Basic Information | |
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Species | Ricinus communis |
Cazyme ID | 32604.m000021 |
Family | GH43 |
Protein Properties | Length: 309 Molecular Weight: 33814.2 Isoelectric Point: 9.3812 |
Chromosome | Chromosome/Scaffold: 32604 Start: 34 End: 960 |
Description | |
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 |
GH43 | 118 | 308 | 1.3e-25 |
FHNPLVLQRADPQVSLQPDGWYYYTATVPEYDRIEIRRARSLDDLGAAPAKTVWRKHATGVMGAHIWAPEMHRIGGKWYIYFTAGSAEHPWEIRLYALEN ASADPFAGEWVERGQIKTGWESFSLDATTFEHRGQRYLVWTQTAPDGSKGTNIYLAKMDTPLSIKGPAVLLTKPEYAWEKVKFAVDEGPAV |
Full Sequence |
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Protein Sequence Length: 309 Download |
RAGRRGGAVR GASAAGGRGR TGIQAFAVDV GGRGRGGDGR PAAQAESLNE YRSREKFHGS 60 DPRKATESGE EGGIMQHRLL PRSLSGDPMY RFALRALPAL TLCVAAACAP AHAAEPVFHN 120 PLVLQRADPQ VSLQPDGWYY YTATVPEYDR IEIRRARSLD DLGAAPAKTV WRKHATGVMG 180 AHIWAPEMHR IGGKWYIYFT AGSAEHPWEI RLYALENASA DPFAGEWVER GQIKTGWESF 240 SLDATTFEHR GQRYLVWTQT APDGSKGTNI YLAKMDTPLS IKGPAVLLTK PEYAWEKVKF 300 AVDEGPAVL |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd08978 | GH_F | 3.0e-14 | 127 | 309 | 187 | + 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. | ||
cd08999 | GH43_ABN_2 | 9.0e-16 | 120 | 309 | 203 | + 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. | ||
pfam04616 | Glyco_hydro_43 | 7.0e-36 | 118 | 309 | 195 | + Glycosyl hydrolases family 43. The glycosyl hydrolase family 43 contains members that are arabinanase. Rabinanases hydrolyses the alpha-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The structure of arabinanase Arb43A from Cellvibrio japonicus reveals a five-bladed beta-propeller fold. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. | ||
cd08980 | GH43_1 | 2.0e-79 | 127 | 309 | 183 | + Glycosyl hydrolase family 43. This glycosyl hydrolase family 43 (GH43) includes enzymes with beta-xylosidase (EC 3.2.1.37) and alpha-L-arabinofuranosidase (EC 3.2.1.55) and possibly bifunctional xylosidase/arabinofuranosidase 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. | ||
COG3940 | COG3940 | 5.0e-80 | 120 | 309 | 194 | + Predicted beta-xylosidase [General function prediction only] |
Gene Ontology | |
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GO Term | Description |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005975 | carbohydrate metabolic process |
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_002536865.1 | 0 | 1 | 309 | 1 | 309 | Alpha-N-arabinofuranosidase 2 precursor, putative [Ricinus communis] |
RefSeq | YP_001038535.1 | 0 | 105 | 309 | 163 | 368 | glycoside hydrolase family protein [Clostridium thermocellum ATCC 27405] |
RefSeq | YP_003487643.1 | 0 | 111 | 309 | 36 | 234 | glycosyl hydrolase [Streptomyces scabiei 87.22] |
RefSeq | ZP_01460278.1 | 0 | 95 | 309 | 13 | 223 | putative alpha-arabinofuranosidase II [Stigmatella aurantiaca DW4/3-1] |
RefSeq | ZP_05428997.1 | 0 | 105 | 309 | 126 | 331 | glycoside hydrolase family 43 [Clostridium thermocellum DSM 2360] |
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 | 3aki_A | 0 | 117 | 309 | 10 | 202 | A Chain A, Contributions Of Left-Handed Helical Residues To The Structure And Stability Of Bacteriophage T4 Lysozyme |
PDB | 3akh_A | 0 | 117 | 309 | 10 | 202 | A Chain A, Contributions Of Left-Handed Helical Residues To The Structure And Stability Of Bacteriophage T4 Lysozyme |
PDB | 3akg_A | 0 | 117 | 309 | 10 | 202 | A Chain A, Contributions Of Left-Handed Helical Residues To The Structure And Stability Of Bacteriophage T4 Lysozyme |
PDB | 3akf_A | 0 | 117 | 309 | 10 | 202 | A Chain A, Crystal Structure Of Exo-1,5-Alpha-L-Arabinofuranosidase |
PDB | 3k1u_A | 0 | 120 | 309 | 11 | 204 | A Chain A, Beta-Xylosidase, Family 43 Glycosyl Hydrolase From Clostridium Acetobutylicum |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
GO890681 | 222 | 117 | 309 | 0.000000000000009 |
GO890785 | 222 | 117 | 309 | 0.000000000000009 |
CI766151 | 73 | 116 | 187 | 0.00000000001 |
HO493636 | 100 | 211 | 308 | 0.000000002 |
BU494469 | 42 | 118 | 159 | 0.0000004 |
Orthologous Group | |||||
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Species | ID | ||||
Ricinus communis | 32250.m000015 | 35285.m000016 |
Sequence Alignments (This image is cropped. Click for full image.) |
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