Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q54SC9 (HEXA2_DICDI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-hexosaminidase subunit A2

EC=3.2.1.52
Alternative name(s):
Beta-N-acetylhexosaminidase subunit A2
N-acetyl-beta-glucosaminidase subunit A2
Gene names
Name:hexa2
ORF Names:DDB_G0282539
OrganismDictyostelium discoideum (Slime mold) [Reference proteome]
Taxonomic identifier44689 [NCBI]
Taxonomic lineageEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium

Protein attributes

Sequence length541 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines By similarity.

Catalytic activity

Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.

Subcellular location

Lysosome By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 20 family.

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentlysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbeta-N-acetylhexosaminidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 541520Beta-hexosaminidase subunit A2
PRO_0000331236

Sites

Active site3141Proton donor By similarity

Amino acid modifications

Glycosylation3221N-linked (GlcNAc...) Potential
Glycosylation3361N-linked (GlcNAc...) Potential
Glycosylation3561N-linked (GlcNAc...) Potential
Glycosylation4351N-linked (GlcNAc...) Potential
Glycosylation4831N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q54SC9 [UniParc].

Last modified May 24, 2005. Version 1.
Checksum: F670234F1DD3D075

FASTA54161,533
        10         20         30         40         50         60 
MINKFLTIFL IFSIVIIKVL SQSSNEQPLN VVPYPQEVTM IGCNIPLSVG SISIKSNIES 

        70         80         90        100        110        120 
TILSISISRY QSLFFPFVSN NVLKDSSSNI ELSLIIASDD ETLELGIDES YFLLVNQDTY 

       130        140        150        160        170        180 
QIKANTIYGA MRGLETFKQM VVYDVVENSY SLTCAEVVDY PTYQWRGLLV DNARHFLPKN 

       190        200        210        220        230        240 
MVLHIIDSMG YNKFNTMHWH LIDTVAFPVE SKTYPKLTEA LLGPGAIITH DDILEVVAYA 

       250        260        270        280        290        300 
KTYGIRVIPE FDVPGHSASW GVGYPELLSN CPGYPQSSIP LDCSNPYTYS FLENFFSEIA 

       310        320        330        340        350        360 
PLFQDSYFHT GGDELVIDCW ANDTSIQKWM KTNNYNTSDA FQYFEDQLDV ILKSINRTKI 

       370        380        390        400        410        420 
AWNDVLQHGV KFDKETTLVQ TWTNINDLRD VLAAGYKTIT SFFFYLDRQS PTGNHYHYEW 

       430        440        450        460        470        480 
QDTWEDFYAS DPRLNITSNA ENILGGEATM FGEQVSTVNW DARVWPRAIG ISERLWSATE 

       490        500        510        520        530        540 
INNITLALPR IGQFSCDMSR RGISSGPLFP DFCSLPDDLS FSFKPVYQLS KDEIKLILKK 


K 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAFI02000047 Genomic DNA. Translation: EAL66129.1.
RefSeqXP_640110.1. XM_635018.1.

3D structure databases

ProteinModelPortalQ54SC9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING44689.DDBDRAFT_0204822.

Proteomic databases

PRIDEQ54SC9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsDDB0304517; DDB0304517; DDB_G0282539.
GeneID8623642.
KEGGddi:DDB_G0282539.

Organism-specific databases

dictyBaseDDB_G0282539. nagB.

Phylogenomic databases

eggNOGCOG3525.
OMASATCKEP.
PhylomeDBQ54SC9.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
3.30.379.10. 1 hit.
InterProIPR025705. Beta_hexosaminidase_sua/sub.
IPR029018. Chitobiase/Hex_dom_2-like.
IPR015883. Glyco_hydro_20_cat-core.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR029019. HEX_eukaryotic_N.
[Graphical view]
PfamPF00728. Glyco_hydro_20. 1 hit.
PF14845. Glycohydro_20b2. 1 hit.
[Graphical view]
PIRSFPIRSF001093. B-hxosamndse_ab_euk_. 1 hit.
PRINTSPR00738. GLHYDRLASE20.
SUPFAMSSF51445. SSF51445. 1 hit.
SSF55545. SSF55545. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHEXA2_DICDI
AccessionPrimary (citable) accession number: Q54SC9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: May 24, 2005
Last modified: July 9, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Dictyostelium discoideum

Dictyostelium discoideum: entries, gene names and cross-references to dictyBase