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Protein

Beta-hexosaminidase subunit A1

Gene

hexa1

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei308 – 3081Proton donorBy similarity

GO - Molecular functioni

  1. beta-N-acetylhexosaminidase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH20. Glycoside Hydrolase Family 20.

Names & Taxonomyi

Protein namesi
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 namesi
Name:hexa1
Synonyms:nagA
ORF Names:DDB_G0287033
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
ProteomesiUP000002195: Chromosome 4, UP000002195: Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0287033. nagA.

Subcellular locationi

Lysosome 1 Publication

GO - Cellular componenti

  1. lysosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 532514Beta-hexosaminidase subunit A1PRO_0000012010Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi72 – 721N-linked (GlcNAc...)Sequence Analysis
Glycosylationi79 – 791N-linked (GlcNAc...)Sequence Analysis
Glycosylationi350 – 3501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi427 – 4271N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

The N-terminus is blocked.
N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiP13723.

Interactioni

Subunit structurei

Dimer.1 Publication

Protein-protein interaction databases

STRINGi44689.DDB_0191256.

Structurei

3D structure databases

ProteinModelPortaliP13723.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 20 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3525.
InParanoidiP13723.
KOiK12373.
OMAiWNDPIDY.
PhylomeDBiP13723.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
3.30.379.10. 1 hit.
InterProiIPR025705. 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]
PfamiPF00728. Glyco_hydro_20. 1 hit.
PF14845. Glycohydro_20b2. 1 hit.
[Graphical view]
PIRSFiPIRSF001093. B-hxosamndse_ab_euk_. 1 hit.
PRINTSiPR00738. GLHYDRLASE20.
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF55545. SSF55545. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P13723-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKKIILFFA VLIAIVIGQQ PLNVVPYPQQ VSIGTCVIPV APGSILIESN
60 70 80 90 100
IESATFSVSM DRYTNLFFPF SNESEPSSNE SFLLSVTIYS DDETLQLGID
110 120 130 140 150
ESYSLSIEQG SYQLKATNIY GAMRGLETFK QLIVYNELEN SYSIVCVSIS
160 170 180 190 200
DSPRYPWRGF MVDSARHYIP KNMILHMIDS LGFSKFNTLH WHMVDAVAFP
210 220 230 240 250
VESTTYPDLT KGAFSPSATF SHDDIQEVVA YAKTYGIRVI PEFDIPGHAA
260 270 280 290 300
AWGIGYPELV ATCPDYAANV NNIPLDISNP ATFTFIQNLF TEIAPLFIDN
310 320 330 340 350
YFHTGGDELV TGCWLEDPAI ANWMTKMGFS TTDAFQYFEN NLDVTMKSIN
360 370 380 390 400
RTKITWNDPI DYGVQLNPET LVQVWSSGSD LQGIVNSGYK ALVSFAWYLD
410 420 430 440 450
KQNPDNNIHY EWQDTWQDFY AADPTNNIST NAENIIGGEA TMWAEQINQV
460 470 480 490 500
NWDVRVWPRA IGIAERLWSA QSVNSVSLAL PRIGHFTCDL SRRGIQSGPL
510 520 530
FPDYCPMQDD LVFTMKPNTK LSKSEIKLIL NK
Length:532
Mass (Da):59,788
Last modified:January 1, 1990 - v1
Checksum:iCE651DD79F456514
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04065 mRNA. Translation: AAA33230.1.
AAFI02000096 Genomic DNA. Translation: EAL63881.1.
PIRiA30766.
RefSeqiXP_637398.1. XM_632306.1.

Genome annotation databases

EnsemblProtistsiDDB0191256; DDB0191256; DDB_G0287033.
GeneIDi8625929.
KEGGiddi:DDB_G0287033.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04065 mRNA. Translation: AAA33230.1.
AAFI02000096 Genomic DNA. Translation: EAL63881.1.
PIRiA30766.
RefSeqiXP_637398.1. XM_632306.1.

3D structure databases

ProteinModelPortaliP13723.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi44689.DDB_0191256.

Protein family/group databases

CAZyiGH20. Glycoside Hydrolase Family 20.

Proteomic databases

PRIDEiP13723.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiDDB0191256; DDB0191256; DDB_G0287033.
GeneIDi8625929.
KEGGiddi:DDB_G0287033.

Organism-specific databases

dictyBaseiDDB_G0287033. nagA.

Phylogenomic databases

eggNOGiCOG3525.
InParanoidiP13723.
KOiK12373.
OMAiWNDPIDY.
PhylomeDBiP13723.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
3.30.379.10. 1 hit.
InterProiIPR025705. 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]
PfamiPF00728. Glyco_hydro_20. 1 hit.
PF14845. Glycohydro_20b2. 1 hit.
[Graphical view]
PIRSFiPIRSF001093. B-hxosamndse_ab_euk_. 1 hit.
PRINTSiPR00738. GLHYDRLASE20.
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF55545. SSF55545. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiHEXA1_DICDI
AccessioniPrimary (citable) accession number: P13723
Secondary accession number(s): Q54KX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: January 7, 2015
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Dictyostelium discoideum
    Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.