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Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 269386 |
Family | GH32 |
Protein Properties | Length: 570 Molecular Weight: 64545.9 Isoelectric Point: 6.725 |
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 | 30 | 352 | 0 |
HFQPVKNWMNDPNGPLFYKGVYHLFYQWNPYAAVWGNITWGHAVSTDLIHWKYVKELALVPDRWYDIKGVWSGSATIVNGEPILLYTGWTNSSTQVQNKA VPKNSSDPLLREWIKVDAENPFAVPPPGINTSDFRDPTTAWIGQDGLWRTAVGSKYRANDTGIILQYRSKDFAKWELLDESLHAVNGTGMWECPDFFPVA VHGQQGSENYLGEENAIQKFVIKVSLDETRFDTYVVGDYDPASEKFLPSFEALDIGTALRYDYGIYYASKSFYDPHKKRRVLLGWINEADKPTSDIRKGW ASVQAIPRVVWLDENQHSLRQWP |
Full Sequence |
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Protein Sequence Length: 570 Download |
MLPGLLPFPW PEQEQPHNNP PQNLLRTGFH FQPVKNWMND PNGPLFYKGV YHLFYQWNPY 60 AAVWGNITWG HAVSTDLIHW KYVKELALVP DRWYDIKGVW SGSATIVNGE PILLYTGWTN 120 SSTQVQNKAV PKNSSDPLLR EWIKVDAENP FAVPPPGINT SDFRDPTTAW IGQDGLWRTA 180 VGSKYRANDT GIILQYRSKD FAKWELLDES LHAVNGTGMW ECPDFFPVAV HGQQGSENYL 240 GEENAIQKFV IKVSLDETRF DTYVVGDYDP ASEKFLPSFE ALDIGTALRY DYGIYYASKS 300 FYDPHKKRRV LLGWINEADK PTSDIRKGWA SVQAIPRVVW LDENQHSLRQ WPVPEINSLR 360 KHPIRHTDLL LKQGEVFKVN GSQGSQLDIE VTFQIPKAHA NDENDEFNFE SSRVEGIPNN 420 TLIYCNGSFP EAEQIIGPFG VHVLASEDLR ERTSVFFKFL KFKGSWKTMV CNDLTSSSLA 480 SDATKGVYGG LVSLSSYKNR QALTMRILVD HSIVETFAQG GRTCITARSY PLLGSDNNAH 540 MFVFNNGSLP VKATHLAVWK MDKIRYTTV* 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR01322 | scrB_fam | 2.0e-60 | 26 | 531 | 535 | + sucrose-6-phosphate hydrolase. [Energy metabolism, Biosynthesis and degradation of polysaccharides]. | ||
COG1621 | SacC | 1.0e-64 | 25 | 372 | 361 | + Beta-fructosidases (levanase/invertase) [Carbohydrate transport and metabolism] | ||
cd08996 | GH32_B_Fructosidase | 2.0e-94 | 36 | 355 | 332 | + 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 | 2.0e-139 | 30 | 352 | 330 | + 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-159 | 30 | 521 | 501 | + Glycosyl hydrolases family 32. |
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 | 2xqr_K | 0 | 26 | 562 | 5 | 532 | B Chain B, Crystal Structure Of Plant Cell Wall Invertase In Complex With A Specific Protein Inhibitor |
PDB | 2xqr_I | 0 | 26 | 562 | 5 | 532 | B Chain B, Crystal Structure Of Plant Cell Wall Invertase In Complex With A Specific Protein Inhibitor |
PDB | 2xqr_G | 0 | 26 | 562 | 5 | 532 | B Chain B, Crystal Structure Of Plant Cell Wall Invertase In Complex With A Specific Protein Inhibitor |
PDB | 2xqr_E | 0 | 26 | 562 | 5 | 532 | B Chain B, Crystal Structure Of Plant Cell Wall Invertase In Complex With A Specific Protein Inhibitor |
PDB | 2xqr_C | 0 | 26 | 562 | 5 | 532 | B Chain B, Crystal Structure Of Plant Cell Wall Invertase In Complex With A Specific Protein Inhibitor |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
sucrose degradation III | RXN-1461 | EC-3.2.1.26 | β-fructofuranosidase |
Sequence Alignments (This image is cropped. Click for full image.) |
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