| Basic Information | |
|---|---|
| Species | Oryza sativa |
| Cazyme ID | LOC_Os12g21789.2 |
| Family | GH43 |
| Protein Properties | Length: 467 Molecular Weight: 53212.9 Isoelectric Point: 6.46 |
| Chromosome | Chromosome/Scaffold: 12 Start: 12264653 End: 12268289 |
| Description | Arabinanase/levansucrase/invertase |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH43 | 160 | 385 | 2e-34 |
| TETYFWYGENKDGKTYKAHSKGADRVDIVGVSCYSSKDLWTWRNEGVVLRGEKKNVTHDLHKSNVLERPKVIYNDRTGKYVMWMHIDDTNYTKASVGVAI SDSPTGPFSYLYSKQPHDCESRDMTIFKDDNGKAYLIYSSEDNSELHIGQLTDDYLDVTDNMRRLLIAQHREAPALFKYEGTYYMITSGCTGWAPNTALA HAATAIMGPWETLGNPCVGGNDIFRS | |||
| Full Sequence |
|---|
| Protein Sequence Length: 467 Download |
| MGLRSKQPKA LAFRCYAASH RSLTLAVWSL AALVVVVNFH LLIIHKEDES TSIHEINRSI 60 VSELEEVEEE KFRVSPPRSR RNPRAVRRKG EQKPPSVVDE FLDESSAVHD MFFPERNMAI 120 DPINGGNDSM YFYYPGRVWL DTDGNPIQAH GGGVLYDEKT ETYFWYGENK DGKTYKAHSK 180 GADRVDIVGV SCYSSKDLWT WRNEGVVLRG EKKNVTHDLH KSNVLERPKV IYNDRTGKYV 240 MWMHIDDTNY TKASVGVAIS DSPTGPFSYL YSKQPHDCES RDMTIFKDDN GKAYLIYSSE 300 DNSELHIGQL TDDYLDVTDN MRRLLIAQHR EAPALFKYEG TYYMITSGCT GWAPNTALAH 360 AATAIMGPWE TLGNPCVGGN DIFRSTTFFS QSTFVLPIPG LSGSFIFMAD RWSPSELRDS 420 RYVWLPLTVG GLPDEAADYS FMFPLWSRVS IYWHRRWRLP EGWRDS* 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd09004 | GH43_bXyl | 8.0e-18 | 191 | 374 | 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. | ||
| cd08990 | GH43_AXH_like | 1.0e-19 | 192 | 370 | 192 | + 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. | ||
| cd08978 | GH_F | 1.0e-39 | 161 | 427 | 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 | 4.0e-118 | 147 | 429 | 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. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
| GO:0005575 | cellular_component |
| GO:0005975 | carbohydrate metabolic process |
| GO:0016787 | hydrolase activity |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | EEC69140.1 | 0 | 1 | 466 | 353 | 818 | hypothetical protein OsI_38068 [Oryza sativa Indica Group] |
| GenBank | EEE53089.1 | 0 | 1 | 466 | 299 | 764 | hypothetical protein OsJ_35850 [Oryza sativa Japonica Group] |
| RefSeq | NP_001066630.1 | 0 | 1 | 466 | 1 | 466 | Os12g0406100 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001151925.1 | 0 | 1 | 466 | 1 | 467 | glycosyl hydrolase, family 43 protein [Zea mays] |
| RefSeq | XP_002468324.1 | 0 | 1 | 466 | 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 | 136 | 451 | 45 | 346 | A Chain A, Crystal Structure Of The Cellulase Cel9m Of C. Cellulolyticum |
| PDB | 3vt2_E | 0 | 136 | 451 | 45 | 346 | A Chain A, Crystal Structure Of The Cellulase Cel9m Of C. Cellulolyticum |
| PDB | 3vt2_D | 0 | 136 | 451 | 45 | 346 | A Chain A, Crystal Structure Of The Cellulase Cel9m Of C. Cellulolyticum |
| PDB | 3vt2_C | 0 | 136 | 451 | 45 | 346 | A Chain A, Crystal Structure Of The Cellulase Cel9m Of C. Cellulolyticum |
| PDB | 3vt2_B | 0 | 136 | 451 | 45 | 346 | A Chain A, Crystal Structure Of The Cellulase Cel9m Of C. Cellulolyticum |
