| Basic Information | |
|---|---|
| Species | Physcomitrella patens |
| Cazyme ID | Pp1s16_243V6.1 |
| Family | GH43 |
| Protein Properties | Length: 477 Molecular Weight: 54226.2 Isoelectric Point: 9.4324 |
| Chromosome | Chromosome/Scaffold: 16 Start: 1944144 End: 1946409 |
| 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 | 169 | 386 | 2.1e-32 |
| FFWYGENKGGRTYHLSKRGTARVDVLGVNCYSSKDLWSWKFEGRALKGEYRNKKSDLYVKNVVERPKVIYNDRSKLYVMWMHIDNGTYSKAAIGVAVSTH PVGPFEYLGSKRPHGCDSRDMTVFKDDNGDAYIVYSSQINNELHVGKLTEDYLDVMERGMEKIFIKQRREAPAVFKHKSIYYMLTSGCTSWNPNGALIHA STSMLGPWVTIGDPCVGG | |||
| Full Sequence |
|---|
| Protein Sequence Length: 477 Download |
| MMHRLFKTCH VGTKCCLLTL IWSFATWIVI FQVYHVLFPS KSEIPELRKS QLMDSVNVSP 60 DISAFQSALK HVSIRGEPLM KESSSVQIRE NSSLKNNTRN RAVEEAKLLR LKKLAGLLFP 120 SKALSMDASK ANHSEVGIYY PGREWRDIAG HPIQAHGGGI IYVPKSETFF WYGENKGGRT 180 YHLSKRGTAR VDVLGVNCYS SKDLWSWKFE GRALKGEYRN KKSDLYVKNV VERPKVIYND 240 RSKLYVMWMH IDNGTYSKAA IGVAVSTHPV GPFEYLGSKR PHGCDSRDMT VFKDDNGDAY 300 IVYSSQINNE LHVGKLTEDY LDVMERGMEK IFIKQRREAP AVFKHKSIYY MLTSGCTSWN 360 PNGALIHAST SMLGPWVTIG DPCVGGDEEL RTLTFFSQGS FVLPLPGLQD TFIFMGDRWL 420 PSDLRDSRYV WLPLTMNGPL YQGVSTDIHF PQLQRVSIRW ADEWKLPQGW NNSQNL* 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd08990 | GH43_AXH_like | 5.0e-19 | 198 | 376 | 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 | 2.0e-21 | 198 | 381 | 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-35 | 163 | 434 | 282 | + 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-128 | 153 | 436 | 285 | + 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 | EEE53089.1 | 0 | 117 | 473 | 409 | 764 | hypothetical protein OsJ_35850 [Oryza sativa Japonica Group] |
| RefSeq | NP_001066630.1 | 0 | 117 | 473 | 111 | 466 | Os12g0406100 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001151925.1 | 0 | 117 | 473 | 113 | 467 | glycosyl hydrolase, family 43 protein [Zea mays] |
| RefSeq | XP_001755081.1 | 0 | 80 | 476 | 1 | 397 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_001784566.1 | 0 | 94 | 473 | 40 | 421 | predicted protein [Physcomitrella patens subsp. patens] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3vt2_F | 0 | 137 | 447 | 40 | 347 | A Chain A, Crystal Structure Of Human Class I Alpha1,2-Mannosidase In Complex With 1-Deoxymannojirimycin |
| PDB | 3vt2_E | 0 | 137 | 447 | 40 | 347 | A Chain A, Crystal Structure Of Human Class I Alpha1,2-Mannosidase In Complex With 1-Deoxymannojirimycin |
| PDB | 3vt2_D | 0 | 137 | 447 | 40 | 347 | A Chain A, Crystal Structure Of Human Class I Alpha1,2-Mannosidase In Complex With 1-Deoxymannojirimycin |
| PDB | 3vt2_C | 0 | 137 | 447 | 40 | 347 | A Chain A, Crystal Structure Of Human Class I Alpha1,2-Mannosidase In Complex With 1-Deoxymannojirimycin |
| PDB | 3vt2_B | 0 | 137 | 447 | 40 | 347 | A Chain A, Crystal Structure Of Human Class I Alpha1,2-Mannosidase In Complex With 1-Deoxymannojirimycin |
