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P13723 (HEXA1_DICDI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 100. 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 A1

EC=3.2.1.52
Alternative name(s):
Beta-N-acetylhexosaminidase subunit A1
N-acetyl-beta-glucosaminidase subunit A1
Gene names
Name:hexa1
Synonyms:nagA
ORF Names:DDB_G0287033
OrganismDictyostelium discoideum (Slime mold) [Reference proteome]
Taxonomic identifier44689 [NCBI]
Taxonomic lineageEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium

Protein attributes

Sequence length532 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Lysosome Ref.1.

Post-translational modification

The N-terminus is blocked.

N-glycosylated. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 20 family.

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Direct protein sequencing
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 – 1818 Potential
Chain19 – 532514Beta-hexosaminidase subunit A1
PRO_0000012010

Sites

Active site3081Proton donor By similarity

Amino acid modifications

Glycosylation721N-linked (GlcNAc...) Potential
Glycosylation791N-linked (GlcNAc...) Potential
Glycosylation3501N-linked (GlcNAc...) Potential
Glycosylation4271N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P13723 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: CE651DD79F456514

FASTA53259,788
        10         20         30         40         50         60 
MIKKIILFFA VLIAIVIGQQ PLNVVPYPQQ VSIGTCVIPV APGSILIESN IESATFSVSM 

        70         80         90        100        110        120 
DRYTNLFFPF SNESEPSSNE SFLLSVTIYS DDETLQLGID ESYSLSIEQG SYQLKATNIY 

       130        140        150        160        170        180 
GAMRGLETFK QLIVYNELEN SYSIVCVSIS DSPRYPWRGF MVDSARHYIP KNMILHMIDS 

       190        200        210        220        230        240 
LGFSKFNTLH WHMVDAVAFP VESTTYPDLT KGAFSPSATF SHDDIQEVVA YAKTYGIRVI 

       250        260        270        280        290        300 
PEFDIPGHAA AWGIGYPELV ATCPDYAANV NNIPLDISNP ATFTFIQNLF TEIAPLFIDN 

       310        320        330        340        350        360 
YFHTGGDELV TGCWLEDPAI ANWMTKMGFS TTDAFQYFEN NLDVTMKSIN RTKITWNDPI 

       370        380        390        400        410        420 
DYGVQLNPET LVQVWSSGSD LQGIVNSGYK ALVSFAWYLD KQNPDNNIHY EWQDTWQDFY 

       430        440        450        460        470        480 
AADPTNNIST NAENIIGGEA TMWAEQINQV NWDVRVWPRA IGIAERLWSA QSVNSVSLAL 

       490        500        510        520        530 
PRIGHFTCDL SRRGIQSGPL FPDYCPMQDD LVFTMKPNTK LSKSEIKLIL NK 

« Hide

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. expand/collapse author list , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., 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.
PIRA30766.
RefSeqXP_637398.1. XM_632306.1.

3D structure databases

ProteinModelPortalP13723.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING44689.DDB_0191256.

Protein family/group databases

CAZyGH20. Glycoside Hydrolase Family 20.

Proteomic databases

PRIDEP13723.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsDDB0191256; DDB0191256; DDB_G0287033.
GeneID8625929.
KEGGddi:DDB_G0287033.

Organism-specific databases

dictyBaseDDB_G0287033. nagA.

Phylogenomic databases

eggNOGCOG3525.
OMASAVEWCK.
PhylomeDBP13723.

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 nameHEXA1_DICDI
AccessionPrimary (citable) accession number: P13723
Secondary accession number(s): Q54KX2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: July 9, 2014
This is version 100 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