y
Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_181765g0010 |
Family | GH43 |
Protein Properties | Length: 290 Molecular Weight: 33032.2 Isoelectric Point: 5.7738 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH43 | 7 | 205 | 3.5e-33 |
GVNCYSSKDLWTWKNEGIVLPGEKVNKTHDLHVSNVLERPKVIYNNHTKQYVMWMHIDNANYSKASVGVAVSSSPTAPFQYLGSKQPHGFDSRDMTIFKD DNGQAYIVYSSEDNSELHIGQLTEDYKDVTKVMRRALVGEHREAPAVFKHRGLYYMITSGCTGWAPNTALAHSAESMLGPWETLGNPCMGGNEDFRRTT |
Full Sequence |
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Protein Sequence Length: 290 Download |
MQVDIVGVNC YSSKDLWTWK NEGIVLPGEK VNKTHDLHVS NVLERPKVIY NNHTKQYVMW 60 MHIDNANYSK ASVGVAVSSS PTAPFQYLGS KQPHGFDSRD MTIFKDDNGQ AYIVYSSEDN 120 SELHIGQLTE DYKDVTKVMR RALVGEHREA PAVFKHRGLY YMITSGCTGW APNTALAHSA 180 ESMLGPWETL GNPCMGGNED FRRTTFFAQG TFVLPLPGMP DTFIFMADRW SPAELRDSRY 240 VWLPLTMDGP ADEPLEDDFE FPIWSRVSIY WHKQWKLPEG WNSPLPNQSS 300 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd08999 | GH43_ABN_2 | 2.0e-8 | 10 | 201 | 213 | + 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. | ||
cd09001 | GH43_XYL_2 | 5.0e-9 | 100 | 231 | 140 | + Glycosyl hydrolase family 43, beta-D-xylosidase. This glycosyl hydrolase family 43 (GH43) includes mostly enzymes that have been characterized to have beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity. They are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. 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. 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 | 8.0e-13 | 10 | 192 | 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 | 8.0e-35 | 7 | 245 | 250 | + 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-109 | 7 | 247 | 242 | + 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 | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CBI33680.1 | 0 | 2 | 282 | 151 | 431 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_001066630.1 | 0 | 2 | 281 | 184 | 463 | Os12g0406100 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_201555.2 | 0 | 2 | 278 | 190 | 466 | glycosyl hydrolase family protein 43 [Arabidopsis thaliana] |
RefSeq | NP_975008.1 | 0 | 2 | 278 | 195 | 471 | glycosyl hydrolase family protein 43 [Arabidopsis thaliana] |
RefSeq | XP_002525277.1 | 0 | 2 | 281 | 216 | 495 | beta-glucanase, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3vt2_F | 0 | 5 | 269 | 83 | 346 | A Chain A, The Crystal Structure Of Rice (Oryza Sativa L.) Os4bglu12 |
PDB | 3vt2_E | 0 | 5 | 269 | 83 | 346 | A Chain A, The Crystal Structure Of Rice (Oryza Sativa L.) Os4bglu12 |
PDB | 3vt2_D | 0 | 5 | 269 | 83 | 346 | A Chain A, The Crystal Structure Of Rice (Oryza Sativa L.) Os4bglu12 |
PDB | 3vt2_C | 0 | 5 | 269 | 83 | 346 | A Chain A, The Crystal Structure Of Rice (Oryza Sativa L.) Os4bglu12 |
PDB | 3vt2_B | 0 | 5 | 269 | 83 | 346 | A Chain A, The Crystal Structure Of Rice (Oryza Sativa L.) Os4bglu12 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
EX425816 | 282 | 5 | 286 | 0 |
ES873055 | 264 | 27 | 290 | 0 |
GT739599 | 249 | 2 | 250 | 0 |
GE477023 | 225 | 2 | 226 | 0 |
GO801753 | 280 | 2 | 281 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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