Basic Information | |
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Species | Phaseolus vulgaris |
Cazyme ID | Phvul.001G036700.3 |
Family | GH32 |
Protein Properties | Length: 499 Molecular Weight: 56953.8 Isoelectric Point: 4.8216 |
Chromosome | Chromosome/Scaffold: 01 Start: 3529595 End: 3532477 |
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 | 31 | 350 | 0 |
HFQPPQCWMNDPNAPMYYKGVYHFFYQHNPHAATFGEKMVWAHSVSYDLINWIHLDHAIEPSEQFDFNGCWSGSATIIPGKEKPVILYTGIDDKKHQVQN IAMPKNPSDPFLREWVKHPQNPVMTPPSGVEVDNFRDPSTAWQGKDGKWRVVIGAQNGDEGKVVLYQSEDFANWTVELKPFFASDNTGVCECPDFFPVSI NSTNGVDTSVQNQSVRHVLKISYLRLHQDYYFLGKYANEDGNFTPDVKFTGTSLDLRLDYGKFYASKSFFDHAKSRRILWGWVEECDTSHDDIEKGWAGL QCIPRQVWLDESGNRLMQWP |
Full Sequence |
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Protein Sequence Length: 499 Download |
MEISGEVASS HNLNSTMYKV PQKQPYRTWY HFQPPQCWMN DPNAPMYYKG VYHFFYQHNP 60 HAATFGEKMV WAHSVSYDLI NWIHLDHAIE PSEQFDFNGC WSGSATIIPG KEKPVILYTG 120 IDDKKHQVQN IAMPKNPSDP FLREWVKHPQ NPVMTPPSGV EVDNFRDPST AWQGKDGKWR 180 VVIGAQNGDE GKVVLYQSED FANWTVELKP FFASDNTGVC ECPDFFPVSI NSTNGVDTSV 240 QNQSVRHVLK ISYLRLHQDY YFLGKYANED GNFTPDVKFT GTSLDLRLDY GKFYASKSFF 300 DHAKSRRILW GWVEECDTSH DDIEKGWAGL QCIPRQVWLD ESGNRLMQWP IEEIETLRDK 360 HISIVGEKLV GGSILEISGI TASQADVEVL FELPELENAE WLEESEVDPR VLCSEEYASR 420 SGIIGPFGLL ALASEDQTEH TAIFFRIYKT SNRYVCFMCS DQSRSSLRQD LDKTTDGTIF 480 DIDPNQKTIS LRSLIYAD* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR01322 | scrB_fam | 7.0e-54 | 22 | 368 | 365 | + sucrose-6-phosphate hydrolase. [Energy metabolism, Biosynthesis and degradation of polysaccharides]. | ||
COG1621 | SacC | 2.0e-73 | 22 | 377 | 365 | + Beta-fructosidases (levanase/invertase) [Carbohydrate transport and metabolism] | ||
cd08996 | GH32_B_Fructosidase | 1.0e-90 | 38 | 353 | 328 | + 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-134 | 31 | 350 | 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 | 9.0e-150 | 31 | 495 | 473 | + 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 |
EMBL | CAC37923.1 | 0 | 1 | 495 | 18 | 514 | fructan 1-exohydrolase IIb [Cichorium intybus] |
EMBL | CAD49079.1 | 0 | 5 | 495 | 24 | 511 | fructan 1-exohydrolase [Campanula rapunculoides] |
RefSeq | XP_002278918.1 | 0 | 1 | 495 | 20 | 502 | PREDICTED: hypothetical protein isoform 3 [Vitis vinifera] |
RefSeq | XP_002309496.1 | 0 | 9 | 495 | 26 | 502 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002309497.1 | 0 | 22 | 495 | 42 | 509 | predicted protein [Populus trichocarpa] |
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 | 2aey_A | 0 | 23 | 495 | 4 | 476 | A Chain A, Crystal Structure Of Fructan 1-Exohydrolase Iia (E201q) From Cichorium Intybus In Complex With 1-Kestose |
PDB | 2ade_A | 0 | 23 | 495 | 4 | 476 | A Chain A, Crystal Structure Of Fructan 1-Exohydrolase Iia (E201q) From Cichorium Intybus In Complex With 1-Kestose |
PDB | 2add_A | 0 | 23 | 495 | 4 | 476 | A Chain A, Crystal Structure Of Fructan 1-Exohydrolase Iia (E201q) From Cichorium Intybus In Complex With 1-Kestose |
PDB | 1st8_A | 0 | 23 | 495 | 4 | 476 | A Chain A, Crystal Structure Of Fructan 1-Exohydrolase Iia From Cichorium Intybus |
PDB | 2aez_A | 0 | 23 | 495 | 4 | 476 | A Chain A, Crystal Structure Of Fructan 1-Exohydrolase Iia (E201q) From Cichorium Intybus In Complex With 1-Kestose |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
FE709664 | 229 | 163 | 391 | 0 |
BG645655 | 265 | 6 | 269 | 0 |
CT842376 | 478 | 27 | 495 | 0 |
FF555008 | 222 | 56 | 276 | 0 |
FF401378 | 213 | 96 | 307 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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