| Identification |
| HMDB Protein ID
| HMDBP12645 |
| Secondary Accession Numbers
| None |
| Name
| Protein-glucosylgalactosylhydroxylysine glucosidase |
| Synonyms
|
- Acid trehalase-like protein 1
|
| Gene Name
| PGGHG |
| Protein Type
| Unknown |
| Biological Properties |
| General Function
| Not Available |
| Specific Function
| Catalyzes the hydrolysis of glucose from the disaccharide unit linked to hydroxylysine residues of collagen and collagen-like proteins. |
| Pathways
|
Not Available
|
| Reactions
| Not Available |
| GO Classification
|
| Biological Process |
| carbohydrate metabolic process |
| Cellular Component |
| cytosol |
| Molecular Function |
| hydrolase activity, hydrolyzing O-glycosyl compounds |
| protein-glucosylgalactosylhydroxylysine glucosidase activity |
|
| Cellular Location
|
Not Available
|
| Gene Properties |
| Chromosome Location
| Not Available |
| Locus
| Not Available |
| SNPs
| Not Available |
| Gene Sequence
|
Not Available
|
| Protein Properties |
| Number of Residues
| 710 |
| Molecular Weight
| 78357.195 |
| Theoretical pI
| 5.805 |
| Pfam Domain Function
|
|
| Signals
|
Not Available
|
|
Transmembrane Regions
|
Not Available
|
| Protein Sequence
|
Not Available
|
| External Links |
| GenBank ID Protein
| Not Available |
| UniProtKB/Swiss-Prot ID
| F1NZI4 |
| UniProtKB/Swiss-Prot Entry Name
| PGGHG_CHICK |
| PDB IDs
|
Not Available |
| GenBank Gene ID
| Not Available |
| GeneCard ID
| Not Available |
| GenAtlas ID
| Not Available |
| HGNC ID
| Not Available |
| References |
| General References
| - Hamazaki H, Hamazaki MH: Catalytic site of human protein-glucosylgalactosylhydroxylysine glucosidase: Three crucial carboxyl residues were determined by cloning and site-directed mutagenesis. Biochem Biophys Res Commun. 2016 Jan 15;469(3):357-62. doi: 10.1016/j.bbrc.2015.12.005. Epub 2015 Dec 9. [PubMed:26682924 ]
- Authors unspecified: Sequence and comparative analysis of the chicken genome provide unique perspectives on vertebrate evolution. Nature. 2004 Dec 9;432(7018):695-716. doi: 10.1038/nature03154. [PubMed:15592404 ]
|