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Q8L7S6 (HEXO3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 82. 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 3

EC=3.2.1.52
Alternative name(s):
Beta-GlcNAcase 3
Beta-N-acetylhexosaminidase 3
Beta-hexosaminidase 1
Short name=AtHEX1
N-acetyl-beta-glucosaminidase 3
Gene names
Name:HEXO3
Synonyms:HEX1
Ordered Locus Names:At1g65590
ORF Names:F5I14.13
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length535 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 pyridylaminated chitotriose, 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. Required for the presence of paucimannosidic N-glycans in glycoproteins of roots and leaves. 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

Slightly inhibited by N-acetylcastanospermine. Ref.4

Subcellular location

Cell membrane Ref.5 Ref.6.

Tissue specificity

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

Post-translational modification

N-glycosylated. Ref.5

Disruption phenotype

Reduced amounts of paucimannosidic N-glycans-containg glycoproteins in roots and leaves. Ref.6

Sequence similarities

Belongs to the glycosyl hydrolase 20 family.

Biophysicochemical properties

Kinetic parameters:

KM=2.2 mM for pNP-GlcNAc (at pH 4.6 and 37 degrees Celsius) Ref.4 Ref.5

Vmax=50.3 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 AAB60911.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 535511Beta-hexosaminidase 3
PRO_0000420288

Sites

Active site3291Proton donor By similarity

Amino acid modifications

Glycosylation921N-linked (GlcNAc...) Potential
Glycosylation3311N-linked (GlcNAc...) Potential
Glycosylation4051N-linked (GlcNAc...) Potential
Glycosylation4411N-linked (GlcNAc...) Potential
Glycosylation4961N-linked (GlcNAc...) Potential
Disulfide bond292 ↔ 334 By similarity
Disulfide bond506 ↔ 532 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8L7S6 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 9295E14DB073F966

FASTA53560,014
        10         20         30         40         50         60 
MRGSGAKIAG VLPLFMLFIA GTISAFEDIE RLRIWPLPAQ VSHGGRRMYL SGDFKLVTEG 

        70         80         90        100        110        120 
SKYGDASGIL KEGFDRMLGV VRLSHVISGD RNSSGTGGSA LLQGLHVIIS SSTDELEYGA 

       130        140        150        160        170        180 
DESYKLVVPS PEKPSYAQLE AKSVYGALHG LQTFSQLCHF NLKKKVIEIL MTPWNIIDQP 

       190        200        210        220        230        240 
RFSYRGLLID TSRHYLPLPV IKNVIDSMTY AKLNVLHWHI VDTQSFPLEI PSYPKLWNGA 

       250        260        270        280        290        300 
YSSSQRYTFE DAAEIVNYAR RRGIHVLAEI DVPGHALSWG KGYPALWPSK NCQEPLDVSS 

       310        320        330        340        350        360 
DFTFKVIDGI LSDFSKIFKF KFVHLGGDEV NTTCWSATPR IAQWLKKHRM SEKEAYQYFV 

       370        380        390        400        410        420 
LRAQKIALSH GYEIINWEET FINFGSKLNR KTVVHNWLNT GLVENVTASG LRCIVSNQEF 

       430        440        450        460        470        480 
WYLDHIDAPW QGFYANEPFQ NITDKKQQSL VLGGEVCMWG EHIDASDIEQ TIWPRAAAAA 

       490        500        510        520        530 
ERLWTPYAKL AKNPNNVTTR LAHFRCLLNQ RGVAAAPLVG GGRVVPFEPG SCLAQ 

« 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]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
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, GLYCOSYLATION, BIOPHYSICOCHEMICAL PROPERTIES, 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, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION.
Strain: cv. Columbia.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC001229 Genomic DNA. Translation: AAB60911.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE34399.1.
AY128283 mRNA. Translation: AAM91092.1.
BT000831 mRNA. Translation: AAN33206.1.
PIRA96681.
RefSeqNP_176737.2. NM_105233.4.
UniGeneAt.24164.

3D structure databases

ProteinModelPortalQ8L7S6.
SMRQ8L7S6. Positions 34-521.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH20. Glycoside Hydrolase Family 20.

Proteomic databases

PRIDEQ8L7S6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G65590.1; AT1G65590.1; AT1G65590.
GeneID842871.
KEGGath:AT1G65590.

Organism-specific databases

TAIRAT1G65590.

Phylogenomic databases

HOGENOMHOG000157972.
InParanoidQ8L7S6.
KOK12373.
OMASATCKEP.
PhylomeDBQ8L7S6.
ProtClustDBCLSN2918416.

Enzyme and pathway databases

BioCycARA:AT1G65590-MONOMER.

Gene expression databases

GenevestigatorQ8L7S6.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR025705. Beta_hexosaminidase_sua/sub.
IPR015883. Glyco_hydro_20_cat-core.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00728. Glyco_hydro_20. 1 hit.
[Graphical view]
PIRSFPIRSF001093. B-hxosamndse_ab_euk_. 1 hit.
PRINTSPR00738. GLHYDRLASE20.
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHEXO3_ARATH
AccessionPrimary (citable) accession number: Q8L7S6
Secondary accession number(s): O04477
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2012
Last sequence update: October 1, 2002
Last modified: April 16, 2014
This is version 82 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