P13723 (HEXA1_DICDI) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 94.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Beta-hexosaminidase subunit A1 EC=3.2.1.52 Alternative name(s): Beta-N-acetylhexosaminidase subunit A1 N-acetyl-beta-glucosaminidase subunit A1 | ||||||
| Gene names |
| ||||||
| Organism | Dictyostelium discoideum (Slime mold) [Reference proteome] | ||||||
| Taxonomic identifier | 44689 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium![]() |
Protein attributes
| Sequence length | 532 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines. This enzyme plays a role during the slug stage of development in the maintenance of pseudoplasmodia of normal size. Ref.1 |
| Catalytic activity | Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. |
| Subunit structure | Dimer. Ref.3 |
| Subcellular location | |
| Post-translational modification | The N-terminus is blocked. N-glycosylated. Ref.1 |
| Sequence similarities | Belongs to the glycosyl hydrolase 20 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Lysosome |
| Domain | Signal |
| Molecular function | Glycosidase Hydrolase |
| PTM | Glycoprotein |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro |
| Cellular_component | lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | beta-N-acetylhexosaminidase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 18 | 18 | Potential | ||||||
| Chain | 19 – 532 | 514 | Beta-hexosaminidase subunit A1 | PRO_0000012010 | |||||
Sites | |||||||||
| Active site | 308 | 1 | Proton donor By similarity | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 72 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 79 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 350 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 427 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Molecular cloning of the cDNA which encodes beta-N-acetylhexosaminidase A from Dictyostelium discoideum. Complete amino acid sequence and homology with the human enzyme." Graham T.R., Zassenhaus H.P., Kaplan A. J. Biol. Chem. 263:16823-16829(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 105-113; 260-276 AND 295-306, FUNCTION, PTM, GLYCOSYLATION, SUBCELLULAR LOCATION. |
| [2] | "The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. Kuspa A.Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4. |
| [3] | "Genetic analysis of the gene for N-acetylglucosaminidase in Dictyostelium discoideum." Loomis W.F. Genetics 88:277-284(1978) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT. Strain: NC-4. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | J04065 mRNA. Translation: AAA33230.1. AAFI02000096 Genomic DNA. Translation: EAL63881.1. |
| PIR | A30766. |
| RefSeq | XP_637398.1. XM_632306.1. |
3D structure databases | |
| ProteinModelPortal | P13723. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 44689.DDB_0191256. |
Protein family/group databases | |
| CAZy | GH20. Glycoside Hydrolase Family 20. |
Proteomic databases | |
| PRIDE | P13723. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblProtists | DDB0191256; DDB0191256; DDB_G0287033. |
| GeneID | 8625929. |
| KEGG | ddi:DDB_G0287033. |
Organism-specific databases | |
| dictyBase | DDB_G0287033. nagA. |
Phylogenomic databases | |
| eggNOG | COG3525. |
| KO | K12373. |
| OMA | SARMADY. |
| ProtClustDB | CLSZ2430037. |
Family and domain databases | |
| Gene3D | 3.20.20.80. 1 hit. |
| InterPro | IPR025705. Beta_hexosaminidase_sua/sub. IPR015883. Glyco_hydro_20_cat-core. IPR015882. Glyco_hydro_20b. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view] |
| Pfam | PF00728. Glyco_hydro_20. 1 hit. PF02838. Glyco_hydro_20b. 1 hit. [Graphical view] |
| PIRSF | PIRSF001093. B-hxosamndse_ab_euk_. 1 hit. |
| PRINTS | PR00738. GLHYDRLASE20. |
| SUPFAM | SSF51445. Glyco_hydro_cat. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | HEXA1_DICDI | ||||||||
| Accession | Primary (citable) accession number: P13723 Secondary accession number(s): Q54KX2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| Dictyostelium discoideum Dictyostelium discoideum: entries, gene names and cross-references to dictyBase |
| SIMILARITY comments Index of protein domains and families |

Clusters with
