| Basic Information | |
|---|---|
| Species | Sorghum bicolor |
| Cazyme ID | Sb01g043810.1 |
| Family | GH43 |
| Protein Properties | Length: 468 Molecular Weight: 53500.6 Isoelectric Point: 6.993 |
| Chromosome | Chromosome/Scaffold: 1 Start: 66895884 End: 66900217 |
| 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 | 161 | 386 | 1e-35 |
| TNTYFWYGENKDGKTYKAHSKGADRVDIIGVSCYSSKDLWTWKNEGLVLRGEEKNVTHDLHKSNVLERPKVIYNDRTGKYVMWMHIDDANYTKASVGVAV SDSPTGPFTYLYSKRPHDCESRDMTIFKDDDGKAYLIYSSEDNSELHIGPLTDDYLDVTDVMRRLLIAQHREAPALFRHEGTYYMVTSGCTGWAPNTALA HAATSVMGPWETLGNPCVGGNEVFRS | |||
| Full Sequence |
|---|
| Protein Sequence Length: 468 Download |
| MGMRSRHPKA LGFRCYPASH RSLTLVLWSL AALVVVVNFH LLIIHKEEAE SMSTHEIRRS 60 IMRELEVVEE EKFRLSPPRS RRNPRAVRRK GEKKPPTIVD EFLDQSSAVH DMFFPELNTA 120 VDPINGGNDS MYFYYPGRIW LDTDGKPIQA HGGGVLYDKR TNTYFWYGEN KDGKTYKAHS 180 KGADRVDIIG VSCYSSKDLW TWKNEGLVLR GEEKNVTHDL HKSNVLERPK VIYNDRTGKY 240 VMWMHIDDAN YTKASVGVAV SDSPTGPFTY LYSKRPHDCE SRDMTIFKDD DGKAYLIYSS 300 EDNSELHIGP LTDDYLDVTD VMRRLLIAQH REAPALFRHE GTYYMVTSGC TGWAPNTALA 360 HAATSVMGPW ETLGNPCVGG NEVFRSTTFF SQSTFVLPVP GLPGSFIFMA DRWNPSDLID 420 SRYVWLPLTI GGIPDEAADY SFMFPLWSRV SIYWHKRWRL PEEWRDS* 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd08990 | GH43_AXH_like | 1.0e-21 | 193 | 371 | 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 | 3.0e-22 | 192 | 375 | 195 | + 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 | 1.0e-44 | 151 | 430 | 291 | + 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 | 5.0e-128 | 148 | 430 | 284 | + 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. | ||
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | ACG45031.1 | 0 | 1 | 467 | 1 | 467 | glycosyl hydrolase, family 43 protein [Zea mays] |
| GenBank | EEE53089.1 | 0 | 1 | 467 | 299 | 764 | hypothetical protein OsJ_35850 [Oryza sativa Japonica Group] |
| RefSeq | NP_001066630.1 | 0 | 1 | 467 | 1 | 466 | Os12g0406100 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001151925.1 | 0 | 1 | 467 | 1 | 467 | glycosyl hydrolase, family 43 protein [Zea mays] |
| RefSeq | XP_002468324.1 | 0 | 1 | 467 | 1 | 467 | hypothetical protein SORBIDRAFT_01g043810 [Sorghum bicolor] |
| 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 | 452 | 45 | 346 | A Chain A, Crystal Structure Of The Catalytic Domain Of Xylanase A From Streptomyces Halstedii Jm8 |
| PDB | 3vt2_E | 0 | 137 | 452 | 45 | 346 | A Chain A, Crystal Structure Of The Catalytic Domain Of Xylanase A From Streptomyces Halstedii Jm8 |
| PDB | 3vt2_D | 0 | 137 | 452 | 45 | 346 | A Chain A, Crystal Structure Of The Catalytic Domain Of Xylanase A From Streptomyces Halstedii Jm8 |
| PDB | 3vt2_C | 0 | 137 | 452 | 45 | 346 | A Chain A, Crystal Structure Of The Catalytic Domain Of Xylanase A From Streptomyces Halstedii Jm8 |
| PDB | 3vt2_B | 0 | 137 | 452 | 45 | 346 | A Chain A, Crystal Structure Of The Catalytic Domain Of Xylanase A From Streptomyces Halstedii Jm8 |
