y
Basic Information | |
---|---|
Species | Arabidopsis lyrata |
Cazyme ID | 909164 |
Family | GH32 |
Protein Properties | Length: 549 Molecular Weight: 61960.5 Isoelectric Point: 4.6689 |
View CDS |
External Links |
---|
NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
GH32 | 21 | 340 | 0 |
HFQPQRNWLNDPNAPMYYKGFYHLFYQHNPLAPDFSKIMIWGHSVSQDMVNWIQLEPALSPSEPFDINSCWSGSATILPDGRPVILYTGLDDNNKQQVTV VAEPKDVSDPLLREWVKPKYNPVMVPPSNVPFNCFRDPTTAWQGQDGKWRVLIGAKEKDTEKGMAILYRSDDFVQWTKYTVPLLESEGTGMWECPDFFPV SVTGKEGVDTSVNNATVRHVVKASFGGNDCYVIGKYSSENEEFSADYEFTNTSADLRYDYGKFYASKAFFDSVKNRRINWGWVIETDSKEDDFKKGWAGL MSLPREMWLDTNGKKLIQWP |
Full Sequence |
---|
Protein Sequence Length: 549 Download |
MAEAMAQNLL QDNQLNRTSF HFQPQRNWLN DPNAPMYYKG FYHLFYQHNP LAPDFSKIMI 60 WGHSVSQDMV NWIQLEPALS PSEPFDINSC WSGSATILPD GRPVILYTGL DDNNKQQVTV 120 VAEPKDVSDP LLREWVKPKY NPVMVPPSNV PFNCFRDPTT AWQGQDGKWR VLIGAKEKDT 180 EKGMAILYRS DDFVQWTKYT VPLLESEGTG MWECPDFFPV SVTGKEGVDT SVNNATVRHV 240 VKASFGGNDC YVIGKYSSEN EEFSADYEFT NTSADLRYDY GKFYASKAFF DSVKNRRINW 300 GWVIETDSKE DDFKKGWAGL MSLPREMWLD TNGKKLIQWP IEEINNLRTK SVSLDCYEFE 360 TGSTFEISGI TAAQADVEVT FNLPFLDDYP EILDADQVDD ATLFDHDNSD GCVYGPFGLL 420 ALATNDLSEQ TAIFFKVIRR GNGYAVVMGS SEKRSSLRDN IKKSSHGTFL DIDPRHEKIS 480 LRCLIDHSII ESYGAGGKSV ITSRVYPKLA IGEAAKLYVF NDGEKGVIMT SLEAWSMRNA 540 QINSNPTY* 600 |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR01322 | scrB_fam | 1.0e-60 | 3 | 508 | 527 | + sucrose-6-phosphate hydrolase. [Energy metabolism, Biosynthesis and degradation of polysaccharides]. | ||
COG1621 | SacC | 6.0e-66 | 17 | 507 | 509 | + Beta-fructosidases (levanase/invertase) [Carbohydrate transport and metabolism] | ||
cd08996 | GH32_B_Fructosidase | 2.0e-90 | 27 | 343 | 322 | + 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-136 | 21 | 340 | 329 | + 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 | 3.0e-161 | 21 | 497 | 488 | + Glycosyl hydrolases family 32. |
Annotations - NR Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CAB87665.1 | 0 | 1 | 548 | 1 | 547 | fructosidase-like protein [Arabidopsis thaliana] |
EMBL | CAD49079.1 | 0 | 2 | 542 | 31 | 568 | fructan 1-exohydrolase [Campanula rapunculoides] |
RefSeq | NP_001078574.1 | 0 | 1 | 410 | 1 | 412 | AtcwINV6 (6-&1-fructan exohydrolase); hydrolase, hydrolyzing O-glycosyl compounds / inulinase/ levanase [Arabidopsis thaliana] |
RefSeq | NP_568254.1 | 0 | 1 | 548 | 1 | 550 | AtcwINV6 (6-&1-fructan exohydrolase); hydrolase, hydrolyzing O-glycosyl compounds / inulinase/ levanase [Arabidopsis thaliana] |
RefSeq | XP_002309497.1 | 0 | 9 | 548 | 39 | 572 | predicted protein [Populus trichocarpa] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 2aey_A | 0 | 11 | 542 | 2 | 533 | A Chain A, High Resolution Structure Of E.coli Wrba With Fmn |
PDB | 2ade_A | 0 | 11 | 542 | 2 | 533 | A Chain A, High Resolution Structure Of E.coli Wrba With Fmn |
PDB | 2add_A | 0 | 11 | 542 | 2 | 533 | A Chain A, High Resolution Structure Of E.coli Wrba With Fmn |
PDB | 1st8_A | 0 | 11 | 542 | 2 | 533 | A Chain A, Crystal Structure Of Fructan 1-Exohydrolase Iia From Cichorium Intybus |
PDB | 2aez_A | 0 | 11 | 542 | 2 | 533 | A Chain A, Crystal Structure Of Fructan 1-Exohydrolase Iia (E201q) From Cichorium Intybus In Complex With 1-Kestose |
EST Download unfiltered results here | ||||
---|---|---|---|---|
Hit | Length | Start | End | EValue |
CT842376 | 543 | 15 | 543 | 0 |
EE591202 | 415 | 138 | 544 | 0 |
EE591202 | 128 | 17 | 142 | 0 |
FD956604 | 219 | 277 | 495 | 0 |
FD949297 | 203 | 15 | 214 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
---|
![]() |