y
Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s177_28V6.5 |
Family | GH32 |
Protein Properties | Length: 609 Molecular Weight: 68624.3 Isoelectric Point: 6.8817 |
Chromosome | Chromosome/Scaffold: 177 Start: 130261 End: 133055 |
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 | 65 | 392 | 0 |
HFQPRKNWMNDPNGPLYYKGWYHFFYQYNRDAAVWGNITWGHAVSRDMVHWRTLHTALKGDKWYDMKGVWSGSATFLDNGVPVLLYTGWAINGTDQSSIR GQTQAMAVPEDPSDPLLREWDKSPHNPIALAPPGFNDSMFRDPTEAWKGYDGVWRMLVGAVKGTDQSIGTALLYKSTDFNKWNFTGEIQSVAGTGMWECP DIYPVHVKEKTGLRLSARGPHVKHVLKVSLDRNKHDYYSVGTYDEKTDLYTPDDTKLDTGLGLRYDYGKFYASKTFFDQNKNRRVLWGWANESSSVQDDI EKGWSSVQCLPRHIWLDEESSANLVQWP |
Full Sequence |
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Protein Sequence Length: 609 Download |
MEQSFHPTMA AKHRVMLLAS AMILLAALFS PVEASHKDWH QLGVESIKSS SSATHVYQPY 60 RTAYHFQPRK NWMNDPNGPL YYKGWYHFFY QYNRDAAVWG NITWGHAVSR DMVHWRTLHT 120 ALKGDKWYDM KGVWSGSATF LDNGVPVLLY TGWAINGTDQ SSIRGQTQAM AVPEDPSDPL 180 LREWDKSPHN PIALAPPGFN DSMFRDPTEA WKGYDGVWRM LVGAVKGTDQ SIGTALLYKS 240 TDFNKWNFTG EIQSVAGTGM WECPDIYPVH VKEKTGLRLS ARGPHVKHVL KVSLDRNKHD 300 YYSVGTYDEK TDLYTPDDTK LDTGLGLRYD YGKFYASKTF FDQNKNRRVL WGWANESSSV 360 QDDIEKGWSS VQCLPRHIWL DEESSANLVQ WPIEEVDKLR RNEMTEKNVE VGVGKVVPVK 420 AAKGAQLDIV VDFALPEKSE GLEQNPNLLA EMGHLTCSDL VTKGSNAAGP HSFGPFGVHV 480 LATGDLQERT SIFFHLIHDG KHQNWKTLFC GDQSQSSLQQ DVDKTVYGSY VRVDDSDKVL 540 SVRILVDHSI VESFAQGGRT VMTSRVYPEL AVKDAAHVFL FNNGTEPVTV KSVSTWEMKS 600 VNIKFYKP* 660 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG1621 | SacC | 1.0e-70 | 52 | 408 | 367 | + Beta-fructosidases (levanase/invertase) [Carbohydrate transport and metabolism] | ||
cd08996 | GH32_B_Fructosidase | 2.0e-97 | 71 | 395 | 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 | 5.0e-129 | 65 | 392 | 336 | + 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-150 | 65 | 558 | 501 | + 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 |
RefSeq | XP_001755639.1 | 0 | 53 | 607 | 25 | 571 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001761961.1 | 0 | 59 | 603 | 4 | 533 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001764172.1 | 0 | 60 | 603 | 34 | 561 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001774490.1 | 0 | 22 | 608 | 1 | 587 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001783601.1 | 0 | 60 | 603 | 8 | 538 | predicted protein [Physcomitrella patens subsp. patens] |
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 | 61 | 604 | 19 | 542 | A Chain A, Crystal Structure Of A 6-Sst6-Sft From Pachysandra Terminalis |
PDB | 3ugh_A | 0 | 61 | 604 | 19 | 542 | A Chain A, Crystal Structure Of A 6-Sst6-Sft From Pachysandra Terminalis |
PDB | 3ugg_B | 0 | 61 | 604 | 19 | 542 | A Chain A, Crystal Structure Of A 6-Sst6-Sft From Pachysandra Terminalis |
PDB | 3ugg_A | 0 | 61 | 604 | 19 | 542 | A Chain A, Crystal Structure Of A 6-Sst6-Sft From Pachysandra Terminalis |
PDB | 3ugf_B | 0 | 61 | 604 | 19 | 542 | A Chain A, Crystal Structure Of A 6-Sst6-Sft From Pachysandra Terminalis |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
sucrose degradation III | RXN-1461 | EC-3.2.1.26 | β-fructofuranosidase |