y
Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna05759.1-v1.0-hybrid |
Family | GH43 |
Protein Properties | Length: 530 Molecular Weight: 60632.3 Isoelectric Point: 7.5066 |
Chromosome | Chromosome/Scaffold: 1 Start: 14961414 End: 14967412 |
Description | Arabinanase/levansucrase/invertase |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH43 | 214 | 437 | 6.8e-34 |
ILYDEKSGTYYWYGEYKDGPTYHAHKKGAARVDILGVGCYSSKDLWKWNNEGIVLAAEKTNETHDLHELNVLERPKVIYNHKTAKYVMWMHIDDVNYTKA SVGVAISDYPTGPFDYLYSKRPHGFDSRDMTVFKDDDGIAYLIYSSDDNSELHIGPLTEDYLDVTNIVRRILVGQHREAPALFKHDGTYYMITSGCTGWA PNEAMAHAAESIMGPWETMGNPCI |
Full Sequence |
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Protein Sequence Length: 530 Download |
MASAYSQSIQ EFLNLYPTLQ SLAYCTFVKD GISEVVRYHC RPIKLAFRLL WASILSLVIF 60 TVFLELLLVA RALQEKGGSR CSISAVVWSL VGCLLMFHLY SLVHHKDGMG REIQFRASVH 120 PQLHELEKVE EESIRMPPPR KRSPRAAKRK PKRPTTIIDE FLDENSQIRH VFFPDQKLAI 180 DPLKDAGNDS YYYYPGRIWL DTEENPIQAH GGGILYDEKS GTYYWYGEYK DGPTYHAHKK 240 GAARVDILGV GCYSSKDLWK WNNEGIVLAA EKTNETHDLH ELNVLERPKV IYNHKTAKYV 300 MWMHIDDVNY TKASVGVAIS DYPTGPFDYL YSKRPHGFDS RDMTVFKDDD GIAYLIYSSD 360 DNSELHIGPL TEDYLDVTNI VRRILVGQHR EAPALFKHDG TYYMITSGCT GWAPNEAMAH 420 AAESIMGPWE TMGNPCIGGN KMSRLATFFA QSTFVIPLPG FPGSFIFMAD RWNPADLRDS 480 RYVWLPLIVG GPVDRPLDYN FGFPLWSRVS IYWHRKWKLP QGWSGWKKM* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd08999 | GH43_ABN_2 | 2.0e-16 | 314 | 435 | 140 | + Glycosyl hydrolase family 43. This glycosyl hydrolase family 43 (GH43) includes mostly enzymes with alpha-L-arabinofuranosidase (AFN; EC 3.2.1.55) and endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain 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. | ||
cd08990 | GH43_AXH_like | 1.0e-17 | 252 | 433 | 196 | + Glycosyl hydrolase family 43, includes arabinoxylan arabinofuranohydrolase, beta-xylosidase, endo-1,4-beta-xylanase, alpha-L-arabinofuranosidase. This glycosyl hydrolase family 43 (GH43) includes enzymes that have been characterized with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55), endo-alpha-L-arabinanase as well as arabinoxylan arabinofuranohydrolase (AXH) activities. These are all inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan. Several of these enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain 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. | ||
cd09004 | GH43_bXyl | 8.0e-21 | 221 | 434 | 228 | + Glycosyl hydrolase family 43, includes mostly 1,4-beta-xylanases. This glycosyl hydrolase family 43 (GH43) includes enzymes that have been characterized with xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase) activities. These are all inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain 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. | ||
cd08978 | GH_F | 6.0e-46 | 210 | 487 | 289 | + Glycosyl hydrolase families 43 and 62 form CAZY clan GH-F. This glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) includes family 43 (GH43) and 62 (GH62). GH43 includes enzymes with beta-xylosidase (EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanases (beta-xylanases) and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. GH62 includes enzymes characterized as arabinofuranosidases (alpha-L-arabinofuranosidases; EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose side chains from xylans. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. GH62 are also predicted to be inverting enzymes. A common structural feature of both, GH43 and GH62 enzymes, is a 5-bladed beta-propeller domain 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. | ||
cd08985 | GH43_6 | 3.0e-130 | 207 | 487 | 282 | + Glycosyl hydrolase family 43. This glycosyl hydrolase family 43 (GH43) includes enzymes with beta-1,4-xylosidase (xylan 1,4-beta-xylosidase; EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanase and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain 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. |
Gene Ontology | |
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GO Term | Description |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005975 | carbohydrate metabolic process |
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 | 3vt2_F | 0 | 196 | 487 | 45 | 328 | A Chain A, Crystal Structure Of Narbonin Refined At 1.8 Angstroms Resolution |
PDB | 3vt2_E | 0 | 196 | 487 | 45 | 328 | A Chain A, Crystal Structure Of Narbonin Refined At 1.8 Angstroms Resolution |
PDB | 3vt2_D | 0 | 196 | 487 | 45 | 328 | A Chain A, Crystal Structure Of Narbonin Refined At 1.8 Angstroms Resolution |
PDB | 3vt2_C | 0 | 196 | 487 | 45 | 328 | A Chain A, Crystal Structure Of Narbonin Refined At 1.8 Angstroms Resolution |
PDB | 3vt2_B | 0 | 196 | 487 | 45 | 328 | A Chain A, Crystal Structure Of Narbonin Refined At 1.8 Angstroms Resolution |