| Basic Information | |
|---|---|
| Species | Eucalyptus grandis |
| Cazyme ID | Eucgr.H02307.1 |
| Family | GH43 |
| Protein Properties | Length: 472 Molecular Weight: 53422.5 Isoelectric Point: 8.6543 |
| Chromosome | Chromosome/Scaffold: 8 Start: 30925770 End: 30929193 |
| Description | Arabinanase/levansucrase/invertase |
| View CDS | |
| External Links |
|---|
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH43 | 160 | 390 | 1.3e-33 |
| DERSGTYYWYGEYKDGPTYHAHKKGAARVDVLGVGCYSSKDLWTWKNEGIVLAATETNETHDLHKSKVLERPKVIYNEKTGKYVMWMHIDNANYTKAAVG IATSDYPTGPFNYLYSKRPHGFDSRDMTIFKDDDGIAYVMYSSENNSVLHVGPLTEDYLDVVNDMRRILVGQHREAPALFKHEGTYYMITSGCTGWAPNE AMAHAAESIMGPWETIGNPCIGGNKMFQLTT | |||
| Full Sequence |
|---|
| Protein Sequence Length: 472 Download |
| MGMRNKYRKP TTLHSNAGSR CSAFAIVWSF MGCLVLLHLI SVCRQKDAAN EGNHLRTSNR 60 PVYLELETVE EDNFQIPQPK GKRSSHAPKN KSRNRKTHPI VDEFLDKKSQ IRHVFFPDKR 120 TAIDPMNSAG NDSFYYFPGR VWLDTEGNPI QAHGGGILYD ERSGTYYWYG EYKDGPTYHA 180 HKKGAARVDV LGVGCYSSKD LWTWKNEGIV LAATETNETH DLHKSKVLER PKVIYNEKTG 240 KYVMWMHIDN ANYTKAAVGI ATSDYPTGPF NYLYSKRPHG FDSRDMTIFK DDDGIAYVMY 300 SSENNSVLHV GPLTEDYLDV VNDMRRILVG QHREAPALFK HEGTYYMITS GCTGWAPNEA 360 MAHAAESIMG PWETIGNPCI GGNKMFQLTT FLAQSTFVIP MPGQPGAFIF MADRWNPAEL 420 RDSRYVWLPL LVGGPVDGPL EYSFGFPLWA RVSIYWHRKW RLPNGSSSST K* 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd08999 | GH43_ABN_2 | 2.0e-16 | 195 | 378 | 209 | + 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 | 8.0e-20 | 195 | 373 | 193 | + 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 | 7.0e-21 | 164 | 377 | 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 | 4.0e-46 | 153 | 430 | 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-129 | 150 | 430 | 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 | |
|---|---|
| GO Term | Description |
| GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
| GO:0005975 | carbohydrate metabolic process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | ACU19498.1 | 0 | 18 | 468 | 15 | 463 | unknown [Glycine max] |
| EMBL | CBI33680.1 | 0 | 1 | 465 | 1 | 429 | unnamed protein product [Vitis vinifera] |
| RefSeq | NP_190557.1 | 0 | 3 | 465 | 4 | 460 | glycosyl hydrolase family protein 43 [Arabidopsis thaliana] |
| RefSeq | NP_201555.2 | 0 | 61 | 463 | 66 | 466 | glycosyl hydrolase family protein 43 [Arabidopsis thaliana] |
| RefSeq | XP_002525277.1 | 0 | 1 | 465 | 32 | 494 | beta-glucanase, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3vt2_F | 0 | 139 | 430 | 45 | 328 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3vt2_E | 0 | 139 | 430 | 45 | 328 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3vt2_D | 0 | 139 | 430 | 45 | 328 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3vt2_C | 0 | 139 | 430 | 45 | 328 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3vt2_B | 0 | 139 | 430 | 45 | 328 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
