Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_10436931g0010 |
Family | GH85 |
Protein Properties | Length: 104 Molecular Weight: 12219.7 Isoelectric Point: 4.5069 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH85 | 4 | 77 | 1.2e-28 |
YDSVTKDGYLDWQNELNEKNKPFFDICDGIFVNYSWQEDYPKQSALVSGKRQFDVYMGIDVFGRGTYGGGQWTV |
Full Sequence |
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Protein Sequence Length: 104 Download |
MYRYDSVTKD GYLDWQNELN EKNKPFFDIC DGIFVNYSWQ EDYPKQSALV SGKRQFDVYM 60 GIDVFGRGTY GGGQWTVMTV HLDECYILVI IFLHSGYFIT YYSG |
Functional Domains Download unfiltered results here | ||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
COG4724 | COG4724 | 4.0e-10 | 4 | 75 | 80 | + Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism] |
pfam03644 | Glyco_hydro_85 | 6.0e-29 | 4 | 73 | 73 | + Glycosyl hydrolase family 85. Family of endo-beta-N-acetylglucosaminidases. These enzymes work on a broad spectrum of substrates. |
cd06547 | GH85_ENGase | 4.0e-32 | 4 | 75 | 75 | + Endo-beta-N-acetylglucosaminidase (ENGase) hydrolyzes the N-N'-diacetylchitobiosyl core of N-glycosylproteins. The beta-1,4-glycosyl bond located between two N-acetylglucosamine residues is hydrolyzed such that N-acetylglucosamine 1 remains with the protein and N-acetylglucosamine 2 forms the reducing end of the released glycan. ENGase is a key enzyme in the processing of free oligosaccharides in the cytosol of eukaryotes. Oligosaccharides formed in the lumen of the endoplasmic reticulum are transported into the cytosol where they are catabolized by cytosolic ENGases and other enzymes, possibly to maximize the reutilization of the component sugars. ENGases have an eight-stranded alpha/beta barrel topology and are classified as a family 85 glycosyl hydrolase (GH85) domain. The GH85 ENGases are sequence-similar to the family 18 glycosyl hydrolases, also known as GH18 chitinases. An ENGase-like protein is also found in bacteria and is included in this alignment model. |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
DDBJ | BAB09989.1 | 5e-33 | 4 | 83 | 210 | 288 | unnamed protein product [Arabidopsis thaliana] |
RefSeq | NP_187715.1 | 4e-32 | 4 | 77 | 215 | 288 | glycosyl hydrolase family 85 protein [Arabidopsis thaliana] |
RefSeq | NP_196165.3 | 5e-33 | 4 | 83 | 210 | 288 | hydrolase, acting on glycosyl bonds / mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase [Arabidopsis thaliana] |
RefSeq | XP_002315137.1 | 8e-33 | 4 | 83 | 215 | 293 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002520784.1 | 1e-31 | 4 | 85 | 212 | 292 | endo beta n-acetylglucosaminidase, 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 | 3fhq_F | 0.00000006 | 4 | 75 | 205 | 282 | A Chain A, Structure Of Endo-Beta-N-Acetylglucosaminidase A |
PDB | 3fhq_D | 0.00000006 | 4 | 75 | 205 | 282 | A Chain A, Structure Of Endo-Beta-N-Acetylglucosaminidase A |
PDB | 3fhq_B | 0.00000006 | 4 | 75 | 205 | 282 | A Chain A, Structure Of Endo-Beta-N-Acetylglucosaminidase A |
PDB | 3fhq_A | 0.00000006 | 4 | 75 | 205 | 282 | A Chain A, Structure Of Endo-Beta-N-Acetylglucosaminidase A |
PDB | 2vtf_B | 0.00000006 | 4 | 75 | 210 | 287 | A Chain A, X-Ray Crystal Structure Of The Endo-Beta-N- Acetylglucosaminidase From Arthrobacter Protophormiae E173q Mutant Reveals A Tim Barrel Catalytic Domain And Two Ancillary Domains |