Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 98949 |
Family | GH32 |
Protein Properties | Length: 623 Molecular Weight: 70032.6 Isoelectric Point: 4.921 |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH32 | 85 | 402 | 0 |
HFQPRNNWMNGPLFYKGYYHLFYQYNPYGVEWGNISWGHAVSTDLLHWQHMDLAMQPDKWYDADGVWSGSATILPNGQVIMLYTGSTNASVQVQNLALPL NTSDPLLREWIKIPENPILVPPPGIAPKDFRDPTTAWLEADGLWRIAIGAKKGRAGLALIYKTFDFLHWELEEEYLHTVQGTGMWECIDFYPVSTATSNG LDTSKVQTNELTKHILKASLDDDKHDYYAIGLYSESSHTWIPDALDNDVGLGLRYDYGKYYASKTFFDSKHQRRILWGWANESDSLQDDIRKGWSSVQTL PRILYLDNLTGTNLIQWP |
Full Sequence |
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Protein Sequence Length: 623 Download |
MDPESQRSYA ELPSGEEAEE IHSNPTAATE NSRNRRIDLV LTLVGICCVV AGTFFWISLP 60 SSNTENFSRI APDGGFLASE RTAFHFQPRN NWMNGPLFYK GYYHLFYQYN PYGVEWGNIS 120 WGHAVSTDLL HWQHMDLAMQ PDKWYDADGV WSGSATILPN GQVIMLYTGS TNASVQVQNL 180 ALPLNTSDPL LREWIKIPEN PILVPPPGIA PKDFRDPTTA WLEADGLWRI AIGAKKGRAG 240 LALIYKTFDF LHWELEEEYL HTVQGTGMWE CIDFYPVSTA TSNGLDTSKV QTNELTKHIL 300 KASLDDDKHD YYAIGLYSES SHTWIPDALD NDVGLGLRYD YGKYYASKTF FDSKHQRRIL 360 WGWANESDSL QDDIRKGWSS VQTLPRILYL DNLTGTNLIQ WPIEEVDALR HDKVSRSNVL 420 LKGGDVVEVD AAQGAQLDIE VGFEYPDASK LDALPESENY DCSQGGATHR GVYGPFGLLV 480 LAEDKLQEMT AVYFYMTLKR DGSWETRFSI HVSDPHVSRS SLEPGIDTTV YGTLFHRLPT 540 EDSLSLRVIV DHSIVETFVQ GGRACITSRV YPTLATGDKA RLFMFNNGTQ PVVVKNLDAW 600 KMRSTTLSVL PVTEWRLAAR QS* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR01322 | scrB_fam | 9.0e-46 | 81 | 572 | 522 | + sucrose-6-phosphate hydrolase. [Energy metabolism, Biosynthesis and degradation of polysaccharides]. | ||
COG1621 | SacC | 7.0e-69 | 81 | 573 | 508 | + Beta-fructosidases (levanase/invertase) [Carbohydrate transport and metabolism] | ||
cd08996 | GH32_B_Fructosidase | 1.0e-90 | 91 | 405 | 330 | + 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-139 | 85 | 402 | 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 | 2.0e-160 | 85 | 562 | 490 | + 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 | ACT21538.1 | 0 | 73 | 611 | 38 | 572 | acid invertase [Vigna radiata] |
EMBL | CAA47636.1 | 0 | 3 | 604 | 4 | 638 | soluble beta-fructosidase [Daucus carota] |
EMBL | CAD19321.1 | 0 | 77 | 607 | 139 | 665 | acid vacuolar invertase [Beta vulgaris] |
Swiss-Prot | Q43857 | 0 | 76 | 604 | 103 | 627 | INVA_VICFA RecName: Full=Acid beta-fructofuranosidase; AltName: Full=Acid sucrose hydrolase; AltName: Full=Acid invertase; Short=AI; AltName: Full=Vacuolar invertase; Flags: Precursor |
RefSeq | XP_001764172.1 | 0 | 81 | 610 | 35 | 564 | 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 | 77 | 604 | 15 | 538 | A Chain A, Crystal Structure Of Endonuclease Iv From Thermus Thermophilus Hb8 |
PDB | 3ugh_A | 0 | 77 | 604 | 15 | 538 | A Chain A, Crystal Structure Of Endonuclease Iv From Thermus Thermophilus Hb8 |
PDB | 3ugg_B | 0 | 77 | 604 | 15 | 538 | A Chain A, Crystal Structure Of Endonuclease Iv From Thermus Thermophilus Hb8 |
PDB | 3ugg_A | 0 | 77 | 604 | 15 | 538 | A Chain A, Crystal Structure Of Endonuclease Iv From Thermus Thermophilus Hb8 |
PDB | 3ugf_B | 0 | 77 | 604 | 15 | 538 | 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 |