| Basic Information | |
|---|---|
| Species | Physcomitrella patens |
| Cazyme ID | Pp1s410_9V6.1 |
| Family | GH43 |
| Protein Properties | Length: 480 Molecular Weight: 54243.8 Isoelectric Point: 8.7146 |
| Chromosome | Chromosome/Scaffold: 410 Start: 41084 End: 43566 |
| Description | Arabinanase/levansucrase/invertase |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH43 | 168 | 380 | 1.5e-31 |
| TQTFYWYGENKDGPTYHAGKHGLARVDVLGISCYSSKDLWAWKFEGMALRGERVDKSSDLYFRNVVERPKVIYNARTKNYIMWMHIDNGNYSKAAVGVAI STQPEGPFEYMGSKRPHGCDSRDMTIFKDDNGDAYIIYSSLTNSELHIGMLTEDYTDIVERGMKKALVSQHREAPAVFKHRNIYYMVTSGCTGWNPNGAL VHVAESMLGPWAT | |||
| Full Sequence |
|---|
| Protein Sequence Length: 480 Download |
| MITMLYRLLK SCNVGNKCRL STLLWSLAAW ILFLHIYNTL FPSGTLLPEP RNPWSKGMDI 60 YADLEVYQRV HKSDRTADVG TKHPPRKKGR FPITIPFKNK GGDRIEEARE QAALQKLAVL 120 FPGRKYAIDP SKTSSGNVGY FYPGRQWRDT DGKTIQAHGG GILYVEGTQT FYWYGENKDG 180 PTYHAGKHGL ARVDVLGISC YSSKDLWAWK FEGMALRGER VDKSSDLYFR NVVERPKVIY 240 NARTKNYIMW MHIDNGNYSK AAVGVAISTQ PEGPFEYMGS KRPHGCDSRD MTIFKDDNGD 300 AYIIYSSLTN SELHIGMLTE DYTDIVERGM KKALVSQHRE APAVFKHRNI YYMVTSGCTG 360 WNPNGALVHV AESMLGPWAT LGDPCIGGED EEFRSHTFFS QGSFVLPLPG LTDSFLFMAD 420 RWRPANLADS RYVWLVLTMG ASAVPIDDAE FSFKFPQCKQ VQIPWAEKWK LPEDWKGSA* 480 540 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd08999 | GH43_ABN_2 | 2.0e-10 | 161 | 378 | 238 | + 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-14 | 200 | 378 | 195 | + 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 | 3.0e-17 | 199 | 383 | 193 | + 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-34 | 170 | 437 | 278 | + 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 | 9.0e-123 | 155 | 439 | 286 | + 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 |
| RefSeq | NP_001066630.1 | 0 | 84 | 478 | 76 | 466 | Os12g0406100 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | XP_001755081.1 | 0 | 97 | 478 | 15 | 394 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_001784566.1 | 0 | 58 | 479 | 1 | 422 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_002468324.1 | 0 | 84 | 478 | 77 | 467 | hypothetical protein SORBIDRAFT_01g043810 [Sorghum bicolor] |
| RefSeq | XP_002525277.1 | 0 | 12 | 477 | 46 | 497 | 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 | 439 | 40 | 330 | A Chain A, 2.35 Angstrom Crystal Structure Of Conserved Hypothetical Protein From Toxoplasma Gondii Me49. |
| PDB | 3vt2_E | 0 | 139 | 439 | 40 | 330 | A Chain A, 2.35 Angstrom Crystal Structure Of Conserved Hypothetical Protein From Toxoplasma Gondii Me49. |
| PDB | 3vt2_D | 0 | 139 | 439 | 40 | 330 | A Chain A, 2.35 Angstrom Crystal Structure Of Conserved Hypothetical Protein From Toxoplasma Gondii Me49. |
| PDB | 3vt2_C | 0 | 139 | 439 | 40 | 330 | A Chain A, 2.35 Angstrom Crystal Structure Of Conserved Hypothetical Protein From Toxoplasma Gondii Me49. |
| PDB | 3vt2_B | 0 | 139 | 439 | 40 | 330 | A Chain A, 2.35 Angstrom Crystal Structure Of Conserved Hypothetical Protein From Toxoplasma Gondii Me49. |
