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Protein

Beta-hexosaminidase A

Gene

hex-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 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. Degrades chitotriose.1 Publication

Catalytic activityi

Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.1 Publication

Kineticsi

  1. KM=1.1 mM for p-nitrophenyl-beta-N-acetylglucosaminide1 Publication

pH dependencei

Optimum pH is 5.5.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei325 – 3251Proton donorBy similarity

GO - Molecular functioni

  1. beta-N-acetylhexosaminidase activity Source: UniProtKB
  2. hexosaminidase activity Source: WormBase

GO - Biological processi

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

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BRENDAi3.2.1.52. 1045.
ReactomeiREACT_197669. Hyaluronan uptake and degradation.
REACT_197713. Glycosphingolipid metabolism.
REACT_197721. Keratan sulfate degradation.
REACT_197754. CS/DS degradation.
SABIO-RKQ22492.

Protein family/group databases

CAZyiGH20. Glycoside Hydrolase Family 20.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-hexosaminidase A (EC:3.2.1.52)
Alternative name(s):
Beta-N-acetylhexosaminidase
N-acetyl-beta-glucosaminidase
Gene namesi
Name:hex-1
ORF Names:T14F9.3
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
ProteomesiUP000001940: Chromosome X

Organism-specific databases

WormBaseiT14F9.3; CE07499; WBGene00020509; hex-1.

Subcellular locationi

Lysosome Curated

GO - Cellular componenti

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

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Disruption phenotypei

Worms show reduced degradation of p-nitrophenyl-beta-N-acetylglucosaminide and no chitotriosidase activity.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 555537Beta-hexosaminidase APRO_0000012009Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi47 – 471N-linked (GlcNAc...)Sequence Analysis
Glycosylationi351 – 3511N-linked (GlcNAc...)3 Publications
Glycosylationi412 – 4121N-linked (GlcNAc...)Sequence Analysis
Glycosylationi460 – 4601N-linked (GlcNAc...)2 Publications

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ22492.

Expressioni

Tissue specificityi

Expressed in coelomocytes and neurons of the pharyngeal region and nerve cord.1 Publication

Developmental stagei

Expressed throughout the life cycle.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ22492.
SMRiQ22492. Positions 90-547.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 20 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3525.
GeneTreeiENSGT00390000008107.
HOGENOMiHOG000157972.
InParanoidiQ22492.
KOiK12373.
OMAiDSESFPY.
PhylomeDBiQ22492.

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.

Q22492-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLLIPILIF ALITTAVTWF YGRDDPDRWS VGGVWPLPKK IVYGSKNRTI
60 70 80 90 100
TYDKIGIDLG DKKDCDILLS MADNYMNKWL FPFPVEMKTG GTEDFIITVT
110 120 130 140 150
VKDECPSGPP VHGASEEYLL RVSLTEAVIN AQTVWGALRA MESLSHLVFY
160 170 180 190 200
DHKSQEYQIR TVEIFDKPRF PVRGIMIDSS RHFLSVNVIK RQLEIMSMNK
210 220 230 240 250
LNVLHWHLVD SESFPYTSVK FPELHGVGAY SPRHVYSRED IADVIAFARL
260 270 280 290 300
RGIRVIPEFD LPGHTSSWRG RKGFLTECFD EKGVETFLPN LVDPMNEANF
310 320 330 340 350
DFISEFLEEV TETFPDQFLH LGGDEVSDYI VECWERNKKI RKFMEEKGFG
360 370 380 390 400
NDTVLLENYF FEKLYKIVEN LKLKRKPIFW QEVFDNNIPD PNAVIHIWKG
410 420 430 440 450
NTHEEIYEQV KNITSQNFPV IVSACWYLNY IKYGADWRDE IRGTAPSNSR
460 470 480 490 500
YYYCDPTNFN GTVAQKELVW GGIAAIWGEL VDNTNIEARL WPRASAAAER
510 520 530 540 550
LWSPAEKTQR AEDAWPRMHE LRCRLVSRGY RIQPNNNPDY CPFEFDEPPA

TKTEL
Length:555
Mass (Da):64,379
Last modified:November 1, 1996 - v1
Checksum:i5E797F9FD82F6BB4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM748820 mRNA. Translation: CAO72174.1.
FO081076 Genomic DNA. Translation: CCD68941.1.
PIRiT29377.
RefSeqiNP_508409.1. NM_076008.6.
UniGeneiCel.353.

Genome annotation databases

EnsemblMetazoaiT14F9.3; T14F9.3; WBGene00020509.
GeneIDi180533.
KEGGicel:CELE_T14F9.3.
UCSCiT14F9.3. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM748820 mRNA. Translation: CAO72174.1.
FO081076 Genomic DNA. Translation: CCD68941.1.
PIRiT29377.
RefSeqiNP_508409.1. NM_076008.6.
UniGeneiCel.353.

3D structure databases

ProteinModelPortaliQ22492.
SMRiQ22492. Positions 90-547.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH20. Glycoside Hydrolase Family 20.

Proteomic databases

PaxDbiQ22492.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiT14F9.3; T14F9.3; WBGene00020509.
GeneIDi180533.
KEGGicel:CELE_T14F9.3.
UCSCiT14F9.3. c. elegans.

Organism-specific databases

CTDi180533.
WormBaseiT14F9.3; CE07499; WBGene00020509; hex-1.

Phylogenomic databases

eggNOGiCOG3525.
GeneTreeiENSGT00390000008107.
HOGENOMiHOG000157972.
InParanoidiQ22492.
KOiK12373.
OMAiDSESFPY.
PhylomeDBiQ22492.

Enzyme and pathway databases

BRENDAi3.2.1.52. 1045.
ReactomeiREACT_197669. Hyaluronan uptake and degradation.
REACT_197713. Glycosphingolipid metabolism.
REACT_197721. Keratan sulfate degradation.
REACT_197754. CS/DS degradation.
SABIO-RKQ22492.

Miscellaneous databases

NextBioi909772.
PROiQ22492.

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. "Biosynthesis of truncated N-linked oligosaccharides results from non-orthologous hexosaminidase-mediated mechanisms in nematodes, plants, and insects."
    Gutternigg M., Kretschmer-Lubich D., Paschinger K., Rendic D., Hader J., Geier P., Ranftl R., Jantsch V., Lochnit G., Wilson I.B.H.
    J. Biol. Chem. 282:27825-27840(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
  2. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.
  3. "Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins."
    Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J., Kasai K., Takahashi N., Isobe T.
    Nat. Biotechnol. 21:667-672(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-351 AND ASN-460, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Bristol N2.
  4. "Identification of the hydrophobic glycoproteins of Caenorhabditis elegans."
    Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J.
    Glycobiology 15:952-964(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-351, IDENTIFICATION BY MASS SPECTROMETRY.
  5. "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins."
    Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T.
    Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-351 AND ASN-460, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Bristol N2.

Entry informationi

Entry nameiHEXA_CAEEL
AccessioniPrimary (citable) accession number: Q22492
Secondary accession number(s): A7DY65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: January 7, 2015
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  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.