Q8L7S6 (HEXO3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	535 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 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.

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	plant-type cell wall Inferred from direct assay PubMed 17526915. Source: TAIR plasma membrane Inferred from direct assay Ref.5. Source: TAIR
Molecular_function	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 – 24	24	Potential
	Chain	25 – 535	511	Beta-hexosaminidase 3		PRO_0000420288
Sites
	Active site	329	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	92	1	N-linked (GlcNAc...) Potential
	Glycosylation	331	1	N-linked (GlcNAc...) Potential
	Glycosylation	405	1	N-linked (GlcNAc...) Potential
	Glycosylation	441	1	N-linked (GlcNAc...) Potential
	Glycosylation	496	1	N-linked (GlcNAc...) Potential
	Disulfide bond	292 ↔ 334		By similarity
	Disulfide bond	506 ↔ 532		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8L7S6 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 9295E14DB073F966	FASTA	535	60,014
	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

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]	"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. , 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.
+	Additional computationally mapped references.

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.
IPI	IPI00522647.
PIR	A96681.
RefSeq	NP_176737.2. NM_105233.4.
UniGene	At.24164.
3D structure databases
HSSP	HSSP built from PDB template 1NOW based on UniProtKB P07686.
ProteinModelPortal	Q8L7S6.
SMR	Q8L7S6. Positions 34-521.
ModBase	Search...
Protein family/group databases
CAZy	GH20. Glycoside Hydrolase Family 20.
Proteomic databases
PRIDE	Q8L7S6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G65590.1; AT1G65590.1; AT1G65590.
GeneID	842871.
KEGG	ath:AT1G65590.
Organism-specific databases
TAIR	At1g65590.
Phylogenomic databases
HOGENOM	HOG000157972.
InParanoid	Q8L7S6.
KO	K12373.
OMA	SATCKEP.
PhylomeDB	Q8L7S6.
ProtClustDB	CLSN2918416.
Gene expression databases
ArrayExpress	Q8L7S6.
Genevestigator	Q8L7S6.
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

HEXO3_ARATH

Accession

Primary (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:	May 1, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program