y
Basic Information | |
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Species | Medicago truncatula |
Cazyme ID | Medtr4g101630.1 |
Family | GH32 |
Protein Properties | Length: 641 Molecular Weight: 71670.9 Isoelectric Point: 6.0148 |
Chromosome | Chromosome/Scaffold: 4 Start: 35143793 End: 35148528 |
Description | Glycosyl hydrolases family 32 protein |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH32 | 116 | 431 | 0 |
HFQPEKNWMNGPMYYKGWYHFFYQYNPNGAVWGDIVWGHAVSRDMIHWLHLPLAMVADQWYDSNGVWTGSATILPDGQVIMLYTGSTNETVQVQNLAYPA DLNDPLLVDWIKYPANPVLVPPPGILPKDFRDPTTAWLTSEGKWRITIGSKINKTGVALVYDTVDFKTYERKEDLLDAVPGTGMWECVDFFPVSMKSENG LDTSVNGEEVKHVMKVSLDDDRHDYYSLGNYDEKKVKFTADDLKNDVGIGLRYDYGIFYASKTFYDQKKDRRVLWGWIGESDSEYADVAKGWASVQSIPR IVKLDKKTGSNLLQWP |
Full Sequence |
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Protein Sequence Length: 641 Download |
MRNNDSPYTP LLNGPHNNNR KELLLIFCGL FLLASLIAFS GYKASDNVSV PHAHVSSSSS 60 ILSHEETKPN MVVSPSVSAG VSEKSNVFLS GPNKVGETES FPWNNTMLSW QRTSFHFQPE 120 KNWMNGPMYY KGWYHFFYQY NPNGAVWGDI VWGHAVSRDM IHWLHLPLAM VADQWYDSNG 180 VWTGSATILP DGQVIMLYTG STNETVQVQN LAYPADLNDP LLVDWIKYPA NPVLVPPPGI 240 LPKDFRDPTT AWLTSEGKWR ITIGSKINKT GVALVYDTVD FKTYERKEDL LDAVPGTGMW 300 ECVDFFPVSM KSENGLDTSV NGEEVKHVMK VSLDDDRHDY YSLGNYDEKK VKFTADDLKN 360 DVGIGLRYDY GIFYASKTFY DQKKDRRVLW GWIGESDSEY ADVAKGWASV QSIPRIVKLD 420 KKTGSNLLQW PVAEVESLRL KSDEFKNLKV KPGSVVSLDI DTATQLDILA EFEIEKEALE 480 KTAHSNVEYE CSNSGGASKR GALGPFGLYV LADGALSEYT PVYFYVVKGS DGKLKTSFCS 540 DQSRSSLAND VHKQIYGSVV PVLEGEKLSL RILVDHSIVE SFAQGGRTCI TSRVYPTRAI 600 YGAARLFLFN NAIETNVTAS LKVWQMNSAF IRPYHPDQKS * 660 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR01322 | scrB_fam | 4.0e-57 | 112 | 596 | 509 | + sucrose-6-phosphate hydrolase. [Energy metabolism, Biosynthesis and degradation of polysaccharides]. | ||
COG1621 | SacC | 6.0e-75 | 112 | 598 | 508 | + Beta-fructosidases (levanase/invertase) [Carbohydrate transport and metabolism] | ||
cd08996 | GH32_B_Fructosidase | 2.0e-93 | 122 | 434 | 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 | 3.0e-146 | 116 | 431 | 327 | + 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 | 0 | 116 | 586 | 484 | + Glycosyl hydrolases family 32. |
Gene Ontology | |
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GO Term | Description |
GO:0004564 | beta-fructofuranosidase activity |
GO:0004575 | sucrose alpha-glucosidase activity |
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 | AAM52062.1 | 0 | 1 | 639 | 1 | 642 | vacuolar acid invertase PsI-1 [Pisum sativum] |
GenBank | ACT21538.1 | 0 | 73 | 640 | 8 | 579 | acid invertase [Vigna radiata] |
Swiss-Prot | O24509 | 0 | 14 | 640 | 15 | 651 | INVA_PHAVU RecName: Full=Acid beta-fructofuranosidase; AltName: Full=Acid sucrose hydrolase; AltName: Full=Acid invertase; Short=AI; AltName: Full=Vacuolar invertase; Flags: Precursor |
Swiss-Prot | P29001 | 0 | 14 | 640 | 15 | 649 | INVA_PHAAU RecName: Full=Acid beta-fructofuranosidase; AltName: Full=Acid sucrose hydrolase; AltName: Full=Acid invertase; Short=AI; AltName: Full=Vacuolar invertase; Contains: RecName: Full=Acid beta-fructofuranosidase 30 kDa subunit; Contains: RecName: Full=Acid beta-fructofuranosidase 38 kDa subunit; Flags: Precursor |
Swiss-Prot | Q43857 | 0 | 1 | 639 | 1 | 638 | INVA_VICFA RecName: Full=Acid beta-fructofuranosidase; AltName: Full=Acid sucrose hydrolase; AltName: Full=Acid invertase; Short=AI; AltName: Full=Vacuolar invertase; Flags: Precursor |
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 | 3ugh_B | 0 | 101 | 635 | 8 | 545 | A Chain A, Raphanus Sativus Anionic Peroxidase. |
PDB | 3ugh_A | 0 | 101 | 635 | 8 | 545 | A Chain A, Raphanus Sativus Anionic Peroxidase. |
PDB | 3ugg_B | 0 | 101 | 635 | 8 | 545 | A Chain A, Raphanus Sativus Anionic Peroxidase. |
PDB | 3ugg_A | 0 | 101 | 635 | 8 | 545 | A Chain A, Raphanus Sativus Anionic Peroxidase. |
PDB | 3ugf_B | 0 | 101 | 635 | 8 | 545 | A Chain A, Crystal Structure Of A 6-Sst6-Sft From Pachysandra Terminalis |