120 |
Description | beta-fructofuranosidase 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 | 13 | 326 | 0 |
PDPNGPMIYKGIYHLFYQYNPYGAVWDVRIVWGHSTSVDLVNWTPQPPAFSPSQPSDINGCWSGSVTILPNGKPVILYTGIDLNKSQVQNVAVPVNVSDP YLREWSKPPLNPLMAPNSVNGIDPDRFRDPTTAWLGLDGEWRVIVGSSTDDRRGLVILYKSRDFLNWTQSTTPLHYEDLTGMWECPDFFPVSITGSDGVE TSSVVQNDVKYVLKVSLIETLHDYYTIGSYDREKDVYVPDLGFVQDRSAPRLDYGKYYASKTFYDDVKKRRILWGWVNESSPAKDDIEKGWAGLQSFPRK IWLDESGKELLQWP |
Full Sequence |
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Protein Sequence Length: 554 Download |
MLDEIQFDQQ KTPDPNGPMI YKGIYHLFYQ YNPYGAVWDV RIVWGHSTSV DLVNWTPQPP 60 AFSPSQPSDI NGCWSGSVTI LPNGKPVILY TGIDLNKSQV QNVAVPVNVS DPYLREWSKP 120 PLNPLMAPNS VNGIDPDRFR DPTTAWLGLD GEWRVIVGSS TDDRRGLVIL YKSRDFLNWT 180 QSTTPLHYED LTGMWECPDF FPVSITGSDG VETSSVVQND VKYVLKVSLI ETLHDYYTIG 240 SYDREKDVYV PDLGFVQDRS APRLDYGKYY ASKTFYDDVK KRRILWGWVN ESSPAKDDIE 300 KGWAGLQSFP RKIWLDESGK ELLQWPIEEI DTLRGTQVSW QNKVLEAGST VQIHGVTAAQ 360 ADVEVSFKVN ELEKADVIDP SWTDPQKICR EEDLSVKSRV GPFGLMVLTS SDMEEYTSVY 420 FRIFKSNDSN KHTKYVVLMC SDQSRSSLNE ENDKSTFGAF VGIDPSQQTL SLRTLIDHSI 480 VESYGGGGRT CITSRVYPKL AIGENANLFA FNKGSESVDV LSLSAWSLKS AQINDESISP 540 FIEREDSHSP KQS* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd08772 | GH43_62_32_68 | 3.0e-41 | 13 | 314 | 314 | + Glycosyl hydrolase families: GH43, GH62, GH32, GH68. Members of the glycosyl hydrolase families 32, 43, 62 and 68 (GH32, GH43, GH62, GH68) all possess 5-bladed beta-propeller domains and comprise clans F and J, as classified by the carbohydrate-active enzymes database (CAZY). Clan F consists of families GH43 and GH62. GH43 includes beta-xylosidases, beta-xylanases, alpha-L-arabinases, and alpha-L-arabinofuranosidases, using aryl-glycosides as substrates, while family GH62 contains alpha-L-arabinofuranosidases (EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose sidechains from xylans. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Clan J consists of families GH32 and GH68. GH32 comprises sucrose-6-phosphate hydrolases, invertases, inulinases, levanases, eukaryotic fructosyltransferases, and bacterial fructanotransferases while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), all of which use sucrose as their preferential donor substrate. Members of this clan are retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) that 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. Structures of all families in the two clans manifest a funnel-shaped active site that comprises two subsites with a single route for access by ligands. | ||
COG1621 | SacC | 5.0e-54 | 14 | 530 | 535 | + Beta-fructosidases (levanase/invertase) [Carbohydrate transport and metabolism] | ||
cd08996 | GH32_B_Fructosidase | 2.0e-89 | 14 | 329 | 327 | + 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 | 4.0e-128 | 14 | 326 | 320 | + 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 | 4.0e-164 | 14 | 488 | 484 | + Glycosyl hydrolases family 32. |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAG50837.1 | 0 | 16 | 552 | 52 | 589 | AC073944_4 beta-fructofuranosidase, putative [Arabidopsis thaliana] |
DDBJ | BAA89048.1 | 0 | 14 | 552 | 53 | 593 | beta-fructofuranosidase [Arabidopsis thaliana] |
DDBJ | BAD44438.1 | 0 | 14 | 552 | 53 | 592 | beta-fructofuranosidase (AtFruct5) [Arabidopsis thaliana] |
RefSeq | NP_001117494.1 | 0 | 17 | 552 | 17 | 553 | ATFRUCT5 (BETA-FRUCTOFURANOSIDASE 5); hydrolase, hydrolyzing O-glycosyl compounds / levanase [Arabidopsis thaliana] |
RefSeq | NP_564676.1 | 0 | 14 | 552 | 53 | 592 | ATFRUCT5 (BETA-FRUCTOFURANOSIDASE 5); hydrolase, hydrolyzing O-glycosyl compounds / levanase [Arabidopsis thaliana] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 2ac1_A | 0 | 14 | 534 | 23 | 541 | A Chain A, Crystal Structure Of A Cell-Wall Invertase From Arabidopsis Thaliana |
PDB | 2xqr_K | 0 | 14 | 534 | 19 | 537 | B Chain B, Crystal Structure Of Plant Cell Wall Invertase In Complex With A Specific Protein Inhibitor |
PDB | 2xqr_I | 0 | 14 | 534 | 19 | 537 | B Chain B, Crystal Structure Of Plant Cell Wall Invertase In Complex With A Specific Protein Inhibitor |
PDB | 2xqr_G | 0 | 14 | 534 | 19 | 537 | B Chain B, Crystal Structure Of Plant Cell Wall Invertase In Complex With A Specific Protein Inhibitor |
PDB | 2xqr_E | 0 | 14 | 534 | 19 | 537 | B Chain B, Crystal Structure Of Plant Cell Wall Invertase In Complex With A Specific Protein Inhibitor |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
CT842376 | 524 | 14 | 534 | 0 |
DY012674 | 246 | 124 | 369 | 0 |
EX137333 | 292 | 243 | 534 | 0 |
DY273985 | 354 | 19 | 370 | 0 |
FC881182 | 307 | 19 | 325 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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