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Q9SYK0 (HEXO2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 89. 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 2

EC=3.2.1.52
Alternative name(s):
Beta-GlcNAcase 2
Beta-N-acetylhexosaminidase 2
Beta-hexosaminidase 3
Short name=AtHEX3
N-acetyl-beta-glucosaminidase 2
Gene names
Name:HEXO2
Synonyms:HEX3
Ordered Locus Names:At1g05590
ORF Names:F3F20.4
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length580 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has a broad substrate specificity. Can use synthetic substrates such as p-nitrophenyl-beta-N-acetylglucosaminide, p-nitrophenyl-2-acetamido-2-deoxy-beta-D-glucopyranoside (pNP-GlcNAc), p-nitrophenyl-2-acetamido-2-deoxy-beta-D-galactopyranoside (pNP-GalNAc), 4-methylumbelliferyl-2-acetamido-2-deoxy-beta-D-glucopyranoside (MU-GlcNAc), and 4-methylumbelliferyl-6-sulfo-2-acetamido-2-deoxy-beta-D-glucopyranoside (MU-GlcNAc-6SO4) as substrates. Removes terminal GlcNAc residues from alpha1,3- and alpha1,6-mannosyl branches of biantennary N-glycans without any strict branch preference. Ref.4 Ref.5 Ref.6

Catalytic activity

Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. Ref.5

Enzyme regulation

Inhibited by N-acetylcastanospermine. Ref.4

Subcellular location

Cell membrane Ref.5.

Tissue specificity

Expressed in roots, leaves, stems, flowers and siliques. Ref.5

Post-translational modification

N-glycosylated. Ref.5

Sequence similarities

Belongs to the glycosyl hydrolase 20 family.

Biophysicochemical properties

Kinetic parameters:

KM=1.2 mM for pNP-GlcNAc (at pH 4.6 and 37 degrees Celsius) Ref.4 Ref.5

Vmax=7.9 µmol/min/mg enzyme with pNP-GlcNAc as substrate (at pH 4.6 and 37 degrees Celsius)

pH dependence:

Optimum pH is 4-5.

Sequence caution

The sequence AK229119 differs from that shown. Reason: Frameshift at position 240.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Chain29 – 580552Beta-hexosaminidase 2
PRO_0000420287

Sites

Active site3371Proton donor By similarity

Amino acid modifications

Glycosylation531N-linked (GlcNAc...) Potential
Glycosylation3681N-linked (GlcNAc...) Potential
Glycosylation3781N-linked (GlcNAc...) Potential
Glycosylation4471N-linked (GlcNAc...) Potential
Disulfide bond279 ↔ 342 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9SYK0 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 4C1421A5CA71C853

FASTA58064,991
        10         20         30         40         50         60 
MLTLSKFHVI LIPILFFITL LSPLFSIALP INIWPKPRFL SWPQHKAIAL SPNFTILAPE 

        70         80         90        100        110        120 
HQYLSASVTR YHNLIRSENY SPLISYPVKL MKRYTLRNLV VTVTDFSLPL HHGVDESYKL 

       130        140        150        160        170        180 
SIPIGSFSAH LLAHSAWGAM RGLETFSQMI WGTSPDLCLP VGIYIQDSPL FGHRGVLLDT 

       190        200        210        220        230        240 
SRNYYGVDDI MRTIKAMSAN KLNVFHWHIT DSQSFPLVLP SEPSLAAKGS LGPDMVYTPE 

       250        260        270        280        290        300 
DVSKIVQYGF EHGVRVLPEI DTPGHTGSWG EAYPEIVTCA NMFWWPAGKS WEERLASEPG 

       310        320        330        340        350        360 
TGQLNPLSPK TYEVVKNVIQ DIVNQFPESF FHGGGDEVIP GCWKTDPAIN SFLSSGGTLS 

       370        380        390        400        410        420 
QLLEKYINST LPYIVSQNRT VVYWEDVLLD AQIKADPSVL PKEHTILQTW NNGPENTKRI 

       430        440        450        460        470        480 
VAAGYRVIVS SSEFYYLDCG HGGFLGNDSI YDQKESGGGS WCAPFKTWQS IYNYDIADGL 

       490        500        510        520        530        540 
LNEEERKLVL GGEVALWSEQ ADSTVLDSRL WPRASALAES LWSGNRDERG VKRCGEAVDR 

       550        560        570        580 
LNLWRYRMVK RGIGAEPIQP LWCLKNPGMC NTVHGALQDQ 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"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: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, REVIEW.
[5]"Enzymatic properties and subcellular localization of Arabidopsis beta-N-acetylhexosaminidases."
Strasser R., Bondili J.S., Schoberer J., Svoboda B., Liebminger E., Glossl J., Altmann F., Steinkellner H., Mach L.
Plant Physiol. 145:5-16(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION, GENE FAMILY, NOMENCLATURE.
[6]"Beta-N-acetylhexosaminidases HEXO1 and HEXO3 are responsible for the formation of paucimannosidic N-glycans in Arabidopsis thaliana."
Liebminger E., Veit C., Pabst M., Batoux M., Zipfel C., Altmann F., Mach L., Strasser R.
J. Biol. Chem. 286:10793-10802(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC007153 Genomic DNA. Translation: AAD30612.1.
CP002684 Genomic DNA. Translation: AEE27861.1.
AK229119 mRNA. No translation available.
PIRH86189.
RefSeqNP_172050.1. NM_100439.2.
UniGeneAt.42389.

3D structure databases

ProteinModelPortalQ9SYK0.
SMRQ9SYK0. Positions 42-563.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT1G05590.1-P.

Protein family/group databases

CAZyGH20. Glycoside Hydrolase Family 20.

Proteomic databases

PaxDbQ9SYK0.
PRIDEQ9SYK0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G05590.1; AT1G05590.1; AT1G05590.
GeneID837064.
KEGGath:AT1G05590.

Organism-specific databases

TAIRAT1G05590.

Phylogenomic databases

eggNOGCOG3525.
HOGENOMHOG000157972.
InParanoidQ9SYK0.
KOK12373.
OMATAVYWED.
PhylomeDBQ9SYK0.

Enzyme and pathway databases

BioCycARA:AT1G05590-MONOMER.

Gene expression databases

GenevestigatorQ9SYK0.

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 nameHEXO2_ARATH
AccessionPrimary (citable) accession number: Q9SYK0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2012
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names