Q9SYK0 (HEXO2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	580 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	plasma membrane Inferred from direct assay Ref.5. Source: TAIR
Molecular_function	UDP-glucosyltransferase activity Inferred from direct assay PubMed 11641410. Source: TAIR beta-N-acetylhexosaminidase activity Inferred from direct assay Ref.5. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 28	28	Potential
	Chain	29 – 580	552	Beta-hexosaminidase 2		PRO_0000420287
Sites
	Active site	337	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	53	1	N-linked (GlcNAc...) Potential
	Glycosylation	368	1	N-linked (GlcNAc...) Potential
	Glycosylation	378	1	N-linked (GlcNAc...) Potential
	Glycosylation	447	1	N-linked (GlcNAc...) Potential
	Disulfide bond	279 ↔ 342		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9SYK0 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 4C1421A5CA71C853	FASTA	580	64,991
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
IPI	IPI00522995.
PIR	H86189.
RefSeq	NP_172050.1. NM_100439.2.
UniGene	At.42389.
3D structure databases
HSSP	HSSP built from PDB template 1NOW based on UniProtKB P07686.
ProteinModelPortal	Q9SYK0.
SMR	Q9SYK0. Positions 42-563.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT1G05590.1-P.
Protein family/group databases
CAZy	GH20. Glycoside Hydrolase Family 20.
Proteomic databases
PaxDb	Q9SYK0.
PRIDE	Q9SYK0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G05590.1; AT1G05590.1; AT1G05590.
GeneID	837064.
KEGG	ath:AT1G05590.
Organism-specific databases
TAIR	At1g05590.
Phylogenomic databases
eggNOG	COG3525.
HOGENOM	HOG000157972.
InParanoid	Q9SYK0.
KO	K12373.
OMA	DTPGHTG.
PhylomeDB	Q9SYK0.
ProtClustDB	CLSN2682032.
Gene expression databases
Genevestigator	Q9SYK0.
Family and domain databases
Gene3D	3.20.20.80. 1 hit.
InterPro	IPR025705. Beta_hexosaminidase_sua/sub. IPR015883. Glyco_hydro_20_cat-core. IPR015882. Glyco_hydro_20b. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Pfam	PF00728. Glyco_hydro_20. 1 hit. PF02838. Glyco_hydro_20b. 1 hit. [Graphical view]
PIRSF	PIRSF001093. B-hxosamndse_ab_euk_. 1 hit.
PRINTS	PR00738. GLHYDRLASE20.
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HEXO2_ARATH

Accession

Primary (citable) accession number: Q9SYK0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2012
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program